Reviewed, UniProtKB/Swiss-Prot Q9NQS7 (INCE_HUMAN)

Names and origin

Protein names

Recommended name:
    Inner centromere protein

Gene names

Name:

INCENP

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	918 AA.
Sequence status	Complete.
Protein existence	Evidence 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
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 CPC at least composed of BIRC5/survivin, CDCA8/borealin, INCENP and AURKB/Aurora-B. Interacts with EVI5. Interacts with CDCA8 and BIRC5; interaction is direct. Ref.2 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.22
Subcellular location	Centromere. Cytoplasm › cytoskeleton › spindle. Nucleus. Kinetochore. 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.2 Ref.1
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 process	Cell cycle Cell division Chromosome partition Mitosis
Cellular component	Centromere Cytoplasm Cytoskeleton Kinetochore Microtubule Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	chromosome segregation Inferred from mutant phenotype. Source: UniProtKB cytokinesis Inferred from mutant phenotype. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	centromeric heterochromatin Ref.6 Inferred from direct assay. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW kinetochore Ref.12 Inferred from direct assay. Source: UniProtKB microtubule Inferred from electronic annotation. Source: UniProtKB-KW spindle Ref.6 Inferred from direct assay. Source: UniProtKB
Molecular function	protein binding Ref.6 Ref.8 Ref.22 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AURKB	Q96GD4	1	EBI-307907,EBI-624291
CBX5	P45973	1	EBI-307907,EBI-78219
CDC2	P06493	1	EBI-307907,EBI-444308

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 918

918

Inner centromere protein

PRO_0000084201

Regions

Coiled coil

528 – 791

264

Potential

Amino acid modifications

Modified residue

50

1

Phosphoserine Ref.15

Modified residue

72

1

Phosphoserine Ref.15 Ref.16 Ref.17

Modified residue

73

1

Phosphotyrosine Ref.15 Ref.17 Ref.13

Modified residue

91

1

Phosphoserine Ref.17

Modified residue

93

1

Phosphoserine Ref.17

Modified residue

94

1

Phosphoserine Ref.17

Modified residue

103

1

Phosphoserine Ref.17

Modified residue

106

1

Phosphoserine Ref.15

Modified residue

119

1

Phosphoserine Ref.15 Ref.13 Ref.18

Modified residue

142

1

Phosphoserine Ref.13

Modified residue

143

1

Phosphoserine Ref.17 Ref.13

Modified residue

145

1

Phosphothreonine Ref.18

Modified residue

148

1

Phosphoserine Ref.17 Ref.13 Ref.18

Modified residue

150

1

Phosphothreonine

Modified residue

195

1

Phosphothreonine Ref.15 Ref.19

Modified residue

197

1

Phosphoserine Ref.15 Ref.13 Ref.18 Ref.21

Modified residue

199

1

Phosphothreonine Ref.15 Ref.13 Ref.21

Modified residue

213

1

Phosphothreonine Ref.13 Ref.18 Ref.19 Ref.21

Modified residue

214

1

Phosphoserine Ref.15 Ref.17 Ref.13 Ref.19 Ref.21

Modified residue

218

1

Phosphoserine Ref.17 Ref.18 Ref.19

Modified residue

219

1

Phosphothreonine Ref.13 Ref.19

Modified residue

230

1

Phosphoserine Ref.15 Ref.13 Ref.18

Modified residue

235

1

Phosphoserine Ref.15

Modified residue

239

1

Phosphothreonine Ref.15 Ref.17 Ref.13 Ref.18 Ref.21

Modified residue

263

1

Phosphoserine Ref.15 Ref.16 Ref.17 Ref.13 Ref.18 Ref.19 Ref.21 Ref.10

Modified residue

269

1

Phosphoserine Ref.15 Ref.16 Ref.17 Ref.13 Ref.18 Ref.21 Ref.10

Modified residue

275

1

Phosphoserine Ref.15 Ref.16 Ref.17 Ref.13 Ref.18 Ref.21 Ref.10

Modified residue

291

1

Phosphoserine Ref.13

Modified residue

292

1

Phosphothreonine Ref.15 Ref.16 Ref.17 Ref.13 Ref.18 Ref.19 Ref.14

Modified residue

294

1

Phosphothreonine Ref.13

Modified residue

296

1

Phosphoserine Ref.16 Ref.17 Ref.13 Ref.18

Modified residue

298

1

Phosphothreonine Ref.18 Ref.10

Modified residue

306

1

Phosphoserine Ref.15 Ref.17 Ref.13 Ref.18 Ref.21

Modified residue

311

1

Phosphoserine

Modified residue

312

1

Phosphoserine Ref.17 Ref.13 Ref.18 Ref.10

Modified residue

314

1

Phosphoserine Ref.13 Ref.18 Ref.21 Ref.10

Modified residue

350

1

Phosphoserine Ref.15

Modified residue

373

1

Phosphoserine Ref.15

Modified residue

400

1

Phosphoserine Ref.17

Modified residue

406

1

Phosphothreonine Ref.17

Modified residue

411

1

Phosphoserine Ref.17

Modified residue

412

1

Phosphothreonine Ref.15

Modified residue

420

1

Phosphoserine Ref.15 Ref.17

Modified residue

421

1

Phosphoserine Ref.15 Ref.17 Ref.13 Ref.19 Ref.10

Modified residue

424

1

Phosphothreonine Ref.15 Ref.17 Ref.13 Ref.19

Modified residue

446

1

Phosphoserine Ref.15 Ref.17 Ref.18

Modified residue

458

1

Phosphoserine Ref.17

Modified residue

476

1

Phosphoserine Ref.17

Modified residue

478

1

Phosphothreonine Ref.17

Modified residue

480

1

Phosphoserine Ref.17

Modified residue

481

1

Phosphoserine Ref.15 Ref.17 Ref.13

Modified residue

507

1

Phosphothreonine Ref.15 Ref.18

Modified residue

509

1

Phosphothreonine Ref.15 Ref.18

Modified residue

510

1

Phosphoserine Ref.15 Ref.18

Modified residue

514

1

Phosphoserine Ref.18

Modified residue

793

1

Phosphothreonine Ref.15

Modified residue

798

1

Phosphoserine Ref.15

Modified residue

822

1

Phosphotyrosine Ref.21

Modified residue

828

1

Phosphoserine Ref.13 Ref.18 Ref.21

Modified residue

831

1

Phosphoserine Ref.13 Ref.18 Ref.21

Modified residue

832

1

Phosphothreonine Ref.13 Ref.18 Ref.21

Modified residue

892

1

Phosphothreonine Ref.13

Modified residue

893

1

Phosphoserine Ref.17 Ref.13 Ref.18

Modified residue

894

1

Phosphoserine Ref.17 Ref.13 Ref.18

Modified residue

899

1

Phosphoserine Ref.15 Ref.17 Ref.13 Ref.18 Ref.21

Modified residue

914

1

Phosphoserine Ref.18 Ref.21

Natural variations

Alternative sequence

532 – 535

4

Missing in isoform 2.

VSP_035651

Natural variant

2

1

G → V: dbSNP rs1792947.

VAR_047127

Natural variant

100

1

R → H: dbSNP rs12281503.

VAR_047128

Natural variant

137

1

A → V: dbSNP rs34441559.

VAR_047129

Natural variant

506

1

M → T: dbSNP rs2277283.

VAR_047130

Natural variant

644

1

E → D: dbSNP rs7129085. Ref.2 Ref.1 Ref.5

VAR_047131

Experimental info

Mutagenesis

22

1

F → R: Loss of binding to CDCA8 and BIRC5; when associated with R-34. Ref.22

Mutagenesis

34

1

L → R: Loss of binding to CDCA8 and BIRC5; when associated with R-22. Ref.22

Mutagenesis

35

1

E → 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.22

Mutagenesis

36

1

E → 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.22

Mutagenesis

39

1

E → 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.22

Mutagenesis

40

1

E → 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.22

Sequence conflict

715

1

Q → QERREQ in AAF87584. Ref.1

Sequence conflict

804 – 806

3

YQM → SPI in AAF87584. Ref.1

Sequence conflict

812

1

R → K in AAF87584. Ref.1

Sequence conflict

816

1

K → Q in AAF87584. Ref.1

Sequence conflict

820

1

D → H in AAF87584. Ref.1

Sequence conflict

861

1

H → Q in AAF87584. Ref.1

Secondary structure

1

.

.

.

.

.

.

918

Helix Strand Turn

Details...

Helix

8 – 10

3

Helix

11 – 28

18

Helix

30 – 45

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 4, 2008. Version 3. Checksum: 644D081DCC9035E8	FASTA	918	105,429
	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
	Isoform 2. Checksum: 6E8C5E65A9C918E8	FASTA	914	104,992
	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 KEKERQRLEN 550 560 570 580 590 600 LRRKEEAEQL RRQKVEEDKR RRLEEVKLKR EERLRKVLQA RERVEQMKEE KKKQIEQKFA 610 620 630 640 650 660 QIDEKTEKAK EERLAEEKAK KKAAAKKMEE VEARRKQEEE ARRLRWLQQE EEERRHQELL 670 680 690 700 710 720 QKKKEEEQER LRKAAEAKRL AEQREQERRE QERREQERRE QERREQERRE QERQLAEQER 730 740 750 760 770 780 RREQERLQAE RELQEREKAL RLQKEQLQRE LEEKKKKEEQ QRLAERQLQE EQEKKAKEAA 790 800 810 820 830 840 GASKALNVTV DVQSPACTSY QMTPQGHRAP PKINPDNYGM DLNSDDSTDD EAHPRKPIPT 850 860 870 880 890 900 WARGTPLSQA IIHQYYHPPN LLELFGTILP LDLEDIFKKS KPRYHKRTSS AVWNSPPLQG 910 ARVPSSLAYS LKKH

References

	« Hide 'large scale' referencesShow '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: 11453556] [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: 15316025] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH AURKB AND AURKC, SUBCELLULAR LOCATION, PHOSPHORYLATION, 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. , 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: 16554811] [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. , 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: 15489334] [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: 9864353] [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: 11139336] [Abstract] Cited for: INTERACTION WITH TUBULIN BETA CHAIN.
[8]	"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: 14610074] [Abstract] Cited for: INTERACTION WITH BIRC5.
[9]	"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: 15249581] [Abstract] Cited for: INTERACTION WITH CDCA8.
[10]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-269; SER-275; THR-298; SER-312; SER-314 AND SER-421, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"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: 16764853] [Abstract] Cited for: INTERACTION WITH EVI5.
[12]	"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: 16760428] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[13]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-73; SER-119; SER-142; SER-143; SER-148; SER-197; THR-199; THR-213; SER-214; THR-219; SER-230; THR-239; SER-263; SER-269; SER-275; SER-291; THR-292; THR-294; SER-296; SER-306; SER-312; SER-314; SER-421; THR-424; SER-481; SER-828; SER-831; THR-832; THR-892; SER-893; SER-894 AND SER-899, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-292, MASS SPECTROMETRY. Tissue: Epithelium.
[15]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-72; TYR-73; SER-106; SER-119; THR-195; SER-197; THR-199; SER-214; SER-230; SER-235; THR-239; SER-263; SER-269; SER-275; THR-292; SER-306; SER-350; SER-373; THR-412; SER-420; SER-421; THR-424; SER-446; SER-481; THR-507; THR-509; SER-510; THR-793; SER-798 AND SER-899, MASS SPECTROMETRY.
[16]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-263; SER-269; SER-275; THR-292 AND SER-296, MASS SPECTROMETRY.
[17]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; TYR-73; SER-91; SER-93; SER-94; SER-103; SER-143; SER-148; SER-214; SER-218; THR-239; SER-263; SER-269; SER-275; THR-292; SER-296; SER-306; SER-312; SER-400; THR-406; SER-411; SER-420; SER-421; THR-424; SER-446; SER-458; SER-476; THR-478; SER-480; SER-481; SER-893; SER-894 AND SER-899, MASS SPECTROMETRY.
[18]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; THR-145; SER-148; SER-197; THR-213; SER-218; SER-230; THR-239; SER-263; SER-269; SER-275; THR-292; SER-296; THR-298; SER-306; SER-312; SER-314; SER-446; THR-507; THR-509; SER-510; SER-514; SER-828; SER-831; THR-832; SER-893; SER-894; SER-899 AND SER-914, MASS SPECTROMETRY.
[19]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-195; THR-213; SER-214; SER-218; THR-219; SER-263; THR-292; SER-421 AND THR-424, MASS SPECTROMETRY.
[20]	"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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-143; THR-145; SER-148; THR-150; SER-197; THR-213; SER-214; SER-263; SER-291; THR-298; SER-311; SER-314; SER-421; SER-828; SER-831; THR-832; THR-892 AND SER-899, MASS SPECTROMETRY.
[21]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; THR-199; THR-213; SER-214; THR-239; SER-263; SER-269; SER-275; SER-306; SER-314; TYR-822; SER-828; SER-831; THR-832; SER-899 AND SER-914, MASS SPECTROMETRY. Tissue: T-cell.
[22]	"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: 17956729] [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.

IPI

IPI00759472.
IPI00876972.

RefSeq

NP_001035784.1.
NP_064623.2.

UniGene

Hs.142179

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QFA	X-ray	1.40	C	1-47	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NQS7. 5 interactions.

STRING

Q9NQS7.

PTM databases

PhosphoSite

Q9NQS7.

Proteomic databases

PRIDE

Q9NQS7.

Genome annotation databases

Ensembl

ENST00000394818; ENSP00000378295; ENSG00000149503; Homo sapiens. [Genome view]

GeneID

3619.

KEGG

hsa:3619.

Organism-specific databases

CTD

3619.

GeneCards

GC11P061648.

H-InvDB

HIX0009706.

HGNC

HGNC:6058. INCENP.

HPA

CAB013292.

MIM

604411. gene.

PharmGKB

PA29868.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17987.

HOGENOM

HBG505351.

HOVERGEN

Q9NQS7.

InParanoid

Q9NQS7.

OMA

PLRTFLH.

OrthoDB

EOG9ZW7X8.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_b_pathway. Aurora B signaling.
aurora_c_pathway. Aurora C signaling.

Reactome

REACT_152. Cell Cycle, Mitotic.

Gene expression databases

ArrayExpress

Q9NQS7.

Bgee

Q9NQS7.

CleanEx

HS_INCENP.

Genevestigator

Q9NQS7.

GermOnline

ENSG00000149503. Homo sapiens.

Family and domain databases

ProtoNet

Search...

Other Resources

NextBio

14153.

SOURCE

Search...

Entry information

Entry name

INCE_HUMAN

Accession

Primary (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:	February 9, 2010
This is version 78 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.