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Q92674

- CENPI_HUMAN

UniProt

Q92674 - CENPI_HUMAN

Protein

Centromere protein I

Gene

CENPI

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (11 Oct 2005)
      Previous versions | rss
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    Functioni

    Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Required for the localization of CENPF, MAD1L1 and MAD2 (MAD2L1 or MAD2L2) to kinetochores. Involved in the response of gonadal tissues to follicle-stimulating hormone.2 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. CENP-A containing nucleosome assembly Source: Reactome
    2. mitotic cell cycle Source: Reactome
    3. nucleosome assembly Source: Reactome
    4. sex differentiation Source: ProtInc

    Enzyme and pathway databases

    ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
    REACT_682. Mitotic Prometaphase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Centromere protein I
    Short name:
    CENP-I
    Alternative name(s):
    FSH primary response protein 1
    Follicle-stimulating hormone primary response protein
    Interphase centromere complex protein 19
    Leucine-rich primary response protein 1
    Gene namesi
    Name:CENPI
    Synonyms:FSHPRH1, ICEN19, LRPR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:3968. CENPI.

    Subcellular locationi

    Nucleus. Chromosomecentromere
    Note: Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. kinetochore Source: UniProtKB
    3. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Centromere, Chromosome, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28385.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 756756Centromere protein IPRO_0000087354Add
    BLAST

    Post-translational modificationi

    Sumoylated. Sumoylated form can be polyubiquitinated by RNF4, leading to its degradation. Desumoylation by SENP6 prevents its degradation.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ92674.
    PaxDbiQ92674.
    PRIDEiQ92674.

    PTM databases

    PhosphoSiteiQ92674.

    Expressioni

    Inductioni

    By follicle-stimulating hormone (FSH).

    Gene expression databases

    ArrayExpressiQ92674.
    BgeeiQ92674.
    CleanExiHS_CENPI.
    GenevestigatoriQ92674.

    Organism-specific databases

    HPAiCAB012356.

    Interactioni

    Subunit structurei

    Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex interacts with the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. Interacts with SENP6.3 Publications

    Protein-protein interaction databases

    BioGridi108769. 11 interactions.
    MINTiMINT-4536309.
    STRINGi9606.ENSP00000218507.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92674.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the mis6 family.Curated

    Phylogenomic databases

    eggNOGiNOG16022.
    HOGENOMiHOG000049199.
    HOVERGENiHBG080256.
    InParanoidiQ92674.
    KOiK11501.
    OMAiLCPYVCH.
    OrthoDBiEOG70PBZG.
    PhylomeDBiQ92674.
    TreeFamiTF101137.

    Family and domain databases

    InterProiIPR012485. CENP-I.
    [Graphical view]
    PANTHERiPTHR15408. PTHR15408. 1 hit.
    PfamiPF07778. CENP-I. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92674-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSPQKRVKNV QAQNRTSQGS SSFQTTLSAW KVKQDPSNSK NISKHGQNNP    50
    VGDYEHADDQ AEEDALQMAV GYFEKGPIKA SQNKDKTLEK HLKTVENVAW 100
    KNGLASEEID ILLNIALSGK FGNAVNTRIL KCMIPATVIS EDSVVKAVSW 150
    LCVGKCSGST KVLFYRWLVA MFDFIDRKEQ INLLYGFFFA SLQDDALCPY 200
    VCHLLYLLTK KENVKPFRVR KLLDLQAKMG MQPHLQALLS LYKFFAPALI 250
    SVSLPVRKKI YFKNSENLWK TALLAVKQRN RGPSPEPLKL MLGPANVRPL 300
    KRKWNSLSVI PVLNSSSYTK ECGKKEMSLS DCLNRSGSFP LEQLQSFPQL 350
    LQNIHCLELP SQMGSVLNNS LLLHYINCVR DEPVLLRFYY WLSQTLQEEC 400
    IWYKVNNYEH GKEFTNFLDT IIRAECFLQE GFYSCEAFLY KSLPLWDGLC 450
    CRSQFLQLVS WIPFSSFSEV KPLLFDHLAQ LFFTSTIYFK CSVLQSLKEL 500
    LQNWLLWLSM DIHMKPVTNS PLETTLGGSM NSVSKLIHYV GWLSTTAMRL 550
    ESNNTFLLHF ILDFYEKVCD IYINYNLPLV VLFPPGIFYS ALLSLDTSIL 600
    NQLCFIMHRY RKNLTAAKKN ELVQKTKSEF NFSSKTYQEF NHYLTSMVGC 650
    LWTSKPFGKG IYIDPEILEK TGVAEYKNSL NVVHHPSFLS YAVSFLLQES 700
    PEERTVNVSS IRGKKWSWYL DYLFSQGLQG LKLFIRSSVH HSSIPRAEGI 750
    NCNNQY 756
    Length:756
    Mass (Da):86,720
    Last modified:October 11, 2005 - v2
    Checksum:iA3439CF1729D7A66
    GO
    Isoform 2 (identifier: Q92674-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         523-756: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:522
    Mass (Da):59,813
    Checksum:iBAB3AA874485BD51
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti262 – 2632FK → LQ in CAA65884. (PubMed:8921378)Curated
    Sequence conflicti389 – 3891Y → H in CAA65884. (PubMed:8921378)Curated
    Sequence conflicti432 – 4321F → Y in CAA65884. (PubMed:8921378)Curated
    Sequence conflicti450 – 4501C → S in CAA65884. (PubMed:8921378)Curated
    Sequence conflicti532 – 5321S → C in CAA65884. (PubMed:8921378)Curated
    Sequence conflicti576 – 5761N → D in CAA65884. (PubMed:8921378)Curated
    Sequence conflicti642 – 6421H → Y in CAA65884. (PubMed:8921378)Curated
    Sequence conflicti658 – 6581G → A in CAA65884. (PubMed:8921378)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei523 – 756234Missing in isoform 2. 1 PublicationVSP_015797Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X97249 mRNA. Translation: CAA65884.1.
    AL109963 Genomic DNA. Translation: CAB72340.1.
    AL109963 Genomic DNA. Translation: CAI42268.1.
    BC012462 mRNA. Translation: AAH12462.1.
    CCDSiCCDS14479.1. [Q92674-1]
    RefSeqiNP_006724.2. NM_006733.2. [Q92674-1]
    XP_005262168.1. XM_005262111.1. [Q92674-1]
    UniGeneiHs.348920.
    Hs.737663.

    Genome annotation databases

    EnsembliENST00000372926; ENSP00000362017; ENSG00000102384. [Q92674-2]
    ENST00000372927; ENSP00000362018; ENSG00000102384. [Q92674-1]
    ENST00000423383; ENSP00000399274; ENSG00000102384. [Q92674-1]
    GeneIDi2491.
    KEGGihsa:2491.
    UCSCiuc004egx.3. human. [Q92674-1]

    Polymorphism databases

    DMDMi77416860.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X97249 mRNA. Translation: CAA65884.1 .
    AL109963 Genomic DNA. Translation: CAB72340.1 .
    AL109963 Genomic DNA. Translation: CAI42268.1 .
    BC012462 mRNA. Translation: AAH12462.1 .
    CCDSi CCDS14479.1. [Q92674-1 ]
    RefSeqi NP_006724.2. NM_006733.2. [Q92674-1 ]
    XP_005262168.1. XM_005262111.1. [Q92674-1 ]
    UniGenei Hs.348920.
    Hs.737663.

    3D structure databases

    ProteinModelPortali Q92674.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108769. 11 interactions.
    MINTi MINT-4536309.
    STRINGi 9606.ENSP00000218507.

    PTM databases

    PhosphoSitei Q92674.

    Polymorphism databases

    DMDMi 77416860.

    Proteomic databases

    MaxQBi Q92674.
    PaxDbi Q92674.
    PRIDEi Q92674.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372926 ; ENSP00000362017 ; ENSG00000102384 . [Q92674-2 ]
    ENST00000372927 ; ENSP00000362018 ; ENSG00000102384 . [Q92674-1 ]
    ENST00000423383 ; ENSP00000399274 ; ENSG00000102384 . [Q92674-1 ]
    GeneIDi 2491.
    KEGGi hsa:2491.
    UCSCi uc004egx.3. human. [Q92674-1 ]

    Organism-specific databases

    CTDi 2491.
    GeneCardsi GC0XP100353.
    H-InvDB HIX0016922.
    HGNCi HGNC:3968. CENPI.
    HPAi CAB012356.
    MIMi 300065. gene.
    neXtProti NX_Q92674.
    PharmGKBi PA28385.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG16022.
    HOGENOMi HOG000049199.
    HOVERGENi HBG080256.
    InParanoidi Q92674.
    KOi K11501.
    OMAi LCPYVCH.
    OrthoDBi EOG70PBZG.
    PhylomeDBi Q92674.
    TreeFami TF101137.

    Enzyme and pathway databases

    Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
    REACT_682. Mitotic Prometaphase.

    Miscellaneous databases

    GeneWikii CENPI.
    GenomeRNAii 2491.
    NextBioi 9839.
    PROi Q92674.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92674.
    Bgeei Q92674.
    CleanExi HS_CENPI.
    Genevestigatori Q92674.

    Family and domain databases

    InterProi IPR012485. CENP-I.
    [Graphical view ]
    PANTHERi PTHR15408. PTHR15408. 1 hit.
    Pfami PF07778. CENP-I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and chromosomal location of a human homologue of LRPR1, an FSH primary response gene."
      Roberts R.G., Kendall E., Vetrie D., Bobrow M.
      Genomics 37:122-124(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    4. "Human CENP-I specifies localization of CENP-F, MAD1 and MAD2 to kinetochores and is essential for mitosis."
      Liu S.-T., Hittle J.C., Jablonski S.A., Campbell M.S., Yoda K., Yen T.J.
      Nat. Cell Biol. 5:341-345(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    5. "Comprehensive analysis of the ICEN (Interphase Centromere Complex) components enriched in the CENP-A chromatin of human cells."
      Izuta H., Ikeno M., Suzuki N., Tomonaga T., Nozaki N., Obuse C., Kisu Y., Goshima N., Nomura F., Nomura N., Yoda K.
      Genes Cells 11:673-684(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    6. "The CENP-H-I complex is required for the efficient incorporation of newly synthesized CENP-A into centromeres."
      Okada M., Cheeseman I.M., Hori T., Okawa K., McLeod I.X., Yates J.R. III, Desai A., Fukagawa T.
      Nat. Cell Biol. 8:446-457(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH CENPH; CENPK; CENPN; CENPO; CENPP; CENPQ; CENPR AND CENPU, FUNCTION, SUBCELLULAR LOCATION.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE CENPA-CAD COMPLEX WITH CENPK; CENPL; CENPO; CENPP; CENPQ; CENPR AND CENPS.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "The SUMO protease SENP6 is essential for inner kinetochore assembly."
      Mukhopadhyay D., Arnaoutov A., Dasso M.
      J. Cell Biol. 188:681-692(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION, UBIQUITINATION BY RNF4, DESUMOYLATION BY SENP6, INTERACTION WITH SENP6.

    Entry informationi

    Entry nameiCENPI_HUMAN
    AccessioniPrimary (citable) accession number: Q92674
    Secondary accession number(s): Q5JWZ9, Q96ED0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 118 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3