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SUCB2_HUMAN
ID   SUCB2_HUMAN             Reviewed;         432 AA.
AC   Q96I99; C9JVT2; O95195; Q6NUH7; Q86VX8; Q8WUQ1;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   03-AUG-2022, entry version 199.
DE   RecName: Full=Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03221};
DE            EC=6.2.1.4 {ECO:0000255|HAMAP-Rule:MF_03221};
DE   AltName: Full=GTP-specific succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_03221};
DE            Short=G-SCS {ECO:0000255|HAMAP-Rule:MF_03221};
DE            Short=GTPSCS {ECO:0000255|HAMAP-Rule:MF_03221};
DE   AltName: Full=Succinyl-CoA synthetase beta-G chain {ECO:0000255|HAMAP-Rule:MF_03221};
DE            Short=SCS-betaG {ECO:0000255|HAMAP-Rule:MF_03221};
DE   Flags: Precursor;
GN   Name=SUCLG2 {ECO:0000255|HAMAP-Rule:MF_03221};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Hippocampus, Mammary gland, Placenta, and Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 29-432 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=9765291; DOI=10.1074/jbc.273.42.27580;
RA   Johnson J.D., Mehus J.G., Tews K., Milavetz B.I., Lambeth D.O.;
RT   "Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA
RT   synthetases in multicellular eucaryotes.";
RL   J. Biol. Chem. 273:27580-27586(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 234-432 (ISOFORM 1).
RC   TISSUE=Brain;
RA   Mei G., Yu W., Gibbs R.A.;
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-227 AND LYS-291, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [7]
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., Buerckstuemmer T.,
RA   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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [9]
RP   CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER TRP-37, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: GTP-specific succinyl-CoA synthetase functions in the citric
CC       acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the
CC       synthesis of GTP and thus represents the only step of substrate-level
CC       phosphorylation in the TCA. The beta subunit provides nucleotide
CC       specificity of the enzyme and binds the substrate succinate, while the
CC       binding sites for coenzyme A and phosphate are found in the alpha
CC       subunit. {ECO:0000255|HAMAP-Rule:MF_03221}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + GTP + succinate = GDP + phosphate + succinyl-CoA;
CC         Xref=Rhea:RHEA:22120, ChEBI:CHEBI:30031, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:58189; EC=6.2.1.4; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03221};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03221};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03221};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC       from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_03221}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta subunit
CC       determines specificity for GTP. {ECO:0000255|HAMAP-Rule:MF_03221}.
CC   -!- INTERACTION:
CC       Q96I99; Q8IWL3: HSCB; NbExp=4; IntAct=EBI-2511878, EBI-1805738;
CC       Q96I99; P53597: SUCLG1; NbExp=2; IntAct=EBI-2511878, EBI-1237145;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03221}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96I99-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96I99-2; Sequence=VSP_042013;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in liver, kidney, heart, spleen
CC       and skeletal muscle. Also found in intestine and colon, and in low
CC       amounts in lung, brain, prostate, testis and ovary.
CC       {ECO:0000269|PubMed:9765291}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC       family. GTP-specific subunit beta subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_03221}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH07716.3; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH47024.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH47024.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK310527; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC099783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC112213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC113169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC114401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC007716; AAH07716.3; ALT_INIT; mRNA.
DR   EMBL; BC019868; AAH19868.1; -; mRNA.
DR   EMBL; BC047024; AAH47024.1; ALT_SEQ; mRNA.
DR   EMBL; BC068602; AAH68602.1; -; mRNA.
DR   EMBL; AF058954; AAC64397.1; -; mRNA.
DR   EMBL; AF131748; AAD20032.1; -; mRNA.
DR   CCDS; CCDS43104.1; -. [Q96I99-1]
DR   CCDS; CCDS54605.1; -. [Q96I99-2]
DR   RefSeq; NP_001171070.1; NM_001177599.1. [Q96I99-2]
DR   RefSeq; NP_003839.2; NM_003848.3. [Q96I99-1]
DR   PDB; 6WCV; X-ray; 1.52 A; B=38-432.
DR   PDBsum; 6WCV; -.
DR   AlphaFoldDB; Q96I99; -.
DR   SMR; Q96I99; -.
DR   BioGRID; 114329; 103.
DR   ComplexPortal; CPX-6175; Mitochondrial succinyl-CoA synthetase complex, GTP-specific variant.
DR   CORUM; Q96I99; -.
DR   DIP; DIP-53563N; -.
DR   IntAct; Q96I99; 25.
DR   MINT; Q96I99; -.
DR   STRING; 9606.ENSP00000419325; -.
DR   DrugBank; DB00787; Acyclovir.
DR   DrugBank; DB12695; Phenethyl Isothiocyanate.
DR   DrugBank; DB00139; Succinic acid.
DR   GlyGen; Q96I99; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q96I99; -.
DR   MetOSite; Q96I99; -.
DR   PhosphoSitePlus; Q96I99; -.
DR   SwissPalm; Q96I99; -.
DR   BioMuta; SUCLG2; -.
DR   DMDM; 52788292; -.
DR   REPRODUCTION-2DPAGE; IPI00096066; -.
DR   EPD; Q96I99; -.
DR   jPOST; Q96I99; -.
DR   MassIVE; Q96I99; -.
DR   MaxQB; Q96I99; -.
DR   PaxDb; Q96I99; -.
DR   PeptideAtlas; Q96I99; -.
DR   PRIDE; Q96I99; -.
DR   ProteomicsDB; 76820; -. [Q96I99-1]
DR   ProteomicsDB; 76821; -. [Q96I99-2]
DR   TopDownProteomics; Q96I99-1; -. [Q96I99-1]
DR   TopDownProteomics; Q96I99-2; -. [Q96I99-2]
DR   Antibodypedia; 31838; 129 antibodies from 26 providers.
DR   DNASU; 8801; -.
DR   Ensembl; ENST00000307227.10; ENSP00000307432.5; ENSG00000172340.15. [Q96I99-1]
DR   Ensembl; ENST00000493112.5; ENSP00000419325.1; ENSG00000172340.15. [Q96I99-2]
DR   GeneID; 8801; -.
DR   KEGG; hsa:8801; -.
DR   MANE-Select; ENST00000307227.10; ENSP00000307432.5; NM_003848.4; NP_003839.2.
DR   UCSC; uc003dna.5; human. [Q96I99-1]
DR   CTD; 8801; -.
DR   DisGeNET; 8801; -.
DR   GeneCards; SUCLG2; -.
DR   HGNC; HGNC:11450; SUCLG2.
DR   HPA; ENSG00000172340; Tissue enhanced (liver).
DR   MIM; 603922; gene.
DR   neXtProt; NX_Q96I99; -.
DR   OpenTargets; ENSG00000172340; -.
DR   PharmGKB; PA36247; -.
DR   VEuPathDB; HostDB:ENSG00000172340; -.
DR   eggNOG; KOG1447; Eukaryota.
DR   GeneTree; ENSGT00390000010170; -.
DR   HOGENOM; CLU_037430_0_2_1; -.
DR   InParanoid; Q96I99; -.
DR   OMA; AIQQFKV; -.
DR   OrthoDB; 973871at2759; -.
DR   PhylomeDB; Q96I99; -.
DR   TreeFam; TF300624; -.
DR   BioCyc; MetaCyc:HS10493-MON; -.
DR   BRENDA; 6.2.1.4; 2681.
DR   PathwayCommons; Q96I99; -.
DR   Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
DR   SignaLink; Q96I99; -.
DR   SIGNOR; Q96I99; -.
DR   UniPathway; UPA00223; UER00999.
DR   BioGRID-ORCS; 8801; 7 hits in 1079 CRISPR screens.
DR   ChiTaRS; SUCLG2; human.
DR   GenomeRNAi; 8801; -.
DR   Pharos; Q96I99; Tbio.
DR   PRO; PR:Q96I99; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q96I99; protein.
DR   Bgee; ENSG00000172340; Expressed in colonic mucosa and 199 other tissues.
DR   ExpressionAtlas; Q96I99; baseline and differential.
DR   Genevisible; Q96I99; HS.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0042709; C:succinate-CoA ligase complex; IBA:GO_Central.
DR   GO; GO:0045244; C:succinate-CoA ligase complex (GDP-forming); IPI:ComplexPortal.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IBA:GO_Central.
DR   GO; GO:1901289; P:succinyl-CoA catabolic process; IC:ComplexPortal.
DR   GO; GO:0006104; P:succinyl-CoA metabolic process; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.261; -; 1.
DR   HAMAP; MF_00558; Succ_CoA_beta; 1.
DR   HAMAP; MF_03221; Succ_CoA_betaG_euk; 1.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR   InterPro; IPR034722; Succ_CoA_betaG_euk.
DR   InterPro; IPR005809; Succ_CoA_synthase_bsu.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR11815; PTHR11815; 1.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001554; SucCS_beta; 1.
DR   SUPFAM; SSF52210; SSF52210; 1.
DR   TIGRFAMs; TIGR01016; sucCoAbeta; 1.
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; GTP-binding; Ligase;
KW   Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT         1..37
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0007744|PubMed:25944712"
FT   CHAIN           38..432
FT                   /note="Succinate--CoA ligase [GDP-forming] subunit beta,
FT                   mitochondrial"
FT                   /id="PRO_0000033356"
FT   DOMAIN          46..274
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT   BINDING         57
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT   BINDING         90..92
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT   BINDING         146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT   BINDING         243
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT   BINDING         257
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT   BINDING         308
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT   BINDING         365..367
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT   SITE            79
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT   SITE            147
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT   MOD_RES         78
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT   MOD_RES         132
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT   MOD_RES         139
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT   MOD_RES         200
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT   MOD_RES         218
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT   MOD_RES         227
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         271
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT   MOD_RES         291
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         338
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT   MOD_RES         347
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT   MOD_RES         386
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT   MOD_RES         423
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT   VAR_SEQ         397..432
FT                   /note="NVQEAQKILNNSGLPITSAIDLEDAAKKAVASVAKK -> FMEKKGSYMHIK
FT                   QETGNSNENITGIQENVAHQNLSKCAISIFLC (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_042013"
FT   VARIANT         347
FT                   /note="K -> R (in dbSNP:rs9843840)"
FT                   /id="VAR_052499"
FT   VARIANT         381
FT                   /note="R -> W (in dbSNP:rs7623258)"
FT                   /id="VAR_052500"
FT   CONFLICT        174..175
FT                   /note="GV -> RS (in Ref. 4; AAC64397)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        220
FT                   /note="Q -> K (in Ref. 3; AAH68602)"
FT                   /evidence="ECO:0000305"
FT   HELIX           42..50
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   TURN            51..53
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          59..64
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           65..75
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          78..84
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          87..89
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          103..108
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           110..118
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   TURN            119..122
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          123..126
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          140..144
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          149..159
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   TURN            160..163
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          164..171
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           177..183
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           185..187
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          189..192
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   TURN            195..197
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           201..210
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           216..234
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          237..247
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          253..255
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          258..262
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           264..269
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           271..275
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           284..291
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          295..298
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          300..309
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           310..322
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          329..332
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           339..349
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          357..363
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           369..382
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          389..397
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           398..406
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          408..417
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           418..427
FT                   /evidence="ECO:0007829|PDB:6WCV"
SQ   SEQUENCE   432 AA;  46511 MW;  56A977A3E50713A1 CRC64;
     MASPVAAQAG KLLRALALRP RFLAAGSQAV QLTSRRWLNL QEYQSKKLMS DNGVRVQRFF
     VADTANEALE AAKRLNAKEI VLKAQILAGG RGKGVFNSGL KGGVHLTKDP NVVGQLAKQM
     IGYNLATKQT PKEGVKVNKV MVAEALDISR ETYLAILMDR SCNGPVLVGS PQGGVDIEEV
     AASNPELIFK EQIDIFEGIK DSQAQRMAEN LGFVGPLKSQ AADQITKLYN LFLKIDATQV
     EVNPFGETPE GQVVCFDAKI NFDDNAEFRQ KDIFAMDDKS ENEPIENEAA KYDLKYIGLD
     GNIACFVNGA GLAMATCDII FLNGGKPANF LDLGGGVKEA QVYQAFKLLT ADPKVEAILV
     NIFGGIVNCA IIANGITKAC RELELKVPLV VRLEGTNVQE AQKILNNSGL PITSAIDLED
     AAKKAVASVA KK
 
 
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