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Q6RT24

- CENPE_MOUSE

UniProt

Q6RT24 - CENPE_MOUSE

Protein

Centromere-associated protein E

Gene

Cenpe

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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 – 938ATPPROSITE-ProRule annotation

    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

    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

    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 EImported
    Alternative name(s):
    Centromere protein E
    Short name:
    CENP-EBy similarity
    Kinesin superfamily protein 101 Publication
    Short name:
    KIF101 Publication
    Motor domain of KIF10Imported
    Gene namesi
    Name:CenpeImported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1098230. Cenpe.

    Subcellular locationi

    Cytoplasmcytoskeletonspindle 2 Publications. Chromosomecentromerekinetochore 2 Publications
    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

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 24712471Centromere-associated protein EPRO_0000365106Add
    BLAST
    Propeptidei2472 – 24743Removed in mature formBy similarityPRO_0000396743

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2471 – 24711Cysteine methyl esterBy similarity
    Lipidationi2471 – 24711S-farnesyl cysteineBy similarity

    Post-translational modificationi

    The C-terminal inhibitory domain is phosphorylated. Phosphorylation relieves autoinhibition of the kinetochore motor By similarity.By similarity
    Sumoylated with SUMO2 and SUMO3. The sumoylation mediates the association to the kinetochore By similarity.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.By similarity

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ6RT24.
    SMRiQ6RT24. Positions 4-339.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 329324Kinesin motorPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1962 – 2252291Kinetochore binding domainBy similarityAdd
    BLAST
    Regioni2286 – 2471186Globular autoinhibitory domainBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili334 – 23662033Sequence AnalysisAdd
    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

    Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.PROSITE-ProRule annotation
    Contains 1 kinesin motor domain.PROSITE-ProRule annotation

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti231 – 24111LNLVDLAGSER → IKLIDTVDLEG in BAA22386. (PubMed:9275178)CuratedAdd
    BLAST
    Sequence conflicti1760 – 17601T → A in BAC33868. (PubMed:16141072)Curated

    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...
    MobiDBi 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

    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/6JImported and Czech IIImported.
      Tissue: BrainImported, EggImported, Mammary tumorImported and Olfactory epitheliumImported.
    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/6JImported.
      Tissue: Spinal cordImported and TestisImported.
    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: ICRImported.
      Tissue: Hippocampus1 Publication.
    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: October 1, 2014
    This is version 74 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