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Protein

Centromere protein I

Gene

CENPI

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 - Biological processi

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_355252. RHO GTPases Activate Formins.
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 Componenti: 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

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • kinetochore Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28385.

Polymorphism and mutation databases

BioMutaiCENPI.
DMDMi77416860.

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

BgeeiQ92674.
CleanExiHS_CENPI.
ExpressionAtlasiQ92674. baseline and differential.
GenevisibleiQ92674. HS.

Organism-specific databases

HPAiCAB012356.
HPA061297.

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. 12 interactions.
MINTiMINT-4536309.
STRINGi9606.ENSP00000362018.

Structurei

3D structure databases

ProteinModelPortaliQ92674.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the mis6 family.Curated

Phylogenomic databases

eggNOGiNOG16022.
GeneTreeiENSGT00390000013235.
HOGENOMiHOG000049199.
HOVERGENiHBG080256.
InParanoidiQ92674.
KOiK11501.
OMAiYVCHLLY.
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. AlignAdd to basket

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

        10         20         30         40         50
MSPQKRVKNV QAQNRTSQGS SSFQTTLSAW KVKQDPSNSK NISKHGQNNP
60 70 80 90 100
VGDYEHADDQ AEEDALQMAV GYFEKGPIKA SQNKDKTLEK HLKTVENVAW
110 120 130 140 150
KNGLASEEID ILLNIALSGK FGNAVNTRIL KCMIPATVIS EDSVVKAVSW
160 170 180 190 200
LCVGKCSGST KVLFYRWLVA MFDFIDRKEQ INLLYGFFFA SLQDDALCPY
210 220 230 240 250
VCHLLYLLTK KENVKPFRVR KLLDLQAKMG MQPHLQALLS LYKFFAPALI
260 270 280 290 300
SVSLPVRKKI YFKNSENLWK TALLAVKQRN RGPSPEPLKL MLGPANVRPL
310 320 330 340 350
KRKWNSLSVI PVLNSSSYTK ECGKKEMSLS DCLNRSGSFP LEQLQSFPQL
360 370 380 390 400
LQNIHCLELP SQMGSVLNNS LLLHYINCVR DEPVLLRFYY WLSQTLQEEC
410 420 430 440 450
IWYKVNNYEH GKEFTNFLDT IIRAECFLQE GFYSCEAFLY KSLPLWDGLC
460 470 480 490 500
CRSQFLQLVS WIPFSSFSEV KPLLFDHLAQ LFFTSTIYFK CSVLQSLKEL
510 520 530 540 550
LQNWLLWLSM DIHMKPVTNS PLETTLGGSM NSVSKLIHYV GWLSTTAMRL
560 570 580 590 600
ESNNTFLLHF ILDFYEKVCD IYINYNLPLV VLFPPGIFYS ALLSLDTSIL
610 620 630 640 650
NQLCFIMHRY RKNLTAAKKN ELVQKTKSEF NFSSKTYQEF NHYLTSMVGC
660 670 680 690 700
LWTSKPFGKG IYIDPEILEK TGVAEYKNSL NVVHHPSFLS YAVSFLLQES
710 720 730 740 750
PEERTVNVSS IRGKKWSWYL DYLFSQGLQG LKLFIRSSVH HSSIPRAEGI

NCNNQY
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:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ92674.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108769. 12 interactions.
MINTiMINT-4536309.
STRINGi9606.ENSP00000362018.

PTM databases

PhosphoSiteiQ92674.

Polymorphism and mutation databases

BioMutaiCENPI.
DMDMi77416860.

Proteomic databases

MaxQBiQ92674.
PaxDbiQ92674.
PRIDEiQ92674.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi2491.
GeneCardsiGC0XP100353.
H-InvDBHIX0016922.
HGNCiHGNC:3968. CENPI.
HPAiCAB012356.
HPA061297.
MIMi300065. gene.
neXtProtiNX_Q92674.
PharmGKBiPA28385.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG16022.
GeneTreeiENSGT00390000013235.
HOGENOMiHOG000049199.
HOVERGENiHBG080256.
InParanoidiQ92674.
KOiK11501.
OMAiYVCHLLY.
OrthoDBiEOG70PBZG.
PhylomeDBiQ92674.
TreeFamiTF101137.

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_355252. RHO GTPases Activate Formins.
REACT_682. Mitotic Prometaphase.

Miscellaneous databases

GeneWikiiCENPI.
GenomeRNAii2491.
NextBioi9839.
PROiQ92674.
SOURCEiSearch...

Gene expression databases

BgeeiQ92674.
CleanExiHS_CENPI.
ExpressionAtlasiQ92674. baseline and differential.
GenevisibleiQ92674. HS.

Family and domain databases

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

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: June 24, 2015
This is version 125 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.