CENPI_HUMAN
ID CENPI_HUMAN Reviewed; 756 AA.
AC Q92674; Q5JWZ9; Q96ED0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 171.
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;
DE AltName: Full=Interphase centromere complex protein 19;
DE AltName: Full=Leucine-rich primary response protein 1;
GN Name=CENPI; Synonyms=FSHPRH1, ICEN19, LRPR1;
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).
RX PubMed=8921378; DOI=10.1006/geno.1996.0528;
RA Roberts R.G., Kendall E., Vetrie D., Bobrow M.;
RT "Sequence and chromosomal location of a human homologue of LRPR1, an FSH
RT primary response gene.";
RL Genomics 37:122-124(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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, AND SUBCELLULAR LOCATION.
RX PubMed=12640463; DOI=10.1038/ncb953;
RA Liu S.-T., Hittle J.C., Jablonski S.A., Campbell M.S., Yoda K., Yen T.J.;
RT "Human CENP-I specifies localization of CENP-F, MAD1 and MAD2 to
RT kinetochores and is essential for mitosis.";
RL Nat. Cell Biol. 5:341-345(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16716197; DOI=10.1111/j.1365-2443.2006.00969.x;
RA Izuta H., Ikeno M., Suzuki N., Tomonaga T., Nozaki N., Obuse C., Kisu Y.,
RA Goshima N., Nomura F., Nomura N., Yoda K.;
RT "Comprehensive analysis of the ICEN (Interphase Centromere Complex)
RT components enriched in the CENP-A chromatin of human cells.";
RL Genes Cells 11:673-684(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH
RP CENPH; CENPK; CENPN; CENPO; CENPP; CENPQ; CENPR AND CENPU, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16622420; DOI=10.1038/ncb1396;
RA Okada M., Cheeseman I.M., Hori T., Okawa K., McLeod I.X., Yates J.R. III,
RA Desai A., Fukagawa T.;
RT "The CENP-H-I complex is required for the efficient incorporation of newly
RT synthesized CENP-A into centromeres.";
RL Nat. Cell Biol. 8:446-457(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE CENPA-CAD
RP COMPLEX WITH CENPK; CENPL; CENPO; CENPP; CENPQ; CENPR AND CENPS.
RX PubMed=16622419; DOI=10.1038/ncb1397;
RA Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III,
RA Cleveland D.W.;
RT "The human CENP-A centromeric nucleosome-associated complex.";
RL Nat. Cell Biol. 8:458-469(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP SUMOYLATION, UBIQUITINATION BY RNF4, DESUMOYLATION BY SENP6, AND
RP INTERACTION WITH SENP6.
RX PubMed=20212317; DOI=10.1083/jcb.200909008;
RA Mukhopadhyay D., Arnaoutov A., Dasso M.;
RT "The SUMO protease SENP6 is essential for inner kinetochore assembly.";
RL J. Cell Biol. 188:681-692(2010).
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. {ECO:0000269|PubMed:12640463,
CC ECO:0000269|PubMed:16622420}.
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.
CC {ECO:0000269|PubMed:16622419, ECO:0000269|PubMed:16622420,
CC ECO:0000269|PubMed:20212317}.
CC -!- INTERACTION:
CC Q92674; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-11085153, EBI-742887;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere. Note=Localizes
CC exclusively in the centromeres. The CENPA-CAD complex is probably
CC recruited on centromeres by the CENPA-NAC complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92674-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92674-2; Sequence=VSP_015797;
CC -!- INDUCTION: By follicle-stimulating hormone (FSH).
CC -!- PTM: Sumoylated. Sumoylated form can be polyubiquitinated by RNF4,
CC leading to its degradation. Desumoylation by SENP6 prevents its
CC degradation. {ECO:0000269|PubMed:20212317}.
CC -!- SIMILARITY: Belongs to the CENP-I/CTF3 family. {ECO:0000305}.
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DR EMBL; X97249; CAA65884.1; -; mRNA.
DR EMBL; AL109963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012462; AAH12462.1; -; mRNA.
DR CCDS; CCDS14479.1; -. [Q92674-1]
DR CCDS; CCDS83482.1; -. [Q92674-2]
DR RefSeq; NP_001305452.1; NM_001318523.1. [Q92674-2]
DR RefSeq; NP_006724.2; NM_006733.3. [Q92674-1]
DR RefSeq; XP_005262168.1; XM_005262111.2. [Q92674-1]
DR RefSeq; XP_011529196.1; XM_011530894.2. [Q92674-1]
DR RefSeq; XP_011529197.1; XM_011530895.2. [Q92674-1]
DR RefSeq; XP_011529199.1; XM_011530897.2. [Q92674-1]
DR RefSeq; XP_011529201.1; XM_011530899.2. [Q92674-1]
DR AlphaFoldDB; Q92674; -.
DR BioGRID; 108769; 35.
DR ComplexPortal; CPX-5646; Kinetochore CCAN complex.
DR CORUM; Q92674; -.
DR IntAct; Q92674; 15.
DR MINT; Q92674; -.
DR STRING; 9606.ENSP00000362018; -.
DR iPTMnet; Q92674; -.
DR PhosphoSitePlus; Q92674; -.
DR BioMuta; CENPI; -.
DR DMDM; 77416860; -.
DR EPD; Q92674; -.
DR jPOST; Q92674; -.
DR MassIVE; Q92674; -.
DR MaxQB; Q92674; -.
DR PaxDb; Q92674; -.
DR PeptideAtlas; Q92674; -.
DR PRIDE; Q92674; -.
DR ProteomicsDB; 75403; -. [Q92674-1]
DR ProteomicsDB; 75404; -. [Q92674-2]
DR Antibodypedia; 28595; 159 antibodies from 27 providers.
DR DNASU; 2491; -.
DR Ensembl; ENST00000372926.5; ENSP00000362017.1; ENSG00000102384.14. [Q92674-2]
DR Ensembl; ENST00000372927.5; ENSP00000362018.1; ENSG00000102384.14. [Q92674-1]
DR Ensembl; ENST00000682095.1; ENSP00000507927.1; ENSG00000102384.14. [Q92674-1]
DR Ensembl; ENST00000684367.1; ENSP00000507595.1; ENSG00000102384.14. [Q92674-1]
DR GeneID; 2491; -.
DR KEGG; hsa:2491; -.
DR MANE-Select; ENST00000682095.1; ENSP00000507927.1; NM_001386188.2; NP_001373117.1.
DR UCSC; uc004egy.4; human. [Q92674-1]
DR CTD; 2491; -.
DR DisGeNET; 2491; -.
DR GeneCards; CENPI; -.
DR HGNC; HGNC:3968; CENPI.
DR HPA; ENSG00000102384; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 300065; gene.
DR neXtProt; NX_Q92674; -.
DR OpenTargets; ENSG00000102384; -.
DR PharmGKB; PA28385; -.
DR VEuPathDB; HostDB:ENSG00000102384; -.
DR eggNOG; ENOG502QU9H; Eukaryota.
DR GeneTree; ENSGT00390000013235; -.
DR HOGENOM; CLU_022189_0_0_1; -.
DR InParanoid; Q92674; -.
DR OMA; LMDICNC; -.
DR PhylomeDB; Q92674; -.
DR TreeFam; TF101137; -.
DR PathwayCommons; Q92674; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q92674; -.
DR SIGNOR; Q92674; -.
DR BioGRID-ORCS; 2491; 295 hits in 722 CRISPR screens.
DR ChiTaRS; CENPI; human.
DR GeneWiki; CENPI; -.
DR GenomeRNAi; 2491; -.
DR Pharos; Q92674; Tbio.
DR PRO; PR:Q92674; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q92674; protein.
DR Bgee; ENSG00000102384; Expressed in secondary oocyte and 130 other tissues.
DR ExpressionAtlas; Q92674; baseline and differential.
DR Genevisible; Q92674; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0034508; P:centromere complex assembly; IEA:InterPro.
DR GO; GO:0007548; P:sex differentiation; TAS:ProtInc.
DR InterPro; IPR012485; CENP-I.
DR Pfam; PF07778; CENP-I; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Centromere; Chromosome; Nucleus; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..756
FT /note="Centromere protein I"
FT /id="PRO_0000087354"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 523..756
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015797"
FT CONFLICT 262..263
FT /note="FK -> LQ (in Ref. 1; CAA65884)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="Y -> H (in Ref. 1; CAA65884)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="F -> Y (in Ref. 1; CAA65884)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="C -> S (in Ref. 1; CAA65884)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="S -> C (in Ref. 1; CAA65884)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="N -> D (in Ref. 1; CAA65884)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="H -> Y (in Ref. 1; CAA65884)"
FT /evidence="ECO:0000305"
FT CONFLICT 658
FT /note="G -> A (in Ref. 1; CAA65884)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 756 AA; 86720 MW; A3439CF1729D7A66 CRC64;
MSPQKRVKNV QAQNRTSQGS SSFQTTLSAW KVKQDPSNSK NISKHGQNNP VGDYEHADDQ
AEEDALQMAV GYFEKGPIKA SQNKDKTLEK HLKTVENVAW KNGLASEEID ILLNIALSGK
FGNAVNTRIL KCMIPATVIS EDSVVKAVSW LCVGKCSGST KVLFYRWLVA MFDFIDRKEQ
INLLYGFFFA SLQDDALCPY VCHLLYLLTK KENVKPFRVR KLLDLQAKMG MQPHLQALLS
LYKFFAPALI SVSLPVRKKI YFKNSENLWK TALLAVKQRN RGPSPEPLKL MLGPANVRPL
KRKWNSLSVI PVLNSSSYTK ECGKKEMSLS DCLNRSGSFP LEQLQSFPQL LQNIHCLELP
SQMGSVLNNS LLLHYINCVR DEPVLLRFYY WLSQTLQEEC IWYKVNNYEH GKEFTNFLDT
IIRAECFLQE GFYSCEAFLY KSLPLWDGLC CRSQFLQLVS WIPFSSFSEV KPLLFDHLAQ
LFFTSTIYFK CSVLQSLKEL LQNWLLWLSM DIHMKPVTNS PLETTLGGSM NSVSKLIHYV
GWLSTTAMRL ESNNTFLLHF ILDFYEKVCD IYINYNLPLV VLFPPGIFYS ALLSLDTSIL
NQLCFIMHRY RKNLTAAKKN ELVQKTKSEF NFSSKTYQEF NHYLTSMVGC LWTSKPFGKG
IYIDPEILEK TGVAEYKNSL NVVHHPSFLS YAVSFLLQES PEERTVNVSS IRGKKWSWYL
DYLFSQGLQG LKLFIRSSVH HSSIPRAEGI NCNNQY
