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Protein

Inner centromere protein

Gene

Incenp

Organism
Mus musculus (Mouse)
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. 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. Controls the kinetochore localization of BUB1.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, Mitosis

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Inner centromere protein
Gene namesi
Name:Incenp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1313288. Incenp.

Subcellular locationi

  • Chromosomecentromere 1 Publication
  • Cytoplasmcytoskeletonspindle 1 Publication
  • Nucleus 1 Publication
  • Chromosomecentromerekinetochore 1 Publication
  • Midbody By similarity

  • Note: Localizes to inner kinetochore. Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. Colocalizes to the equatorial cell cortex at anaphase (By similarity). Localized at synaptonemal complex central element from zygotene up to late pachytene when it begins to relocalize to heterochromatic chromocenters (PubMed:12584241). Colocalizes with AURKB at a connecting strand traversing the centromere region and joining sister kinetochores, in metaphase II centromeres. This strand disappears at the metaphase II/anaphase II transition and relocalizes to the spindle midzone (PubMed:12584241).By similarity1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000842021 – 880Inner centromere proteinAdd BLAST880

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei72PhosphoserineBy similarity1
Modified residuei142PhosphoserineBy similarity1
Modified residuei147PhosphoserineBy similarity1
Modified residuei149PhosphothreonineCombined sources1
Modified residuei189PhosphothreonineBy similarity1
Modified residuei190PhosphoserineCombined sources1
Modified residuei195PhosphothreonineCombined sources1
Modified residuei215PhosphothreonineCombined sources1
Modified residuei218PhosphoserineCombined sources1
Modified residuei239PhosphoserineCombined sources1
Modified residuei245PhosphoserineCombined sources1
Modified residuei248PhosphoserineCombined sources1
Modified residuei251PhosphoserineCombined sources1
Modified residuei259PhosphoserineCombined sources1
Modified residuei270PhosphothreonineBy similarity1
Modified residuei284PhosphoserineCombined sources1
Modified residuei290PhosphoserineBy similarity1
Modified residuei376PhosphoserineBy similarity1
Modified residuei382PhosphothreonineBy similarity1
Modified residuei421PhosphoserineBy similarity1
Glycosylationi450N-linked (GlcNAc...)1 Publication1
Modified residuei452PhosphothreonineCombined sources1
Modified residuei454PhosphoserineCombined sources1
Modified residuei488PhosphoserineBy similarity1
Modified residuei796PhosphoserineCombined sources1
Modified residuei799PhosphoserineCombined sources1
Modified residuei800PhosphothreonineCombined sources1
Modified residuei860Phosphothreonine; by AURKBBy similarity1
Modified residuei861PhosphoserineCombined sources1
Modified residuei862PhosphoserineCombined sources1
Modified residuei867PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylation by AURKB at its C-terminal part is important for AURKB activation by INCENP.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9WU62.
PeptideAtlasiQ9WU62.
PRIDEiQ9WU62.

PTM databases

iPTMnetiQ9WU62.
PhosphoSitePlusiQ9WU62.

Expressioni

Gene expression databases

BgeeiENSMUSG00000024660.
CleanExiMM_INCENP.
GenevisibleiQ9WU62. MM.

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. The reported homodimerization is questioned as the SAH domain is shown to be monomeric. Interacts with H2AFZ. Interacts with CBX1 and CBX3. Interacts with tubulin beta chain. Interacts with EVI5. Interacts with CBX5; POGZ and INCENP compete for interaction with CBX5. Interacts with POGZ. Interacts with JTB.By similarity1 Publication

Protein-protein interaction databases

BioGridi200760. 6 interactors.
DIPiDIP-56678N.
IntActiQ9WU62. 8 interactors.
STRINGi10090.ENSMUSP00000025562.

Structurei

3D structure databases

ProteinModelPortaliQ9WU62.
SMRiQ9WU62.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni506 – 733SAHBy similarityAdd BLAST228
Regioni794 – 868IN boxCuratedAdd BLAST75

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili506 – 759Sequence analysisAdd BLAST254

Domaini

The IN box mediates interaction with AURKB and AURKC.By similarity
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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4456. Eukaryota.
ENOG410XRQ9. LUCA.
GeneTreeiENSGT00730000111073.
HOGENOMiHOG000113069.
HOVERGENiHBG006157.
InParanoidiQ9WU62.
KOiK11515.
OMAiARIICHS.
OrthoDBiEOG091G0CPA.
PhylomeDBiQ9WU62.
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: Q9WU62-1) [UniParc]FASTAAdd to basket
Also known as: B

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
MGTTAPGPIC LLDLCDQKLL DFVCNVDNKD FMWLKEIEEE AERMFIREFS
60 70 80 90 100
NEPELMPKTP SQKNRRKKRR VSNIQDENRD PVRKRLSRRK SRSSQVGTRH
110 120 130 140 150
LRSKPVTIVE ENGFPVLQRI TRATAAAAAA AAAASVASAS SSSTAGSPTV
160 170 180 190 200
LTKKAVVEIS TSERLSAELQ LTKLKGSLPP SPVSQGTLTS EEELTPKKSE
210 220 230 240 250
AGKLDSVTVN SLKATPQSPK NRGVGEGRSV SKLKIARASW GLQDSPGSTD
260 270 280 290 300
SPWQERVLSP ILLNNILPTT AKSPLGNIRS VRRSLISQDS QVPLASKYNL
310 320 330 340 350
VAKQENGSRR SSRRIAKKAG KEPEASARII CHSYLERLLN VEVPQNVGLE
360 370 380 390 400
QEPVEVAEPE EAEEEQEVSK NSGCPSKPRS ATKIAISTPT SKPAAAGQTT
410 420 430 440 450
TVEEQEAELD QTDGHREPPQ SVRRKRSYKQ AISEPDEEQL EDEELQPCQN
460 470 480 490 500
KTPSPPCPAN KVVRPLRTFL HTVQKNQMLM TPTLASRSSV MKSFIKRNTP
510 520 530 540 550
LRVDPKCSFV EKERQRLESL RRKEEAEQRR RQKVEEDKRR RLEEVKLKRE
560 570 580 590 600
ERLRKVLQAR ERVEQMKEEK KKQIEQKFAQ IDEKTEKAKE ERLAEKAKKK
610 620 630 640 650
ATAKKMEEVE ARRKQEEEAR RLRWLQQEEE ERRHQEMLQR KKEEEQERRK
660 670 680 690 700
AAEARRLAEQ REQERRREQE RREQERREQE RREQERKEQE RREQEQERLR
710 720 730 740 750
AKREMQEREK ALRLQKERLQ KELEEKKRKE EQQRLAEQQL QEEQAKKAKE
760 770 780 790 800
VAAARKVLNM TVDVQSPVCT SYQMTPQGPK SIPKISVDDY GMDLNSDDST
810 820 830 840 850
DDESHPRKPI PSWAKGTQLS QAIVHQYYHP PNILELFGSI LPLDLEDIFK
860 870 880
KRKTRYHKRT SSAVWNSPPL KATMVPSSGD
Note: Major isoform in thymic lymphoma 3SB cells. Fourfold more abundant than isoform 2.
Length:880
Mass (Da):101,209
Last modified:April 23, 2003 - v2
Checksum:i92169889A921FEFC
GO
Isoform 2 (identifier: Q9WU62-2) [UniParc]FASTAAdd to basket
Also known as: A

The sequence of this isoform differs from the canonical sequence as follows:
     507-510: Missing.

Note: Minor isoform in thymic lymphoma 3SB cells.
Show »
Length:876
Mass (Da):100,772
Checksum:i836922856F05C81E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti397G → S in AAD32094 (PubMed:10087305).Curated1
Sequence conflicti412T → I in AAH52414 (PubMed:15489334).Curated1
Sequence conflicti448C → F in AAD32094 (PubMed:10087305).Curated1
Sequence conflicti687K → R in AAD32094 (PubMed:10087305).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_007233507 – 510Missing in isoform 2. 2 Publications4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF117610 mRNA. Translation: AAD32094.1.
AB100432 mRNA. Translation: BAC55879.1.
AB100433 mRNA. Translation: BAC55880.1.
AK081841 mRNA. Translation: BAC38346.1.
AK088627 mRNA. Translation: BAC40462.1.
BC037011 mRNA. Translation: AAH37011.1.
BC052414 mRNA. Translation: AAH52414.1.
CCDSiCCDS37912.1. [Q9WU62-2]
RefSeqiNP_057901.2. NM_016692.3. [Q9WU62-2]
XP_006526775.1. XM_006526712.1. [Q9WU62-1]
UniGeneiMm.29755.

Genome annotation databases

EnsembliENSMUST00000025562; ENSMUSP00000025562; ENSMUSG00000024660. [Q9WU62-2]
GeneIDi16319.
KEGGimmu:16319.
UCSCiuc008gor.2. mouse. [Q9WU62-1]
uc008gos.2. mouse. [Q9WU62-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF117610 mRNA. Translation: AAD32094.1.
AB100432 mRNA. Translation: BAC55879.1.
AB100433 mRNA. Translation: BAC55880.1.
AK081841 mRNA. Translation: BAC38346.1.
AK088627 mRNA. Translation: BAC40462.1.
BC037011 mRNA. Translation: AAH37011.1.
BC052414 mRNA. Translation: AAH52414.1.
CCDSiCCDS37912.1. [Q9WU62-2]
RefSeqiNP_057901.2. NM_016692.3. [Q9WU62-2]
XP_006526775.1. XM_006526712.1. [Q9WU62-1]
UniGeneiMm.29755.

3D structure databases

ProteinModelPortaliQ9WU62.
SMRiQ9WU62.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200760. 6 interactors.
DIPiDIP-56678N.
IntActiQ9WU62. 8 interactors.
STRINGi10090.ENSMUSP00000025562.

PTM databases

iPTMnetiQ9WU62.
PhosphoSitePlusiQ9WU62.

Proteomic databases

PaxDbiQ9WU62.
PeptideAtlasiQ9WU62.
PRIDEiQ9WU62.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025562; ENSMUSP00000025562; ENSMUSG00000024660. [Q9WU62-2]
GeneIDi16319.
KEGGimmu:16319.
UCSCiuc008gor.2. mouse. [Q9WU62-1]
uc008gos.2. mouse. [Q9WU62-2]

Organism-specific databases

CTDi3619.
MGIiMGI:1313288. Incenp.

Phylogenomic databases

eggNOGiKOG4456. Eukaryota.
ENOG410XRQ9. LUCA.
GeneTreeiENSGT00730000111073.
HOGENOMiHOG000113069.
HOVERGENiHBG006157.
InParanoidiQ9WU62.
KOiK11515.
OMAiARIICHS.
OrthoDBiEOG091G0CPA.
PhylomeDBiQ9WU62.
TreeFamiTF101172.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiIncenp. mouse.
PROiQ9WU62.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024660.
CleanExiMM_INCENP.
GenevisibleiQ9WU62. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: Q9WU62
Secondary accession number(s): Q7TN28, Q8BGN4, Q8CGI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: April 23, 2003
Last modified: November 30, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Originally predicted to contain a coiled coil domain but shown to contain a stable SAH domain instead.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.