Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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. Acts as a scaffold regulating CPC localization and activity. The C-terminus associates with AURKB or AURKC, the N-terminus asssociated with BIRC5/survivin and CDCA8/borealin tethers the CPC to the inner centromere, and the microtubule binding activity within the central SAH domain directs AURKB/C toward substrates near microtubules (PubMed:15316025, PubMed:12925766, PubMed:27332895). The flexibility of the SAH domain is proposed to allow AURKB/C to follow substrates on dynamic microtubules while ensuring CPC docking to static chromatin (By similarity). Activates AURKB and AURKC (PubMed:27332895). Required for localization of CBX5 to mitotic centromeres (PubMed:21346195). Controls the kinetochore localization of BUB1 (PubMed:16760428).By similarity5 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

BioCyciZFISH:ENSG00000149503-MONOMER.
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)DescriptionActionsGraphical viewLength
Mutagenesisi22F → R: Loss of binding to CDCA8 and BIRC5; when associated with R-34. 1 Publication1
Mutagenesisi34L → R: Loss of binding to CDCA8 and BIRC5; when associated with R-22. 1 Publication1
Mutagenesisi35E → 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 Publication1
Mutagenesisi36E → 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 Publication1
Mutagenesisi39E → 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 Publication1
Mutagenesisi40E → 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 Publication1
Mutagenesisi167P → A: Decreases interaction with CBX5, abolishes localization to centromeres in interphase; when associated with A-169 and A-171. 1 Publication1
Mutagenesisi169V → A: Decreases interaction with CBX5, abolishes localization to centromeres in interphase; when associated with A-167 and A-171. 1 Publication1
Mutagenesisi169V → E: Abolishes interaction with CBX5. 1 Publication1
Mutagenesisi171I → A: Decreases interaction with CBX5, abolishes localization to centromeres in interphase; when associated with A-167 and A-169. 1 Publication1
Mutagenesisi171I → E: Abolishes interaction with CBX5 and AURKB. 1 Publication1

Organism-specific databases

DisGeNETi3619.
OpenTargetsiENSG00000149503.
PharmGKBiPA29868.

Chemistry databases

ChEMBLiCHEMBL3430907.

Polymorphism and mutation databases

BioMutaiINCENP.
DMDMi212276501.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000842011 – 918Inner centromere proteinAdd BLAST918

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei72PhosphoserineCombined sources1
Modified residuei119PhosphoserineCombined sources1
Modified residuei143PhosphoserineCombined sources1
Modified residuei148PhosphoserineCombined sources1
Modified residuei150PhosphothreonineBy similarity1
Modified residuei195Phosphothreonine1 Publication1
Modified residuei197PhosphoserineCombined sources1
Modified residuei199PhosphothreonineCombined sources1
Modified residuei213PhosphothreonineCombined sources1
Modified residuei214PhosphoserineCombined sources1
Modified residuei219PhosphothreonineBy similarity1
Modified residuei239PhosphothreonineCombined sources1
Modified residuei263PhosphoserineCombined sources1
Modified residuei269PhosphoserineCombined sources1
Modified residuei275PhosphoserineCombined sources1
Modified residuei292PhosphothreonineCombined sources1
Modified residuei296PhosphoserineCombined sources1
Modified residuei306PhosphoserineCombined sources1
Modified residuei312PhosphoserineCombined sources1
Modified residuei314PhosphoserineCombined sources1
Modified residuei330PhosphoserineCombined sources1
Modified residuei400PhosphoserineCombined sources1
Modified residuei406PhosphothreonineCombined sources1
Modified residuei446PhosphoserineCombined sources1
Modified residuei476PhosphoserineCombined sources1
Modified residuei478PhosphothreonineBy similarity1
Modified residuei480PhosphoserineBy similarity1
Modified residuei510PhosphoserineCombined sources1
Modified residuei514PhosphoserineCombined sources1
Modified residuei828PhosphoserineCombined sources1
Modified residuei831PhosphoserineCombined sources1
Modified residuei832PhosphothreonineCombined sources1
Modified residuei892Phosphothreonine; by AURKB and AURKC2 Publications1
Modified residuei893Phosphoserine; by AURKB and AURKC2 Publications1
Modified residuei894Phosphoserine; by AURKB and AURKCCombined sources2 Publications1
Modified residuei899PhosphoserineCombined sources1
Modified residuei914PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylation by AURKB or AURKC at its C-terminal part is important for AURKB or AURKC activation by INCENP.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NQS7.
MaxQBiQ9NQS7.
PaxDbiQ9NQS7.
PeptideAtlasiQ9NQS7.
PRIDEiQ9NQS7.

PTM databases

iPTMnetiQ9NQS7.
PhosphoSitePlusiQ9NQS7.

Expressioni

Gene expression databases

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

Organism-specific databases

HPAiCAB013292.
HPA054857.

Interactioni

Subunit structurei

Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; in the complex binds directly to AURKB or AURKC via the IN box, and forms a triple-helix bundle-based subcomplex with BIRC5 and CDCA8 via its N-terminus (PubMed:17956729, PubMed:27332895). The reported homodimerization is questioned as the SAH domain is shown to be monomeric (By similarity). Interacts with H2AFZ (By similarity). Interacts with CBX1 and CBX3. Interacts with tubulin beta chain. Interacts with EVI5. Interacts with CBX5; POGZ and INCENP compete for interaction with CBX5; regulates INCENP (and probably CPC) localization to centromeres in interphase and not required for proper mitotic progression or sister chromatid cohesion. Interacts with POGZ. Interacts with JTB.By similarity13 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 interactors.
DIPiDIP-31304N.
IntActiQ9NQS7. 15 interactors.
MINTiMINT-1488062.
STRINGi9606.ENSP00000378295.

Chemistry databases

BindingDBiQ9NQS7.

Structurei

Secondary structure

1918
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 10Combined sources3
Helixi11 – 28Combined sources18
Helixi30 – 45Combined sources16
Helixi844 – 846Combined sources3
Helixi848 – 860Combined sources13
Helixi865 – 869Combined sources5
Turni878 – 880Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9NQS7.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni124 – 248Interaction with CBX51 PublicationAdd BLAST125
Regioni531 – 765SAHBy similarityAdd BLAST235
Regioni822 – 897Interaction with AURKC1 PublicationAdd BLAST76
Regioni826 – 900IN boxCuratedAdd BLAST75

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi167 – 171PXVXL/I motif1 Publication5

Domaini

The IN box mediates interaction with AURKB and AURKC.By similarity1 Publication
The SAH (single alpha-helix) region is characterized by a high content of charged residues which are predicted to stabilize the alpha-helical structure by ionic bonds. It can refold after extension suggesting an in vivo force-dependent function. The isolated SAH domain is monomeric.By similarity

Sequence similaritiesi

Belongs to the INCENP family.Curated

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)DescriptionActionsGraphical viewLength
Sequence conflicti715Q → QERREQ in AAF87584 (PubMed:11453556).Curated1
Sequence conflicti804 – 806YQM → SPI in AAF87584 (PubMed:11453556).Curated3
Sequence conflicti812R → K in AAF87584 (PubMed:11453556).Curated1
Sequence conflicti816K → Q in AAF87584 (PubMed:11453556).Curated1
Sequence conflicti820D → H in AAF87584 (PubMed:11453556).Curated1
Sequence conflicti861H → Q in AAF87584 (PubMed:11453556).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0471272G → V.Corresponds to variant rs1792947dbSNPEnsembl.1
Natural variantiVAR_047128100R → H.Corresponds to variant rs12281503dbSNPEnsembl.1
Natural variantiVAR_047129137A → V.Corresponds to variant rs34441559dbSNPEnsembl.1
Natural variantiVAR_047130506M → T.Corresponds to variant rs2277283dbSNPEnsembl.1
Natural variantiVAR_047131644E → D.3 PublicationsCorresponds to variant rs7129085dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_035651532 – 535Missing in isoform 2. 1 Publication4

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QFAX-ray1.40C1-47[»]
4AF3X-ray2.75D835-903[»]
ProteinModelPortaliQ9NQS7.
SMRiQ9NQS7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiQ9NQS7.
ChEMBLiCHEMBL3430907.

PTM databases

iPTMnetiQ9NQS7.
PhosphoSitePlusiQ9NQS7.

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.
DisGeNETi3619.
GeneCardsiINCENP.
H-InvDBHIX0009706.
HGNCiHGNC:6058. INCENP.
HPAiCAB013292.
HPA054857.
MIMi604411. gene.
neXtProtiNX_Q9NQS7.
OpenTargetsiENSG00000149503.
PharmGKBiPA29868.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000149503-MONOMER.
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: November 30, 2016
This is version 144 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
Originally predicted to contain a coiled coil domain but shown to contain a stable SAH domain instead.By similarity

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.