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Q9NQS7 (INCE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length918 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. Ref.2 Ref.8 Ref.13

Subunit structure

Homodimer or heterodimer. Interacts with H2AFZ By similarity. Interacts with CBX3. Interacts with tubulin beta chain. Interacts with AURKB and AURKC. Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB and AURKC. Interacts with EVI5. Interacts with CDCA8 and BIRC5; interaction is direct. Interacts with CBX5; POGZ and INCENP compete for interaction with CBX5. Interacts with POGZ. Interacts with JTB. Ref.2 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.20 Ref.22 Ref.24

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. Colocalizes with AURKB at mitotic chromosomes. Ref.1 Ref.2 Ref.8 Ref.13 Ref.22

Post-translational modification

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

Sequence similarities

Belongs to the INCENP family.

Caution

Ref.7 experiments have been carried out partly in chicken and partly in human.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Chromosome partition
Mitosis
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Kinetochore
Microtubule
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromosome segregation

Inferred from mutant phenotype PubMed 16239925. Source: UniProtKB

cytokinesis

Inferred from mutant phenotype PubMed 16239925. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

   Cellular_componentcentral element

Inferred from electronic annotation. Source: Ensembl

centromeric heterochromatin

Inferred from direct assay Ref.6. Source: UniProtKB

chromocenter

Inferred from electronic annotation. Source: Ensembl

chromosome, centromeric region

Inferred from direct assay PubMed 16239925. Source: UniProtKB

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

kinetochore

Inferred from direct assay Ref.13. Source: UniProtKB

lateral element

Inferred from electronic annotation. Source: Ensembl

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

midbody

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from direct assay PubMed 16239925. Source: UniProtKB

spindle

Inferred from direct assay Ref.6. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NQS7-1)

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.
Isoform 2 (identifier: Q9NQS7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     532-535: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 918918Inner centromere protein
PRO_0000084201

Regions

Coiled coil528 – 791264 Potential

Amino acid modifications

Modified residue1191Phosphoserine Ref.16 Ref.21
Modified residue1431Phosphoserine Ref.21
Modified residue1481Phosphoserine Ref.16
Modified residue1951Phosphothreonine Ref.2
Modified residue1971Phosphoserine Ref.19
Modified residue1991Phosphothreonine Ref.19
Modified residue2131Phosphothreonine Ref.19
Modified residue2141Phosphoserine Ref.19
Modified residue2391Phosphothreonine Ref.15 Ref.16 Ref.19 Ref.21
Modified residue2631Phosphoserine Ref.11 Ref.15 Ref.18 Ref.21 Ref.23
Modified residue2691Phosphoserine Ref.15
Modified residue2751Phosphoserine Ref.11 Ref.15 Ref.21
Modified residue2921Phosphothreonine Ref.16 Ref.21
Modified residue2961Phosphoserine Ref.16
Modified residue3061Phosphoserine Ref.15 Ref.16 Ref.19 Ref.23
Modified residue3121Phosphoserine Ref.16 Ref.21
Modified residue3141Phosphoserine Ref.16 Ref.19 Ref.21 Ref.23
Modified residue3301Phosphoserine Ref.21
Modified residue4001Phosphoserine Ref.15
Modified residue4061Phosphothreonine Ref.15
Modified residue4461Phosphoserine Ref.16
Modified residue4761Phosphoserine Ref.15
Modified residue5101Phosphoserine Ref.16
Modified residue5141Phosphoserine Ref.16
Modified residue8281Phosphoserine Ref.16 Ref.18 Ref.19 Ref.23
Modified residue8311Phosphoserine Ref.16 Ref.19
Modified residue8321Phosphothreonine Ref.16 Ref.19
Modified residue8921Phosphothreonine; by AURKB Ref.8
Modified residue8931Phosphoserine; by AURKB Ref.8
Modified residue8941Phosphoserine; by AURKB Ref.8 Ref.16
Modified residue8991Phosphoserine Ref.15 Ref.16 Ref.18 Ref.19 Ref.21
Modified residue9141Phosphoserine Ref.16

Natural variations

Alternative sequence532 – 5354Missing in isoform 2.
VSP_035651
Natural variant21G → V.
Corresponds to variant rs1792947 [ dbSNP | Ensembl ].
VAR_047127
Natural variant1001R → H.
Corresponds to variant rs12281503 [ dbSNP | Ensembl ].
VAR_047128
Natural variant1371A → V.
Corresponds to variant rs34441559 [ dbSNP | Ensembl ].
VAR_047129
Natural variant5061M → T.
Corresponds to variant rs2277283 [ dbSNP | Ensembl ].
VAR_047130
Natural variant6441E → D. Ref.1 Ref.2 Ref.5
Corresponds to variant rs7129085 [ dbSNP | Ensembl ].
VAR_047131

Experimental info

Mutagenesis221F → R: Loss of binding to CDCA8 and BIRC5; when associated with R-34. Ref.24
Mutagenesis341L → R: Loss of binding to CDCA8 and BIRC5; when associated with R-22. Ref.24
Mutagenesis351E → R: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-36; R-39 and R-40. Ref.24
Mutagenesis361E → R: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-35; R-39 and R-40. Ref.24
Mutagenesis391E → R: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-35; R-36 and R-40. Ref.24
Mutagenesis401E → R: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-35; R-36 and R-39. Ref.24
Mutagenesis1691V → E: Abolishes interaction with CBX5. Ref.20
Mutagenesis1711I → E: Abolishes interaction with CBX5 and AURKB. Ref.20
Sequence conflict7151Q → QERREQ in AAF87584. Ref.1
Sequence conflict804 – 8063YQM → SPI in AAF87584. Ref.1
Sequence conflict8121R → K in AAF87584. Ref.1
Sequence conflict8161K → Q in AAF87584. Ref.1
Sequence conflict8201D → H in AAF87584. Ref.1
Sequence conflict8611H → Q in AAF87584. Ref.1

Secondary structure

.............. 918
Helix Strand Turn

Details...

Sequences

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

Last modified November 4, 2008. Version 3.
Checksum: 644D081DCC9035E8

FASTA918105,429
        10         20         30         40         50         60 
MGTTAPGPIH LLELCDQKLM EFLCNMDNKD LVWLEEIQEE AERMFTREFS KEPELMPKTP 

        70         80         90        100        110        120 
SQKNRRKKRR ISYVQDENRD PIRRRLSRRK SRSSQLSSRR LRSKDSVEKL ATVVGENGSV 

       130        140        150        160        170        180 
LRRVTRAAAA AAAATMALAA PSSPTPESPT MLTKKPEDNH TQCQLVPVVE IGISERQNAE 

       190        200        210        220        230        240 
QHVTQLMSTE PLPRTLSPTP ASATAPTSQG IPTSDEESTP KKSKARILES ITVSSLMATP 

       250        260        270        280        290        300 
QDPKGQGVGT GRSASKLRIA QVSPGPRDSP AFPDSPWRER VLAPILPDNF STPTGSRTDS 

       310        320        330        340        350        360 
QSVRHSPIAP SSPSPQVLAQ KYSLVAKQES VVRRASRRLA KKTAEEPAAS GRIICHSYLE 

       370        380        390        400        410        420 
RLLNVEVPQK VGSEQKEPPE EAEPVAAAEP EVPENNGNNS WPHNDTEIAN STPNPKPAAS 

       430        440        450        460        470        480 
SPETPSAGQQ EAKTDQADGP REPPQSARRK RSYKQAVSEL DEEQHLEDEE LQPPRSKTPS 

       490        500        510        520        530        540 
SPCPASKVVR PLRTFLHTVQ RNQMLMTPTS APRSVMKSFI KRNTPLRMDP KCSFVEKERQ 

       550        560        570        580        590        600 
RLENLRRKEE AEQLRRQKVE EDKRRRLEEV KLKREERLRK VLQARERVEQ MKEEKKKQIE 

       610        620        630        640        650        660 
QKFAQIDEKT EKAKEERLAE EKAKKKAAAK KMEEVEARRK QEEEARRLRW LQQEEEERRH 

       670        680        690        700        710        720 
QELLQKKKEE EQERLRKAAE AKRLAEQREQ ERREQERREQ ERREQERREQ ERREQERQLA 

       730        740        750        760        770        780 
EQERRREQER LQAERELQER EKALRLQKEQ LQRELEEKKK KEEQQRLAER QLQEEQEKKA 

       790        800        810        820        830        840 
KEAAGASKAL NVTVDVQSPA CTSYQMTPQG HRAPPKINPD NYGMDLNSDD STDDEAHPRK 

       850        860        870        880        890        900 
PIPTWARGTP LSQAIIHQYY HPPNLLELFG TILPLDLEDI FKKSKPRYHK RTSSAVWNSP 

       910 
PLQGARVPSS LAYSLKKH 

« Hide

Isoform 2 [UniParc].

Checksum: 6E8C5E65A9C918E8
Show »

FASTA914104,992

References

« Hide 'large scale' references
[1]"Human INCENP colocalizes with the Aurora-B/AIRK2 kinase on chromosomes and is overexpressed in tumour cells."
Adams R.R., Eckley D.M., Vagnarelli P., Wheatley S.P., Gerloff D.L., Mackay A.M., Svingen P.A., Kaufmann S.H., Earnshaw W.C.
Chromosoma 110:65-74(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, VARIANT ASP-644.
Tissue: Cervix carcinoma.
[2]"Direct association with inner centromere protein (INCENP) activates the novel chromosomal passenger protein, Aurora-C."
Li X., Sakashita G., Matsuzaki H., Sugimoto K., Kimura K., Hanaoka F., Taniguchi H., Furukawa K., Urano T.
J. Biol. Chem. 279:47201-47211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH AURKB AND AURKC, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-195, VARIANT ASP-644.
Tissue: Testis.
[3]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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 1), VARIANT ASP-644.
Tissue: Lung.
[6]"INCENP centromere and spindle targeting: identification of essential conserved motifs and involvement of heterochromatin protein HP1."
Ainsztein A.M., Kandels-Lewis S.E., Mackay A.M., Earnshaw W.C.
J. Cell Biol. 143:1763-1774(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBX3.
[7]"INCENP binds directly to tubulin and requires dynamic microtubules to target to the cleavage furrow."
Wheatley S.P., Kandels-Lewis S.E., Adams R.R., Ainsztein A.M., Earnshaw W.C.
Exp. Cell Res. 262:122-127(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TUBULIN BETA CHAIN.
[8]"Exploring the functional interactions between Aurora B, INCENP, and survivin in mitosis."
Honda R., Korner R., Nigg E.A.
Mol. Biol. Cell 14:3325-3341(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CPC COMPLEX, FUNCTION OF THE CPC COMPLEX, INDUCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-892; SER-893 AND SER-894.
[9]"Aurora-B phosphorylation in vitro identifies a residue of survivin that is essential for its localization and binding to inner centromere protein (INCENP) in vivo."
Wheatley S.P., Henzing A.J., Dodson H., Khaled W., Earnshaw W.C.
J. Biol. Chem. 279:5655-5660(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BIRC5.
[10]"Borealin: a novel chromosomal passenger required for stability of the bipolar mitotic spindle."
Gassmann R., Carvalho A., Henzing A.J., Ruchaud S., Hudson D.F., Honda R., Nigg E.A., Gerloff D.L., Earnshaw W.C.
J. Cell Biol. 166:179-191(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDCA8.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"EVI5 protein associates with the INCENP-aurora B kinase-survivin chromosomal passenger complex and is involved in the completion of cytokinesis."
Faitar S.L., Sossey-Alaoui K., Ranalli T.A., Cowell J.K.
Exp. Cell Res. 312:2325-2335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EVI5.
[13]"Phosphorylation- and polo-box-dependent binding of Plk1 to Bub1 is required for the kinetochore localization of Plk1."
Qi W., Tang Z., Yu H.
Mol. Biol. Cell 17:3705-3716(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-239; SER-263; SER-269; SER-275; SER-306; SER-400; THR-406; SER-476 AND SER-899, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-148; THR-239; THR-292; SER-296; SER-306; SER-312; SER-314; SER-446; SER-510; SER-514; SER-828; SER-831; THR-832; SER-894; SER-899 AND SER-914, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-828 AND SER-899, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; THR-199; THR-213; SER-214; THR-239; SER-306; SER-314; SER-828; SER-831; THR-832 AND SER-899, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms through Aurora B activation."
Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N., Kimura H., Obuse C.
Nat. Cell Biol. 12:719-727(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBX5; POGZ AND AURKB, MUTAGENESIS OF VAL-169 AND ILE-171.
[21]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-143; THR-239; SER-263; SER-275; THR-292; SER-312; SER-314; SER-330 AND SER-899, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"PAR, a protein involved in the cell cycle, is functionally related to chromosomal passenger proteins."
Platica M., Ionescu A., Ivan E., Holland J.F., Mandeli J., Platica O.
Int. J. Oncol. 38:777-785(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH JTB.
[23]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-306; SER-314 AND SER-828, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Structure of a Survivin-Borealin-INCENP core complex reveals how chromosomal passengers travel together."
Jeyaprakash A.A., Klein U.R., Lindner D., Ebert J., Nigg E.A., Conti E.
Cell 131:271-285(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 3-46, INTERACTION WITH CDCA8 AND BIRC5, MUTAGENESIS OF PHE-22; LEU-34; GLU-35; GLU-36; GLU-39 AND GLU-40.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001035784.1. NM_001040694.1.
NP_064623.2. NM_020238.2.
UniGeneHs.142179.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QFAX-ray1.40C1-47[»]
4AF3X-ray2.75D835-903[»]
ProteinModelPortalQ9NQS7.
SMRQ9NQS7. Positions 3-47, 840-882.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109831. 17 interactions.
DIPDIP-31304N.
IntActQ9NQS7. 10 interactions.
MINTMINT-1488062.
STRING9606.ENSP00000378295.

Chemistry

BindingDBQ9NQS7.

PTM databases

PhosphoSiteQ9NQS7.

Polymorphism databases

DMDM212276501.

Proteomic databases

PaxDbQ9NQS7.
PRIDEQ9NQS7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000278849; ENSP00000278849; ENSG00000149503. [Q9NQS7-2]
ENST00000394818; ENSP00000378295; ENSG00000149503. [Q9NQS7-1]
GeneID3619.
KEGGhsa:3619.
UCSCuc001nsw.1. human. [Q9NQS7-1]
uc001nsx.1. human. [Q9NQS7-2]

Organism-specific databases

CTD3619.
GeneCardsGC11P061891.
H-InvDBHIX0009706.
HGNCHGNC:6058. INCENP.
HPACAB013292.
HPA054857.
MIM604411. gene.
neXtProtNX_Q9NQS7.
PharmGKBPA29868.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327385.
HOGENOMHOG000113069.
HOVERGENHBG006157.
InParanoidQ9NQS7.
KOK11515.
OMALCDQKLM.
OrthoDBEOG71VSWZ.
PhylomeDBQ9NQS7.
TreeFamTF101172.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ9NQS7.
BgeeQ9NQS7.
CleanExHS_INCENP.
GenevestigatorQ9NQS7.

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

EvolutionaryTraceQ9NQS7.
GeneWikiINCENP.
GenomeRNAi3619.
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Entry information

Entry nameINCE_HUMAN
AccessionPrimary (citable) accession number: Q9NQS7
Secondary accession number(s): A8MQD2, Q5Y192
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: November 4, 2008
Last modified: April 16, 2014
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM