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UniProtKB - Q9NQS7 (INCE_HUMAN)

Protein

Inner centromere protein

Gene

INCENP

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

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

GO - Biological processi

  • chromosome segregation Source: UniProtKB
  • mitotic cytokinesis Source: UniProtKB
  • mitotic sister chromatid segregation Source: InterPro
  • regulation of mitotic cytokinesis Source: InterPro
View the complete GO annotation on QuickGO ...

Keywordsi

Biological processCell cycle, Cell division, Chromosome partition, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000149503.12
HGNCiHGNC:6058 INCENP
MIMi604411 gene
neXtProtiNX_Q9NQS7

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
ProteomicsDBi82181
82182 [Q9NQS7-2]

PTM databases

iPTMnetiQ9NQS7
PhosphoSitePlusiQ9NQS7

Expressioni

Gene expression databases

BgeeiENSG00000149503 Expressed in 130 organ(s), highest expression level in cerebellum
CleanExiHS_INCENP
ExpressionAtlasiQ9NQS7 baseline and differential
GenevisibleiQ9NQS7 HS

Organism-specific databases

HPAiCAB013292
HPA051339
HPA070550

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

Protein-protein interaction databases

BioGridi109831, 26 interactors
ComplexPortaliCPX-116 Chromosomal passenger complex
CORUMiQ9NQS7
DIPiDIP-31304N
IntActiQ9NQS7, 19 interactors
MINTiQ9NQS7
STRINGi9606.ENSP00000378295

Chemistry databases

BindingDBiQ9NQS7

Structurei

Secondary structure

1918
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
OMAiRVDPKCS
OrthoDBiEOG091G0CPA
PhylomeDBiQ9NQS7
TreeFamiTF101172

Family and domain databases

InterProiView protein in InterPro
IPR039130 INCENP
IPR022006 INCENP_N
IPR005635 Inner_centromere_prot_ARK-bd
PANTHERiPTHR13142 PTHR13142, 1 hit
PfamiView protein in Pfam
PF03941 INCENP_ARK-bind, 1 hit
PF12178 INCENP_N, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PM67E9PM67_HUMAN
Inner centromere protein
INCENP
167Annotation score:

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 dbSNP:rs1792947Ensembl.1
Natural variantiVAR_047128100R → H. Corresponds to variant dbSNP:rs12281503Ensembl.1
Natural variantiVAR_047129137A → V. Corresponds to variant dbSNP:rs34441559Ensembl.1
Natural variantiVAR_047130506M → T. Corresponds to variant dbSNP:rs2277283Ensembl.1
Natural variantiVAR_047131644E → D3 PublicationsCorresponds to variant dbSNP:rs7129085Ensembl.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

Similar proteinsi

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[»]
5IEHX-ray1.50C47-55[»]
5IEKX-ray1.80C47-55[»]
ProteinModelPortaliQ9NQS7
SMRiQ9NQS7
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109831, 26 interactors
ComplexPortaliCPX-116 Chromosomal passenger complex
CORUMiQ9NQS7
DIPiDIP-31304N
IntActiQ9NQS7, 19 interactors
MINTiQ9NQS7
STRINGi9606.ENSP00000378295

Chemistry databases

BindingDBiQ9NQS7
ChEMBLiCHEMBL3430907

PTM databases

iPTMnetiQ9NQS7
PhosphoSitePlusiQ9NQS7

Polymorphism and mutation databases

BioMutaiINCENP
DMDMi212276501

Proteomic databases

EPDiQ9NQS7
MaxQBiQ9NQS7
PaxDbiQ9NQS7
PeptideAtlasiQ9NQS7
PRIDEiQ9NQS7
ProteomicsDBi82181
82182 [Q9NQS7-2]

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
EuPathDBiHostDB:ENSG00000149503.12
GeneCardsiINCENP
H-InvDBiHIX0009706
HGNCiHGNC:6058 INCENP
HPAiCAB013292
HPA051339
HPA070550
MIMi604411 gene
neXtProtiNX_Q9NQS7
OpenTargetsiENSG00000149503
PharmGKBiPA29868
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiR-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-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
PROiPR:Q9NQS7
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000149503 Expressed in 130 organ(s), highest expression level in cerebellum
CleanExiHS_INCENP
ExpressionAtlasiQ9NQS7 baseline and differential
GenevisibleiQ9NQS7 HS

Family and domain databases

InterProiView protein in InterPro
IPR039130 INCENP
IPR022006 INCENP_N
IPR005635 Inner_centromere_prot_ARK-bd
PANTHERiPTHR13142 PTHR13142, 1 hit
PfamiView protein in Pfam
PF03941 INCENP_ARK-bind, 1 hit
PF12178 INCENP_N, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiINCE_HUMAN
AccessioniPrimary (citable) accession number: Q9NQS7
Secondary accession number(s): A8MQD2, Q5Y192
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: November 4, 2008
Last modified: November 7, 2018
This is version 161 of the entry and version 3 of the sequence. See 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
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