ID A0A1W2PRH4_HUMAN Unreviewed; 149 AA. AC A0A1W2PRH4; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 16-JAN-2019, entry version 9. DE RecName: Full=Glycine cleavage system H protein {ECO:0000256|RuleBase:RU364055}; 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:ENSP00000492599, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000492599, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [2] {ECO:0000313|Ensembl:ENSP00000492599} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2017) to UniProtKB. CC -!- FUNCTION: The H protein shuttles the methylamine group of glycine CC from the P protein to the T protein. CC {ECO:0000256|RuleBase:RU364055}. CC -!- COFACTOR: CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; CC Evidence={ECO:0000256|RuleBase:RU364055}; CC Note=Binds 1 lipoyl cofactor covalently. CC {ECO:0000256|RuleBase:RU364055}; CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: CC P, T, L and H. {ECO:0000256|RuleBase:RU364055}. CC -!- SUBCELLULAR LOCATION: Mitochondrion CC {ECO:0000256|RuleBase:RU364055}. CC -!- SIMILARITY: Belongs to the GcvH family. CC {ECO:0000256|RuleBase:RU364055}. 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; AC092718; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR BioMuta; ENSG00000260643; -. DR jPOST; A0A1W2PRH4; -. DR PeptideAtlas; A0A1W2PRH4; -. DR Ensembl; ENST00000640370; ENSP00000492599; ENSG00000260643. DR GeneCards; ENSG00000260643; -. DR GeneTree; ENSGT00390000011666; -. DR Proteomes; UP000005640; Chromosome 16. DR ExpressionAtlas; A0A1W2PRH4; baseline and differential. DR GO; GO:0005960; C:glycine cleavage complex; IEA:UniProtKB-UniRule. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule. DR CDD; cd06848; GCS_H; 1. DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS. DR InterPro; IPR000089; Biotin_lipoyl. DR InterPro; IPR002930; GCV_H. DR InterPro; IPR033753; GCV_H/Fam206. DR InterPro; IPR017453; GCV_H_sub. DR InterPro; IPR011053; Single_hybrid_motif. DR PANTHER; PTHR11715; PTHR11715; 1. DR Pfam; PF01597; GCV_H; 1. DR SUPFAM; SSF51230; SSF51230; 1. DR TIGRFAMs; TIGR00527; gcvH; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. DR PROSITE; PS00189; LIPOYL; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Lipoyl {ECO:0000256|PIRSR:PIRSR617453-50, KW ECO:0000256|RuleBase:RU364055}; KW Mitochondrion {ECO:0000256|RuleBase:RU364055}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transit peptide {ECO:0000256|RuleBase:RU364055}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 149 Glycine cleavage system H protein. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5012213143. FT DOMAIN 66 149 Lipoyl-binding. FT {ECO:0000259|PROSITE:PS50968}. FT MOD_RES 107 107 N6-lipoyllysine. FT {ECO:0000256|PIRSR:PIRSR617453-50}. SQ SEQUENCE 149 AA; 16010 MW; 07B2200121460F08 CRC64; MALRVVRSVR ALLCTLRAVP SPAAPCPPRP WQLGVGAVRT LRTGPALLSV RKFTEKHEWV TTENGIGTVG ISNFAQEALG DVVYCSLPEV GTKLNKQDEF GALESVKAAS ELYSPLSGEV TEINEALAEN PGLVNKSCYE DGKDPNILF //