ID Q53XL7_HUMAN Unreviewed; 173 AA. AC Q53XL7; DT 24-MAY-2005, integrated into UniProtKB/TrEMBL. DT 24-MAY-2005, sequence version 1. DT 03-OCT-2012, entry version 54. DE SubName: Full=Glycine cleavage system protein H (Aminomethyl carrier); DE SubName: Full=Glycine cleavage system protein H (Aminomethyl carrier), isoform CRA_a; DE SubName: Full=cDNA, FLJ92251, Homo sapiens glycine cleavage system protein H (aminomethyl carrier) (GCSH), mRNA; GN Name=GCSH; Synonyms=GCVHC; ORFNames=hCG_1980047; 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; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=21108353; PubMed=11181995; DOI=10.1126/science.1058040; RA Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., RA Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., RA Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., RA Kodira C.D., Zheng X.H., Chen L., Skupski M., Subramanian G., RA Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., RA Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., RA Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., RA Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., RA Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., RA Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., RA Brandon R., Cargill M., Chandramouliswaran I., Charlab R., RA Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., RA Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., RA Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., RA Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., RA Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., RA Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., RA Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., RA Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., RA Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., RA Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., RA Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., RA Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., RA Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., RA Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., RA Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., RA Kline L., Koduru S., Love A., Mann F., May D., McCawley S., RA McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., RA Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., RA Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., RA Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., RA Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., RA Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., RA Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., RA Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., RA Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., RA Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., RA Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., RA Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., RA Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., RA Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., RA Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., RA Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., RA McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., RA Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., RA Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., RA Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.; RT "The sequence of the human genome."; RL Science 291:1304-1351(2001). RN [2] RP NUCLEOTIDE SEQUENCE. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Small intestine; RA Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y., RA Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R., RA Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N., RA Isogai T.; RT "NEDO functional analysis of protein and research application RT project."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of CC glycine. The H protein shuttles the methylamine group of glycine CC from the P protein to the T protein (By similarity). CC -!- COFACTOR: Binds 1 lipoyl cofactor covalently (By similarity). CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: CC P, T, L and H (By similarity). CC -!- SIMILARITY: Belongs to the GcvH family. CC -!- SIMILARITY: Contains 1 lipoyl-binding domain. 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; BT009827; AAP88829.1; -; mRNA. DR EMBL; AK311978; BAG34917.1; -; mRNA. DR EMBL; CH471114; EAW95545.1; -; Genomic_DNA. DR IPI; IPI00011604; -. DR UniGene; Hs.546256; -. DR ProteinModelPortal; Q53XL7; -. DR SMR; Q53XL7; 49-173. DR STRING; Q53XL7; -. DR PRIDE; Q53XL7; -. DR HOVERGEN; HBG001129; -. DR GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro. DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:InterPro. DR HAMAP; MF_00272; GcvH; 1; -. DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS. DR InterPro; IPR002930; GCV_H. 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; Hybrid_motif; 1. DR TIGRFAMs; TIGR00527; gcvH; 1. DR PROSITE; PS00189; LIPOYL; 1. PE 2: Evidence at transcript level; KW Lipoyl. FT MOD_RES 107 107 N6-lipoyllysine (By similarity). SQ SEQUENCE 173 AA; 18911 MW; BA1C1AFCB6C13ACC CRC64; MALRVVRSVR ALLCTLRAVP LPAAPCPPRP WQLGVGAVRT LRTGPALLSV RKFTEKHEWV TTENGIGTVG ISNFAQEALG DVVYCSLPEV GTKLNKQDEF GALESVKAAS ELYSPLSGEV TEINEALAEN PGLVNKSCYE DGWLIKMTLS NPSELDELMS EEAYEKYIKS IEE //