Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9NQS7

- INCE_HUMAN

UniProt

Q9NQS7 - INCE_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Inner centromere protein

Gene

INCENP

Organism
Homo sapiens (Human)
Status
Reviewed - 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 BUB1.3 Publications

GO - Biological processi

  1. chromosome segregation Source: UniProtKB
  2. cytokinesis Source: UniProtKB
  3. mitotic cell cycle Source: Reactome
  4. mitotic nuclear division Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, Mitosis

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_682. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
Inner centromere protein
Gene namesi
Name:INCENP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:6058. INCENP.

Subcellular locationi

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.

GO - Cellular componenti

  1. central element Source: Ensembl
  2. chromocenter Source: Ensembl
  3. chromosome, centromeric region Source: UniProtKB
  4. cytosol Source: Reactome
  5. kinetochore Source: UniProtKB
  6. lateral element Source: Ensembl
  7. microtubule Source: UniProtKB-KW
  8. midbody Source: Ensembl
  9. pericentric heterochromatin Source: UniProtKB
  10. protein complex Source: UniProtKB
  11. spindle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221F → R: Loss of binding to CDCA8 and BIRC5; when associated with R-34. 1 Publication
Mutagenesisi34 – 341L → R: Loss of binding to CDCA8 and BIRC5; when associated with R-22. 1 Publication
Mutagenesisi35 – 351E → 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 Publication
Mutagenesisi36 – 361E → 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 Publication
Mutagenesisi39 – 391E → 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 Publication
Mutagenesisi40 – 401E → 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 Publication
Mutagenesisi169 – 1691V → E: Abolishes interaction with CBX5. 1 Publication
Mutagenesisi171 – 1711I → E: Abolishes interaction with CBX5 and AURKB. 1 Publication

Organism-specific databases

PharmGKBiPA29868.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 918918Inner centromere proteinPRO_0000084201Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei119 – 1191Phosphoserine2 Publications
Modified residuei143 – 1431Phosphoserine1 Publication
Modified residuei148 – 1481Phosphoserine1 Publication
Modified residuei195 – 1951Phosphothreonine1 Publication
Modified residuei197 – 1971Phosphoserine1 Publication
Modified residuei199 – 1991Phosphothreonine1 Publication
Modified residuei213 – 2131Phosphothreonine1 Publication
Modified residuei214 – 2141Phosphoserine1 Publication
Modified residuei239 – 2391Phosphothreonine4 Publications
Modified residuei263 – 2631Phosphoserine5 Publications
Modified residuei269 – 2691Phosphoserine1 Publication
Modified residuei275 – 2751Phosphoserine3 Publications
Modified residuei292 – 2921Phosphothreonine2 Publications
Modified residuei296 – 2961Phosphoserine1 Publication
Modified residuei306 – 3061Phosphoserine4 Publications
Modified residuei312 – 3121Phosphoserine2 Publications
Modified residuei314 – 3141Phosphoserine4 Publications
Modified residuei330 – 3301Phosphoserine1 Publication
Modified residuei400 – 4001Phosphoserine1 Publication
Modified residuei406 – 4061Phosphothreonine1 Publication
Modified residuei446 – 4461Phosphoserine1 Publication
Modified residuei476 – 4761Phosphoserine1 Publication
Modified residuei510 – 5101Phosphoserine1 Publication
Modified residuei514 – 5141Phosphoserine1 Publication
Modified residuei828 – 8281Phosphoserine4 Publications
Modified residuei831 – 8311Phosphoserine2 Publications
Modified residuei832 – 8321Phosphothreonine2 Publications
Modified residuei892 – 8921Phosphothreonine; by AURKB1 Publication
Modified residuei893 – 8931Phosphoserine; by AURKB1 Publication
Modified residuei894 – 8941Phosphoserine; by AURKB2 Publications
Modified residuei899 – 8991Phosphoserine5 Publications
Modified residuei914 – 9141Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation by AURKB at its C-terminal part is important for AURKB activation by INCENP.9 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NQS7.
PaxDbiQ9NQS7.
PRIDEiQ9NQS7.

PTM databases

PhosphoSiteiQ9NQS7.

Expressioni

Gene expression databases

BgeeiQ9NQS7.
CleanExiHS_INCENP.
ExpressionAtlasiQ9NQS7. baseline and differential.
GenevestigatoriQ9NQS7.

Organism-specific databases

HPAiCAB013292.
HPA054857.

Interactioni

Subunit structurei

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.By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AURKBQ96GD47EBI-307907,EBI-624291
BIRC5O1539210EBI-307907,EBI-518823
CBX5P459736EBI-307907,EBI-78219
CDCA8Q53HL24EBI-307907,EBI-979174

Protein-protein interaction databases

BioGridi109831. 17 interactions.
DIPiDIP-31304N.
IntActiQ9NQS7. 10 interactions.
MINTiMINT-1488062.
STRINGi9606.ENSP00000378295.

Structurei

Secondary structure

1
918
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 103
Helixi11 – 2818
Helixi30 – 4516
Helixi844 – 8463
Helixi848 – 86013
Helixi865 – 8695
Turni878 – 8803

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QFAX-ray1.40C1-47[»]
4AF3X-ray2.75D835-903[»]
ProteinModelPortaliQ9NQS7.
SMRiQ9NQS7. Positions 3-47, 840-882.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NQS7.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili528 – 791264Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the INCENP family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG327385.
GeneTreeiENSGT00730000111073.
HOGENOMiHOG000113069.
HOVERGENiHBG006157.
InParanoidiQ9NQS7.
KOiK11515.
OMAiLCDQKLM.
OrthoDBiEOG71VSWZ.
PhylomeDBiQ9NQS7.
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. Align

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti715 – 7151Q → QERREQ in AAF87584. (PubMed:11453556)Curated
Sequence conflicti804 – 8063YQM → SPI in AAF87584. (PubMed:11453556)Curated
Sequence conflicti812 – 8121R → K in AAF87584. (PubMed:11453556)Curated
Sequence conflicti816 – 8161K → Q in AAF87584. (PubMed:11453556)Curated
Sequence conflicti820 – 8201D → H in AAF87584. (PubMed:11453556)Curated
Sequence conflicti861 – 8611H → Q in AAF87584. (PubMed:11453556)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21G → V.
Corresponds to variant rs1792947 [ dbSNP | Ensembl ].
VAR_047127
Natural varianti100 – 1001R → H.
Corresponds to variant rs12281503 [ dbSNP | Ensembl ].
VAR_047128
Natural varianti137 – 1371A → V.
Corresponds to variant rs34441559 [ dbSNP | Ensembl ].
VAR_047129
Natural varianti506 – 5061M → T.
Corresponds to variant rs2277283 [ dbSNP | Ensembl ].
VAR_047130
Natural varianti644 – 6441E → D.3 Publications
Corresponds to variant rs7129085 [ dbSNP | Ensembl ].
VAR_047131

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei532 – 5354Missing in isoform 2. 1 PublicationVSP_035651

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.1. human. [Q9NQS7-1]
uc001nsx.1. human. [Q9NQS7-2]

Polymorphism databases

DMDMi212276501.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS31582.1. [Q9NQS7-2 ]
CCDS44624.1. [Q9NQS7-1 ]
RefSeqi NP_001035784.1. NM_001040694.1. [Q9NQS7-1 ]
NP_064623.2. NM_020238.2. [Q9NQS7-2 ]
UniGenei Hs.142179.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2QFA X-ray 1.40 C 1-47 [» ]
4AF3 X-ray 2.75 D 835-903 [» ]
ProteinModelPortali Q9NQS7.
SMRi Q9NQS7. Positions 3-47, 840-882.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109831. 17 interactions.
DIPi DIP-31304N.
IntActi Q9NQS7. 10 interactions.
MINTi MINT-1488062.
STRINGi 9606.ENSP00000378295.

Chemistry

BindingDBi Q9NQS7.

PTM databases

PhosphoSitei Q9NQS7.

Polymorphism databases

DMDMi 212276501.

Proteomic databases

MaxQBi Q9NQS7.
PaxDbi Q9NQS7.
PRIDEi Q9NQS7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000278849 ; ENSP00000278849 ; ENSG00000149503 . [Q9NQS7-2 ]
ENST00000394818 ; ENSP00000378295 ; ENSG00000149503 . [Q9NQS7-1 ]
GeneIDi 3619.
KEGGi hsa:3619.
UCSCi uc001nsw.1. human. [Q9NQS7-1 ]
uc001nsx.1. human. [Q9NQS7-2 ]

Organism-specific databases

CTDi 3619.
GeneCardsi GC11P061891.
H-InvDB HIX0009706.
HGNCi HGNC:6058. INCENP.
HPAi CAB013292.
HPA054857.
MIMi 604411. gene.
neXtProti NX_Q9NQS7.
PharmGKBi PA29868.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG327385.
GeneTreei ENSGT00730000111073.
HOGENOMi HOG000113069.
HOVERGENi HBG006157.
InParanoidi Q9NQS7.
KOi K11515.
OMAi LCDQKLM.
OrthoDBi EOG71VSWZ.
PhylomeDBi Q9NQS7.
TreeFami TF101172.

Enzyme and pathway databases

Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_682. Mitotic Prometaphase.

Miscellaneous databases

EvolutionaryTracei Q9NQS7.
GeneWikii INCENP.
GenomeRNAii 3619.
NextBioi 14153.
PROi Q9NQS7.
SOURCEi Search...

Gene expression databases

Bgeei Q9NQS7.
CleanExi HS_INCENP.
ExpressionAtlasi Q9NQS7. baseline and differential.
Genevestigatori Q9NQS7.

Family and domain databases

InterProi IPR022006. INCENP_N.
IPR005635. Inner_centromere_prot_ARK-bd.
[Graphical view ]
Pfami PF03941. INCENP_ARK-bind. 1 hit.
PF12178. INCENP_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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. 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. 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.

Entry informationi

Entry nameiINCE_HUMAN
AccessioniPrimary (citable) accession number: Q9NQS7
Secondary accession number(s): A8MQD2, Q5Y192
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: November 4, 2008
Last modified: October 29, 2014
This is version 123 of the entry and version 3 of the sequence. [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

Caution

PubMed:11139336 experiments have been carried out partly in chicken and partly in human.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3