BCL7B_HUMAN
ID BCL7B_HUMAN Reviewed; 202 AA.
AC Q9BQE9; A8K226; C9JWD3; D3DXF0; O43769; Q13845; Q6ZW75;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=B-cell CLL/lymphoma 7 protein family member B;
DE AltName: Allergen=Hom s 3;
GN Name=BCL7B;
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).
RC TISSUE=Brain;
RX PubMed=8605326;
RA Zani V.J., Asou N., Jadayel D., Heward J.M., Shipley J., Nacheva E.,
RA Takasuki K., Catovsky D., Dyer M.J.S.;
RT "Molecular cloning of complex chromosomal translocation
RT t(8;14;12)(q24.1;q32.3;q24.1) in a Burkitt lymphoma cell line defines a new
RT gene (BCL7A) with homology to caldesmon.";
RL Blood 87:3124-3134(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), DISEASE, 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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DISEASE, AND TISSUE SPECIFICITY.
RX PubMed=9860302; DOI=10.1007/s004390050874;
RA Meng X., Lu X., Li Z., Green E.D., Massa H., Trask B.J., Morris C.A.,
RA Keating M.T.;
RT "Complete physical map of the common deletion region in Williams syndrome
RT and identification and characterization of three novel genes.";
RL Hum. Genet. 103:590-599(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Subthalamic nucleus, and Thalamus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix, Pancreas, and Placenta;
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 [9]
RP ALLERGEN.
RX PubMed=9806765; DOI=10.1096/fasebj.12.14.1559;
RA Natter S., Seiberler S., Hufnagl P., Binder B.R., Hirschl A.M., Ring J.,
RA Abeck D., Schmidt T., Valent P., Valenta R.;
RT "Isolation of cDNA clones coding for IgE autoantigens with serum IgE from
RT atopic dermatitis patients.";
RL FASEB J. 12:1559-1569(1998).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-118 AND SER-122, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [12]
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 [13]
RP IDENTIFICATION BY 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-122, 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 [15]
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 [16]
RP FUNCTION.
RX PubMed=25569233; DOI=10.1371/journal.pgen.1004921;
RA Uehara T., Kage-Nakadai E., Yoshina S., Imae R., Mitani S.;
RT "The tumor suppressor BCL7B functions in the Wnt signaling pathway.";
RL PLoS Genet. 11:E1004921-E1004921(2015).
CC -!- FUNCTION: Positive regulator of apoptosis. Plays a role in the Wnt
CC signaling pathway, negatively regulating the expression of Wnt
CC signaling components CTNNB1 and HMGA1 (PubMed:25569233). Involved in
CC cell cycle progression, maintenance of the nuclear structure and stem
CC cell differentiation (PubMed:25569233). May play a role in lung tumor
CC development or progression (By similarity).
CC {ECO:0000250|UniProtKB:Q921K9, ECO:0000269|PubMed:25569233}.
CC -!- INTERACTION:
CC Q9BQE9; P43357: MAGEA3; NbExp=3; IntAct=EBI-2560588, EBI-5651459;
CC Q9BQE9; P43360: MAGEA6; NbExp=6; IntAct=EBI-2560588, EBI-1045155;
CC Q9BQE9; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-2560588, EBI-750109;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BQE9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQE9-2; Sequence=VSP_019276, VSP_019277;
CC Name=3;
CC IsoId=Q9BQE9-3; Sequence=VSP_019278, VSP_019279;
CC Name=4;
CC IsoId=Q9BQE9-4; Sequence=VSP_045923;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9860302,
CC ECO:0000269|PubMed:9931421}.
CC -!- DISEASE: Note=BCL7B is located in the Williams-Beuren syndrome (WBS)
CC critical region. WBS results from a hemizygous deletion of several
CC genes on chromosome 7q11.23, thought to arise as a consequence of
CC unequal crossing over between highly homologous low-copy repeat
CC sequences flanking the deleted region. Haploinsufficiency of BCL7B may
CC be the cause of certain cardiovascular and musculo-skeletal
CC abnormalities observed in the disease. {ECO:0000269|PubMed:9860302,
CC ECO:0000269|PubMed:9931421}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE from
CC atopic dermatitis (AD) patients. Identified as an IgE autoantigen in
CC atopic dermatitis (AD) patients with severe skin manifestations.
CC {ECO:0000269|PubMed:9806765}.
CC -!- SIMILARITY: Belongs to the BCL7 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BCL7BID779ch7q11.html";
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DR EMBL; X89985; CAA62012.1; -; mRNA.
DR EMBL; AJ223979; CAA11753.1; -; mRNA.
DR EMBL; BX333744; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK123497; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK290091; BAF82780.1; -; mRNA.
DR EMBL; AC005089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471200; EAW69676.1; -; Genomic_DNA.
DR EMBL; CH471200; EAW69678.1; -; Genomic_DNA.
DR EMBL; BC000956; AAH00956.1; -; mRNA.
DR EMBL; BC001967; AAH01967.1; -; mRNA.
DR EMBL; BC009548; AAH09548.1; -; mRNA.
DR CCDS; CCDS5550.1; -. [Q9BQE9-1]
DR CCDS; CCDS56489.1; -. [Q9BQE9-4]
DR PIR; S58284; S58284.
DR RefSeq; NP_001184173.1; NM_001197244.1. [Q9BQE9-4]
DR RefSeq; NP_001287990.1; NM_001301061.1.
DR RefSeq; NP_001698.2; NM_001707.3. [Q9BQE9-1]
DR AlphaFoldDB; Q9BQE9; -.
DR BioGRID; 114692; 164.
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; Q9BQE9; 42.
DR MINT; Q9BQE9; -.
DR STRING; 9606.ENSP00000411073; -.
DR ChEMBL; CHEMBL4630852; -.
DR Allergome; 3324; Hom s 3.0101.
DR Allergome; 413; Hom s 3.
DR iPTMnet; Q9BQE9; -.
DR PhosphoSitePlus; Q9BQE9; -.
DR BioMuta; BCL7B; -.
DR EPD; Q9BQE9; -.
DR jPOST; Q9BQE9; -.
DR MassIVE; Q9BQE9; -.
DR MaxQB; Q9BQE9; -.
DR PaxDb; Q9BQE9; -.
DR PeptideAtlas; Q9BQE9; -.
DR PRIDE; Q9BQE9; -.
DR ProteomicsDB; 11968; -.
DR ProteomicsDB; 78666; -. [Q9BQE9-1]
DR ProteomicsDB; 78667; -. [Q9BQE9-2]
DR ProteomicsDB; 78668; -. [Q9BQE9-3]
DR Antibodypedia; 28430; 253 antibodies from 27 providers.
DR DNASU; 9275; -.
DR Ensembl; ENST00000223368.7; ENSP00000223368.2; ENSG00000106635.8. [Q9BQE9-1]
DR Ensembl; ENST00000411832.5; ENSP00000393230.1; ENSG00000106635.8. [Q9BQE9-4]
DR GeneID; 9275; -.
DR KEGG; hsa:9275; -.
DR MANE-Select; ENST00000223368.7; ENSP00000223368.2; NM_001707.4; NP_001698.2.
DR UCSC; uc003tyf.3; human. [Q9BQE9-1]
DR CTD; 9275; -.
DR DisGeNET; 9275; -.
DR GeneCards; BCL7B; -.
DR HGNC; HGNC:1005; BCL7B.
DR HPA; ENSG00000106635; Low tissue specificity.
DR MIM; 605846; gene.
DR neXtProt; NX_Q9BQE9; -.
DR OpenTargets; ENSG00000106635; -.
DR Orphanet; 904; Williams syndrome.
DR PharmGKB; PA25315; -.
DR VEuPathDB; HostDB:ENSG00000106635; -.
DR eggNOG; KOG4095; Eukaryota.
DR GeneTree; ENSGT00390000002172; -.
DR HOGENOM; CLU_110835_1_0_1; -.
DR InParanoid; Q9BQE9; -.
DR OMA; VRKXKEK; -.
DR OrthoDB; 1517597at2759; -.
DR PhylomeDB; Q9BQE9; -.
DR TreeFam; TF317441; -.
DR PathwayCommons; Q9BQE9; -.
DR SignaLink; Q9BQE9; -.
DR BioGRID-ORCS; 9275; 19 hits in 1074 CRISPR screens.
DR ChiTaRS; BCL7B; human.
DR GenomeRNAi; 9275; -.
DR Pharos; Q9BQE9; Tbio.
DR PRO; PR:Q9BQE9; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9BQE9; protein.
DR Bgee; ENSG00000106635; Expressed in lower esophagus muscularis layer and 198 other tissues.
DR ExpressionAtlas; Q9BQE9; baseline and differential.
DR Genevisible; Q9BQE9; 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:0003779; F:actin binding; NAS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; 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 GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR006804; BCL7.
DR PANTHER; PTHR12767; PTHR12767; 1.
DR Pfam; PF04714; BCL_N; 1.
PE 1: Evidence at protein level;
KW Allergen; Alternative splicing; Apoptosis; Differentiation; Phosphoprotein;
KW Reference proteome; Williams-Beuren syndrome; Wnt signaling pathway.
FT CHAIN 1..202
FT /note="B-cell CLL/lymphoma 7 protein family member B"
FT /id="PRO_0000239829"
FT REGION 53..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q921K9"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q921K9"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q921K9"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q921K9"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019276"
FT VAR_SEQ 61..88
FT /note="KSNSSAAREPNGFPSDASANSSLLLEFQ -> MPGPWLCPEFLLRKMTTLSC
FT CLCSVWFS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019277"
FT VAR_SEQ 89..145
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045923"
FT VAR_SEQ 163
FT /note="K -> F (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9931421"
FT /id="VSP_019278"
FT VAR_SEQ 164..202
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9931421"
FT /id="VSP_019279"
FT CONFLICT 199
FT /note="A -> R (in Ref. 1; CAA62012)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 22195 MW; 0280371283A02107 CRC64;
MSGRSVRAET RSRAKDDIKK VMAAIEKVRK WEKKWVTVGD TSLRIFKWVP VTDSKEKEKS
KSNSSAAREP NGFPSDASAN SSLLLEFQDE NSNQSSVSDV YQLKVDSSTN SSPSPQQSES
LSPAHTSDFR TDDSQPPTLG QEILEEPSLP SSEVADEPPT LTKEEPVPLE TQVVEEEEDS
GAPPLKRFCV DQPTVPQTAS ES
