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Q92674 (CENPI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CENPI
Synonyms:FSHPRH1, ICEN19, LRPR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length756 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.6

Subunit structure

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. Ref.6 Ref.7 Ref.9

Subcellular location

Nucleus. Chromosomecentromere. Note: Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex. Ref.4 Ref.6

Induction

By follicle-stimulating hormone (FSH).

Post-translational modification

Sumoylated. Sumoylated form can be polyubiquitinated by RNF4, leading to its degradation. Desumoylation by SENP6 prevents its degradation. Ref.9

Sequence similarities

Belongs to the mis6 family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92674-1)

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.
Isoform 2 (identifier: Q92674-2)

The sequence of this isoform differs from the canonical sequence as follows:
     523-756: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 756756Centromere protein I
PRO_0000087354

Natural variations

Alternative sequence523 – 756234Missing in isoform 2.
VSP_015797

Experimental info

Sequence conflict262 – 2632FK → LQ in CAA65884. Ref.1
Sequence conflict3891Y → H in CAA65884. Ref.1
Sequence conflict4321F → Y in CAA65884. Ref.1
Sequence conflict4501C → S in CAA65884. Ref.1
Sequence conflict5321S → C in CAA65884. Ref.1
Sequence conflict5761N → D in CAA65884. Ref.1
Sequence conflict6421H → Y in CAA65884. Ref.1
Sequence conflict6581G → A in CAA65884. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 11, 2005. Version 2.
Checksum: A3439CF1729D7A66

FASTA75686,720
        10         20         30         40         50         60 
MSPQKRVKNV QAQNRTSQGS SSFQTTLSAW KVKQDPSNSK NISKHGQNNP VGDYEHADDQ 

        70         80         90        100        110        120 
AEEDALQMAV GYFEKGPIKA SQNKDKTLEK HLKTVENVAW KNGLASEEID ILLNIALSGK 

       130        140        150        160        170        180 
FGNAVNTRIL KCMIPATVIS EDSVVKAVSW LCVGKCSGST KVLFYRWLVA MFDFIDRKEQ 

       190        200        210        220        230        240 
INLLYGFFFA SLQDDALCPY VCHLLYLLTK KENVKPFRVR KLLDLQAKMG MQPHLQALLS 

       250        260        270        280        290        300 
LYKFFAPALI SVSLPVRKKI YFKNSENLWK TALLAVKQRN RGPSPEPLKL MLGPANVRPL 

       310        320        330        340        350        360 
KRKWNSLSVI PVLNSSSYTK ECGKKEMSLS DCLNRSGSFP LEQLQSFPQL LQNIHCLELP 

       370        380        390        400        410        420 
SQMGSVLNNS LLLHYINCVR DEPVLLRFYY WLSQTLQEEC IWYKVNNYEH GKEFTNFLDT 

       430        440        450        460        470        480 
IIRAECFLQE GFYSCEAFLY KSLPLWDGLC CRSQFLQLVS WIPFSSFSEV KPLLFDHLAQ 

       490        500        510        520        530        540 
LFFTSTIYFK CSVLQSLKEL LQNWLLWLSM DIHMKPVTNS PLETTLGGSM NSVSKLIHYV 

       550        560        570        580        590        600 
GWLSTTAMRL ESNNTFLLHF ILDFYEKVCD IYINYNLPLV VLFPPGIFYS ALLSLDTSIL 

       610        620        630        640        650        660 
NQLCFIMHRY RKNLTAAKKN ELVQKTKSEF NFSSKTYQEF NHYLTSMVGC LWTSKPFGKG 

       670        680        690        700        710        720 
IYIDPEILEK TGVAEYKNSL NVVHHPSFLS YAVSFLLQES PEERTVNVSS IRGKKWSWYL 

       730        740        750 
DYLFSQGLQG LKLFIRSSVH HSSIPRAEGI NCNNQY 

« Hide

Isoform 2 [UniParc].

Checksum: BAB3AA874485BD51
Show »

FASTA52259,813

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The human CENP-A centromeric nucleosome-associated complex."
Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III, Cleveland D.W.
Nat. Cell Biol. 8:458-469(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X97249 mRNA. Translation: CAA65884.1.
AL109963 Genomic DNA. Translation: CAB72340.1.
AL109963 Genomic DNA. Translation: CAI42268.1.
BC012462 mRNA. Translation: AAH12462.1.
RefSeqNP_006724.2. NM_006733.2.
XP_005262168.1. XM_005262111.1.
UniGeneHs.348920.
Hs.737663.

3D structure databases

ProteinModelPortalQ92674.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108769. 11 interactions.
MINTMINT-4536309.
STRING9606.ENSP00000218507.

PTM databases

PhosphoSiteQ92674.

Polymorphism databases

DMDM77416860.

Proteomic databases

PaxDbQ92674.
PRIDEQ92674.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372926; ENSP00000362017; ENSG00000102384. [Q92674-2]
ENST00000372927; ENSP00000362018; ENSG00000102384. [Q92674-1]
ENST00000423383; ENSP00000399274; ENSG00000102384. [Q92674-1]
GeneID2491.
KEGGhsa:2491.
UCSCuc004egx.3. human. [Q92674-1]

Organism-specific databases

CTD2491.
GeneCardsGC0XP100353.
H-InvDBHIX0016922.
HGNCHGNC:3968. CENPI.
HPACAB012356.
MIM300065. gene.
neXtProtNX_Q92674.
PharmGKBPA28385.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG16022.
HOGENOMHOG000049199.
HOVERGENHBG080256.
InParanoidQ92674.
KOK11501.
OMALCPYVCH.
OrthoDBEOG70PBZG.
PhylomeDBQ92674.
TreeFamTF101137.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ92674.
BgeeQ92674.
CleanExHS_CENPI.
GenevestigatorQ92674.

Family and domain databases

InterProIPR012485. CENP-I.
[Graphical view]
PANTHERPTHR15408. PTHR15408. 1 hit.
PfamPF07778. CENP-I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCENPI.
GenomeRNAi2491.
NextBio9839.
PROQ92674.
SOURCESearch...

Entry information

Entry nameCENPI_HUMAN
AccessionPrimary (citable) accession number: Q92674
Secondary accession number(s): Q5JWZ9, Q96ED0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 11, 2005
Last modified: April 16, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM