BCL7B_MOUSE
ID BCL7B_MOUSE Reviewed; 202 AA.
AC Q921K9; O89022; Q3TV31; Q3U2W0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=B-cell CLL/lymphoma 7 protein family member B;
GN Name=Bcl7b;
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).
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 MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, and Pancreas;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 FUNCTION.
RX PubMed=14647414; DOI=10.1038/sj.onc.1207234;
RA Bonner A.E., Lemon W.J., Devereux T.R., Lubet R.A., You M.;
RT "Molecular profiling of mouse lung tumors: association with tumor
RT progression, lung development, and human lung adenocarcinomas.";
RL Oncogene 23:1166-1176(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-122, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-118; SER-120;
RP SER-122; SER-127; SER-148 AND SER-152, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, 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: 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 (By similarity). Involved in cell
CC cycle progression, maintenance of the nuclear structure and stem cell
CC differentiation (By similarity). May play a role in lung tumor
CC development or progression. {ECO:0000250|UniProtKB:Q9BQE9,
CC ECO:0000269|PubMed:14647414}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q921K9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q921K9-2; Sequence=VSP_019280, VSP_019281;
CC -!- SIMILARITY: Belongs to the BCL7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA09501.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ011145; CAA09501.1; ALT_INIT; mRNA.
DR EMBL; AK131643; BAE20736.1; -; mRNA.
DR EMBL; AK155076; BAE33030.1; -; mRNA.
DR EMBL; AK160439; BAE35789.1; -; mRNA.
DR EMBL; BC011471; AAH11471.1; -; mRNA.
DR CCDS; CCDS51660.1; -. [Q921K9-1]
DR RefSeq; NP_033875.2; NM_009745.2. [Q921K9-1]
DR AlphaFoldDB; Q921K9; -.
DR BioGRID; 198328; 19.
DR ComplexPortal; CPX-1251; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
DR ComplexPortal; CPX-4202; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4204; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4221; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4222; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant.
DR ComplexPortal; CPX-4227; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4228; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4229; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4230; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant.
DR IntAct; Q921K9; 18.
DR STRING; 10090.ENSMUSP00000031692; -.
DR iPTMnet; Q921K9; -.
DR PhosphoSitePlus; Q921K9; -.
DR EPD; Q921K9; -.
DR MaxQB; Q921K9; -.
DR PaxDb; Q921K9; -.
DR PeptideAtlas; Q921K9; -.
DR PRIDE; Q921K9; -.
DR ProteomicsDB; 273659; -. [Q921K9-1]
DR ProteomicsDB; 273660; -. [Q921K9-2]
DR Antibodypedia; 28430; 253 antibodies from 27 providers.
DR DNASU; 12054; -.
DR Ensembl; ENSMUST00000031692; ENSMUSP00000031692; ENSMUSG00000029681. [Q921K9-1]
DR Ensembl; ENSMUST00000111187; ENSMUSP00000106818; ENSMUSG00000029681. [Q921K9-2]
DR GeneID; 12054; -.
DR KEGG; mmu:12054; -.
DR UCSC; uc012een.1; mouse. [Q921K9-1]
DR CTD; 9275; -.
DR MGI; MGI:1332238; Bcl7b.
DR VEuPathDB; HostDB:ENSMUSG00000029681; -.
DR eggNOG; KOG4095; Eukaryota.
DR GeneTree; ENSGT00390000002172; -.
DR HOGENOM; CLU_197698_0_0_1; -.
DR InParanoid; Q921K9; -.
DR OMA; VRKXKEK; -.
DR OrthoDB; 1517597at2759; -.
DR PhylomeDB; Q921K9; -.
DR TreeFam; TF317441; -.
DR BioGRID-ORCS; 12054; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Bcl7b; mouse.
DR PRO; PR:Q921K9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q921K9; protein.
DR Bgee; ENSMUSG00000029681; Expressed in retinal neural layer and 234 other tissues.
DR ExpressionAtlas; Q921K9; baseline and differential.
DR Genevisible; Q921K9; MM.
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: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 Alternative splicing; Apoptosis; Differentiation; Phosphoprotein;
KW Reference proteome; Wnt signaling pathway.
FT CHAIN 1..202
FT /note="B-cell CLL/lymphoma 7 protein family member B"
FT /id="PRO_0000239830"
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:21183079"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 57..58
FT /note="KE -> GF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019280"
FT VAR_SEQ 59..202
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019281"
FT CONFLICT 24
FT /note="A -> D (in Ref. 2; BAE33030)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="Q -> K (in Ref. 2; BAE33030)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 22238 MW; B5976CFF00AB3CC3 CRC64;
MSGRSVRAET RSRAKDDIKK VMAAIEKVRK WEKKWVTVGD TSLRIFKWVP VTDSKEKEKS
KSNNTAAREP NGFPSDASAN SSLLLEFQDE NSNQSSVSDV YQLKVDSSTN SSPSPQQSES
LSPAHTSDFR TDDSQPPTLG QEILEEPSLP ASEVADEPPT LTKEEPVPVE TQTTEEEEDS
GAPPLKRFCV DQPVVPQTTS ES
