BCL7C_HUMAN
ID BCL7C_HUMAN Reviewed; 217 AA.
AC Q8WUZ0; O43770; Q6PD89;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=B-cell CLL/lymphoma 7 protein family member C;
GN Name=BCL7C;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=9931421; DOI=10.1016/s0378-1119(98)00514-9;
RA Jadayel D.M., Osborne L.R., Coignet L.J.A., Zani V.J., Tsui L.-C.,
RA Scherer S.W., Dyer M.J.S.;
RT "The BCL7 gene family: deletion of BCL7B in Williams syndrome.";
RL Gene 224:35-44(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Pancreas;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-111; SER-114; SER-122 AND
RP SER-126, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-111; THR-118 AND SER-126, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-100; THR-111;
RP THR-118; SER-122 AND SER-126, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100 AND SER-126, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118; SER-126 AND SER-156, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-111; THR-118; SER-122 AND
RP SER-126, AND 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).
CC -!- FUNCTION: May play an anti-apoptotic role. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WUZ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WUZ0-2; Sequence=VSP_019282;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9931421}.
CC -!- SIMILARITY: Belongs to the BCL7 family. {ECO:0000305}.
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DR EMBL; AJ223980; CAA11754.1; -; mRNA.
DR EMBL; AC135048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019071; AAH19071.1; -; mRNA.
DR EMBL; BC058863; AAH58863.1; -; mRNA.
DR CCDS; CCDS10693.1; -. [Q8WUZ0-1]
DR CCDS; CCDS67012.1; -. [Q8WUZ0-2]
DR RefSeq; NP_001273455.1; NM_001286526.1. [Q8WUZ0-2]
DR RefSeq; NP_004756.2; NM_004765.3. [Q8WUZ0-1]
DR AlphaFoldDB; Q8WUZ0; -.
DR BioGRID; 114691; 107.
DR ComplexPortal; CPX-1195; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
DR ComplexPortal; CPX-4084; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4203; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4206; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4207; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant.
DR ComplexPortal; CPX-4223; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4224; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4225; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4226; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant.
DR IntAct; Q8WUZ0; 99.
DR MINT; Q8WUZ0; -.
DR STRING; 9606.ENSP00000369674; -.
DR iPTMnet; Q8WUZ0; -.
DR MetOSite; Q8WUZ0; -.
DR PhosphoSitePlus; Q8WUZ0; -.
DR BioMuta; BCL7C; -.
DR EPD; Q8WUZ0; -.
DR jPOST; Q8WUZ0; -.
DR MassIVE; Q8WUZ0; -.
DR MaxQB; Q8WUZ0; -.
DR PaxDb; Q8WUZ0; -.
DR PeptideAtlas; Q8WUZ0; -.
DR PRIDE; Q8WUZ0; -.
DR ProteomicsDB; 74730; -. [Q8WUZ0-1]
DR ProteomicsDB; 74731; -. [Q8WUZ0-2]
DR Antibodypedia; 13852; 190 antibodies from 26 providers.
DR DNASU; 9274; -.
DR Ensembl; ENST00000215115.5; ENSP00000215115.4; ENSG00000099385.12. [Q8WUZ0-1]
DR Ensembl; ENST00000380317.8; ENSP00000369674.4; ENSG00000099385.12. [Q8WUZ0-2]
DR GeneID; 9274; -.
DR KEGG; hsa:9274; -.
DR MANE-Select; ENST00000215115.5; ENSP00000215115.4; NM_004765.4; NP_004756.2.
DR UCSC; uc002dzv.5; human. [Q8WUZ0-1]
DR CTD; 9274; -.
DR DisGeNET; 9274; -.
DR GeneCards; BCL7C; -.
DR HGNC; HGNC:1006; BCL7C.
DR HPA; ENSG00000099385; Low tissue specificity.
DR MIM; 605847; gene.
DR neXtProt; NX_Q8WUZ0; -.
DR OpenTargets; ENSG00000099385; -.
DR PharmGKB; PA25316; -.
DR VEuPathDB; HostDB:ENSG00000099385; -.
DR eggNOG; KOG4095; Eukaryota.
DR GeneTree; ENSGT00390000002172; -.
DR HOGENOM; CLU_110835_1_1_1; -.
DR InParanoid; Q8WUZ0; -.
DR OMA; KRICPDA; -.
DR OrthoDB; 1517597at2759; -.
DR PhylomeDB; Q8WUZ0; -.
DR TreeFam; TF317441; -.
DR PathwayCommons; Q8WUZ0; -.
DR SignaLink; Q8WUZ0; -.
DR BioGRID-ORCS; 9274; 13 hits in 1076 CRISPR screens.
DR ChiTaRS; BCL7C; human.
DR GenomeRNAi; 9274; -.
DR Pharos; Q8WUZ0; Tdark.
DR PRO; PR:Q8WUZ0; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8WUZ0; protein.
DR Bgee; ENSG00000099385; Expressed in lower esophagus mucosa and 182 other tissues.
DR ExpressionAtlas; Q8WUZ0; baseline and differential.
DR Genevisible; Q8WUZ0; HS.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0140288; C:GBAF complex; IC:ComplexPortal.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0070316; P:regulation of G0 to G1 transition; IC:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IC:ComplexPortal.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR InterPro; IPR006804; BCL7.
DR PANTHER; PTHR12767; PTHR12767; 1.
DR Pfam; PF04714; BCL_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..217
FT /note="B-cell CLL/lymphoma 7 protein family member C"
FT /id="PRO_0000239833"
FT REGION 49..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..137
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08664"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT MOD_RES 118
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 177..217
FT /note="APEAYPVFEPVPPVPEAAQGDTEDSEGAPPLKRICPNAPDP -> DSGVRMT
FT RRALHEKGLKTEPLRRLLPRRGLRTNVRPSSMAVPDTRAPGGGSKAPRAPRTIPQGKGR
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019282"
FT CONFLICT 108
FT /note="Q -> P (in Ref. 1; CAA11754)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="E -> G (in Ref. 1; CAA11754)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 217 AA; 23468 MW; 379CDFFF250195A5 CRC64;
MAGRTVRAET RSRAKDDIKK VMATIEKVRR WEKRWVTVGD TSLRIFKWVP VVDPQEEERR
RAGGGAERSR GRERRGRGAS PRGGGPLILL DLNDENSNQS FHSEGSLQKG TEPSPGGTPQ
PSRPVSPAGP PEGVPEEAQP PRLGQERDPG GITAGSTDEP PMLTKEEPVP ELLEAEAPEA
YPVFEPVPPV PEAAQGDTED SEGAPPLKRI CPNAPDP