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 27-MAR-2024, entry version 208.
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 PDB; 7MSR; X-ray; 1.58 A; B=38-432.
DR PDB; 7MSS; X-ray; 1.75 A; B=38-432.
DR PDB; 7MST; X-ray; 1.61 A; B=38-432.
DR PDBsum; 6WCV; -.
DR PDBsum; 7MSR; -.
DR PDBsum; 7MSS; -.
DR PDBsum; 7MST; -.
DR AlphaFoldDB; Q96I99; -.
DR SMR; Q96I99; -.
DR BioGRID; 114329; 114.
DR ComplexPortal; CPX-6175; Mitochondrial succinyl-CoA synthetase complex, GTP-specific variant.
DR CORUM; Q96I99; -.
DR DIP; DIP-53563N; -.
DR IntAct; Q96I99; 27.
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 CPTAC; CPTAC-2776; -.
DR EPD; Q96I99; -.
DR jPOST; Q96I99; -.
DR MassIVE; Q96I99; -.
DR MaxQB; Q96I99; -.
DR PaxDb; 9606-ENSP00000419325; -.
DR PeptideAtlas; Q96I99; -.
DR ProteomicsDB; 76820; -. [Q96I99-1]
DR ProteomicsDB; 76821; -. [Q96I99-2]
DR Pumba; Q96I99; -.
DR TopDownProteomics; Q96I99-1; -. [Q96I99-1]
DR TopDownProteomics; Q96I99-2; -. [Q96I99-2]
DR Antibodypedia; 31838; 143 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 AGR; HGNC:11450; -.
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; RCADEIQ; -.
DR OrthoDB; 1384037at2759; -.
DR PhylomeDB; Q96I99; -.
DR TreeFam; TF300624; -.
DR BioCyc; MetaCyc:HS10493-MONOMER; -.
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; 8 hits in 1160 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 201 other cell types or 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:0019003; F:GDP binding; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IBA:GO_Central.
DR GO; GO:0006105; P:succinate metabolic process; IEA:Ensembl.
DR GO; GO:1901289; P:succinyl-CoA catabolic process; NAS: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; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 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; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR005811; SUCC_ACL_C.
DR InterPro; IPR034722; Succ_CoA_betaG_euk.
DR InterPro; IPR005809; Succ_CoA_ligase-like_bsu.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR NCBIfam; TIGR01016; sucCoAbeta; 1.
DR PANTHER; PTHR11815:SF21; SUCCINATE--COA LIGASE [GDP-FORMING] SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11815; SUCCINYL-COA SYNTHETASE BETA CHAIN; 1.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF001554; SucCS_beta; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 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
//
