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Q6RT24 (CENPE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centromere-associated protein E
Alternative name(s):
Centromere protein E
Short name=CENP-E
Kinesin superfamily protein 10
Short name=KIF10
Motor domain of KIF10
Gene names
Name:Cenpe
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2474 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for the maintenance of chromosomal stability through efficient stabilization of microtubule capture at kinetochores. Plays a key role in the movement of chromosomes toward the metaphase plate during mitosis. Is a slow plus end-directed motor whose activity is essential for metaphase chromosome alignment. Couples chromosome position to microtubule depolymerizing activity. The highly processive microtubule-dependent motor activity of CENPE serves to power chromosome congression and provides a flexible, motile tether linking kinetochores to dynamic spindle microtubules. Necessary for the mitotic checkpoint signal at individual kinetochores to prevent aneuploidy due to single chromosome loss. Required for the efficient recruitment of BUBR1, MAD1 and MAD2 to attached and newly unattached kinetochores. Stimulates mammalian BUBR1 kinase activity. Accumulates just before mitosis at the G2 phase of the cell cycle. Ref.1 Ref.5

Subunit structure

Monomer. Interacts with CENPF, SEPT7 KIF18A and PRC1 By similarity. Interacts with BUBR1 kinase. Interacts with SKAP; this interaction greatly favors SKAP binding to microtubules By similarity. Ref.1

Subcellular location

Cytoplasmcytoskeletonspindle. Chromosomecentromerekinetochore. Note: Associates with kinetochores during congression (as early as prometaphase), relocates to the spindle midzone at anaphase, and is quantitatively discarded at the end of the cell division. Ref.1 Ref.5

Tissue specificity

Expressed in hippocampus. Also detected in liver and fibroblasts (at protein level). Ref.4 Ref.5

Domain

The protein is composed of a N-terminal kinesin-motor domain involved in the chromosome movements, a long coil-coiled region involved in the homodimerization and an inhibitory C-tail involved in autoinhibition of the N-terminal catalytic part By similarity.

Post-translational modification

The C-terminal inhibitory domain is phosphorylated. Phosphorylation relieves autoinhibition of the kinetochore motor By similarity.

Sumoylated with SUMO2 and SUMO3. The sumoylation mediates the association to the kinetochore By similarity.

Sequence similarities

Belongs to the kinesin-like protein family.

Contains 1 kinesin-motor domain.

Sequence caution

The sequence AAH52843.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAI06097.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAC33868.1 differs from that shown. Reason: Frameshift at position 1759.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Kinetochore
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Motor protein
   PTMLipoprotein
Methylation
Phosphoprotein
Prenylation
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processattachment of spindle microtubules to kinetochore

Inferred from mutant phenotype Ref.1. Source: UniProtKB

establishment of protein localization

Inferred from mutant phenotype Ref.1. Source: UniProtKB

microtubule-based movement

Inferred from electronic annotation. Source: InterPro

mitotic metaphase plate congression

Inferred from electronic annotation. Source: InterPro

mitotic spindle assembly checkpoint

Inferred from mutant phenotype Ref.1. Source: UniProtKB

multicellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of attachment of spindle microtubules to kinetochore

Inferred from mutant phenotype Ref.5. Source: UniProtKB

positive regulation of chromosome segregation

Inferred from mutant phenotype Ref.1. Source: UniProtKB

positive regulation of mitotic metaphase/anaphase transition

Inferred from mutant phenotype Ref.1. Source: UniProtKB

positive regulation of protein kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of developmental process

Inferred from mutant phenotype Ref.5. Source: UniProtKB

regulation of mitosis

Inferred from mutant phenotype Ref.5. Source: UniProtKB

   Cellular_componentchromosome, centromeric region

Inferred from sequence orthology PubMed 11084331. Source: MGI

condensed chromosome outer kinetochore

Inferred from direct assay PubMed 19283064. Source: MGI

condensed nuclear chromosome kinetochore

Inferred from direct assay PubMed 18765791. Source: MGI

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

kinesin complex

Inferred from electronic annotation. Source: InterPro

kinetochore

Inferred from direct assay Ref.1. Source: UniProtKB

spindle midzone

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

kinetochore binding

Inferred from direct assay Ref.1. Source: UniProtKB

microtubule motor activity

Inferred from electronic annotation. Source: InterPro

protein kinase binding

Inferred from physical interaction Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24712471Centromere-associated protein E
PRO_0000365106
Propeptide2472 – 24743Removed in mature form By similarity
PRO_0000396743

Regions

Domain3 – 260258Kinesin-motor
Nucleotide binding86 – 938ATP Potential
Region1962 – 2252291Kinetochore binding domain By similarity UniProtKB Q02224
Region2286 – 2471186Globular autoinhibitory domain By similarity
Coiled coil334 – 23662033 Potential

Amino acid modifications

Modified residue24711Cysteine methyl ester By similarity
Lipidation24711S-farnesyl cysteine By similarity UniProtKB Q02224

Experimental info

Sequence conflict231 – 24111LNLVDLAGSER → IKLIDTVDLEG in BAA22386. Ref.4
Sequence conflict17601T → A in BAC33868. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q6RT24 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: BAF52DD6068A2903

FASTA2,474286,525
        10         20         30         40         50         60 
MAEEASVAVC VRVRPLNSRE EELGEATHIY WKTDKNAIYQ SDGGKSFQFD RVFDSNETTK 

        70         80         90        100        110        120 
NVYEEIAVPI ISSAIQGYNG TIFAYGQTAS GKTHTMMGSE DCLGVIPRAI HDIFQRIKKF 

       130        140        150        160        170        180 
PEREFLLRVS YMEIYNETIT DLLCNAQKMK PLIIREDTNR TVYVSDLTEE VVYTAEMALK 

       190        200        210        220        230        240 
WLATGEKNRH YGITKMNQRS SRSHTIFRMI LESREKAEPS NCDGSVKVSH LNLVDLAGSE 

       250        260        270        280        290        300 
RAAQTGAEGV RLKEGCFINR NLFILGQVIK KLSDGQVGGF INYRDSKLTR ILQNSLGGNA 

       310        320        330        340        350        360 
KTRIICTITP ASLDETLTTL QFASTAKYMK NTPYVNEVSN DEALLKRYRR EIADLRKQLE 

       370        380        390        400        410        420 
EVNTKTRAQE MEKDQLAQLL DEKDLLQKVQ DEKINNLKRM LVTSSSIALQ QELEIKRKRR 

       430        440        450        460        470        480 
VTWCYGKMKD SNYEKEFKVP TSITTRKRKT SVTSLRENSL MKFGESAASS EFEMLNNTLE 

       490        500        510        520        530        540 
SLAEVEWSSA TTLLSEENVE SELNSLNAQY NDLVLDYEQL RRENEDLKLK LKEKNELEEF 

       550        560        570        580        590        600 
ELLEQKEERD QEMQLMHEVS NLKNLIKHAE EYNQDLENDL SSKVKLLKEK EEQIKNLQEY 

       610        620        630        640        650        660 
IDAQKSEKMK IDLSYTSDAT EDLKQAMRTL SDLDTVALDA KKESAFLRSE NLELKEKINE 

       670        680        690        700        710        720 
LSDSRKQMES DIQMYQRQLE AKKKMQTDLD KELQLAFQEI SKLSALVDGK GLLSNLELEK 

       730        740        750        760        770        780 
RITDLQKELN KEAEEKQTLQ EEVNLLSELK SLPSEVETLR RELYEKSEEL HIITTEREKL 

       790        800        810        820        830        840 
FSEMAHKDSR IQGLLEEIGN TRDDLATSQL SRRGSDGEWQ ALESLHAELE HRHAGVLEER 

       850        860        870        880        890        900 
ERLKQEIGAL SKEAESLAFS LDSVKAELSH KTQELEQKTV EGQERLNKME ALREELESRD 

       910        920        930        940        950        960 
SSLQSVEKEK VLLTEKLQQA LKEVKALTQE KKNLKQLQES LQTERDQLRS DIQDTVNMNI 

       970        980        990       1000       1010       1020 
DTQEQLLNAL ESLKQHQETI NMLKMKAAEE LSDNLHVKDR GGARDEAQQK MDGIDEQNES 

      1030       1040       1050       1060       1070       1080 
AHTLLGGGKD NEVTEEQRKI DSLMQENSGL QQTLESVRAE KEQLKMDLKE NIEMSIENQE 

      1090       1100       1110       1120       1130       1140 
ELRILRDELK RQQEVAAQEK DHATEKTQEL SRTQERLAKT EEKLEEKNQK LQETQQQLLS 

      1150       1160       1170       1180       1190       1200 
TQEAMSKLQA KVIDMESLQN EFRNQGLALE RVETEKLELA QRLHESYEEV KSITKERNDL 

      1210       1220       1230       1240       1250       1260 
KELQESFEIE KKQLKEYARE IEAEGLQAKE ELNIAHANLK EYQEIITELR GSISENEAQG 

      1270       1280       1290       1300       1310       1320 
ASTQDTAKSA PELQGEVPEL LEQELLPVVK EARHSAEKVN GLEPVGAHSR TVHSMTMEGI 

      1330       1340       1350       1360       1370       1380 
EIGNLRLTKK LEESQMEISC LTREREDLRR TQETLQVECT QLKEDARRTL ANHLETEEEL 

      1390       1400       1410       1420       1430       1440 
NLARCCLKEQ ENKIDTLITS LSQRETELSS VRGQLALTTA ELERKVQELC EKQEELTRKE 

      1450       1460       1470       1480       1490       1500 
TSEAQGKMSE LEQLRELLLA QASALQNAES DRLRLNTQLE ESQEEMKTLR EEREELRRMQ 

      1510       1520       1530       1540       1550       1560 
EALHVESEQQ KESMKEISSK LQELQNKEYE CLAMKTINET QGSRCEMDHL NQQLEAQKST 

      1570       1580       1590       1600       1610       1620 
LEKVEMENVN LTQRLHETLE EMRSVAKERD ELWSMEERLT VERDQLKKSL EETVTKGMEK 

      1630       1640       1650       1660       1670       1680 
EEELRVAHVH LEEHQETINK LRKMVSDYTD EISHTQGDLK HTNAVVEAQN QDLREKEHQL 

      1690       1700       1710       1720       1730       1740 
SQVKADLRET VDQMEQLKKK LEAQSSTLES REIEKLELTQ QLNENLKKIT LVTKENDSLK 

      1750       1760       1770       1780       1790       1800 
IMDEALREER DQLRKSLQQT EARDLENQEK LRIAHMNLKE HQETIDRLME TMSEKTEEIS 

      1810       1820       1830       1840       1850       1860 
NMKMELENVN MKLQEKVQEL KTSERQRVKL KADASEAKKE LKEQGLTLSK IEMENLNLAQ 

      1870       1880       1890       1900       1910       1920 
KIHENLEEMK SVRKERDDLK KLEEILRMER DQLKDNLREA MLKAHQNHEE TMKCGKGLLC 

      1930       1940       1950       1960       1970       1980 
AGEYCTGRLR EKCFRIEKLL KRYSEMANDY ECLNKVSLDL ERETKTQKEL SVTVRTKLSL 

      1990       2000       2010       2020       2030       2040 
PHTQTKEMEK LLTANQRCSL EFHRALKRLK YVLSSIARIK EEQHESINKR EMAFIQEVEK 

      2050       2060       2070       2080       2090       2100 
QNELQIQIQS LSQTYRIPAR DLQIKLSQEM DLHIEEMLKD FSENDFLTIK TEVQQVLNNR 

      2110       2120       2130       2140       2150       2160 
KEITEFLGKW LNTLFDTENL KSTIQKENKS IGLVNNFYHS RITAMINEST EFEERSATRS 

      2170       2180       2190       2200       2210       2220 
KDLDQYLKSL KETTEQLSEV YQTLTASQSV VHLHPTVQPS TRDSERPQAA SGAEQLTSKN 

      2230       2240       2250       2260       2270       2280 
KIALGAVPYK EEIEDLKMQL VKSDLEKKAT AKEFDKKILS LKATVEHQEE MIRLLRENLR 

      2290       2300       2310       2320       2330       2340 
GHQQAQDTSM ISEQDSQLLS KPLTCGGGSG IVQSTKALIL KSEYKRMGSE ISKLKQQNEQ 

      2350       2360       2370       2380       2390       2400 
LRKQNNQLLS DNSQLSNEVK TWEERTLKRD SYRETTCENS PKSPKVTRTD SKRRQNTTSQ 

      2410       2420       2430       2440       2450       2460 
CRAQNLQDPV PKDSPKSWFF DNRSKSLPAP HPIRYFDNSS LGLCPEPDDV ENVEPKTDLC 

      2470 
QASLEKDVSQ CKTQ 

« Hide

References

« Hide 'large scale' references
[1]"Centromere-associated protein-E is essential for the mammalian mitotic checkpoint to prevent aneuploidy due to single chromosome loss."
Weaver B.A., Bonday Z.Q., Putkey F.R., Kops G.J., Silk A.D., Cleveland D.W.
J. Cell Biol. 162:551-563(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH BUBR1, SUBCELLULAR LOCATION.
[2]"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] OF 1-546 AND 1652-2474.
Strain: C57BL/6J and Czech II.
Tissue: Brain, Egg, Mammary tumor and Olfactory epithelium.
[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. expand/collapse author list , 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] OF 1-520 AND 1705-2474.
Strain: C57BL/6J.
Tissue: Spinal cord and Testis.
[4]"Identification and classification of 16 new kinesin superfamily (KIF) proteins in mouse genome."
Nakagawa T., Tanaka Y., Matsuoka E., Kondo S., Okada Y., Noda Y., Kanai Y., Hirokawa N.
Proc. Natl. Acad. Sci. U.S.A. 94:9654-9659(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 82-241, TISSUE SPECIFICITY.
Strain: ICR.
Tissue: Hippocampus.
[5]"Unstable kinetochore-microtubule capture and chromosomal instability following deletion of CENP-E."
Putkey F.R., Cramer T., Morphew M.K., Silk A.D., Johnson R.S., McIntosh J.R., Cleveland D.W.
Dev. Cell 3:351-365(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY493378 mRNA. Translation: AAR85498.1.
BC049989 mRNA. Translation: AAH49989.1.
BC052843 mRNA. Translation: AAH52843.1. Sequence problems.
BC059032 mRNA. Translation: AAH59032.1.
BC106096 mRNA. Translation: AAI06097.1. Sequence problems.
AK049676 mRNA. Translation: BAC33868.1. Frameshift.
AK133445 mRNA. Translation: BAE21661.1.
AB001426 mRNA. Translation: BAA22386.1.
RefSeqNP_776123.3. NM_173762.4.
UniGeneMm.161470.

3D structure databases

ProteinModelPortalQ6RT24.
SMRQ6RT24. Positions 4-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid230907. 4 interactions.
IntActQ6RT24. 3 interactions.
STRING10090.ENSMUSP00000057938.

PTM databases

PhosphoSiteQ6RT24.

Proteomic databases

PaxDbQ6RT24.
PRIDEQ6RT24.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID229841.
KEGGmmu:229841.

Organism-specific databases

CTD1062.
MGIMGI:1098230. Cenpe.

Phylogenomic databases

eggNOGCOG5059.
HOVERGENHBG097734.
InParanoidQ7TPX4.
KOK11498.
PhylomeDBQ6RT24.

Gene expression databases

GenevestigatorQ6RT24.

Family and domain databases

Gene3D3.40.850.10. 1 hit.
InterProIPR028368. CENPE.
IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR24115. PTHR24115. 1 hit.
PTHR24115:SF72. PTHR24115:SF72. 1 hit.
PfamPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSPR00380. KINESINHEAVY.
SMARTSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio379688.
PROQ6RT24.
SOURCESearch...

Entry information

Entry nameCENPE_MOUSE
AccessionPrimary (citable) accession number: Q6RT24
Secondary accession number(s): O35059 expand/collapse secondary AC list , Q3KQQ6, Q3V044, Q6PD00, Q7TPX4, Q80YB4, Q8BWX6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot