BCCIP_MOUSE
ID BCCIP_MOUSE Reviewed; 316 AA.
AC Q9CWI3; Q9D1E0;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=BRCA2 and CDKN1A-interacting protein;
GN Name=Bccip;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic stem cell;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and Spleen;
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).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28394342; DOI=10.1038/onc.2017.92;
RA Huhn S.C., Liu J., Ye C., Lu H., Jiang X., Feng X., Ganesan S., White E.,
RA Shen Z.;
RT "Regulation of spindle integrity and mitotic fidelity by BCCIP.";
RL Oncogene 36:4750-4766(2017).
CC -!- FUNCTION: During interphase, required for microtubule organizing and
CC anchoring activities. During mitosis, required for the organization and
CC stabilization of the spindle pole (PubMed:28394342). May promote cell
CC cycle arrest by enhancing the inhibition of CDK2 activity by CDKN1A.
CC May be required for repair of DNA damage by homologous recombination in
CC conjunction with BRCA2. May not be involved in non-homologous end
CC joining (NHEJ) (By similarity). {ECO:0000250|UniProtKB:Q9P287,
CC ECO:0000269|PubMed:28394342}.
CC -!- SUBUNIT: Interacts with BRCA2, CDKN1A and MTDH/LYRIC. Interacts with
CC DCTN1/p150-glued and ACTR1A/ARP1. Interacts with alpha-, beta- and
CC gamma-tubulins. Interacts with TENT5C; the interaction has no effect on
CC TENT5C poly(A) polymerase function (By similarity).
CC {ECO:0000250|UniProtKB:Q9P287}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9P287}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriole {ECO:0000269|PubMed:28394342}. Cytoplasm, cytoskeleton,
CC spindle pole {ECO:0000269|PubMed:28394342}. Note=Colocalizes with BRCA2
CC in discrete nuclear foci (By similarity). In interphase, preferential
CC localizes to the mother centriole (PubMed:28394342). Recruited to the
CC spindle pole matrix and centrosome by microtubules and dynein/dynactin
CC activity (By similarity). {ECO:0000250|UniProtKB:Q9P287,
CC ECO:0000269|PubMed:28394342}.
CC -!- SIMILARITY: Belongs to the BCP1 family. {ECO:0000305}.
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DR EMBL; AK003666; BAB22925.1; -; mRNA.
DR EMBL; AK010684; BAB27116.1; -; mRNA.
DR EMBL; BC048465; AAH48465.1; -; mRNA.
DR CCDS; CCDS21935.1; -.
DR RefSeq; NP_079668.2; NM_025392.2.
DR AlphaFoldDB; Q9CWI3; -.
DR SMR; Q9CWI3; -.
DR BioGRID; 211263; 20.
DR IntAct; Q9CWI3; 1.
DR MINT; Q9CWI3; -.
DR STRING; 10090.ENSMUSP00000033282; -.
DR iPTMnet; Q9CWI3; -.
DR PhosphoSitePlus; Q9CWI3; -.
DR EPD; Q9CWI3; -.
DR MaxQB; Q9CWI3; -.
DR PaxDb; Q9CWI3; -.
DR PeptideAtlas; Q9CWI3; -.
DR PRIDE; Q9CWI3; -.
DR ProteomicsDB; 273736; -.
DR Antibodypedia; 32428; 163 antibodies from 28 providers.
DR DNASU; 66165; -.
DR Ensembl; ENSMUST00000033282; ENSMUSP00000033282; ENSMUSG00000030983.
DR GeneID; 66165; -.
DR KEGG; mmu:66165; -.
DR UCSC; uc009kdi.1; mouse.
DR CTD; 56647; -.
DR MGI; MGI:1913415; Bccip.
DR VEuPathDB; HostDB:ENSMUSG00000030983; -.
DR eggNOG; KOG3034; Eukaryota.
DR GeneTree; ENSGT00390000000696; -.
DR HOGENOM; CLU_068770_1_1_1; -.
DR InParanoid; Q9CWI3; -.
DR OMA; MPQEPAR; -.
DR OrthoDB; 1120393at2759; -.
DR PhylomeDB; Q9CWI3; -.
DR TreeFam; TF320301; -.
DR BioGRID-ORCS; 66165; 29 hits in 109 CRISPR screens.
DR ChiTaRS; Bccip; mouse.
DR PRO; PR:Q9CWI3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CWI3; protein.
DR Bgee; ENSMUSG00000030983; Expressed in otic placode and 251 other tissues.
DR Genevisible; Q9CWI3; MM.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
DR GO; GO:0019908; C:nuclear cyclin-dependent protein kinase holoenzyme complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019207; F:kinase regulator activity; ISO:MGI.
DR GO; GO:0015631; F:tubulin binding; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:CACAO.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:MGI.
DR GO; GO:0034453; P:microtubule anchoring; IMP:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; ISO:MGI.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0061101; P:neuroendocrine cell differentiation; ISO:MGI.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:MGI.
DR InterPro; IPR025602; BCP1_family.
DR PANTHER; PTHR13261; PTHR13261; 1.
DR Pfam; PF13862; BCCIP; 1.
DR PIRSF; PIRSF028983; BCP1; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; Cytoskeleton; DNA damage; DNA repair; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..316
FT /note="BRCA2 and CDKN1A-interacting protein"
FT /id="PRO_0000249688"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..169
FT /note="Interaction with BRCA2"
FT /evidence="ECO:0000250"
FT REGION 163..261
FT /note="Interaction with CDKN1A"
FT /evidence="ECO:0000250"
FT COMPBIAS 24..57
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P287"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P287"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 83
FT /note="L -> P (in Ref. 1; BAB22925)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="D -> G (in Ref. 1; BAB22925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 35942 MW; 49E59C1AF93A149B CRC64;
MASKAKKRAV GNGIQRPLGA PGQREEEEEE EDEVEDEEED EDDSDEEEDE VDEIVDEEVN
IEFEAYSISD NDYGGIKKLL QQLFLKAPVN TAELTNLLMQ QNHIGSVIKQ TDVSEDSDDE
VDEDEIFGFI SLLNLTERKG TQCAEQIKEL VLSFCEKTCE QSMVEQLDKL LNDTSKPVGL
LLSERFINVP PQIALPMHQQ LQKELSEARR TNKPCGKCCF YLLISKTFME AGKSSSRKRQ
DSLQQGALMF ANAEEEFFYE KAILKFSYSV QGESDTRLGG RWSFDDVPMT PLRTVMVIPD
DRMNEIMETL KDHLSV
