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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. Probably acts through association with AURKB or AURKC. Seems to bind directly to microtubules. Controls the kinetochore localization of BUB1 (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, Mitosis

Enzyme and pathway databases

ReactomeiREACT_306375. Mitotic Prometaphase.
REACT_321346. Separation of Sister Chromatids.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_358264. RHO GTPases Activate Formins.

Names & Taxonomyi

Protein namesi
Recommended name:
Inner centromere protein
Gene namesi
Name:Incenp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1313288. Incenp.

Subcellular locationi

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 880880Inner centromere proteinPRO_0000084202Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei142 – 1421PhosphoserineBy similarity
Modified residuei147 – 1471PhosphoserineBy similarity
Modified residuei189 – 1891PhosphothreonineBy similarity
Modified residuei190 – 1901PhosphoserineBy similarity
Modified residuei215 – 2151Phosphothreonine1 Publication
Modified residuei218 – 2181Phosphoserine1 Publication
Modified residuei239 – 2391PhosphoserineBy similarity
Modified residuei245 – 2451PhosphoserineBy similarity
Modified residuei251 – 2511PhosphoserineBy similarity
Modified residuei270 – 2701PhosphothreonineBy similarity
Modified residuei284 – 2841PhosphoserineBy similarity
Modified residuei290 – 2901PhosphoserineBy similarity
Modified residuei376 – 3761PhosphoserineBy similarity
Modified residuei382 – 3821PhosphothreonineBy similarity
Modified residuei421 – 4211PhosphoserineBy similarity
Glycosylationi450 – 4501N-linked (GlcNAc...)1 Publication
Modified residuei488 – 4881PhosphoserineBy similarity
Modified residuei796 – 7961Phosphoserine1 Publication
Modified residuei799 – 7991Phosphoserine1 Publication
Modified residuei800 – 8001Phosphothreonine1 Publication
Modified residuei860 – 8601Phosphothreonine; by AURKBBy similarity
Modified residuei861 – 8611Phosphoserine; by AURKBBy similarity
Modified residuei862 – 8621Phosphoserine; by AURKBBy similarity
Modified residuei867 – 8671PhosphoserineBy similarity

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

MaxQBiQ9WU62.
PRIDEiQ9WU62.

PTM databases

PhosphoSiteiQ9WU62.

Expressioni

Gene expression databases

BgeeiQ9WU62.
CleanExiMM_INCENP.
GenevisibleiQ9WU62. MM.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ9WU62.
SMRiQ9WU62. Positions 3-47, 581-752, 808-850.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili506 – 759254Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the INCENP family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG327385.
GeneTreeiENSGT00730000111073.
HOGENOMiHOG000113069.
HOVERGENiHBG006157.
InParanoidiQ9WU62.
KOiK11515.
OMAiARIICHS.
OrthoDBiEOG71VSWZ.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti397 – 3971G → S in AAD32094 (PubMed:10087305).Curated
Sequence conflicti412 – 4121T → I in AAH52414 (PubMed:15489334).Curated
Sequence conflicti448 – 4481C → F in AAD32094 (PubMed:10087305).Curated
Sequence conflicti687 – 6871K → R in AAD32094 (PubMed:10087305).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei507 – 5104Missing in isoform 2. 2 PublicationsVSP_007233

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. Positions 3-47, 581-752, 808-850.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ9WU62.

Proteomic databases

MaxQBiQ9WU62.
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

eggNOGiNOG327385.
GeneTreeiENSGT00730000111073.
HOGENOMiHOG000113069.
HOVERGENiHBG006157.
InParanoidiQ9WU62.
KOiK11515.
OMAiARIICHS.
OrthoDBiEOG71VSWZ.
PhylomeDBiQ9WU62.
TreeFamiTF101172.

Enzyme and pathway databases

ReactomeiREACT_306375. Mitotic Prometaphase.
REACT_321346. Separation of Sister Chromatids.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_358264. RHO GTPases Activate Formins.

Miscellaneous databases

ChiTaRSiIncenp. mouse.
NextBioi289382.
PROiQ9WU62.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WU62.
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...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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].
  10. "Sialic acid-focused quantitative mouse serum glycoproteomics by multiple reaction monitoring assay."
    Kurogochi M., Matsushista T., Amano M., Furukawa J., Shinohara Y., Aoshima M., Nishimura S.
    Mol. Cell. Proteomics 9:2354-2368(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-450, IDENTIFICATION BY MASS SPECTROMETRY.

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: July 22, 2015
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

External Data

Dasty 3

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 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.