GenomeNet

Database: UniProt
Entry: Q96I99
LinkDB: Q96I99
Original site: Q96I99 
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   16-JAN-2019, entry version 178.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   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.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   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
RT   project: 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
RP   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
RT   succinyl-CoA 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.,
RA   Walther T.C., 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.,
RA   Buerckstuemmer 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   [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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver 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.,
RA   Ayoub D., 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
CC       citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA
CC       to the synthesis of GTP and thus represents the only step of
CC       substrate-level phosphorylation in the TCA. The beta subunit
CC       provides nucleotide specificity of the enzyme and binds the
CC       substrate succinate, while the binding sites for coenzyme A and
CC       phosphate are found in the alpha subunit. {ECO:0000255|HAMAP-
CC       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-
CC       Rule:MF_03221};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_03221}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta
CC       subunit determines specificity for GTP. {ECO:0000255|HAMAP-
CC       Rule:MF_03221}.
CC   -!- INTERACTION:
CC       Q8IWL3:HSCB; NbExp=4; IntAct=EBI-2511878, EBI-1805738;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-
CC       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         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in liver, kidney, heart,
CC       spleen and skeletal muscle. Also found in intestine and colon, and
CC       in low amounts in lung, brain, prostate, testis and ovary.
CC       {ECO:0000269|PubMed:9765291}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC       subunit family. GTP-specific subunit beta subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03221}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH07716.3; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH47024.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=AAH47024.1; Type=Erroneous termination; Positions=31; Note=Translated as Gln.; Evidence={ECO:0000305};
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   UniGene; Hs.644919; -.
DR   ProteinModelPortal; Q96I99; -.
DR   SMR; Q96I99; -.
DR   BioGrid; 114329; 44.
DR   CORUM; Q96I99; -.
DR   DIP; DIP-53563N; -.
DR   IntAct; Q96I99; 11.
DR   MINT; Q96I99; -.
DR   STRING; 9606.ENSP00000419325; -.
DR   DrugBank; DB00139; Succinic acid.
DR   iPTMnet; Q96I99; -.
DR   PhosphoSitePlus; Q96I99; -.
DR   SwissPalm; Q96I99; -.
DR   BioMuta; SUCLG2; -.
DR   DMDM; 52788292; -.
DR   REPRODUCTION-2DPAGE; IPI00096066; -.
DR   EPD; Q96I99; -.
DR   jPOST; Q96I99; -.
DR   MaxQB; Q96I99; -.
DR   PaxDb; Q96I99; -.
DR   PeptideAtlas; Q96I99; -.
DR   PRIDE; Q96I99; -.
DR   ProteomicsDB; 76820; -.
DR   ProteomicsDB; 76821; -. [Q96I99-2]
DR   TopDownProteomics; Q96I99-1; -. [Q96I99-1]
DR   TopDownProteomics; Q96I99-2; -. [Q96I99-2]
DR   Ensembl; ENST00000307227; ENSP00000307432; ENSG00000172340. [Q96I99-1]
DR   Ensembl; ENST00000493112; ENSP00000419325; ENSG00000172340. [Q96I99-2]
DR   GeneID; 8801; -.
DR   KEGG; hsa:8801; -.
DR   UCSC; uc003dna.5; human. [Q96I99-1]
DR   CTD; 8801; -.
DR   DisGeNET; 8801; -.
DR   EuPathDB; HostDB:ENSG00000172340.14; -.
DR   GeneCards; SUCLG2; -.
DR   HGNC; HGNC:11450; SUCLG2.
DR   HPA; HPA046705; -.
DR   HPA; HPA051998; -.
DR   MIM; 603922; gene.
DR   neXtProt; NX_Q96I99; -.
DR   OpenTargets; ENSG00000172340; -.
DR   PharmGKB; PA36247; -.
DR   eggNOG; KOG2799; Eukaryota.
DR   eggNOG; COG0045; LUCA.
DR   GeneTree; ENSGT00390000010170; -.
DR   HOGENOM; HOG000007059; -.
DR   HOVERGEN; HBG055555; -.
DR   InParanoid; Q96I99; -.
DR   KO; K01900; -.
DR   OMA; VQIEINP; -.
DR   OrthoDB; 973871at2759; -.
DR   PhylomeDB; Q96I99; -.
DR   TreeFam; TF300624; -.
DR   BioCyc; MetaCyc:HS10493-MONOMER; -.
DR   BRENDA; 6.2.1.4; 2681.
DR   Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; UER00999.
DR   ChiTaRS; SUCLG2; human.
DR   GenomeRNAi; 8801; -.
DR   PRO; PR:Q96I99; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; ENSG00000172340; Expressed in 222 organ(s), highest expression level in colonic mucosa.
DR   CleanEx; HS_SUCLG2; -.
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:0045244; C:succinate-CoA ligase complex (GDP-forming); IEA:Ensembl.
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:0046982; F:protein heterodimerization activity; IEA:Ensembl.
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; NAS:UniProtKB.
DR   GO; GO:0006105; P:succinate metabolic process; IEA:Ensembl.
DR   GO; GO:0006104; P:succinyl-CoA metabolic process; NAS:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
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   Acetylation; Alternative splicing; Complete proteome; GTP-binding;
KW   Ligase; Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding;
KW   Phosphoprotein; Polymorphism; Reference proteome; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT       1     37       Mitochondrion.
FT                                {ECO:0000244|PubMed:25944712}.
FT   CHAIN        38    432       Succinate--CoA ligase [GDP-forming]
FT                                subunit beta, mitochondrial.
FT                                /FTId=PRO_0000033356.
FT   DOMAIN       46    274       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_03221}.
FT   NP_BIND      90     92       GTP. {ECO:0000255|HAMAP-Rule:MF_03221}.
FT   REGION      365    367       Substrate binding; shared with subunit
FT                                alpha. {ECO:0000255|HAMAP-Rule:MF_03221}.
FT   METAL       243    243       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_03221}.
FT   METAL       257    257       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_03221}.
FT   BINDING      57     57       GTP. {ECO:0000255|HAMAP-Rule:MF_03221}.
FT   BINDING     146    146       GTP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_03221}.
FT   BINDING     308    308       Substrate; shared with subunit alpha.
FT                                {ECO:0000255|HAMAP-Rule:MF_03221}.
FT   SITE         79     79       Important for substrate specificity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03221}.
FT   SITE        147    147       Important for substrate specificity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03221}.
FT   MOD_RES      73     73       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES      78     78       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     132    132       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     139    139       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     161    161       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     200    200       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     218    218       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     227    227       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     271    271       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     291    291       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     338    338       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     347    347       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     386    386       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     423    423       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   VAR_SEQ     397    432       NVQEAQKILNNSGLPITSAIDLEDAAKKAVASVAKK -> F
FT                                MEKKGSYMHIKQETGNSNENITGIQENVAHQNLSKCAISIF
FT                                LC (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_042013.
FT   VARIANT     347    347       K -> R (in dbSNP:rs9843840).
FT                                /FTId=VAR_052499.
FT   VARIANT     381    381       R -> W (in dbSNP:rs7623258).
FT                                /FTId=VAR_052500.
FT   CONFLICT    174    175       GV -> RS (in Ref. 4; AAC64397).
FT                                {ECO:0000305}.
FT   CONFLICT    220    220       Q -> K (in Ref. 3; AAH68602).
FT                                {ECO:0000305}.
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
//
DBGET integrated database retrieval system