BCCIP_HUMAN
ID BCCIP_HUMAN Reviewed; 314 AA.
AC Q9P287; B3KP45; Q8ND15; Q96GC4; Q9P288;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=BRCA2 and CDKN1A-interacting protein;
DE AltName: Full=P21- and CDK-associated protein 1;
DE AltName: Full=Protein TOK-1;
GN Name=BCCIP; Synonyms=TOK1;
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] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH
RP CDKN1A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=10878006; DOI=10.1074/jbc.m003031200;
RA Ono T., Kitaura H., Ugai H., Murata T., Yokoyama K.K., Iguchi-Ariga S.M.M.,
RA Ariga H.;
RT "TOK-1, a novel p21Cip1-binding protein that cooperatively enhances p21-
RT dependent inhibitory activity toward CDK2 kinase.";
RL J. Biol. Chem. 275:31145-31154(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RX PubMed=12527204; DOI=10.1016/s0378-1119(02)01098-3;
RA Meng X., Liu J., Shen Z.;
RT "Genomic structure of the human BCCIP gene and its expression in cancer.";
RL Gene 302:139-146(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP INTERACTION WITH BRCA2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11313963; DOI=10.1038/sj.onc.1204098;
RA Liu J., Yuan Y., Huan J., Shen Z.;
RT "Inhibition of breast and brain cancer cell growth by BCCIPalpha, an
RT evolutionarily conserved nuclear protein that interacts with BRCA2.";
RL Oncogene 20:336-345(2001).
RN [8]
RP FUNCTION, AND INTERACTION WITH CDKN1A.
RX PubMed=14726710;
RA Meng X., Liu J., Shen Z.;
RT "Inhibition of G1 to S cell cycle progression by BCCIP beta.";
RL Cell Cycle 3:343-348(2004).
RN [9]
RP FUNCTION.
RX PubMed=15539944; DOI=10.4161/cc.3.11.1213;
RA Meng X., Lu H., Shen Z.;
RT "BCCIP functions through p53 to regulate the expression of p21Waf1/Cip1.";
RL Cell Cycle 3:1457-1462(2004).
RN [10]
RP FUNCTION, INTERACTION WITH BRCA2, AND SUBCELLULAR LOCATION.
RX PubMed=15713648; DOI=10.1128/mcb.25.5.1949-1957.2005;
RA Lu H., Guo X., Meng X., Liu J., Allen C., Wray J., Nickoloff J.A., Shen Z.;
RT "The BRCA2-interacting protein BCCIP functions in RAD51 and BRCA2 focus
RT formation and homologous recombinational repair.";
RL Mol. Cell. Biol. 25:1949-1957(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP FUNCTION.
RX PubMed=17947333; DOI=10.1093/nar/gkm732;
RA Lu H., Yue J., Meng X., Nickoloff J.A., Shen Z.;
RT "BCCIP regulates homologous recombination by distinct domains and
RT suppresses spontaneous DNA damage.";
RL Nucleic Acids Res. 35:7160-7170(2007).
RN [13]
RP INTERACTION WITH MTDH.
RX PubMed=18440304; DOI=10.1016/j.bbrc.2008.04.084;
RA Ash S.C., Yang D.Q., Britt D.E.;
RT "LYRIC/AEG-1 overexpression modulates BCCIPalpha protein levels in prostate
RT tumor cells.";
RL Biochem. Biophys. Res. Commun. 371:333-338(2008).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP 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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION BY
RP 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 [19]
RP INTERACTION WITH TENT5C.
RX PubMed=28931820; DOI=10.1038/s41467-017-00578-5;
RA Mroczek S., Chlebowska J., Kulinski T.M., Gewartowska O., Gruchota J.,
RA Cysewski D., Liudkovska V., Borsuk E., Nowis D., Dziembowski A.;
RT "The non-canonical poly(A) polymerase FAM46C acts as an onco-suppressor in
RT multiple myeloma.";
RL Nat. Commun. 8:619-619(2017).
RN [20]
RP FUNCTION, INTERACTION WITH DCTN1; ACTR1A AND TUBULINS, AND SUBCELLULAR
RP 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). Isoform 2/alpha is
CC particularly important for the regulation of microtubule anchoring,
CC microtubule stability, spindle architecture and spindle orientation,
CC compared to isoform 1/beta (PubMed:28394342). May promote cell cycle
CC arrest by enhancing the inhibition of CDK2 activity by CDKN1A. May be
CC 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). {ECO:0000269|PubMed:10878006,
CC ECO:0000269|PubMed:14726710, ECO:0000269|PubMed:15539944,
CC ECO:0000269|PubMed:15713648, ECO:0000269|PubMed:17947333,
CC ECO:0000269|PubMed:28394342}.
CC -!- SUBUNIT: Interacts with BRCA2, CDKN1A and MTDH/LYRIC (PubMed:10878006,
CC PubMed:11313963, PubMed:14726710, PubMed:15713648, PubMed:18440304).
CC Isoform 2/alpha, but not isoform 1/beta, interacts with DCTN1/p150-
CC glued and ACTR1A/ARP1 (PubMed:28394342). Both isoform 1 and isoform 2
CC interact with alpha-, beta- and gamma-tubulins (PubMed:28394342).
CC Interacts with TENT5C; the interaction has no effect on TENT5C poly(A)
CC polymerase function (PubMed:28931820). {ECO:0000269|PubMed:10878006,
CC ECO:0000269|PubMed:11313963, ECO:0000269|PubMed:14726710,
CC ECO:0000269|PubMed:15713648, ECO:0000269|PubMed:18440304,
CC ECO:0000269|PubMed:28394342, ECO:0000269|PubMed:28931820}.
CC -!- INTERACTION:
CC Q9P287; Q9HC77: CENPJ; NbExp=3; IntAct=EBI-711154, EBI-946194;
CC Q9P287; Q9Y324: FCF1; NbExp=3; IntAct=EBI-711154, EBI-5455734;
CC Q9P287; P82933: MRPS9; NbExp=3; IntAct=EBI-711154, EBI-721385;
CC Q9P287; P01127: PDGFB; NbExp=3; IntAct=EBI-711154, EBI-1554925;
CC Q9P287; Q53GL6: RALY; NbExp=3; IntAct=EBI-711154, EBI-9512693;
CC Q9P287; P62829: RPL23; NbExp=7; IntAct=EBI-711154, EBI-353303;
CC Q9P287; P63173: RPL38; NbExp=3; IntAct=EBI-711154, EBI-359141;
CC Q9P287; P52744: ZNF138; NbExp=3; IntAct=EBI-711154, EBI-10746567;
CC Q9P287; P17023: ZNF19; NbExp=3; IntAct=EBI-711154, EBI-12884200;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10878006,
CC ECO:0000269|PubMed:11313963, ECO:0000269|PubMed:15713648}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:28394342}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:28394342}. Note=Colocalizes with BRCA2 in discrete
CC nuclear foci (PubMed:15713648). In interphase, preferential localizes
CC to the mother centriole (PubMed:28394342). Recruited to the spindle
CC pole matrix and centrosome by microtubules and dynein/dynactin activity
CC (PubMed:28394342). {ECO:0000269|PubMed:15713648,
CC ECO:0000269|PubMed:28394342}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:28394342}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:28394342}. Note=Isoform
CC 1/beta tends to be less abundant at, and less strongly associated with,
CC centrosomes than isoform 2/alpha. {ECO:0000269|PubMed:28394342}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:28394342}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:28394342}. Note=Isoform
CC 2/alpha tends to be more abundant at, and more strongly associated
CC with, centrosomes than isoform 1/beta. {ECO:0000269|PubMed:28394342}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Beta;
CC IsoId=Q9P287-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha;
CC IsoId=Q9P287-2; Sequence=VSP_020540;
CC Name=3;
CC IsoId=Q9P287-3; Sequence=VSP_020541;
CC Name=4;
CC IsoId=Q9P287-4; Sequence=VSP_042023;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in testis and skeletal
CC muscle and at lower levels in brain, heart, kidney, liver, lung, ovary,
CC pancreas, placenta, and spleen. {ECO:0000269|PubMed:10878006,
CC ECO:0000269|PubMed:11313963}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 is expressed throughout the cell cycle.
CC Isoform 2 is expressed following mitosis and peaks in the G1/S phase of
CC the cell cycle. {ECO:0000269|PubMed:10878006}.
CC -!- MISCELLANEOUS: HT1080 cells that constitutively express low levels of
CC BCCIP display increased levels of spontaneous single-stranded DNA and
CC double-strand breaks.
CC -!- SIMILARITY: Belongs to the BCP1 family. {ECO:0000305}.
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DR EMBL; AB040450; BAA92927.1; -; mRNA.
DR EMBL; AB040451; BAA92928.1; -; mRNA.
DR EMBL; AY064247; AAL55436.1; -; Genomic_DNA.
DR EMBL; AY064247; AAL55438.1; -; Genomic_DNA.
DR EMBL; AY064248; AAL55439.1; -; mRNA.
DR EMBL; AY064249; AAL55440.1; -; mRNA.
DR EMBL; AK055691; BAG51557.1; -; mRNA.
DR EMBL; AL834458; CAD39118.1; -; mRNA.
DR EMBL; AL360176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009771; AAH09771.1; -; mRNA.
DR CCDS; CCDS7649.1; -. [Q9P287-2]
DR CCDS; CCDS7650.1; -. [Q9P287-4]
DR CCDS; CCDS7651.1; -. [Q9P287-1]
DR RefSeq; NP_057651.1; NM_016567.3. [Q9P287-2]
DR RefSeq; NP_510868.1; NM_078468.2. [Q9P287-1]
DR RefSeq; NP_510869.1; NM_078469.2. [Q9P287-4]
DR PDB; 7KYQ; X-ray; 3.06 A; A=61-314.
DR PDB; 7KYS; X-ray; 2.20 A; A/B/C=61-314.
DR PDBsum; 7KYQ; -.
DR PDBsum; 7KYS; -.
DR AlphaFoldDB; Q9P287; -.
DR SMR; Q9P287; -.
DR BioGRID; 121161; 114.
DR CORUM; Q9P287; -.
DR IntAct; Q9P287; 45.
DR MINT; Q9P287; -.
DR STRING; 9606.ENSP00000357748; -.
DR GlyGen; Q9P287; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P287; -.
DR PhosphoSitePlus; Q9P287; -.
DR BioMuta; BCCIP; -.
DR DMDM; 74753124; -.
DR EPD; Q9P287; -.
DR jPOST; Q9P287; -.
DR MassIVE; Q9P287; -.
DR MaxQB; Q9P287; -.
DR PaxDb; Q9P287; -.
DR PeptideAtlas; Q9P287; -.
DR PRIDE; Q9P287; -.
DR ProteomicsDB; 83752; -. [Q9P287-1]
DR ProteomicsDB; 83753; -. [Q9P287-2]
DR ProteomicsDB; 83754; -. [Q9P287-3]
DR ProteomicsDB; 83755; -. [Q9P287-4]
DR Antibodypedia; 32428; 163 antibodies from 28 providers.
DR DNASU; 56647; -.
DR Ensembl; ENST00000278100.11; ENSP00000278100.6; ENSG00000107949.17. [Q9P287-1]
DR Ensembl; ENST00000299130.7; ENSP00000299130.3; ENSG00000107949.17. [Q9P287-4]
DR Ensembl; ENST00000368759.5; ENSP00000357748.5; ENSG00000107949.17. [Q9P287-2]
DR GeneID; 56647; -.
DR KEGG; hsa:56647; -.
DR MANE-Select; ENST00000278100.11; ENSP00000278100.6; NM_078468.3; NP_510868.1.
DR UCSC; uc001ljb.5; human. [Q9P287-1]
DR CTD; 56647; -.
DR DisGeNET; 56647; -.
DR GeneCards; BCCIP; -.
DR HGNC; HGNC:978; BCCIP.
DR HPA; ENSG00000107949; Low tissue specificity.
DR MIM; 611883; gene.
DR neXtProt; NX_Q9P287; -.
DR OpenTargets; ENSG00000107949; -.
DR PharmGKB; PA25290; -.
DR VEuPathDB; HostDB:ENSG00000107949; -.
DR eggNOG; KOG3034; Eukaryota.
DR GeneTree; ENSGT00390000000696; -.
DR HOGENOM; CLU_068770_1_1_1; -.
DR InParanoid; Q9P287; -.
DR OMA; MYTMLLE; -.
DR OrthoDB; 1120393at2759; -.
DR PhylomeDB; Q9P287; -.
DR TreeFam; TF320301; -.
DR PathwayCommons; Q9P287; -.
DR SignaLink; Q9P287; -.
DR BioGRID-ORCS; 56647; 392 hits in 1091 CRISPR screens.
DR ChiTaRS; BCCIP; human.
DR GeneWiki; BCCIP; -.
DR GenomeRNAi; 56647; -.
DR Pharos; Q9P287; Tbio.
DR PRO; PR:Q9P287; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9P287; protein.
DR Bgee; ENSG00000107949; Expressed in ventricular zone and 198 other tissues.
DR Genevisible; Q9P287; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
DR GO; GO:0019908; C:nuclear cyclin-dependent protein kinase holoenzyme complex; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019207; F:kinase regulator activity; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0061101; P:neuroendocrine cell differentiation; IDA:UniProtKB.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IDA: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 3D-structure; Alternative splicing; Cell cycle; Cytoplasm; Cytoskeleton;
KW DNA damage; DNA repair; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..314
FT /note="BRCA2 and CDKN1A-interacting protein"
FT /id="PRO_0000249687"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..167
FT /note="Interaction with BRCA2"
FT REGION 161..259
FT /note="Interaction with CDKN1A"
FT COMPBIAS 28..56
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CWI3"
FT VAR_SEQ 259..314
FT /note="KAILKFNYSVQEESDTCLGGKWSFDDVPMTPLRTVMLIPGDKMNEIMDKLKE
FT YLSV -> EQGKPEVLGGPDTRRGLEPVPIQHNGGSRGQVTALVSLKAGLIQSRSTLSD
FT FQGTFMTVGIALS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10878006,
FT ECO:0000303|PubMed:12527204"
FT /id="VSP_020540"
FT VAR_SEQ 259..314
FT /note="KAILKFNYSVQEESDTCLGGKWSFDDVPMTPLRTVMLIPGDKMNEIMDKLKE
FT YLSV -> EQGKPEVLGGPDTRRGLEPVPIQHNGWSVPPVLE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042023"
FT VAR_SEQ 285..314
FT /note="VPMTPLRTVMLIPGDKMNEIMDKLKEYLSV -> WSVPPVLE (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_020541"
FT VARIANT 254
FT /note="E -> Q (in dbSNP:rs17153610)"
FT /id="VAR_046642"
FT CONFLICT 75
FT /note="K -> R (in Ref. 3; BAG51557)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="G -> E (in Ref. 6; AAH09771)"
FT /evidence="ECO:0000305"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:7KYS"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:7KYS"
FT HELIX 71..82
FT /evidence="ECO:0007829|PDB:7KYS"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:7KYS"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:7KYQ"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:7KYS"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:7KYS"
FT TURN 133..138
FT /evidence="ECO:0007829|PDB:7KYS"
FT HELIX 140..156
FT /evidence="ECO:0007829|PDB:7KYS"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:7KYS"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:7KYQ"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:7KYS"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:7KYS"
FT HELIX 192..208
FT /evidence="ECO:0007829|PDB:7KYS"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:7KYS"
FT STRAND 217..227
FT /evidence="ECO:0007829|PDB:7KYS"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:7KYS"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:7KYS"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:7KYS"
FT STRAND 288..297
FT /evidence="ECO:0007829|PDB:7KYS"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:7KYS"
FT HELIX 301..312
FT /evidence="ECO:0007829|PDB:7KYS"
SQ SEQUENCE 314 AA; 35979 MW; 203CA32F7BE0A806 CRC64;
MASRSKRRAV ESGVPQPPDP PVQRDEEEEK EVENEDEDDD DSDKEKDEED EVIDEEVNIE
FEAYSLSDND YDGIKKLLQQ LFLKAPVNTA ELTDLLIQQN HIGSVIKQTD VSEDSNDDMD
EDEVFGFISL LNLTERKGTQ CVEQIQELVL RFCEKNCEKS MVEQLDKFLN DTTKPVGLLL
SERFINVPPQ IALPMYQQLQ KELAGAHRTN KPCGKCYFYL LISKTFVEAG KNNSKKKPSN
KKKAALMFAN AEEEFFYEKA ILKFNYSVQE ESDTCLGGKW SFDDVPMTPL RTVMLIPGDK
MNEIMDKLKE YLSV
