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Q6RT24

- CENPE_MOUSE

UniProt

Q6RT24 - CENPE_MOUSE

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Protein
Centromere-associated protein E
Gene
Cenpe
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi86 – 938ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. kinetochore binding Source: UniProtKB
  3. microtubule motor activity Source: InterPro
  4. protein kinase binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. attachment of spindle microtubules to kinetochore Source: UniProtKB
  2. establishment of protein localization Source: UniProtKB
  3. microtubule-based movement Source: InterPro
  4. mitotic nuclear division Source: UniProtKB-KW
  5. mitotic spindle assembly checkpoint Source: UniProtKB
  6. multicellular organismal development Source: UniProtKB-KW
  7. positive regulation of attachment of spindle microtubules to kinetochore Source: UniProtKB
  8. positive regulation of chromosome segregation Source: UniProtKB
  9. positive regulation of mitotic metaphase/anaphase transition Source: UniProtKB
  10. positive regulation of protein kinase activity Source: UniProtKB
  11. regulation of developmental process Source: UniProtKB
  12. regulation of mitosis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Motor protein

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Cenpe
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1098230. Cenpe.

Subcellular locationi

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.2 Publications

GO - Cellular componenti

  1. chromosome, centromeric region Source: MGI
  2. condensed chromosome outer kinetochore Source: MGI
  3. condensed nuclear chromosome kinetochore Source: MGI
  4. cytoplasm Source: UniProtKB-KW
  5. kinesin complex Source: InterPro
  6. kinetochore Source: UniProtKB
  7. spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24712471Centromere-associated protein E
PRO_0000365106Add
BLAST
Propeptidei2472 – 24743Removed in mature form By similarity
PRO_0000396743

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2471 – 24711Cysteine methyl ester By similarity
Lipidationi2471 – 24711S-farnesyl cysteine By similarityBy similarity

Post-translational modificationi

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.

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

Proteomic databases

PaxDbiQ6RT24.
PRIDEiQ6RT24.

PTM databases

PhosphoSiteiQ6RT24.

Expressioni

Tissue specificityi

Expressed in hippocampus. Also detected in liver and fibroblasts (at protein level).2 Publications

Gene expression databases

GenevestigatoriQ6RT24.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi230907. 4 interactions.
IntActiQ6RT24. 3 interactions.
STRINGi10090.ENSMUSP00000057938.

Structurei

3D structure databases

ProteinModelPortaliQ6RT24.
SMRiQ6RT24. Positions 4-339.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 329324Kinesin motor
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1962 – 2252291Kinetochore binding domain By similarityBy similarity
Add
BLAST
Regioni2286 – 2471186Globular autoinhibitory domain By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili334 – 23662033 Reviewed prediction
Add
BLAST

Domaini

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.

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5059.
HOVERGENiHBG097734.
InParanoidiQ7TPX4.
KOiK11498.
PhylomeDBiQ6RT24.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 1 hit.
PfamiPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6RT24-1 [UniParc]FASTAAdd to Basket

« Hide

MAEEASVAVC VRVRPLNSRE EELGEATHIY WKTDKNAIYQ SDGGKSFQFD     50
RVFDSNETTK NVYEEIAVPI ISSAIQGYNG TIFAYGQTAS GKTHTMMGSE 100
DCLGVIPRAI HDIFQRIKKF PEREFLLRVS YMEIYNETIT DLLCNAQKMK 150
PLIIREDTNR TVYVSDLTEE VVYTAEMALK WLATGEKNRH YGITKMNQRS 200
SRSHTIFRMI LESREKAEPS NCDGSVKVSH LNLVDLAGSE RAAQTGAEGV 250
RLKEGCFINR NLFILGQVIK KLSDGQVGGF INYRDSKLTR ILQNSLGGNA 300
KTRIICTITP ASLDETLTTL QFASTAKYMK NTPYVNEVSN DEALLKRYRR 350
EIADLRKQLE EVNTKTRAQE MEKDQLAQLL DEKDLLQKVQ DEKINNLKRM 400
LVTSSSIALQ QELEIKRKRR VTWCYGKMKD SNYEKEFKVP TSITTRKRKT 450
SVTSLRENSL MKFGESAASS EFEMLNNTLE SLAEVEWSSA TTLLSEENVE 500
SELNSLNAQY NDLVLDYEQL RRENEDLKLK LKEKNELEEF ELLEQKEERD 550
QEMQLMHEVS NLKNLIKHAE EYNQDLENDL SSKVKLLKEK EEQIKNLQEY 600
IDAQKSEKMK IDLSYTSDAT EDLKQAMRTL SDLDTVALDA KKESAFLRSE 650
NLELKEKINE LSDSRKQMES DIQMYQRQLE AKKKMQTDLD KELQLAFQEI 700
SKLSALVDGK GLLSNLELEK RITDLQKELN KEAEEKQTLQ EEVNLLSELK 750
SLPSEVETLR RELYEKSEEL HIITTEREKL FSEMAHKDSR IQGLLEEIGN 800
TRDDLATSQL SRRGSDGEWQ ALESLHAELE HRHAGVLEER ERLKQEIGAL 850
SKEAESLAFS LDSVKAELSH KTQELEQKTV EGQERLNKME ALREELESRD 900
SSLQSVEKEK VLLTEKLQQA LKEVKALTQE KKNLKQLQES LQTERDQLRS 950
DIQDTVNMNI DTQEQLLNAL ESLKQHQETI NMLKMKAAEE LSDNLHVKDR 1000
GGARDEAQQK MDGIDEQNES AHTLLGGGKD NEVTEEQRKI DSLMQENSGL 1050
QQTLESVRAE KEQLKMDLKE NIEMSIENQE ELRILRDELK RQQEVAAQEK 1100
DHATEKTQEL SRTQERLAKT EEKLEEKNQK LQETQQQLLS TQEAMSKLQA 1150
KVIDMESLQN EFRNQGLALE RVETEKLELA QRLHESYEEV KSITKERNDL 1200
KELQESFEIE KKQLKEYARE IEAEGLQAKE ELNIAHANLK EYQEIITELR 1250
GSISENEAQG ASTQDTAKSA PELQGEVPEL LEQELLPVVK EARHSAEKVN 1300
GLEPVGAHSR TVHSMTMEGI EIGNLRLTKK LEESQMEISC LTREREDLRR 1350
TQETLQVECT QLKEDARRTL ANHLETEEEL NLARCCLKEQ ENKIDTLITS 1400
LSQRETELSS VRGQLALTTA ELERKVQELC EKQEELTRKE TSEAQGKMSE 1450
LEQLRELLLA QASALQNAES DRLRLNTQLE ESQEEMKTLR EEREELRRMQ 1500
EALHVESEQQ KESMKEISSK LQELQNKEYE CLAMKTINET QGSRCEMDHL 1550
NQQLEAQKST LEKVEMENVN LTQRLHETLE EMRSVAKERD ELWSMEERLT 1600
VERDQLKKSL EETVTKGMEK EEELRVAHVH LEEHQETINK LRKMVSDYTD 1650
EISHTQGDLK HTNAVVEAQN QDLREKEHQL SQVKADLRET VDQMEQLKKK 1700
LEAQSSTLES REIEKLELTQ QLNENLKKIT LVTKENDSLK IMDEALREER 1750
DQLRKSLQQT EARDLENQEK LRIAHMNLKE HQETIDRLME TMSEKTEEIS 1800
NMKMELENVN MKLQEKVQEL KTSERQRVKL KADASEAKKE LKEQGLTLSK 1850
IEMENLNLAQ KIHENLEEMK SVRKERDDLK KLEEILRMER DQLKDNLREA 1900
MLKAHQNHEE TMKCGKGLLC AGEYCTGRLR EKCFRIEKLL KRYSEMANDY 1950
ECLNKVSLDL ERETKTQKEL SVTVRTKLSL PHTQTKEMEK LLTANQRCSL 2000
EFHRALKRLK YVLSSIARIK EEQHESINKR EMAFIQEVEK QNELQIQIQS 2050
LSQTYRIPAR DLQIKLSQEM DLHIEEMLKD FSENDFLTIK TEVQQVLNNR 2100
KEITEFLGKW LNTLFDTENL KSTIQKENKS IGLVNNFYHS RITAMINEST 2150
EFEERSATRS KDLDQYLKSL KETTEQLSEV YQTLTASQSV VHLHPTVQPS 2200
TRDSERPQAA SGAEQLTSKN KIALGAVPYK EEIEDLKMQL VKSDLEKKAT 2250
AKEFDKKILS LKATVEHQEE MIRLLRENLR GHQQAQDTSM ISEQDSQLLS 2300
KPLTCGGGSG IVQSTKALIL KSEYKRMGSE ISKLKQQNEQ LRKQNNQLLS 2350
DNSQLSNEVK TWEERTLKRD SYRETTCENS PKSPKVTRTD SKRRQNTTSQ 2400
CRAQNLQDPV PKDSPKSWFF DNRSKSLPAP HPIRYFDNSS LGLCPEPDDV 2450
ENVEPKTDLC QASLEKDVSQ CKTQ 2474
Length:2,474
Mass (Da):286,525
Last modified:July 5, 2004 - v1
Checksum:iBAF52DD6068A2903
GO

Sequence cautioni

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti231 – 24111LNLVDLAGSER → IKLIDTVDLEG in BAA22386. 1 Publication
Add
BLAST
Sequence conflicti1760 – 17601T → A in BAC33868. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiNP_776123.3. NM_173762.4.
UniGeneiMm.161470.

Genome annotation databases

GeneIDi229841.
KEGGimmu:229841.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
RefSeqi NP_776123.3. NM_173762.4.
UniGenei Mm.161470.

3D structure databases

ProteinModelPortali Q6RT24.
SMRi Q6RT24. Positions 4-339.
ModBasei Search...

Protein-protein interaction databases

BioGridi 230907. 4 interactions.
IntActi Q6RT24. 3 interactions.
STRINGi 10090.ENSMUSP00000057938.

PTM databases

PhosphoSitei Q6RT24.

Proteomic databases

PaxDbi Q6RT24.
PRIDEi Q6RT24.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 229841.
KEGGi mmu:229841.

Organism-specific databases

CTDi 1062.
MGIi MGI:1098230. Cenpe.

Phylogenomic databases

eggNOGi COG5059.
HOVERGENi HBG097734.
InParanoidi Q7TPX4.
KOi K11498.
PhylomeDBi Q6RT24.

Miscellaneous databases

NextBioi 379688.
PROi Q6RT24.
SOURCEi Search...

Gene expression databases

Genevestigatori Q6RT24.

Family and domain databases

Gene3Di 3.40.850.10. 1 hit.
InterProi IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR24115. PTHR24115. 1 hit.
Pfami PF00225. Kinesin. 1 hit.
[Graphical view ]
PRINTSi PR00380. KINESINHEAVY.
SMARTi SM00129. KISc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiCENPE_MOUSE
AccessioniPrimary (citable) accession number: Q6RT24
Secondary accession number(s): O35059
, Q3KQQ6, Q3V044, Q6PD00, Q7TPX4, Q80YB4, Q8BWX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: July 5, 2004
Last modified: September 3, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi