ID H0YIY6_HUMAN Unreviewed; 505 AA. AC H0YIY6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 2. DT 16-JAN-2019, entry version 60. DE RecName: Full=Non-specific serine/threonine protein kinase {ECO:0000256|SAAS:SAAS00804148}; DE EC=2.7.11.1 {ECO:0000256|SAAS:SAAS00804148}; DE Flags: Fragment; GN Name=MARK3 {ECO:0000313|Ensembl:ENSP00000450460}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000450460, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000450460, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., RA Quetier F., Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [2] {ECO:0000213|PubMed:18220336} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.D., Yates J.R.; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [3] {ECO:0000213|PubMed:18691976} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [4] {ECO:0000213|PubMed:18669648} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [5] {ECO:0000213|PubMed:19413330} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [6] {ECO:0000213|PubMed:19369195} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [7] {ECO:0000213|PubMed:19690332} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:ra46-RA46(2009). RN [8] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] {ECO:0000213|PubMed:21406692} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:rs3-RS3(2011). RN [10] {ECO:0000313|Ensembl:ENSP00000450460} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. RN [11] {ECO:0000213|PubMed:23186163} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23186163; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000256|SAAS:SAAS01117232}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000256|SAAS:SAAS01117231}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL133367; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF456011; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H0YIY6; -. DR jPOST; H0YIY6; -. DR PeptideAtlas; H0YIY6; -. DR PRIDE; H0YIY6; -. DR Ensembl; ENST00000554627; ENSP00000450460; ENSG00000075413. DR UCSC; uc059fqm.1; human. DR EuPathDB; HostDB:ENSG00000075413.17; -. DR HGNC; HGNC:6897; MARK3. DR OpenTargets; ENSG00000075413; -. DR eggNOG; KOG0586; Eukaryota. DR eggNOG; ENOG410XNQ0; LUCA. DR GeneTree; ENSGT00940000154862; -. DR SignaLink; H0YIY6; -. DR ChiTaRS; MARK3; human. DR Proteomes; UP000005640; Chromosome 14. DR Bgee; ENSG00000075413; Expressed in 228 organ(s), highest expression level in cerebellar hemisphere. DR ExpressionAtlas; H0YIY6; baseline and differential. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0030010; P:establishment of cell polarity; IEA:InterPro. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:InterPro. DR InterPro; IPR028375; KA1/Ssp2_C. DR InterPro; IPR001772; KA1_dom. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR033624; MARK/par1. DR InterPro; IPR033628; MARK3. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR015940; UBA. DR PANTHER; PTHR24346; PTHR24346; 1. DR PANTHER; PTHR24346:SF1; PTHR24346:SF1; 1. DR Pfam; PF02149; KA1; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00627; UBA; 1. DR SMART; SM00165; UBA; 1. DR SUPFAM; SSF103243; SSF103243; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS50032; KA1; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS50030; UBA; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|SAAS:SAAS00804144}; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Kinase {ECO:0000256|SAAS:SAAS00804166}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00804144}; KW Proteomics identification {ECO:0000213|EPD:H0YIY6, KW ECO:0000213|MaxQB:H0YIY6, ECO:0000213|PeptideAtlas:H0YIY6}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Serine/threonine-protein kinase {ECO:0000256|SAAS:SAAS00804166}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|SAAS:SAAS00804166}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 505 Non-specific serine/threonine protein FT kinase. {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003545963. FT DOMAIN 1 75 Protein kinase. FT {ECO:0000259|PROSITE:PS50011}. FT DOMAIN 94 133 UBA. {ECO:0000259|PROSITE:PS50030}. FT DOMAIN 456 505 KA1. {ECO:0000259|PROSITE:PS50032}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000450460}. SQ SEQUENCE 505 AA; 56614 MW; 9E5BF3354D6C8D5C CRC64; XVDVWSLGVI LYTLVSGSLP FDGQNLKELR ERVLRGKYRI PFYMSTDCEN LLKRFLVLNP IKRGTLEQIM KDRWINAGHE EDELKPFVEP ELDISDQKRI DIMVGMGYSQ EEIQESLSKM KYDEITATYL LLGRKSSEVR PSSDLNNSTG QSPHHKVQRS VSSSQKQRRY SDHAGPAIPS VVAYPKRSQT STADSDLKED GISSRKSSGS AVGGKGIAPA SPMLGNASNP NKADIPERKK SSTVPSSNTA SGGMTRRNTY VCSERTTADR HSVIQNGKEN STIPDQRTPV ASTHSISSAA TPDRIRFPRG TASRSTFHGQ PRERRTATYN GPPASPSLSH EATPLSQTRS RGSTNLFSKL TSKLTRRNMS FRFIKRLPTE YERNGRYEGS SRNVSAEQKD ENKEAKPRSL RFTWSMKTTS SMDPGDMMRE IRKVLDANNC DYEQRERFLL FCVHGDGHAE NLVQWEMEVC KLPRLSLNGV RFKRISGTSI AFKNIASKIA NELKL //