The human kinetochore, is a complex proteinaceous structure that assembles on centromeric DNA and mediates the association of mitotic chromosomes with spindle microtubules in prometaphase. The molecular composition of the human kinetochore is reviewed in detail in Cheeseman et al., 2008. This complex structure is composed of numerous protein complexes and networks including: the constitutive centromere-associated network (CCAN) containing several sub-networks such as (CENP-H, I, K), (CENP-50/U, O, P, Q, R), the KMN network (containing KNL1, the Mis12 complex, and the Ndc80 complex), the chromosomal passenger complex, the mitotic checkpoint complex, the nucleoporin 107-160 complex and the RZZ complex.
At prometaphase, following breakdown of the nuclear envelope, the kinetochores of condensed chromosomes begin to interact with spindle microtubules. In humans, 15-20 microtubules are bound to each kinetochore (McEwen et al., 2001), and the attachment of 15 microtubules to the kinetochore is shown in this reaction. Recently, it was found that the core kinetochore-microtubule attachment site is within the KMN network and is likely to be formed by two closely apposed low-affinity microtubule-binding sites, one in the Ndc80 complex and a second in KNL1 (Cheeseman et al., 2006).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P67775-1",
"P60953-2",
"Q96GD4-1",
"O43683-1",
"P36873-1",
"P68363-1",
"Q2NKX8-1",
"P53350-1",
"P62714-1",
"Q7L7X3-1",
"P49792-1",
"O60566-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-5666169",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5666169"
}
]
},
{
"id": "R-HSA-5672329",
"name": "IQGAP1 binds CLIP1 and microtubules",
"equation": "",
"summary": "Once bound to activated RAC1 (RAC1:GTP) or CDC42 (CDC42:GTP), IQGAP1 binds CLIP1 (CLIP-170) via the C-terminus of IQGAP1 and the N-terminus of CLIP1. CLIP1 simultaneously interacts with IQGAP1 and the positive end of microtubules. Formation of the RAC1 or CDC42 complex with IQGAP1, CLIP1 and microtubules determines the orientation of microtubules and results in a polarized cellular morphology (Fukata et al. 2002). The RAC1:GTP:IQGAP1:CLIP1 complex is also involved in the regulation of lamellipodia formation and cell invasion in human breast cancer cells (Suzuki and Takahashi 2008).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P60953-2",
"P63000-1",
"P68363-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-5672329",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5672329"
}
]
},
{
"id": "R-HSA-6809003",
"name": "ERGIC-to-Golgi vesicles bind dynein:dynactin",
"equation": "",
"summary": "Unlike COPII-mediated traffic from the ER, COPI traffic to the Golgi is microtubule- and dynein-dependent (Scales et al, 1997; Presley et al, 1997; Ben-Tekaya et al, 2005). Recruitment of the dynein:dynactin complex may in turn rely on interaction with the ankyrin-spectrin network, which may contact integral membrane cargo proteins as they are incorporated into nascent COPI vesicles (Devarajan et al, 1997; Godi et al, 1998; Holleran et al, 1996; Holleran et al, 2001). Although not depicted in this reaction, dynein-dependent vesicle transport is energy dependent.",
"cellular_location": "transport vesicle",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"P62820-1",
"O15498-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"Q9H0U4-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-6809003",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6809003"
}
]
},
{
"id": "R-HSA-6809006",
"name": "Vesicle is tethered through binding GOLGA2:GORASP1, GOLGB1 and the COG complex",
"equation": "",
"summary": "Vesicles tethering at the cis-Golgi is mediated both by long coiled-coil tethers and by large multisubunit complexes. Vesicle-bound USO1 homodimers associate with the Golgi localized GOLGA2:GORASP1 complex and with the Golgi-localized octameric COG tethering complex (Allan et al, 2000; Moyer et al, 2001; Weide et al, 2001; Nakamura et al, 1997; Seeman et al, 2000; Sohda et al, 2007). GOLGB1 is another Golgi localized tether that may facilitate vesicle tethering at the cis-Golgi, although it is also implicated in intra-Golgi retrograde trafficking (Linstedt and Hauri, 1993; Sonnichsen et al, 1998; Alvarez et al, 2001; Beard et al, 2005; reviewed in Appenzeller-Herzog et al, 2006). In addition to binding to USO1, the COG complex also interacts with components of the COPI coat, as well as with SNARE proteins and the TMEM115 protein (Suvorova et al, 2002; Zolov et al, 2005; Shestakova et al, 2007; Ong et al, 2014; reviewed in Willet et al, 2013).",
"cellular_location": "Golgi membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"P62820-1",
"O15498-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"Q9H0U4-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-6809006",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6809006"
}
]
},
{
"id": "R-HSA-6811423",
"name": "Retrograde vesicle is tethered at the ER by the NRZ complex and t-SNAREs",
"equation": "",
"summary": "Retrograde COPI vesicles destined for fusion with the ER are tethered to the ER membrane by interactions with the ER t-SNARE proteins and with the CATCHR ('complexes associated with tethering containing helical rods') complex NRZ (reviewed in Szul and Sztul, 2011; Tagaya et al, 2014). The trimeric NRZ complex, known as Dsl in yeast, is composed of NBAS, RINT1 and ZW10 and is recruited to the ER through association with the ER t-SNAREs USE1L, STX18 and BNIP1 (Hirose et al, 2004; Aoki et al, 2004; Nakajima et al, 2004; Arasaki et al, 2006; Ren et al, 2009; Civril et al, 2010; reviewed in Tagaya et al, 2014). Evidence in yeast suggests components of the Dsl complex also interact with the coatomer coat; these interactions contribute to vesicle fusion both by aiding in the recruitment of the vesicle to the ER membrane and also to the depolymerization of coatomer and thus vesicle uncoating Interactions (Andag et al, 2001; Andag et al, 2003; Reilly et al, 2001; Hsia and Hoelz, 2010; Meiringer et al, 2011; Zink et al, 2009). Note that although this pathway shows COPI vesicles from the Golgi being 'received' exclusively at the ER, vesicles are also tethered and fused at the ERGIC. The SNAREs and tethering complexes that mediate this fusion are not identified.",
"cellular_location": "endoplasmic reticulum membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"P62820-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"Q9H0U4-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-6811423",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6811423"
}
]
},
{
"id": "R-HSA-6811426",
"name": "Retrograde COPI vesicles bind kinesin and microtubules",
"equation": "",
"summary": "COPI-mediated retrograde traffic is dependent on microtubules and the plus-end motor kinsesin. Although it is not shown in this reaction, vesicle translocation along the microtubules by kinesin depends on ATP hydrolysis (Lippincott-Scwartz et al, 1995; Stauber et al, 2006; Tomas et al, 2010)",
"cellular_location": "transport vesicle",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"P62820-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"Q9H0U4-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-6811426",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6811426"
}
]
},
{
"id": "R-HSA-8849350",
"name": "RAB6:GTP displaces PAFAH1B1 from dynein:dynactin complex",
"equation": "",
"summary": "Retrograde tubule formation may depend on the minus-end directed dynein-dynactin motor complex, which is recruited to the Golgi through interaction with both RAB6 and BICD (Short et al, 2002; Hoogenraad et al, 2001; Matanis et al, 2002; Young et al, 2005; Januschke et al, 2007). Interaction of dynein:dynactin with RAB6:GTP activates the motor protein by displacing the PAFAH1B1 protein, which otherwise keeps the motor \\idling\\ (Yamada et al, 2013; reviewed in Heffernan and Simpson, 2014).",
"cellular_location": "Golgi membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"Q9NRW1-1",
"P68363-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"Q10471-1",
"Q10472-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-8849350",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8849350"
}
]
},
{
"id": "R-HSA-8849353",
"name": "Dynein drives COPI-independent retrograde traffic from the Golgi to the ER",
"equation": "",
"summary": "The RAB6 pathway moves select retrograde cargo from the Golgi to the ER in a motor-dependent manner, although the precise details of this translocation remain to be worked out (Girod et al, 1999; White et al, 1999; reviewed in Heffernan and Simpson, 2014). Active RAB18 at the ER membrane may contribute to targeting and fusion of COPI-independent retrograde carriers through interaction with ER-localized tethering factors (Dejgaard et al, 2008; Gerondopoulos et al, 2014; Gillingham et al, 2014)",
"cellular_location": "endoplasmic reticulum membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"Q9NRW1-1",
"P68363-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"Q10471-1",
"Q10472-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-8849353",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8849353"
}
]
},
{
"id": "R-HSA-8852280",
"name": "GTSE1 binds microtubule lattice in interphase cells",
"equation": "",
"summary": "In interphase cells, GTSE1 localizes to the microtubule lattice, probably due to direct binding to tubulin (Scolz et al. 2012).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-8852280",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8852280"
}
]
},
{
"id": "R-HSA-8852298",
"name": "GTSE1 binds MAPRE1 (EB1) at microtubule plus ends",
"equation": "",
"summary": "During interphase, GTSE1 localizes to the growing plus-end tip of microtubules by binding to the microtubule plus end protein MAPRE1 (EB1). This interaction involves two SKIP-like EB1-interaction motifs of GTSE1 and the C-terminal EB-homology (EBH) domain of MAPRE1. The interaction between GTSE1 and MAPRE1 is evolutionarily conserved. The interaction between GTSE1 and MAPRE1 at growing microtubule plus ends promotes cell migration, likely through microtubule-induced disassembly of focal adhesions. GTSE1 expression levels in G1 phase correlate with invasiveness of breast cancer cell lines (Scolz et al. 2012).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-8852298",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8852298"
}
]
},
{
"id": "R-HSA-8852306",
"name": "Mitotic phosphorylation-induced dissociation of GTSE1 from microtubule plus ends",
"equation": "",
"summary": "Starting in mitotic prometaphase, GTSE1 becomes phosphorylated at threonine residues T513 and T526 (and possibly other sites), located adjacent to the two SKIP-like motifs involved in binding to MAPRE1 (EB1). Mitotic phosphorylation of GTSE1 inhibits its association with microtubule plus ends. CDK1 activity inhibits the association of recombinant human GTSE1 with microtubule plus ends in Xenopus extracts, but it is not certain whether CDK1 or another mitotic kinase phosphorylates GTSE1 (Scolz et al. 2012).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-8852308"
],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"P06493-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-8852306",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8852306"
}
]
},
{
"id": "R-HSA-8865774",
"name": "TTLLs polyglutamylate tubulin",
"equation": "",
"summary": "Tubulin is modified by glutamylation and glycylation, the additon of peptide branches made of glutamyl or glycyl residues respectively, which are attached to the gamma-carboxyl group of glutamic acids within the C-terminal tail domains of alpha- and beta-tubulin. Glutamylation, the most prevalent tubulin posttranslational modification, marks stable microtubules and regulates recruitment and activity of microtubule-interacting proteins. Hyperglutamylation in Purkinje cell degeneration (pcd) mice leads to neurodegeneration (Rogowski et al. 2010).
Nine enzymes of the tubulin tyrosine ligase-like (TTLL) family catalyze glutamylation (Garhnam & Roll-Mecak 2012, Garnham et al. 2015). TTLLs can have a preference for either alpha- or beta-tubulin, although many are able to modify either (Janke et al. 2005, Ikegami et al. 2006, van Dijk et al. 2007). Initial characterization of the mouse TTLL family showed that TTLL1, 5, 6, 11, and 13 preferentially poly-glutamylate alpha-tubulin, while TTLL4 and 7 prefer beta-tubulin. While TTLL1 has a preference for alpha-tubulin (Janke et al. 2005), TTLL1 knockout mice displayed decreased glutamylation on alpha- and beta-tubulin (Ikegami et al. 2010). The molecular determinants for specificity are poorly understood and specificity can differ between organisms, preventing an unambiguous classification of TTLLs by their alpha/beta preference. TTLL4, 5, and 7 have been described as initiases, adding a branched glutamic acid to the tubulin tail, while TTLL6, 11, and 13 were suggested to be elongases, adding poly-Glu chains of variable lengths to the branched glutamic acid (Garhnam & Roll-Mecak 2012). The specificity of mammalian TTLL2, 9, and TTLL12 are unknown.
TTLL3, 8, and 10 are glycylases that glycate rather than glutamylate tubulin (Ikegami et al. 2008, Ikegami & Setou 2009, Rogowski et al. 2009, Wloga et al. 2009), with TTLL3 and 8 serving as initiases, and TTLL10 serving as an elongase.
TTLL7, the most abundant glutamylase in neurons, modifies both alpha- and beta-tubulin tail peptides in isolation but shows a preference for beta-tubulin when presented with microtubules. TTLL7 catalyzes the initiatial glutamylation of Beta-tubulin glutamates at multiple internal positions in the Beta-tail, and also the addition of subsequent glutamates to existing branched glutamates (Mukai et al. 2009).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q6ZT98-1",
"P0DPH7-1",
"P68363-1",
"Q14679-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"Q3SXZ7-1",
"Q6EMB2-1",
"Q8N841-1",
"Q9BWV7-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"A6NNM8-1",
"Q8NHH1-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-8865774",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8865774"
}
]
},
{
"id": "R-HSA-8866105",
"name": "CCPs deglutamylate tubulin",
"equation": "",
"summary": "Cytosolic carboxypeptidases (CCPs) catalyze the removal of glutamate residues from the C-terminal tails of both alpha- and beta-tubulin. These glutamate residues are either enzymatically added in the polyglutamylation reaction, or gene-encoded glutamate residues are removed from alpha-tubulin after detyrosination to generate delta2-tubulin (Kimura et al. 2010, Rogowski et al. 2010). CCPs are members of the MC clan, M14 family, subfamily M14D of metallopeptidases (Kalinina et al. 2007, Rodriguez de la Vega et al. 2007). Mouse Ccp1, 2, 3, 4, and 6 are functionally homologous and remove linearly added glutamates from tubulin (alpha-peptide bonds), while Ccp5 specifically removes branching-point glutamates (gamma-peptide bonds) which are generated as first step of the polyglutamylation reaction (Rogowski et al. 2010; Tort et al. 2014). The catalytic activities of the human proteins are inferred from the properties of their mouse homologues and limited studies of human proteins expressed in cultured cells (Rogowski et al. 2010). In this event polyglutamylation is arbitrarily shown on only one tubulin protofilament within the polyglutamylated microtubule.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"Q5U5Z8-1",
"Q8NDL9-1",
"Q8NEM8-1",
"Q5VU57-1",
"Q96MI9-1",
"Q9UPW5-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-8866105",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8866105"
}
]
},
{
"id": "R-HSA-8867370",
"name": "TTLL3, TTLL8, TTLL10 polyglycylate tubulin",
"equation": "",
"summary": "Tubulin is modified by glutamylation and glycylation, the additon of peptide branches made of glutamyl or glycyl residues respectively, which are attached to the gamma-carboxyl group of glutamic acids within the C-terminal tail domains of alpha- and beta-tubulin. They are added by members of the tubulin tyrosine ligase (TTL family). TTLL3, 8, and 10 are glycylases (Ikegami et al. 2008, Ikegami and Setou, 2009; Rogowski et al. 2009; Wloga et al. 2009) with TTLL3 and 8 serving as initiases, and TTLL10 serving as an elongase. In this event polyglycation is arbitrarily shown on only one tubulin protofilament within the microtubule.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"A6PVC2-1",
"P0DPH7-1",
"P68363-1",
"Q9Y4R7-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-8867370",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8867370"
}
]
},
{
"id": "R-HSA-8955706",
"name": "TTL ligates L-Tyr to the carboxy terminus of detyr-alpha tubulin:beta tubulin",
"equation": "",
"summary": "TTL (tubulin tyrosine ligase) ligates tyrosine (L-Tyr) to the carboxy terminus of the alpha-tubulin subunit of an alpha tubulin:beta tubulin dimer in an ATP-dependent reaction. Human TTL has not been characterized in detail; the reaction mechanism annotated here has been worked out with bovine proteins (Deans et al. 1992), and structural studies with chicken proteins demonstrate the basis of the enzyme's specificity for the carboxy terminus of tubulin alpha chains (Prota et al. 2013).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q8NG68-1",
"P0DPH7-1",
"P68363-1",
"Q6PEY2-1",
"Q71U36-1",
"Q9BQE3-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-8955706",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8955706"
}
]
},
{
"id": "R-HSA-8955712",
"name": "SVBP:VASH1,VASH2 hydrolyzes the terminal L-Tyr residue from alphaY-beta tubulin dimer",
"equation": "",
"summary": "TTCP (tubulinyl-tyrosine carboxypeptidase) hydrolyzes the terminal L-Tyr residue from the alpha-tubulin subunit of an alpha tubulin:beta tubulin dimer to yield delY-alpha tubulin and L-tyrosine (L-Tyr). Although TTCP enzyme has not been purified from any species, studies of material partially purified from chicken brain have allowed its activity to be defined and distinguished from those of widely expressed carboxypeptidases with broader substrate specificities (Argarana et al. 1980). This reaction is known to occur in humans (Song & Brody 2015; Yu et al. 2015) and its properties have been inferred from those of its chicken counterpart.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q7L8A9-1",
"Q86V25-1",
"P0DPH7-1",
"P68363-1",
"Q6PEY2-1",
"Q71U36-1",
"Q9BQE3-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-8955712",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8955712"
}
]
},
{
"id": "R-HSA-8955869",
"name": "Polyglutamylase complex (TTLL1) polyglutamylates alpha subunits of tubulin",
"equation": "",
"summary": "Polyglutamylase complex polyglutamylates alpha subunits of tubulin in the brain. The complex contains TTLL1 (Tubulin tyrosine ligase-like 1) protein. The human complex has not been characterized experimentally. Its organization and function have been inferred from biochemical and genetic studies of its mouse counterpart. The mouse complex has been isolated and four additional protein components have been identified (Janke et al. 2005). A mouse mutation that disrupts one of these, Tpgs1, is associated with failure of polyglytamylation of alpha-chains in microtubules (Ikegami et al. 2007). In this event polyglutamylation is arbitrarily shown on only one tubulin protofilament within the microtubule.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O95922-1",
"P0DPH7-1",
"P68363-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-8955869",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8955869"
}
]
},
{
"id": "R-HSA-9610408",
"name": "GluN1:GluN2B (GRIN1:GRIN2B) di-heterotetramers bind LIN7:CASK:APBA1, DLG1 and KIF17",
"equation": "",
"summary": "GluN1:GluN2B (GRIN1:GRIN2B) di-heteromers are transported to the plasma membrane from the endoplasmic reticulum (ER) via transport vesicles. At the membrane of transport vesicles, GluN1:GluN2B NMDA receptors associate with the complex of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1. The microtubule-associated kinesin motor protein KIF17 binds to the LIN7:CASK:APBA1 complex (Jo et al. 1999, Setou et al. 2000). During transport from ER to the plasma membrane, NMDA receptors are diverted from the somatic Golgi network and go through the dendritic ER subcompartment and dendritic Golgi instead. Besides CASK, interaction with DLG1 (SAP97) is required for GluN1:GluN2B NMDA receptors to go through this transport route (Jeyifous et al. 2009).",
"cellular_location": "cytosol, endoplasmic reticulum membrane, transport vesicle membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"O14936-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-9610408",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9610408"
}
]
},
{
"id": "R-HSA-9610627",
"name": "KIF17 transports GluN1:GluN2B (GRIN1:GRIN2B) NMDA receptors to the plasma membrane",
"equation": "",
"summary": "Kinesin KIF17 transports vesicles that contain GluN1:GluN2B (GRIN1:GRIN2B) NMDA receptor to the plasma membrane (Setou et al. 2000).",
"cellular_location": "plasma membrane, transport vesicle membrane",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-3928507"
],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"O14936-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-9610627",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9610627"
}
]
},
{
"id": "R-HSA-9614343",
"name": "Viral UL47:UL48 Proteins Bind HCMV Tegumented Virion to Host Microtuble and Dynein complexs",
"equation": "",
"summary": "Tegument proteins help deliver the Human Cytomegalovirus (HCMV) genome-containing capsid to the nucleus during the viral entry process. Signals initiated upon receptor binding induce cellular antiviral responses but may also prime the cell for subsequent events during viral entry. The Capsid-associated tegument proteins UL47 and UL48 (and perhaps pp150) direct capsids along microtubules (MTs) toward nuclear pore complexes driven by cellular motor proteins such as dynein.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-9614343",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9614343"
}
]
},
{
"id": "R-HSA-9614367",
"name": "HCMV Nuclear Pore Docking",
"equation": "",
"summary": "Virion capsids eventually dissociate from microtubules, dock at nuclear pores, and release their DNA into the nucleus. The role of tegument proteins in this process is implicated but has not been described in detail.",
"cellular_location": "nuclear envelope",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"P49792-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-9614367",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9614367"
}
]
},
{
"id": "R-HSA-9619542",
"name": "AMPK negatively regulates binding of MAPT to microtubules",
"equation": "",
"summary": "AMPK-mediated phosphorylation of MAPT (Tau) interferes with binding of MAPT to the microtubules (Thornton et al. 2011).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P54646-1",
"Q13131-1",
"P68363-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-9619542",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9619542"
}
]
},
{
"id": "R-HSA-9646383",
"name": "Dynein motors transport misfolded proteins",
"equation": "",
"summary": "Misfolded proteins are transported from the microtubule to the microtubule-organizing center (MTOC) in a dynein-mediated mechanism. Dynein motors carry the cargo along the microtubules from the plus end to the minus end (Garcia Mata R et al. 1999). Confirmatory experiments were performed in grivet cell lines.",
"cellular_location": "cytosol, microtubule organizing center",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"Q99497-1",
"P68363-1",
"Q9UBN7-1",
"P13569-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-9646383",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9646383"
}
]
},
{
"id": "R-HSA-9646390",
"name": "Misfolded proteins:HDAC6:Dynein motor binds microtubule",
"equation": "",
"summary": "Histone deacetylase 6 (HDAC6) binds misfolded proteins destined to form aggresomes and subsequently delivers this to dynein motor proteins. HDAC6 can also bind to microtubules thereby anchoring the misfolded proteins and the dynein motor to the microtubule (Hubbert C et al. 2002). Following this, the dynein motors traverse the microtubule to reach the microtubule-organizing center (MTOC).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"Q99497-1",
"P68363-1",
"Q9UBN7-1",
"P13569-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-9646390",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9646390"
}
]
},
{
"id": "R-HSA-9646679",
"name": "PolyUb-Misfolded proteins bind vimentin to form aggresome",
"equation": "",
"summary": "Dynein motor complex drives the multi-ubiquitinated misfolded proteins along the microtubule towards the microtubule organizing center. Here, intermediate filament proteins such as vimentin (VIM) are redistributed to ensheath misfolded proteins to form the aggresome (Johnston JA et al. 1998). Subsequently, the aggresome is removed with the help of autophagy machinery.",
"cellular_location": "microtubule organizing center",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"Q99497-1",
"P68363-1",
"Q9UBN7-1",
"P13569-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-9646679",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9646679"
}
]
},
{
"id": "R-HSA-9646685",
"name": "Aggresome dissociates from dynein and microtubule",
"equation": "",
"summary": "Misfolded proteins are transformed into aggresomes at the microtubule organizing center. Dynein motor proteins facilitate the transport of misfolded proteins along the microtubule. Subsequently, the system disassembles to release the aggresome. The aggresome then recruits chaperone to be degraded by the autophagy machinery (Garcia Mata R et al. 1999).",
"cellular_location": "microtubule organizing center",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"Q99497-1",
"P68363-1",
"Q9UBN7-1",
"P13569-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-9646685",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9646685"
}
]
},
{
"id": "R-HSA-9648017",
"name": "EML4 binds to microtubules",
"equation": "",
"summary": "In interphase cells, EML4 associates with cytosolic microtubules. The interaction involves the N-terminal domain of EML4 (Pollmann et al. 2006). EML4 trimerization is needed for microtubule binding (Richards et al. 2015). EML4 binding stabilizes interphase microtubules (Houtman et al. 2007, Adib et al. 2019).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q8TD19-1",
"P0DPH7-1",
"Q9HC98-1",
"P68363-1",
"Q8TDX7-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-9648017",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9648017"
}
]
},
{
"id": "R-HSA-9648114",
"name": "EML4 recruits NUDC to mitotic spindle",
"equation": "",
"summary": "EML4 binds to NUDC and recruits it to the kinetochores of the mitotic spindle. The interaction involves the WD40 repeats of EML4 and the C-terminus of NUDC (Chen et al. 2015). Knockdown of EML4 produces similar mitotic defects as the knockdown of NUDC. The knockdown of either of these two genes frequently results in post-mitotic cell death, due to activation of the mitotic spindle checkpoint (Chen et al. 2015, Adib et al. 2019). It is uncertain if PLK1-mediated phosphorylation of NUDC precedes its binding to EML4.",
"cellular_location": "cytosol, spindle",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P67775-1",
"Q96GD4-1",
"O43683-1",
"P36873-1",
"P68363-1",
"Q2NKX8-1",
"P53350-1",
"P62714-1",
"Q7L7X3-1",
"P49792-1",
"O60566-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-9648114",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9648114"
}
]
},
{
"id": "R-HSA-9668419",
"name": "SPAST (spastin) mediates the severing of microtubules at chromosome attachment sites",
"equation": "",
"summary": "The AAA+ ATPase activity of spastin (SPAST) removes attached microtubules from chromosomes, allowing formation of a sealed nuclear envelope (Vietri et al. 2015, Ventimiglia et al. 2018).",
"cellular_location": "cytosol, nuclear envelope",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"Q9UBP0-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-9668419",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9668419"
}
]
},
{
"id": "R-HSA-983259",
"name": "Kinesins move along microtubules consuming ATP",
"equation": "",
"summary": "Kinesins consume ATP to power the motor which allows them to move along microtubules. The motor region contains highly conserved Switch 1 (SSRSH) and 2 (DLAGSE) motifs which change conformation during ATP hydrolysis (Rice et al. 1999). These form a salt-bridge that, in myosin, closes the nucleotide-binding cleft, enabling the motor to hydrolyze ATP (Geeves & Holmes 1999). This closed conformation has now been seen by cryo-electron microscopy in human conventional kinesin (Sindelar & Downing 2010) and in a crystal structure of the frog kinesin-5 Eg5 (Parke et al. 2010).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-983259",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-983259"
}
]
},
{
"id": "R-HSA-983266",
"name": "Kinesins bind microtubules",
"equation": "",
"summary": "All kinesins contain a motor domain or head, the position varies but it is structurally highly conserved (Kull et al. 1996, Sablin et al. 1996). The microtubule-binding site includes structural elements which interact with tubulin and undergo movement between the ADP and ATP bound states. The highly conserved switch I (SSRSH) and II (DLAGSE) motifs, which change in conformation during the ATP hydrolysis cycle, form a salt-bridge that, in myosin, closes the nucleotide-binding cleft, enabling the motor to hydrolyze ATP (Geeves & Holmes 1999). This closed conformation has now been seen in a crystal structure of the frog kinesin-5 Eg5 (Parke et al. 2010).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-983266",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-983266"
}
]
},
{
"id": "R-HSA-9836404",
"name": "p-PKR dimer phosphorylates MAPT",
"equation": "",
"summary": "Activated PKR phosphorylates the 2N4F isoform of microtubule-associated protein tau (tau-F, tau-8, MAPT-8) at several serine and threonine residues. In neurons phosphorylated tau dissociates from microtubules, leaving them unstable, and accumulates outside the axon. Accumulation and self-assembly of tau are parts of so-called tau pathology in several neurodegenerative diseases (Reimer et al, 2021).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-9836400"
],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"P19525-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-HSA-9836404",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9836404"
}
]
},
{
"id": "R-NUL-8867463",
"name": "Ccps deglutamylate tubulin",
"equation": "",
"summary": "Cytosolic carboxypeptidases (CCPs) catalyze the removal of glutamate residues from the C-terminal tails of both alpha- and beta-tubulin (Kalinina et al. 2007, Rodriguez de la Vega et al. 2007, Kimura et al. 2010, Rogowski et al. 2010). They are members of the MC clan, M14 family, subfamily M14D of metallopeptidases (Kalinina et al. 2007). Mouse Ccp1, 2, 3, 4, and 6 are functionally homologous and remove long glutamate chains from tubulin, while Ccp5 specifically removes branching-point glutamates (Rogowski et al. 2010; Tort et al. 2014).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-NUL-8867463",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-NUL-8867463"
}
]
},
{
"id": "R-NUL-8955873",
"name": "Polyglutamylase complex (Ttll1) polyglutamylates alpha subunits of tubulin",
"equation": "",
"summary": "Polyglutamylase complex polyglutamylates alpha subunits of tubulin. The complex contains Ttll1 (Tubulin tyrosine ligase-like 1) protein. The complex has been isolated from mouse tissue and four additional protein components have been identified (Janke et al. 2005). A mouse mutation that disrupts one of these, Tpgs1, is associated with failure of polyglytamylation of alpha-chains in microtubules (Ikegami et al. 2007).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P0DPH7-1",
"P68363-1",
"Q6PEY2-1",
"P68366-1",
"Q71U36-1",
"A6NHL2-1",
"Q9NY65-1",
"Q9BQE3-1",
"Q9H853-1",
"P0DPH8-1"
],
"evidence": [
{
"id": "R-NUL-8955873",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-NUL-8955873"
}
]
}
],
"reaction_participants": [
{
"participant_id": "R-HSA-379539",
"participant_name": "TBCE [cytosol]",
"crossref": [
{
"id": "Q15813",
"database": "UniProt",
"url": ""
},
{
"id": "ENSG00000285053-TBCE",
"database": "HPA",
"url": ""
},
{
"id": "4ICV",
"database": "PDB",
"url": ""
},
{
"id": "4ICU",
"database": "PDB",
"url": ""
},
{
"id": "NP_001072983.1",
"database": "RefSeq",
"url": ""
},
{
"id": "Q15813",
"database": "GeneCards",
"url": ""
},
{
"id": "NP_001274730.1",
"database": "RefSeq",
"url": ""
},
{
"id": "Q15813",
"database": "Pharos - Targets",
"url": ""
},
{
"id": "ENSG00000284770",
"database": "OpenTargets",
"url": ""
},
{
"id": "ENST00000647186",
"database": "Ensembl",
"url": ""
},
{
"id": "ENST00000645351",
"database": "Ensembl",
"url": ""
},
{
"id": "ENST00000543662",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSG00000285053",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSP00000384571",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSP00000494796",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSP00000495202",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSG00000284770",
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},
{
"id": "ENSP00000495823",
"database": "Ensembl",
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},
{
"id": "ENSP00000494775",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSP00000494319",
"database": "Ensembl",
"url": ""
},
{
"id": "Q15813",
"database": "PRO",
"url": ""
},
{
"id": "ENST00000645655",
"database": "Ensembl",
"url": ""
},
{
"id": "ENST00000642610",
"database": "Ensembl",
"url": ""
},
{
"id": "ENST00000646624",
"database": "Ensembl",
"url": ""
},
{
"id": "ENST00000645205",
"database": "Ensembl",
"url": ""
},
{
"id": "ENST00000406207",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSG00000284770-TBCE",
"database": "HPA",
"url": ""
},
{
"id": "NP_001274731.1",
"database": "RefSeq",
"url": ""
},
{
"id": "NP_003184.1",
"database": "RefSeq",
"url": ""
},
{
"id": "ENSP00000494575",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSP00000439170",
"database": "Ensembl",
"url": ""
},
{
"id": "15581",
"database": "Orphanet",
"url": ""
}
]
},
{
"participant_id": "R-HSA-379546",
"participant_name": "TBCB [cytosol]",
"crossref": [
{
"id": "ENST00000221855",
"database": "Ensembl",
"url": ""
},
{
"id": "NP_001272.2",
"database": "RefSeq",
"url": ""
},
{
"id": "Q99426",
"database": "PRO",
"url": ""
},
{
"id": "NP_001287900.1",
"database": "RefSeq",
"url": ""
},
{
"id": "ENST00000585746",
"database": "Ensembl",
"url": ""
},
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}
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},
{
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}
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{
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}
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},
{
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}
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},
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}
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},
{
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}
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}
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{
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}
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},
{
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}
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}
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{
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}
]
}
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}
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}
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}
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}
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}
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}
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{
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"activity": "",
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}
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}
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}
]
}
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},
{
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}
]
}
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},
{
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"ec_number": "3.6.5.2",
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}
]
},
{
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"id": "P70426",
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}
]
}
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},
{
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{
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}
]
},
{
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{
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]
}
]
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{
"ec_number": "3.6.5.2",
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}
]
},
{
"ec_number": "3.6.5.2",
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{
"id": "P84077",
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}
]
}
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},
{
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{
"ec_number": "3.6.5.2",
"activity": "GTP + H2O = GDP + H(+) + phosphate.",
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}
]
},
{
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}
]
}
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},
{
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{
"ec_number": "3.6.5.2",
"activity": "GTP + H2O = GDP + H(+) + phosphate.",
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}
]
},
{
"ec_number": "3.6.5.2",
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{
"id": "P84079",
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}
]
}
]
},
{
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{
"ec_number": "3.6.5.2",
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}
]
},
{
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]
}
]
},
{
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{
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]
},
{
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]
}
]
},
{
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{
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}
]
},
{
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]
}
]
},
{
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{
"ec_number": "3.6.5.-",
"activity": "",
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]
}
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},
{
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{
"ec_number": "3.6.1.-",
"activity": "",
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]
},
{
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}
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},
{
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{
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},
{
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{
"id": "Q02790",
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]
}
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},
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{
"ec_number": "3.6.5.2",
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},
{
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}
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},
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{
"ec_number": "3.6.5.5",
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]
},
{
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{
"id": "Q05193",
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]
}
]
},
{
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{
"ec_number": "3.6.5.3",
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"id": "Q05D44",
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]
},
{
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{
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]
}
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},
{
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{
"ec_number": "3.6.5.5",
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"id": "Q08877",
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]
},
{
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"id": "Q08877",
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]
}
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},
{
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{
"ec_number": "3.6.5.2",
"activity": "GTP + H2O = GDP + H(+) + phosphate.",
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"id": "Q08AT1",
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]
},
{
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{
"id": "Q08AT1",
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]
}
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},
{
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{
"ec_number": "3.6.5.-",
"activity": "",
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]
}
]
},
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"ec_number": "2.4.1.41",
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{
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]
},
{
"ec_number": "2.4.1.41",
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{
"id": "Q10471",
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]
}
]
},
{
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{
"ec_number": "2.4.1.41",
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{
"id": "Q10472",
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]
},
{
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"evidence": [
{
"id": "Q10472",
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]
}
]
},
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{
"ec_number": "2.7.11.1",
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]
},
{
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{
"id": "Q13131",
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]
},
{
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"id": "Q13131",
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]
},
{
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]
},
{
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]
}
]
},
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]
},
{
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{
"id": "Q14674",
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]
}
]
},
{
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{
"ec_number": "6.3.2.-",
"activity": "",
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{
"id": "Q14679",
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]
}
]
},
{
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{
"ec_number": "3.6.5.-",
"activity": "",
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{
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]
}
]
},
{
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{
"ec_number": "5.3.99.3",
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]
},
{
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{
"id": "Q15185",
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]
}
]
},
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