CENPI_MOUSE
ID CENPI_MOUSE Reviewed; 746 AA.
AC Q8K1K4; Q8BXU9;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Centromere protein I;
DE Short=CENP-I;
DE AltName: Full=FSH primary response protein 1;
DE AltName: Full=Follicle-stimulating hormone primary response protein;
GN Name=Cenpi; Synonyms=Fshprh1;
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=Cerebellum;
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 STRAIN=FVB/N-3; 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).
CC -!- FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a
CC complex recruited to centromeres which is involved in assembly of
CC kinetochore proteins, mitotic progression and chromosome segregation.
CC May be involved in incorporation of newly synthesized CENPA into
CC centromeres via its interaction with the CENPA-NAC complex. Required
CC for the localization of CENPF, MAD1L1 and MAD2 (MAD2L1 or MAD2L2) to
CC kinetochores. Involved in the response of gonadal tissues to follicle-
CC stimulating hormone (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the CENPA-CAD complex, composed of CENPI, CENPK,
CC CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex
CC interacts with the CENPA-NAC complex, at least composed of CENPA,
CC CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. Interacts with SENP6 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere
CC {ECO:0000250}. Note=Localizes exclusively in the centromeres. The
CC CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC
CC complex (By similarity). {ECO:0000250}.
CC -!- PTM: Sumoylated. Sumoylated form can be polyubiquitinated by RNF4,
CC leading to its degradation. Desumoylation by SENP6 prevents its
CC degradation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CENP-I/CTF3 family. {ECO:0000305}.
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DR EMBL; AK043344; BAC31525.1; -; mRNA.
DR EMBL; BC030328; AAH30328.1; -; mRNA.
DR CCDS; CCDS30393.1; -.
DR RefSeq; NP_001292560.1; NM_001305631.1.
DR RefSeq; NP_666036.1; NM_145924.3.
DR RefSeq; XP_017173829.1; XM_017318340.1.
DR RefSeq; XP_017173830.1; XM_017318341.1.
DR AlphaFoldDB; Q8K1K4; -.
DR SMR; Q8K1K4; -.
DR BioGRID; 221978; 29.
DR ComplexPortal; CPX-5704; Kinetochore CCAN complex.
DR IntAct; Q8K1K4; 4.
DR MINT; Q8K1K4; -.
DR STRING; 10090.ENSMUSP00000079851; -.
DR iPTMnet; Q8K1K4; -.
DR PhosphoSitePlus; Q8K1K4; -.
DR MaxQB; Q8K1K4; -.
DR PaxDb; Q8K1K4; -.
DR PRIDE; Q8K1K4; -.
DR ProteomicsDB; 281581; -.
DR Antibodypedia; 28595; 159 antibodies from 27 providers.
DR Ensembl; ENSMUST00000081064; ENSMUSP00000079851; ENSMUSG00000031262.
DR Ensembl; ENSMUST00000101251; ENSMUSP00000098809; ENSMUSG00000031262.
DR GeneID; 102920; -.
DR KEGG; mmu:102920; -.
DR UCSC; uc009ufu.2; mouse.
DR CTD; 2491; -.
DR MGI; MGI:2147897; Cenpi.
DR VEuPathDB; HostDB:ENSMUSG00000031262; -.
DR eggNOG; ENOG502QU9H; Eukaryota.
DR GeneTree; ENSGT00390000013235; -.
DR HOGENOM; CLU_022189_0_0_1; -.
DR InParanoid; Q8K1K4; -.
DR OMA; LMDICNC; -.
DR OrthoDB; 278624at2759; -.
DR PhylomeDB; Q8K1K4; -.
DR TreeFam; TF101137; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 102920; 22 hits in 60 CRISPR screens.
DR ChiTaRS; Cenpi; mouse.
DR PRO; PR:Q8K1K4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8K1K4; protein.
DR Bgee; ENSMUSG00000031262; Expressed in manus and 135 other tissues.
DR ExpressionAtlas; Q8K1K4; baseline and differential.
DR Genevisible; Q8K1K4; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0034508; P:centromere complex assembly; IEA:InterPro.
DR InterPro; IPR012485; CENP-I.
DR Pfam; PF07778; CENP-I; 1.
PE 2: Evidence at transcript level;
KW Centromere; Chromosome; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..746
FT /note="Centromere protein I"
FT /id="PRO_0000087355"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 42
FT /note="V -> D (in Ref. 1; BAC31525)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="I -> V (in Ref. 1; BAC31525)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 746 AA; 85403 MW; 134CB0D40CC449F3 CRC64;
MATQRVTRNS QQQNRISQGS NSRQTSLLDW MVKDKSGNFK SVLKESSSVE DSTRTDDRTE
GALQVAVGYF QKGPKKASLS KDKVLEKHLT TVENVALSNG LAPEAIDILL NVALSGKFGN
AVNSRILKCM IPESHISEDS VLKAVSWLCV DKCSGNTKVL FYRWLVAMFD FIDHKKQISS
LYGFFFASLQ DDTLCPYVCH LLYLLTKREN VKPFRVRKLL DLQAKMGMQP HLQALLSLYK
FFAPTLISVS LPVRKKIFFN NSKNLWTSAS LAVRLRNQGA FPEPLNLPLR PTTGRSLKRK
WNSHSVIPAL NSANKEYGEK TASLFDYLSS ERSLPLEQLQ RFPQLLESIH CLELPSQMCS
VLNSPLLLHY INCVKDESIL LRISYWLSQA LQEECVWYNI NNYEQEKEFI NFLDLVIRVQ
CFLQEGFYSC EAFLYKSLPL WDGSSCRSQY LQLLAWIPFS SFSEVKPLLS DHLAPLFFTS
SIYFKCSVLQ SLQELLQNWL LWLSTDAHVQ PTTDSPLETT LGGSMSSVSQ LIEYTGWLCV
VAMRLESSST LLLHFILDFY EKVCDIYINY DLPIVVLFPP VIFHSALLSL DATILNQLCY
IMYRYRNNWT AAKKNRYLQK AKPEFSLSSK ICKEYNYYLT AMVCCLWTSR PFKAGVYTDP
ETIENTGGTQ YKSTLNIVYH PSLLSYAASF LLQESPEEMT EHLSSIQGKK WNWYLDYLYS
EGFQGLKLFI KSSVHSSVPK PEENTE
