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Q92674

- CENPI_HUMAN

UniProt

Q92674 - CENPI_HUMAN

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Protein

Centromere protein I

Gene
CENPI, FSHPRH1, ICEN19, LRPR1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. centromere-specific nucleosome assembly Source: Reactome
  2. mitotic cell cycle Source: Reactome
  3. nucleosome assembly Source: Reactome
  4. sex differentiation Source: ProtInc
Complete GO annotation...

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.2 Publications

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. kinetochore Source: UniProtKB
  3. nucleoplasm Source: Reactome
Complete GO annotation...

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.

Family & Domainsi

Sequence similaritiesi

Belongs to the mis6 family.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei523 – 756234Missing in isoform 2. VSP_015797Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti262 – 2632FK → LQ in CAA65884. 1 Publication
Sequence conflicti389 – 3891Y → H in CAA65884. 1 Publication
Sequence conflicti432 – 4321F → Y in CAA65884. 1 Publication
Sequence conflicti450 – 4501C → S in CAA65884. 1 Publication
Sequence conflicti532 – 5321S → C in CAA65884. 1 Publication
Sequence conflicti576 – 5761N → D in CAA65884. 1 Publication
Sequence conflicti642 – 6421H → Y in CAA65884. 1 Publication
Sequence conflicti658 – 6581G → A in CAA65884. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 117 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

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