Q9WU62 (INCE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inner centromere protein

Gene names

Name:

Incenp

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	880 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 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	Chromosome › centromere. Cytoplasm › cytoskeleton › spindle. Nucleus. Chromosome › centromere › 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. 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 process	Cell cycle Cell division Chromosome partition Mitosis
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Kinetochore Microtubule Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromosome segregation Inferred from sequence or structural similarity. Source: UniProtKB cytokinesis Inferred from sequence or structural similarity. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	central 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 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 spindle Inferred from sequence or structural similarity. Source: UniProtKB
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 880	880	Inner centromere protein		PRO_0000084202
Regions
	Coiled coil	506 – 759	254	Potential
Amino acid modifications
	Modified residue	142	1	Phosphoserine By similarity
	Modified residue	147	1	Phosphoserine By similarity
	Modified residue	189	1	Phosphothreonine By similarity
	Modified residue	190	1	Phosphoserine By similarity
	Modified residue	215	1	Phosphothreonine Ref.8
	Modified residue	218	1	Phosphoserine Ref.8
	Modified residue	239	1	Phosphoserine By similarity
	Modified residue	245	1	Phosphoserine By similarity
	Modified residue	251	1	Phosphoserine By similarity
	Modified residue	270	1	Phosphothreonine By similarity
	Modified residue	284	1	Phosphoserine By similarity
	Modified residue	290	1	Phosphoserine By similarity
	Modified residue	376	1	Phosphoserine By similarity
	Modified residue	382	1	Phosphothreonine By similarity
	Modified residue	421	1	Phosphoserine By similarity
	Modified residue	489	1	Phosphoserine By similarity
	Modified residue	796	1	Phosphoserine Ref.9
	Modified residue	799	1	Phosphoserine Ref.9
	Modified residue	800	1	Phosphothreonine Ref.9
	Modified residue	860	1	Phosphothreonine; by AURKB By similarity
	Modified residue	861	1	Phosphoserine; by AURKB By similarity
	Modified residue	862	1	Phosphoserine; by AURKB By similarity
	Modified residue	867	1	Phosphoserine Ref.8
Natural variations
	Alternative sequence	507 – 510	4	Missing in isoform 2.		VSP_007233
Experimental info
	Sequence conflict	397	1	G → S in AAD32094. Ref.1
	Sequence conflict	412	1	T → I in AAH52414. Ref.4
	Sequence conflict	448	1	C → F in AAD32094. Ref.1
	Sequence conflict	687	1	K → R in AAD32094. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (B) [UniParc]. Last modified April 23, 2003. Version 2. Checksum: 92169889A921FEFC	FASTA	880	101,209
	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
	Isoform 2 (A) [UniParc]. Checksum: 836922856F05C81E	FASTA	876	100,772
	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 LRVDPKEKER QRLESLRRKE EAEQRRRQKV EEDKRRRLEE 550 560 570 580 590 600 VKLKREERLR KVLQARERVE QMKEEKKKQI EQKFAQIDEK TEKAKEERLA EKAKKKATAK 610 620 630 640 650 660 KMEEVEARRK QEEEARRLRW LQQEEEERRH QEMLQRKKEE EQERRKAAEA RRLAEQREQE 670 680 690 700 710 720 RRREQERREQ ERREQERREQ ERKEQERREQ EQERLRAKRE MQEREKALRL QKERLQKELE 730 740 750 760 770 780 EKKRKEEQQR LAEQQLQEEQ AKKAKEVAAA RKVLNMTVDV QSPVCTSYQM TPQGPKSIPK 790 800 810 820 830 840 ISVDDYGMDL NSDDSTDDES HPRKPIPSWA KGTQLSQAIV HQYYHPPNIL ELFGSILPLD 850 860 870 LEDIFKKRKT RYHKRTSSAV WNSPPLKATM VPSSGD

References

	« Hide 'large scale' referencesShow '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. , 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; SER-218; SER-862 AND SER-867, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Macrophage.
+	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.
IPI	IPI00265986. IPI00265987.
RefSeq	NP_057901.2. NM_016692.3.
UniGene	Mm.29755.
3D structure databases
ProteinModelPortal	Q9WU62.
SMR	Q9WU62. Positions 3-47, 581-752, 808-850.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-56678N.
IntAct	Q9WU62. 8 interactions.
PTM databases
PhosphoSite	Q9WU62.
Proteomic databases
PRIDE	Q9WU62.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000025562; ENSMUSP00000025562; ENSMUSG00000024660.
GeneID	16319.
KEGG	mmu:16319.
UCSC	uc008gor.2. mouse. uc008gos.2. mouse.
Organism-specific databases
CTD	3619.
MGI	MGI:1313288. Incenp.
Phylogenomic databases
eggNOG	NOG327385.
GeneTree	ENSGT00660000095160.
HOGENOM	HOG000113069.
HOVERGEN	HBG006157.
InParanoid	Q9WU62.
KO	K11515.
OMA	HTVQRNQ.
OrthoDB	EOG4RJG17.
Gene expression databases
Bgee	Q9WU62.
CleanEx	MM_INCENP.
Genevestigator	Q9WU62.
GermOnline	ENSMUSG00000024660. Mus musculus.
Family and domain databases
InterPro	IPR022006. INCENP_N. IPR005635. Inner_centromere_prot_ARK-bd. [Graphical view]
Pfam	PF03941. INCENP_ARK-bind. 1 hit. PF12178. INCENP_N. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	INCENP. mouse.
NextBio	289382.
SOURCE	Search...

Entry information

Entry name

INCE_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program