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Q9WU62 (INCE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Inner centromere protein
Gene names
Name:Incenp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length880 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

Subunit structure

Homodimer or heterodimer By similarity. Interacts with CDCA8 and BIRC5; interaction is direct By similarity. Interacts with CBX3. Interacts with tubulin beta chain. Interacts with AURKB and AURKC. Component of the CPC at least composed of BIRC5/survivin, CDCA8/borealin, INCENP and AURKB/Aurora-B. Interacts with EVI5 By similarity. Interacts with H2AFZ By similarity. Interacts with H2AFZ. Interacts with CBX5; POGZ and INCENP compete for interaction with CBX5. Interacts with POGZ. Interacts with JTB By similarity. Ref.5

Subcellular location

Chromosomecentromere. Cytoplasmcytoskeletonspindle. Nucleus. Chromosomecentromerekinetochore. 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. Localized at synaptonemal complex central element from zygotene up to late pachytene when it begins to relocalize to heterochromatic chromocenters. 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. Ref.6

Post-translational modification

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

Sequence similarities

Belongs to the INCENP family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Chromosome partition
Mitosis
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Kinetochore
Microtubule
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromosome segregation

Inferred from sequence or structural similarity. Source: UniProtKB

cytokinesis

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentral element

Inferred from direct assay Ref.6. Source: MGI

centromeric heterochromatin

Inferred from sequence or structural similarity. Source: UniProtKB

chromocenter

Inferred from direct assay PubMed 19283064. Source: MGI

chromosome, centromeric region

Inferred from sequence or structural similarity. Source: UniProtKB

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

kinetochore

Inferred from sequence or structural similarity. Source: UniProtKB

lateral element

Inferred from direct assay PubMed 19283064. Source: MGI

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

midbody

Inferred from direct assay Ref.6. Source: MGI

protein complex

Inferred from sequence or structural similarity. Source: UniProtKB

spindle

Inferred from sequence or structural similarity. Source: UniProtKB

synaptonemal complex

Inferred from direct assay Ref.6. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9WU62-1)

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.
Note: Major isoform in thymic lymphoma 3SB cells. Fourfold more abundant than isoform 2.
Isoform 2 (identifier: Q9WU62-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 880880Inner centromere protein
PRO_0000084202

Regions

Coiled coil506 – 759254 Potential

Amino acid modifications

Modified residue1421Phosphoserine By similarity
Modified residue1471Phosphoserine By similarity
Modified residue1891Phosphothreonine By similarity
Modified residue1901Phosphoserine By similarity
Modified residue2151Phosphothreonine Ref.8
Modified residue2181Phosphoserine Ref.8
Modified residue2391Phosphoserine By similarity
Modified residue2451Phosphoserine By similarity
Modified residue2511Phosphoserine By similarity
Modified residue2701Phosphothreonine By similarity
Modified residue2841Phosphoserine By similarity
Modified residue2901Phosphoserine By similarity
Modified residue3761Phosphoserine By similarity
Modified residue3821Phosphothreonine By similarity
Modified residue4211Phosphoserine By similarity
Modified residue4881Phosphoserine By similarity
Modified residue7961Phosphoserine Ref.9
Modified residue7991Phosphoserine Ref.9
Modified residue8001Phosphothreonine Ref.9
Modified residue8601Phosphothreonine; by AURKB By similarity
Modified residue8611Phosphoserine; by AURKB By similarity
Modified residue8621Phosphoserine; by AURKB By similarity
Modified residue8671Phosphoserine By similarity

Natural variations

Alternative sequence507 – 5104Missing in isoform 2.
VSP_007233

Experimental info

Sequence conflict3971G → S in AAD32094. Ref.1
Sequence conflict4121T → I in AAH52414. Ref.4
Sequence conflict4481C → F in AAD32094. Ref.1
Sequence conflict6871K → R in AAD32094. Ref.1

Sequences

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

Last modified April 23, 2003. Version 2.
Checksum: 92169889A921FEFC

FASTA880101,209
        10         20         30         40         50         60 
MGTTAPGPIC LLDLCDQKLL DFVCNVDNKD FMWLKEIEEE AERMFIREFS NEPELMPKTP 

        70         80         90        100        110        120 
SQKNRRKKRR VSNIQDENRD PVRKRLSRRK SRSSQVGTRH LRSKPVTIVE ENGFPVLQRI 

       130        140        150        160        170        180 
TRATAAAAAA AAAASVASAS SSSTAGSPTV LTKKAVVEIS TSERLSAELQ LTKLKGSLPP 

       190        200        210        220        230        240 
SPVSQGTLTS EEELTPKKSE AGKLDSVTVN SLKATPQSPK NRGVGEGRSV SKLKIARASW 

       250        260        270        280        290        300 
GLQDSPGSTD SPWQERVLSP ILLNNILPTT AKSPLGNIRS VRRSLISQDS QVPLASKYNL 

       310        320        330        340        350        360 
VAKQENGSRR SSRRIAKKAG KEPEASARII CHSYLERLLN VEVPQNVGLE QEPVEVAEPE 

       370        380        390        400        410        420 
EAEEEQEVSK NSGCPSKPRS ATKIAISTPT SKPAAAGQTT TVEEQEAELD QTDGHREPPQ 

       430        440        450        460        470        480 
SVRRKRSYKQ AISEPDEEQL EDEELQPCQN KTPSPPCPAN KVVRPLRTFL HTVQKNQMLM 

       490        500        510        520        530        540 
TPTLASRSSV MKSFIKRNTP LRVDPKCSFV EKERQRLESL RRKEEAEQRR RQKVEEDKRR 

       550        560        570        580        590        600 
RLEEVKLKRE ERLRKVLQAR ERVEQMKEEK KKQIEQKFAQ IDEKTEKAKE ERLAEKAKKK 

       610        620        630        640        650        660 
ATAKKMEEVE ARRKQEEEAR RLRWLQQEEE ERRHQEMLQR KKEEEQERRK AAEARRLAEQ 

       670        680        690        700        710        720 
REQERRREQE RREQERREQE RREQERKEQE RREQEQERLR AKREMQEREK ALRLQKERLQ 

       730        740        750        760        770        780 
KELEEKKRKE EQQRLAEQQL QEEQAKKAKE VAAARKVLNM TVDVQSPVCT SYQMTPQGPK 

       790        800        810        820        830        840 
SIPKISVDDY GMDLNSDDST DDESHPRKPI PSWAKGTQLS QAIVHQYYHP PNILELFGSI 

       850        860        870        880 
LPLDLEDIFK KRKTRYHKRT SSAVWNSPPL KATMVPSSGD 

« Hide

Isoform 2 (A) [UniParc].

Checksum: 836922856F05C81E
Show »

FASTA876100,772

References

« Hide 'large scale' references
[1]"Cloning, expression, and promoter structure of a mammalian inner centromere protein (INCENP)."
Saffery R., Irvine D.V., Kile B.T., Hudson D.F., Cutts S.M., Choo K.H.
Mamm. Genome 10:415-418(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: 129.
[2]"Cloning of mouse inner centromere protein (INCENP) cDNAs."
Katayama H., Terada Y., Tatsuka M.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Thymus.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J and NOD.
Tissue: Head and Thymus.
[4]"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).
Strain: C57BL/6 and FVB/N.
[5]"Pericentric heterochromatin becomes enriched with H2A.Z during early mammalian development."
Rangasamy D., Berven L., Ridgway P., Tremethick D.J.
EMBO J. 22:1599-1607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH H2AFZ.
[6]"Dynamic relocalization of the chromosomal passenger complex proteins inner centromere protein (INCENP) and aurora-B kinase during male mouse meiosis."
Parra M.T., Viera A., Gomez R., Page J., Carmena M., Earnshaw W.C., Rufas J.S., Suja J.A.
J. Cell Sci. 116:961-974(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"Autophosphorylation of a newly identified site of Aurora-B is indispensable for cytokinesis."
Yasui Y., Urano T., Kawajiri A., Nagata K., Tatsuka M., Saya H., Furukawa K., Takahashi T., Izawa I., Inagaki M.
J. Biol. Chem. 279:12997-13003(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY AURKB.
[8]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-215 AND SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-796; SER-799 AND THR-800, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS37912.1. [Q9WU62-2]
RefSeqNP_057901.2. NM_016692.3. [Q9WU62-2]
XP_006526775.1. XM_006526712.1. [Q9WU62-1]
UniGeneMm.29755.

3D structure databases

ProteinModelPortalQ9WU62.
SMRQ9WU62. Positions 3-47, 581-752, 808-850.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200760. 6 interactions.
DIPDIP-56678N.
IntActQ9WU62. 8 interactions.

PTM databases

PhosphoSiteQ9WU62.

Proteomic databases

PRIDEQ9WU62.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025562; ENSMUSP00000025562; ENSMUSG00000024660. [Q9WU62-2]
GeneID16319.
KEGGmmu:16319.
UCSCuc008gor.2. mouse. [Q9WU62-1]
uc008gos.2. mouse. [Q9WU62-2]

Organism-specific databases

CTD3619.
MGIMGI:1313288. Incenp.

Phylogenomic databases

eggNOGNOG327385.
GeneTreeENSGT00730000111073.
HOGENOMHOG000113069.
HOVERGENHBG006157.
InParanoidQ9WU62.
KOK11515.
OMALCDQKLM.
OrthoDBEOG71VSWZ.
PhylomeDBQ9WU62.
TreeFamTF101172.

Gene expression databases

BgeeQ9WU62.
CleanExMM_INCENP.
GenevestigatorQ9WU62.

Family and domain databases

InterProIPR022006. INCENP_N.
IPR005635. Inner_centromere_prot_ARK-bd.
[Graphical view]
PfamPF03941. INCENP_ARK-bind. 1 hit.
PF12178. INCENP_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSINCENP. mouse.
NextBio289382.
PROQ9WU62.
SOURCESearch...

Entry information

Entry nameINCE_MOUSE
AccessionPrimary (citable) accession number: Q9WU62
Secondary accession number(s): Q7TN28, Q8BGN4, Q8CGI4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: April 23, 2003
Last modified: July 9, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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