CTBP1_MOUSE
ID CTBP1_MOUSE Reviewed; 441 AA.
AC O88712; Q3TAT1; Q3TDL5; Q3TUM5; Q91WI6; Q91YX3; Q9QYG2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=C-terminal-binding protein 1;
DE Short=CtBP1;
DE EC=1.1.1.-;
GN Name=Ctbp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10369679; DOI=10.1093/emboj/18.12.3392;
RA Criqui-Filipe P., Ducret C., Maira S.-M., Wasylyk B.;
RT "Net, a negative Ras-switchable TCF, contains a second inhibition domain,
RT the CID, that mediates repression through interactions with CtBP and de-
RT acetylation.";
RL EMBO J. 18:3392-3403(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=ICR;
RX PubMed=10567582; DOI=10.1128/mcb.19.12.8581;
RA Furusawa T., Moribe H., Kondoh H., Higashi Y.;
RT "Identification of CtBP1 and CtBP2 as corepressors of zinc finger-
RT homeodomain factor deltaEF1.";
RL Mol. Cell. Biol. 19:8581-8590(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=129, FVB/N, and FVB/N-3; TISSUE=Mammary tumor, and Salivary gland;
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 [5]
RP PROTEIN SEQUENCE OF 98-108 AND 286-305, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP INTERACTION WITH HDAC4; HDAC5 AND HDAC9.
RX PubMed=11022042; DOI=10.1074/jbc.m007364200;
RA Zhang C.L., McKinsey T.A., Lu J.R., Olson E.N.;
RT "Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting
RT transcription repressor (MITR) contributes to transcriptional repression of
RT the MEF2 transcription factor.";
RL J. Biol. Chem. 276:35-39(2001).
RN [7]
RP INTERACTION WITH HIPK2.
RX PubMed=14567915; DOI=10.1016/s0092-8674(03)00802-x;
RA Zhang Q., Yoshimatsu Y., Hildebrand J., Frisch S.M., Goodman R.H.;
RT "Homeodomain interacting protein kinase 2 promotes apoptosis by
RT downregulating the transcriptional corepressor CtBP.";
RL Cell 115:177-186(2003).
RN [8]
RP INTERACTION WITH NRIP1.
RX PubMed=14736873; DOI=10.1074/jbc.m313906200;
RA Christian M., Tullet J.M.A., Parker M.G.;
RT "Characterization of four autonomous repression domains in the corepressor
RT receptor interacting protein 140.";
RL J. Biol. Chem. 279:15645-15651(2004).
RN [9]
RP INTERACTION WITH FOXP1 AND FOXP2.
RX PubMed=14701752; DOI=10.1128/mcb.24.2.809-822.2004;
RA Li S., Weidenfeld J., Morrisey E.E.;
RT "Transcriptional and DNA binding activity of the Foxp1/2/4 family is
RT modulated by heterotypic and homotypic protein interactions.";
RL Mol. Cell. Biol. 24:809-822(2004).
RN [10]
RP INTERACTION WITH GLIS2, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16326862; DOI=10.1093/nar/gki985;
RA Kim S.-C., Kim Y.-S., Jetten A.M.;
RT "Kruppel-like zinc finger protein Gli-similar 2 (Glis2) represses
RT transcription through interaction with C-terminal binding protein 1
RT (CtBP1).";
RL Nucleic Acids Res. 33:6805-6815(2005).
RN [11]
RP INTERACTION WITH WIZ.
RX PubMed=16702210; DOI=10.1074/jbc.m603087200;
RA Ueda J., Tachibana M., Ikura T., Shinkai Y.;
RT "Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the
RT co-repressor molecule CtBP.";
RL J. Biol. Chem. 281:20120-20128(2006).
RN [12]
RP FUNCTION, INTERACTION WITH PRDM16, AND SUBCELLULAR LOCATION.
RX PubMed=18483224; DOI=10.1101/gad.1666108;
RA Kajimura S., Seale P., Tomaru T., Erdjument-Bromage H., Cooper M.P.,
RA Ruas J.L., Chin S., Tempst P., Lazar M.A., Spiegelman B.M.;
RT "Regulation of the brown and white fat gene programs through a PRDM16/CtBP
RT transcriptional complex.";
RL Genes Dev. 22:1397-1409(2008).
RN [13]
RP FUNCTION, AND INTERACTION WITH SATB1.
RX PubMed=19103759; DOI=10.1128/mcb.00822-08;
RA Purbey P.K., Singh S., Notani D., Kumar P.P., Limaye A.S., Galande S.;
RT "Acetylation-dependent interaction of SATB1 and CtBP1 mediates
RT transcriptional repression by SATB1.";
RL Mol. Cell. Biol. 29:1321-1337(2009).
RN [14]
RP INTERACTION WITH IKZF4.
RX PubMed=19696312; DOI=10.1126/science.1176077;
RA Pan F., Yu H., Dang E.V., Barbi J., Pan X., Grosso J.F., Jinasena D.,
RA Sharma S.M., McCadden E.M., Getnet D., Drake C.G., Liu J.O.,
RA Ostrowski M.C., Pardoll D.M.;
RT "Eos mediates Foxp3-dependent gene silencing in CD4+ regulatory T cells.";
RL Science 325:1142-1146(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Corepressor targeting diverse transcription regulators such
CC as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling
CC the equilibrium between tubular and stacked structures in the Golgi
CC complex. Functions in brown adipose tissue (BAT) differentiation.
CC {ECO:0000269|PubMed:10369679, ECO:0000269|PubMed:10567582,
CC ECO:0000269|PubMed:16326862, ECO:0000269|PubMed:18483224,
CC ECO:0000269|PubMed:19103759}.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC Note=Cofactor binding induces a conformational change. {ECO:0000250};
CC -!- SUBUNIT: Homo- or heterodimer. Heterodimer with CTBP2. Interacts with
CC ELK3 (via its PXDLS motif). Interacts with RBBP8 (via its PXDLS motif).
CC Interacts with PNN, MECOM and ZFHX1B. Interacts with ZNF366 (via PXDLS
CC motif) (By similarity). Interaction with SATB1 (non-acetylated form);
CC the interaction stabilizes its attachment to DNA and promotes
CC transcription repression. Interacts with PRDM16; the interaction
CC represses white adipose tissue (WAT)-specific genes expression.
CC Interacts with GLIS2, HIPK2, FOXP1, FOXP2, HDAC4, HDAC5, HDAC9, NRIP1,
CC WIZ and ZNF217. Interacts with BCL6; the interaction is required for
CC BCL6 transcriptional autoinhibition and inhibition of some BCL6 target
CC genes. Interacts with IKZF4. Interacts with MCRIP1 (unphosphorylated
CC form, via the PXDLS motif); competitively inhibiting CTBP-ZEB1
CC interaction (By similarity). Interacts with Bassoon/BSN; this
CC interaction targets and anchors CTBP1 to presynapses (By similarity).
CC Interacts with SIMC1 (By similarity). {ECO:0000250|UniProtKB:Q13363,
CC ECO:0000269|PubMed:11022042, ECO:0000269|PubMed:14567915,
CC ECO:0000269|PubMed:14701752, ECO:0000269|PubMed:14736873,
CC ECO:0000269|PubMed:16326862, ECO:0000269|PubMed:16702210,
CC ECO:0000269|PubMed:18483224, ECO:0000269|PubMed:19103759,
CC ECO:0000269|PubMed:19696312}.
CC -!- INTERACTION:
CC O88712; Q64318: Zeb1; NbExp=5; IntAct=EBI-604547, EBI-8560245;
CC O88712; Q14526: HIC1; Xeno; NbExp=10; IntAct=EBI-604547, EBI-2507362;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13363}. Nucleus
CC {ECO:0000250|UniProtKB:Q13363}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O88712-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88712-2; Sequence=VSP_024738;
CC Name=3;
CC IsoId=O88712-3; Sequence=VSP_024737;
CC -!- TISSUE SPECIFICITY: Expressed in a wide range of adult tissues.
CC {ECO:0000269|PubMed:10567582}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the developmental stages.
CC {ECO:0000269|PubMed:10567582}.
CC -!- PTM: ADP-ribosylated; when cells are exposed to brefeldin A.
CC {ECO:0000250}.
CC -!- PTM: The level of phosphorylation appears to be regulated during the
CC cell cycle. Phosphorylation by HIPK2 on Ser-423 induces proteasomal
CC degradation (By similarity). {ECO:0000250}.
CC -!- PTM: Sumoylation on Lys-429 is promoted by the E3 SUMO-protein ligase
CC CBX4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE41586.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ010483; CAA09219.1; -; mRNA.
DR EMBL; AB033122; BAA85180.1; -; mRNA.
DR EMBL; AK133816; BAE21859.1; -; mRNA.
DR EMBL; AK160658; BAE35946.1; -; mRNA.
DR EMBL; AK165276; BAE38115.1; -; mRNA.
DR EMBL; AK170133; BAE41586.1; ALT_INIT; mRNA.
DR EMBL; AK171650; BAE42587.1; -; mRNA.
DR EMBL; BC013702; AAH13702.1; -; mRNA.
DR EMBL; BC015071; AAH15071.1; -; mRNA.
DR EMBL; BC042425; AAH42425.1; -; mRNA.
DR CCDS; CCDS19201.1; -. [O88712-1]
DR CCDS; CCDS80255.1; -. [O88712-3]
DR RefSeq; NP_001185788.1; NM_001198859.1.
DR RefSeq; NP_001185789.1; NM_001198860.1.
DR RefSeq; NP_001185790.1; NM_001198861.1. [O88712-2]
DR RefSeq; NP_001297464.1; NM_001310535.1. [O88712-3]
DR RefSeq; NP_038530.1; NM_013502.3. [O88712-1]
DR AlphaFoldDB; O88712; -.
DR SMR; O88712; -.
DR BioGRID; 198961; 39.
DR CORUM; O88712; -.
DR DIP; DIP-33907N; -.
DR IntAct; O88712; 19.
DR MINT; O88712; -.
DR STRING; 10090.ENSMUSP00000078682; -.
DR iPTMnet; O88712; -.
DR PhosphoSitePlus; O88712; -.
DR SwissPalm; O88712; -.
DR EPD; O88712; -.
DR MaxQB; O88712; -.
DR PaxDb; O88712; -.
DR PeptideAtlas; O88712; -.
DR PRIDE; O88712; -.
DR ProteomicsDB; 283973; -. [O88712-1]
DR ProteomicsDB; 283974; -. [O88712-2]
DR ProteomicsDB; 283975; -. [O88712-3]
DR Antibodypedia; 3783; 700 antibodies from 43 providers.
DR DNASU; 13016; -.
DR Ensembl; ENSMUST00000079746; ENSMUSP00000078682; ENSMUSG00000037373. [O88712-1]
DR Ensembl; ENSMUST00000201575; ENSMUSP00000144554; ENSMUSG00000037373. [O88712-3]
DR GeneID; 13016; -.
DR KEGG; mmu:13016; -.
DR UCSC; uc008xaj.2; mouse. [O88712-1]
DR UCSC; uc008xak.2; mouse. [O88712-2]
DR CTD; 1487; -.
DR MGI; MGI:1201685; Ctbp1.
DR VEuPathDB; HostDB:ENSMUSG00000037373; -.
DR eggNOG; KOG0067; Eukaryota.
DR GeneTree; ENSGT00940000157061; -.
DR InParanoid; O88712; -.
DR OrthoDB; 700058at2759; -.
DR PhylomeDB; O88712; -.
DR TreeFam; TF313593; -.
DR Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-4641265; Repression of WNT target genes.
DR BioGRID-ORCS; 13016; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Ctbp1; mouse.
DR PRO; PR:O88712; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O88712; protein.
DR Bgee; ENSMUSG00000037373; Expressed in metanephric loop of Henle and 264 other tissues.
DR ExpressionAtlas; O88712; baseline and differential.
DR Genevisible; O88712; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0001221; F:transcription coregulator binding; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:0031507; P:heterochromatin assembly; ISO:MGI.
DR GO; GO:0035067; P:negative regulation of histone acetylation; ISO:MGI.
DR GO; GO:0090241; P:negative regulation of histone H4 acetylation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; ISO:MGI.
DR GO; GO:0099526; P:presynapse to nucleus signaling pathway; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0050872; P:white fat cell differentiation; IDA:UniProtKB.
DR CDD; cd05299; CtBP_dh; 1.
DR InterPro; IPR043322; CtBP.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 1: Evidence at protein level;
KW ADP-ribosylation; Alternative splicing; Cytoplasm; Differentiation;
KW Direct protein sequencing; Isopeptide bond; NAD; Nucleus; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..441
FT /note="C-terminal-binding protein 1"
FT /id="PRO_0000076042"
FT REGION 1..70
FT /note="Interaction with GLIS2 1"
FT REGION 288..360
FT /note="Interaction with GLIS2 2"
FT REGION 409..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 266
FT /evidence="ECO:0000250"
FT ACT_SITE 295
FT /evidence="ECO:0000250"
FT ACT_SITE 315
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 180..185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 237..243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 264..266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 315..318
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 375..376
FT /note="Cleavage; by CAPN1"
FT /evidence="ECO:0000250|UniProtKB:Q13363"
FT SITE 388..389
FT /note="Cleavage; by CAPN1"
FT /evidence="ECO:0000250|UniProtKB:Q13363"
FT SITE 410..411
FT /note="Cleavage; by CAPN1 and CAPN3"
FT /evidence="ECO:0000250|UniProtKB:Q13363"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13363"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13363"
FT CROSSLNK 429
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..74
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024737"
FT VAR_SEQ 1..13
FT /note="MGSSHLLNKGLPL -> MS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_024738"
FT CONFLICT 55
FT /note="D -> G (in Ref. 3; BAE41586/BAE42587)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="K -> R (in Ref. 3; BAE35946)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="Missing (in Ref. 1; CAA09219 and 3; BAE35946)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 47745 MW; 2105CC8D69D915F4 CRC64;
MGSSHLLNKG LPLGVRPPIM NGPMHPRPLV ALLDGRDCTV EMPILKDVAT VAFCDAQSTQ
EIHEKVLNEA VGALMYHTIT LTREDLEKFK ALRIIVRIGS GFDNIDIKSA GDLGIAVCNV
PAASVEETAD STLCHILNLY RRTTWLHQAL REGTRVQSVE QIREVASGAA RIRGETLGII
GLGRVGQAVA LRAKAFGFNV LFYDPYLSDG IERALGLQRV STLQDLLFHS DCVTLHCGLN
EHNHHLINDF TVKQMRQGAF LVNTARGGLV DEKALAQALK EGRIRGAALD VHESEPFSFS
QGPLKDAPNL ICTPHAAWYS EQASIEMREE AAREIRRAIT GRIPDSLKNC VNKDHLTAAT
HWASMDPAVV HPELNGAAYS RYPPGVVSVA PTGIPAAVEG IVPSAMSLSH GLPPVAHPPH
APSPGQTVKP EADRDHTSDQ L
