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Protein

Inner centromere protein

Gene

INCENP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Probably acts through association with AURKB or AURKC. Seems to bind directly to microtubules. Controls the kinetochore localization of BUB1.3 Publications

GO - Biological processi

  • chromosome segregation Source: UniProtKB
  • cytokinesis Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • protein sumoylation Source: Reactome
  • sister chromatid cohesion Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
SIGNORiQ9NQS7.

Names & Taxonomyi

Protein namesi
Recommended name:
Inner centromere protein
Gene namesi
Name:INCENP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:6058. INCENP.

Subcellular locationi

GO - Cellular componenti

  • central element Source: Ensembl
  • chromocenter Source: Ensembl
  • chromosome, centromeric region Source: UniProtKB
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • kinetochore Source: UniProtKB
  • lateral element Source: Ensembl
  • microtubule Source: UniProtKB-KW
  • midbody Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • pericentric heterochromatin Source: UniProtKB
  • protein complex Source: UniProtKB
  • spindle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221F → R: Loss of binding to CDCA8 and BIRC5; when associated with R-34. 1 Publication
Mutagenesisi34 – 341L → R: Loss of binding to CDCA8 and BIRC5; when associated with R-22. 1 Publication
Mutagenesisi35 – 351E → R: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-36; R-39 and R-40. 1 Publication
Mutagenesisi36 – 361E → R: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-35; R-39 and R-40. 1 Publication
Mutagenesisi39 – 391E → R: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-35; R-36 and R-40. 1 Publication
Mutagenesisi40 – 401E → R: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-35; R-36 and R-39. 1 Publication
Mutagenesisi169 – 1691V → E: Abolishes interaction with CBX5. 1 Publication
Mutagenesisi171 – 1711I → E: Abolishes interaction with CBX5 and AURKB. 1 Publication

Organism-specific databases

PharmGKBiPA29868.

Polymorphism and mutation databases

BioMutaiINCENP.
DMDMi212276501.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 918918Inner centromere proteinPRO_0000084201Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei72 – 721PhosphoserineCombined sources
Modified residuei119 – 1191PhosphoserineCombined sources
Modified residuei143 – 1431PhosphoserineCombined sources
Modified residuei148 – 1481PhosphoserineCombined sources
Modified residuei150 – 1501PhosphothreonineBy similarity
Modified residuei195 – 1951Phosphothreonine1 Publication
Modified residuei197 – 1971PhosphoserineCombined sources
Modified residuei199 – 1991PhosphothreonineCombined sources
Modified residuei213 – 2131PhosphothreonineCombined sources
Modified residuei214 – 2141PhosphoserineCombined sources
Modified residuei219 – 2191PhosphothreonineBy similarity
Modified residuei239 – 2391PhosphothreonineCombined sources
Modified residuei263 – 2631PhosphoserineCombined sources
Modified residuei269 – 2691PhosphoserineCombined sources
Modified residuei275 – 2751PhosphoserineCombined sources
Modified residuei292 – 2921PhosphothreonineCombined sources
Modified residuei296 – 2961PhosphoserineCombined sources
Modified residuei306 – 3061PhosphoserineCombined sources
Modified residuei312 – 3121PhosphoserineCombined sources
Modified residuei314 – 3141PhosphoserineCombined sources
Modified residuei330 – 3301PhosphoserineCombined sources
Modified residuei400 – 4001PhosphoserineCombined sources
Modified residuei406 – 4061PhosphothreonineCombined sources
Modified residuei446 – 4461PhosphoserineCombined sources
Modified residuei476 – 4761PhosphoserineCombined sources
Modified residuei478 – 4781PhosphothreonineBy similarity
Modified residuei480 – 4801PhosphoserineBy similarity
Modified residuei510 – 5101PhosphoserineCombined sources
Modified residuei514 – 5141PhosphoserineCombined sources
Modified residuei828 – 8281PhosphoserineCombined sources
Modified residuei831 – 8311PhosphoserineCombined sources
Modified residuei832 – 8321PhosphothreonineCombined sources
Modified residuei892 – 8921Phosphothreonine; by AURKB1 Publication
Modified residuei893 – 8931Phosphoserine; by AURKB1 Publication
Modified residuei894 – 8941Phosphoserine; by AURKBCombined sources1 Publication
Modified residuei899 – 8991PhosphoserineCombined sources
Modified residuei914 – 9141PhosphoserineCombined sources

Post-translational modificationi

Phosphorylation by AURKB at its C-terminal part is important for AURKB activation by INCENP.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NQS7.
MaxQBiQ9NQS7.
PaxDbiQ9NQS7.
PeptideAtlasiQ9NQS7.
PRIDEiQ9NQS7.

PTM databases

iPTMnetiQ9NQS7.
PhosphoSiteiQ9NQS7.

Expressioni

Gene expression databases

BgeeiENSG00000149503.
CleanExiHS_INCENP.
ExpressionAtlasiQ9NQS7. baseline and differential.
GenevisibleiQ9NQS7. HS.

Organism-specific databases

HPAiCAB013292.
HPA054857.

Interactioni

Subunit structurei

Homodimer or heterodimer. Interacts with H2AFZ (By similarity). Interacts with CBX3. Interacts with tubulin beta chain. Interacts with AURKB and AURKC. Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB and AURKC. Interacts with EVI5. Interacts with CDCA8 and BIRC5; interaction is direct. Interacts with CBX5; POGZ and INCENP compete for interaction with CBX5. Interacts with POGZ. Interacts with JTB.By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AURKBQ96GD47EBI-307907,EBI-624291
BIRC5O1539210EBI-307907,EBI-518823
CBX5P459736EBI-307907,EBI-78219
CDCA8Q53HL24EBI-307907,EBI-979174

Protein-protein interaction databases

BioGridi109831. 24 interactions.
DIPiDIP-31304N.
IntActiQ9NQS7. 15 interactions.
MINTiMINT-1488062.
STRINGi9606.ENSP00000378295.

Chemistry

BindingDBiQ9NQS7.

Structurei

Secondary structure

1
918
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 103Combined sources
Helixi11 – 2818Combined sources
Helixi30 – 4516Combined sources
Helixi844 – 8463Combined sources
Helixi848 – 86013Combined sources
Helixi865 – 8695Combined sources
Turni878 – 8803Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QFAX-ray1.40C1-47[»]
4AF3X-ray2.75D835-903[»]
ProteinModelPortaliQ9NQS7.
SMRiQ9NQS7. Positions 3-47, 840-882.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NQS7.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili528 – 791264Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the INCENP family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4456. Eukaryota.
ENOG410XRQ9. LUCA.
GeneTreeiENSGT00730000111073.
HOGENOMiHOG000113069.
HOVERGENiHBG006157.
InParanoidiQ9NQS7.
KOiK11515.
OMAiARIICHS.
OrthoDBiEOG091G0CPA.
PhylomeDBiQ9NQS7.
TreeFamiTF101172.

Family and domain databases

InterProiIPR022006. INCENP_N.
IPR005635. Inner_centromere_prot_ARK-bd.
[Graphical view]
PfamiPF03941. INCENP_ARK-bind. 1 hit.
PF12178. INCENP_N. 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: Q9NQS7-1) [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
MGTTAPGPIH LLELCDQKLM EFLCNMDNKD LVWLEEIQEE AERMFTREFS
60 70 80 90 100
KEPELMPKTP SQKNRRKKRR ISYVQDENRD PIRRRLSRRK SRSSQLSSRR
110 120 130 140 150
LRSKDSVEKL ATVVGENGSV LRRVTRAAAA AAAATMALAA PSSPTPESPT
160 170 180 190 200
MLTKKPEDNH TQCQLVPVVE IGISERQNAE QHVTQLMSTE PLPRTLSPTP
210 220 230 240 250
ASATAPTSQG IPTSDEESTP KKSKARILES ITVSSLMATP QDPKGQGVGT
260 270 280 290 300
GRSASKLRIA QVSPGPRDSP AFPDSPWRER VLAPILPDNF STPTGSRTDS
310 320 330 340 350
QSVRHSPIAP SSPSPQVLAQ KYSLVAKQES VVRRASRRLA KKTAEEPAAS
360 370 380 390 400
GRIICHSYLE RLLNVEVPQK VGSEQKEPPE EAEPVAAAEP EVPENNGNNS
410 420 430 440 450
WPHNDTEIAN STPNPKPAAS SPETPSAGQQ EAKTDQADGP REPPQSARRK
460 470 480 490 500
RSYKQAVSEL DEEQHLEDEE LQPPRSKTPS SPCPASKVVR PLRTFLHTVQ
510 520 530 540 550
RNQMLMTPTS APRSVMKSFI KRNTPLRMDP KCSFVEKERQ RLENLRRKEE
560 570 580 590 600
AEQLRRQKVE EDKRRRLEEV KLKREERLRK VLQARERVEQ MKEEKKKQIE
610 620 630 640 650
QKFAQIDEKT EKAKEERLAE EKAKKKAAAK KMEEVEARRK QEEEARRLRW
660 670 680 690 700
LQQEEEERRH QELLQKKKEE EQERLRKAAE AKRLAEQREQ ERREQERREQ
710 720 730 740 750
ERREQERREQ ERREQERQLA EQERRREQER LQAERELQER EKALRLQKEQ
760 770 780 790 800
LQRELEEKKK KEEQQRLAER QLQEEQEKKA KEAAGASKAL NVTVDVQSPA
810 820 830 840 850
CTSYQMTPQG HRAPPKINPD NYGMDLNSDD STDDEAHPRK PIPTWARGTP
860 870 880 890 900
LSQAIIHQYY HPPNLLELFG TILPLDLEDI FKKSKPRYHK RTSSAVWNSP
910
PLQGARVPSS LAYSLKKH
Length:918
Mass (Da):105,429
Last modified:November 4, 2008 - v3
Checksum:i644D081DCC9035E8
GO
Isoform 2 (identifier: Q9NQS7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     532-535: Missing.

Show »
Length:914
Mass (Da):104,992
Checksum:i6E8C5E65A9C918E8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti715 – 7151Q → QERREQ in AAF87584 (PubMed:11453556).Curated
Sequence conflicti804 – 8063YQM → SPI in AAF87584 (PubMed:11453556).Curated
Sequence conflicti812 – 8121R → K in AAF87584 (PubMed:11453556).Curated
Sequence conflicti816 – 8161K → Q in AAF87584 (PubMed:11453556).Curated
Sequence conflicti820 – 8201D → H in AAF87584 (PubMed:11453556).Curated
Sequence conflicti861 – 8611H → Q in AAF87584 (PubMed:11453556).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21G → V.
Corresponds to variant rs1792947 [ dbSNP | Ensembl ].
VAR_047127
Natural varianti100 – 1001R → H.
Corresponds to variant rs12281503 [ dbSNP | Ensembl ].
VAR_047128
Natural varianti137 – 1371A → V.
Corresponds to variant rs34441559 [ dbSNP | Ensembl ].
VAR_047129
Natural varianti506 – 5061M → T.
Corresponds to variant rs2277283 [ dbSNP | Ensembl ].
VAR_047130
Natural varianti644 – 6441E → D.3 Publications
Corresponds to variant rs7129085 [ dbSNP | Ensembl ].
VAR_047131

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei532 – 5354Missing in isoform 2. 1 PublicationVSP_035651

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF282265 mRNA. Translation: AAF87584.1.
AY714053 mRNA. Translation: AAU04398.1.
AP002793 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74004.1.
BC098576 mRNA. Translation: AAH98576.1.
CCDSiCCDS31582.1. [Q9NQS7-2]
CCDS44624.1. [Q9NQS7-1]
RefSeqiNP_001035784.1. NM_001040694.1. [Q9NQS7-1]
NP_064623.2. NM_020238.2. [Q9NQS7-2]
UniGeneiHs.142179.

Genome annotation databases

EnsembliENST00000278849; ENSP00000278849; ENSG00000149503. [Q9NQS7-2]
ENST00000394818; ENSP00000378295; ENSG00000149503. [Q9NQS7-1]
GeneIDi3619.
KEGGihsa:3619.
UCSCiuc001nsw.2. human. [Q9NQS7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF282265 mRNA. Translation: AAF87584.1.
AY714053 mRNA. Translation: AAU04398.1.
AP002793 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74004.1.
BC098576 mRNA. Translation: AAH98576.1.
CCDSiCCDS31582.1. [Q9NQS7-2]
CCDS44624.1. [Q9NQS7-1]
RefSeqiNP_001035784.1. NM_001040694.1. [Q9NQS7-1]
NP_064623.2. NM_020238.2. [Q9NQS7-2]
UniGeneiHs.142179.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QFAX-ray1.40C1-47[»]
4AF3X-ray2.75D835-903[»]
ProteinModelPortaliQ9NQS7.
SMRiQ9NQS7. Positions 3-47, 840-882.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109831. 24 interactions.
DIPiDIP-31304N.
IntActiQ9NQS7. 15 interactions.
MINTiMINT-1488062.
STRINGi9606.ENSP00000378295.

Chemistry

BindingDBiQ9NQS7.

PTM databases

iPTMnetiQ9NQS7.
PhosphoSiteiQ9NQS7.

Polymorphism and mutation databases

BioMutaiINCENP.
DMDMi212276501.

Proteomic databases

EPDiQ9NQS7.
MaxQBiQ9NQS7.
PaxDbiQ9NQS7.
PeptideAtlasiQ9NQS7.
PRIDEiQ9NQS7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000278849; ENSP00000278849; ENSG00000149503. [Q9NQS7-2]
ENST00000394818; ENSP00000378295; ENSG00000149503. [Q9NQS7-1]
GeneIDi3619.
KEGGihsa:3619.
UCSCiuc001nsw.2. human. [Q9NQS7-1]

Organism-specific databases

CTDi3619.
GeneCardsiINCENP.
H-InvDBHIX0009706.
HGNCiHGNC:6058. INCENP.
HPAiCAB013292.
HPA054857.
MIMi604411. gene.
neXtProtiNX_Q9NQS7.
PharmGKBiPA29868.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4456. Eukaryota.
ENOG410XRQ9. LUCA.
GeneTreeiENSGT00730000111073.
HOGENOMiHOG000113069.
HOVERGENiHBG006157.
InParanoidiQ9NQS7.
KOiK11515.
OMAiARIICHS.
OrthoDBiEOG091G0CPA.
PhylomeDBiQ9NQS7.
TreeFamiTF101172.

Enzyme and pathway databases

ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
SIGNORiQ9NQS7.

Miscellaneous databases

EvolutionaryTraceiQ9NQS7.
GeneWikiiINCENP.
GenomeRNAii3619.
PROiQ9NQS7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000149503.
CleanExiHS_INCENP.
ExpressionAtlasiQ9NQS7. baseline and differential.
GenevisibleiQ9NQS7. HS.

Family and domain databases

InterProiIPR022006. INCENP_N.
IPR005635. Inner_centromere_prot_ARK-bd.
[Graphical view]
PfamiPF03941. INCENP_ARK-bind. 1 hit.
PF12178. INCENP_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiINCE_HUMAN
AccessioniPrimary (citable) accession number: Q9NQS7
Secondary accession number(s): A8MQD2, Q5Y192
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: November 4, 2008
Last modified: September 7, 2016
This is version 141 of the entry and version 3 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

Caution

PubMed:11139336 experiments have been carried out partly in chicken and partly in human.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.