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Q02224

- CENPE_HUMAN

UniProt

Q02224 - CENPE_HUMAN

Protein

Centromere-associated protein E

Gene

CENPE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (23 Oct 2007)
      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 – 938ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. kinetochore binding Source: UniProtKB
    3. microtubule motor activity Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    2. blood coagulation Source: Reactome
    3. kinetochore assembly Source: UniProtKB
    4. metabolic process Source: GOC
    5. microtubule-based movement Source: Reactome
    6. mitotic cell cycle Source: Reactome
    7. mitotic chromosome movement towards spindle pole Source: ProtInc
    8. mitotic metaphase Source: ProtInc
    9. mitotic metaphase plate congression Source: ProtInc
    10. multicellular organismal development Source: UniProtKB-KW
    11. positive regulation of protein kinase activity Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein, Motor protein

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_121399. MHC class II antigen presentation.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_25201. Kinesins.
    REACT_682. Mitotic Prometaphase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Centromere-associated protein E
    Alternative name(s):
    Centromere protein E
    Short name:
    CENP-E
    Kinesin-related protein CENPE
    Gene namesi
    Name:CENPE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:1856. CENPE.

    Subcellular locationi

    Chromosomecentromerekinetochore. Cytoplasmcytoskeletonspindle
    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.

    GO - Cellular componenti

    1. chromosome, centromeric region Source: MGI
    2. condensed chromosome, centromeric region Source: UniProtKB
    3. condensed chromosome outer kinetochore Source: Ensembl
    4. condensed nuclear chromosome kinetochore Source: Ensembl
    5. cytoplasm Source: HPA
    6. cytosol Source: Reactome
    7. kinesin complex Source: InterPro
    8. kinetochore Source: UniProtKB
    9. membrane Source: UniProtKB
    10. microtubule Source: UniProtKB
    11. microtubule cytoskeleton Source: HPA
    12. nucleus Source: UniProtKB
    13. spindle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26400.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 26982698Centromere-associated protein EPRO_0000125436Add
    BLAST
    Propeptidei2699 – 27013Removed in mature formCuratedPRO_0000396742

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki1937 – 1937Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei2647 – 26471Phosphoserine1 Publication
    Modified residuei2698 – 26981Cysteine methyl esterCurated
    Lipidationi2698 – 26981S-farnesyl cysteine1 Publication

    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.1 Publication

    Keywords - PTMi

    Isopeptide bond, Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

    Proteomic databases

    MaxQBiQ02224.
    PaxDbiQ02224.
    PRIDEiQ02224.

    PTM databases

    PhosphoSiteiQ02224.

    Expressioni

    Gene expression databases

    ArrayExpressiQ02224.
    BgeeiQ02224.
    CleanExiHS_CENPE.
    GenevestigatoriQ02224.

    Organism-specific databases

    HPAiHPA042294.

    Interactioni

    Subunit structurei

    Monomer. Interacts with CENPF, SEPT7, KIF18A, BUB1B kinase and PRC1. Interacts with NUF2; this interaction determines kinetochore localization. Interacts with SKAP; this interaction greatly favors SKAP binding to microtubules.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BUB1BO605664EBI-1375040,EBI-1001438
    NUF2Q9BZD49EBI-1375040,EBI-724102

    Protein-protein interaction databases

    BioGridi107491. 18 interactions.
    IntActiQ02224. 9 interactions.
    MINTiMINT-5002721.
    STRINGi9606.ENSP00000265148.

    Structurei

    Secondary structure

    1
    2701
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 137
    Turni22 – 254
    Beta strandi31 – 344
    Beta strandi37 – 404
    Beta strandi46 – 483
    Helixi59 – 657
    Helixi68 – 758
    Beta strandi80 – 878
    Helixi92 – 965
    Beta strandi100 – 1034
    Helixi105 – 11612
    Helixi117 – 1193
    Beta strandi123 – 13513
    Beta strandi138 – 1469
    Turni157 – 1593
    Helixi175 – 18713
    Beta strandi190 – 1978
    Turni199 – 2024
    Beta strandi204 – 21512
    Beta strandi226 – 23510
    Helixi239 – 2413
    Beta strandi254 – 2563
    Helixi260 – 27415
    Helixi283 – 2853
    Helixi287 – 2915
    Helixi293 – 2953
    Beta strandi298 – 30811
    Helixi314 – 32613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1T5CX-ray2.50A/B2-342[»]
    ProteinModelPortaliQ02224.
    SMRiQ02224. Positions 4-339.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ02224.

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2126 – 2476351Kinetochore-binding domainAdd
    BLAST
    Regioni2510 – 2698189Globular autoinhibitory domainBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili336 – 25902255Sequence 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.
    HOGENOMiHOG000111540.
    HOVERGENiHBG097734.
    InParanoidiQ02224.
    KOiK11498.
    OMAiNERMNQE.
    OrthoDBiEOG7J9VNX.
    PhylomeDBiQ02224.
    TreeFamiTF330343.

    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]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q02224-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAEEGAVAVC VRVRPLNSRE ESLGETAQVY WKTDNNVIYQ VDGSKSFNFD     50
    RVFHGNETTK NVYEEIAAPI IDSAIQGYNG TIFAYGQTAS GKTYTMMGSE 100
    DHLGVIPRAI HDIFQKIKKF PDREFLLRVS YMEIYNETIT DLLCGTQKMK 150
    PLIIREDVNR NVYVADLTEE VVYTSEMALK WITKGEKSRH YGETKMNQRS 200
    SRSHTIFRMI LESREKGEPS NCEGSVKVSH LNLVDLAGSE RAAQTGAAGV 250
    RLKEGCNINR SLFILGQVIK KLSDGQVGGF INYRDSKLTR ILQNSLGGNA 300
    KTRIICTITP VSFDETLTAL QFASTAKYMK NTPYVNEVST DEALLKRYRK 350
    EIMDLKKQLE EVSLETRAQA MEKDQLAQLL EEKDLLQKVQ NEKIENLTRM 400
    LVTSSSLTLQ QELKAKRKRR VTWCLGKINK MKNSNYADQF NIPTNITTKT 450
    HKLSINLLRE IDESVCSESD VFSNTLDTLS EIEWNPATKL LNQENIESEL 500
    NSLRADYDNL VLDYEQLRTE KEEMELKLKE KNDLDEFEAL ERKTKKDQEM 550
    QLIHEISNLK NLVKHAEVYN QDLENELSSK VELLREKEDQ IKKLQEYIDS 600
    QKLENIKMDL SYSLESIEDP KQMKQTLFDA ETVALDAKRE SAFLRSENLE 650
    LKEKMKELAT TYKQMENDIQ LYQSQLEAKK KMQVDLEKEL QSAFNEITKL 700
    TSLIDGKVPK DLLCNLELEG KITDLQKELN KEVEENEALR EEVILLSELK 750
    SLPSEVERLR KEIQDKSEEL HIITSEKDKL FSEVVHKESR VQGLLEEIGK 800
    TKDDLATTQS NYKSTDQEFQ NFKTLHMDFE QKYKMVLEEN ERMNQEIVNL 850
    SKEAQKFDSS LGALKTELSY KTQELQEKTR EVQERLNEME QLKEQLENRD 900
    STLQTVEREK TLITEKLQQT LEEVKTLTQE KDDLKQLQES LQIERDQLKS 950
    DIHDTVNMNI DTQEQLRNAL ESLKQHQETI NTLKSKISEE VSRNLHMEEN 1000
    TGETKDEFQQ KMVGIDKKQD LEAKNTQTLT ADVKDNEIIE QQRKIFSLIQ 1050
    EKNELQQMLE SVIAEKEQLK TDLKENIEMT IENQEELRLL GDELKKQQEI 1100
    VAQEKNHAIK KEGELSRTCD RLAEVEEKLK EKSQQLQEKQ QQLLNVQEEM 1150
    SEMQKKINEI ENLKNELKNK ELTLEHMETE RLELAQKLNE NYEEVKSITK 1200
    ERKVLKELQK SFETERDHLR GYIREIEATG LQTKEELKIA HIHLKEHQET 1250
    IDELRRSVSE KTAQIINTQD LEKSHTKLQE EIPVLHEEQE LLPNVKEVSE 1300
    TQETMNELEL LTEQSTTKDS TTLARIEMER LRLNEKFQES QEEIKSLTKE 1350
    RDNLKTIKEA LEVKHDQLKE HIRETLAKIQ ESQSKQEQSL NMKEKDNETT 1400
    KIVSEMEQFK PKDSALLRIE IEMLGLSKRL QESHDEMKSV AKEKDDLQRL 1450
    QEVLQSESDQ LKENIKEIVA KHLETEEELK VAHCCLKEQE ETINELRVNL 1500
    SEKETEISTI QKQLEAINDK LQNKIQEIYE KEEQFNIKQI SEVQEKVNEL 1550
    KQFKEHRKAK DSALQSIESK MLELTNRLQE SQEEIQIMIK EKEEMKRVQE 1600
    ALQIERDQLK ENTKEIVAKM KESQEKEYQF LKMTAVNETQ EKMCEIEHLK 1650
    EQFETQKLNL ENIETENIRL TQILHENLEE MRSVTKERDD LRSVEETLKV 1700
    ERDQLKENLR ETITRDLEKQ EELKIVHMHL KEHQETIDKL RGIVSEKTNE 1750
    ISNMQKDLEH SNDALKAQDL KIQEELRIAH MHLKEQQETI DKLRGIVSEK 1800
    TDKLSNMQKD LENSNAKLQE KIQELKANEH QLITLKKDVN ETQKKVSEME 1850
    QLKKQIKDQS LTLSKLEIEN LNLAQKLHEN LEEMKSVMKE RDNLRRVEET 1900
    LKLERDQLKE SLQETKARDL EIQQELKTAR MLSKEHKETV DKLREKISEK 1950
    TIQISDIQKD LDKSKDELQK KIQELQKKEL QLLRVKEDVN MSHKKINEME 2000
    QLKKQFEAQN LSMQSVRMDN FQLTKKLHES LEEIRIVAKE RDELRRIKES 2050
    LKMERDQFIA TLREMIARDR QNHQVKPEKR LLSDGQQHLT ESLREKCSRI 2100
    KELLKRYSEM DDHYECLNRL SLDLEKEIEF QKELSMRVKA NLSLPYLQTK 2150
    HIEKLFTANQ RCSMEFHRIM KKLKYVLSYV TKIKEEQHES INKFEMDFID 2200
    EVEKQKELLI KIQHLQQDCD VPSRELRDLK LNQNMDLHIE EILKDFSESE 2250
    FPSIKTEFQQ VLSNRKEMTQ FLEEWLNTRF DIEKLKNGIQ KENDRICQVN 2300
    NFFNNRIIAI MNESTEFEER SATISKEWEQ DLKSLKEKNE KLFKNYQTLK 2350
    TSLASGAQVN PTTQDNKNPH VTSRATQLTT EKIRELENSL HEAKESAMHK 2400
    ESKIIKMQKE LEVTNDIIAK LQAKVHESNK CLEKTKETIQ VLQDKVALGA 2450
    KPYKEEIEDL KMKLVKIDLE KMKNAKEFEK EISATKATVE YQKEVIRLLR 2500
    ENLRRSQQAQ DTSVISEHTD PQPSNKPLTC GGGSGIVQNT KALILKSEHI 2550
    RLEKEISKLK QQNEQLIKQK NELLSNNQHL SNEVKTWKER TLKREAHKQV 2600
    TCENSPKSPK VTGTASKKKQ ITPSQCKERN LQDPVPKESP KSCFFDSRSK 2650
    SLPSPHPVRY FDNSSLGLCP EVQNAGAESV DSQPGPWHAS SGKDVPECKT 2700
    Q 2701
    Length:2,701
    Mass (Da):316,415
    Last modified:October 23, 2007 - v2
    Checksum:i4BC59C2EF0B02D88
    GO
    Isoform 2 (identifier: Q02224-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2131-2166: Missing.

    Show »
    Length:2,665
    Mass (Da):312,149
    Checksum:iFD0951C16BECB82A
    GO
    Isoform 3 (identifier: Q02224-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         549-573: Missing.
         1972-2068: IQELQKKELQ...IATLREMIAR → Q

    Show »
    Length:2,580
    Mass (Da):301,789
    Checksum:iC5EC35EE9A5E5524
    GO

    Sequence cautioni

    The sequence BAE06078.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti51 – 511R → H in BAF83051. (PubMed:14702039)Curated
    Sequence conflicti300 – 3001A → P in CAA78727. (PubMed:1406971)Curated
    Sequence conflicti440 – 4401F → S in BAE06078. 1 PublicationCurated
    Sequence conflicti566 – 5661A → R in CAA78727. (PubMed:1406971)Curated
    Sequence conflicti902 – 9021T → P in CAA78727. (PubMed:1406971)Curated
    Sequence conflicti1297 – 12971E → K in CAA78727. (PubMed:1406971)Curated
    Sequence conflicti1546 – 15461K → N in CAA78727. (PubMed:1406971)Curated
    Sequence conflicti1876 – 18761K → E in CAA78727. (PubMed:1406971)Curated
    Sequence conflicti2008 – 201710AQNLSMQSVR → PNYLCKCE in CAA78727. (PubMed:1406971)Curated
    Sequence conflicti2190 – 21901S → C in CAA78727. (PubMed:1406971)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1535 – 15351F → L.1 Publication
    Corresponds to variant rs2615542 [ dbSNP | Ensembl ].
    VAR_049689
    Natural varianti1581 – 15811S → R.
    Corresponds to variant rs35100664 [ dbSNP | Ensembl ].
    VAR_049690
    Natural varianti1911 – 19111S → T.
    Corresponds to variant rs1381657 [ dbSNP | Ensembl ].
    VAR_059370
    Natural varianti1925 – 19251E → D.
    Corresponds to variant rs2306106 [ dbSNP | Ensembl ].
    VAR_049691
    Natural varianti2090 – 20901T → M.1 Publication
    Corresponds to variant rs2243682 [ dbSNP | Ensembl ].
    VAR_049692

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei549 – 57325Missing in isoform 3. 1 PublicationVSP_028820Add
    BLAST
    Alternative sequencei1972 – 206897IQELQ…EMIAR → Q in isoform 3. 1 PublicationVSP_028821Add
    BLAST
    Alternative sequencei2131 – 216636Missing in isoform 2. 1 PublicationVSP_028822Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z15005 mRNA. Translation: CAA78727.1.
    AB209996 mRNA. Translation: BAE06078.1. Different initiation.
    AC079919 Genomic DNA. No translation available.
    CH471057 Genomic DNA. Translation: EAX06171.1.
    AK290362 mRNA. Translation: BAF83051.1.
    CCDSiCCDS34042.1. [Q02224-1]
    CCDS68768.1. [Q02224-3]
    PIRiS28261.
    RefSeqiNP_001273663.1. NM_001286734.1. [Q02224-3]
    NP_001804.2. NM_001813.2. [Q02224-1]
    UniGeneiHs.75573.

    Genome annotation databases

    EnsembliENST00000265148; ENSP00000265148; ENSG00000138778. [Q02224-1]
    ENST00000380026; ENSP00000369365; ENSG00000138778. [Q02224-3]
    GeneIDi1062.
    KEGGihsa:1062.
    UCSCiuc003hxb.1. human. [Q02224-1]
    uc003hxc.1. human. [Q02224-3]

    Polymorphism databases

    DMDMi160358869.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z15005 mRNA. Translation: CAA78727.1 .
    AB209996 mRNA. Translation: BAE06078.1 . Different initiation.
    AC079919 Genomic DNA. No translation available.
    CH471057 Genomic DNA. Translation: EAX06171.1 .
    AK290362 mRNA. Translation: BAF83051.1 .
    CCDSi CCDS34042.1. [Q02224-1 ]
    CCDS68768.1. [Q02224-3 ]
    PIRi S28261.
    RefSeqi NP_001273663.1. NM_001286734.1. [Q02224-3 ]
    NP_001804.2. NM_001813.2. [Q02224-1 ]
    UniGenei Hs.75573.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1T5C X-ray 2.50 A/B 2-342 [» ]
    ProteinModelPortali Q02224.
    SMRi Q02224. Positions 4-339.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107491. 18 interactions.
    IntActi Q02224. 9 interactions.
    MINTi MINT-5002721.
    STRINGi 9606.ENSP00000265148.

    Chemistry

    BindingDBi Q02224.
    ChEMBLi CHEMBL5870.

    PTM databases

    PhosphoSitei Q02224.

    Polymorphism databases

    DMDMi 160358869.

    Proteomic databases

    MaxQBi Q02224.
    PaxDbi Q02224.
    PRIDEi Q02224.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265148 ; ENSP00000265148 ; ENSG00000138778 . [Q02224-1 ]
    ENST00000380026 ; ENSP00000369365 ; ENSG00000138778 . [Q02224-3 ]
    GeneIDi 1062.
    KEGGi hsa:1062.
    UCSCi uc003hxb.1. human. [Q02224-1 ]
    uc003hxc.1. human. [Q02224-3 ]

    Organism-specific databases

    CTDi 1062.
    GeneCardsi GC04M104027.
    H-InvDB HIX0031416.
    HGNCi HGNC:1856. CENPE.
    HPAi HPA042294.
    MIMi 117143. gene.
    neXtProti NX_Q02224.
    PharmGKBi PA26400.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5059.
    HOGENOMi HOG000111540.
    HOVERGENi HBG097734.
    InParanoidi Q02224.
    KOi K11498.
    OMAi NERMNQE.
    OrthoDBi EOG7J9VNX.
    PhylomeDBi Q02224.
    TreeFami TF330343.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_25201. Kinesins.
    REACT_682. Mitotic Prometaphase.

    Miscellaneous databases

    EvolutionaryTracei Q02224.
    GeneWikii Centromere_protein_E.
    GenomeRNAii 1062.
    NextBioi 4442.
    PROi Q02224.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q02224.
    Bgeei Q02224.
    CleanExi HS_CENPE.
    Genevestigatori Q02224.

    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. "CENP-E is a putative kinetochore motor that accumulates just before mitosis."
      Yen T.J., Li G., Schaar B.T., Szilak I., Cleveland D.W.
      Nature 359:536-539(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS LEU-1535 AND MET-2090.
    2. "Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
      Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1126 (ISOFORMS 1/2).
      Tissue: Tongue.
    6. "Mitotic HeLa cells contain a CENP-E-associated minus end-directed microtubule motor."
      Thrower D.A., Jordan M.A., Schaar B.T., Yen T.J., Wilson L.
      EMBO J. 14:918-926(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    7. "Characterization of the kinetochore binding domain of CENP-E reveals interactions with the kinetochore proteins CENP-F and hBUBR1."
      Chan G.K.T., Schaar B.T., Yen T.J.
      J. Cell Biol. 143:49-63(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CENPF AND BUBR1, SUBCELLULAR LOCATION.
    8. "Farnesyl transferase inhibitors block the farnesylation of CENP-E and CENP-F and alter the association of CENP-E with the microtubules."
      Ashar H.R., James L., Gray K., Carr D., Black S., Armstrong L., Bishop W.R., Kirschmeier P.
      J. Biol. Chem. 275:30451-30457(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISOPRENYLATION AT CYS-2698.
    9. "Essential roles of KIF4 and its binding partner PRC1 in organized central spindle midzone formation."
      Kurasawa Y., Earnshaw W.C., Mochizuki Y., Dohmae N., Todokoro K.
      EMBO J. 23:3237-3248(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRC1.
    10. "Human NUF2 interacts with centromere-associated protein E and is essential for a stable spindle microtubule-kinetochore attachment."
      Liu D., Ding X., Du J., Cai X., Huang Y., Ward T., Shaw A., Yang Y., Hu R., Jin C., Yao X.
      J. Biol. Chem. 282:21415-21424(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NUF2, SUBCELLULAR LOCATION.
    11. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
      Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
      Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1937.
      Tissue: Mammary cancer.
    12. "Septin 7 interacts with centromere-associated protein E and is required for its kinetochore localization."
      Zhu M., Wang F., Yan F., Yao P.Y., Du J., Gao X., Wang X., Wu Q., Ward T., Li J., Kioko S., Hu R., Xie W., Ding X., Yao X.
      J. Biol. Chem. 283:18916-18925(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SEPT7, SUBCELLULAR LOCATION.
    13. "SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis."
      Zhang X.-D., Goeres J., Zhang H., Yen T.J., Porter A.C.G., Matunis M.J.
      Mol. Cell 29:729-741(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION, SUBCELLULAR LOCATION.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2647, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Defects in chromosome congression and mitotic progression in KIF18A-deficient cells are partly mediated through impaired functions of CENP-E."
      Huang Y., Yao Y., Xu H.-Z., Wang Z.-G., Lu L., Dai W.
      Cell Cycle 8:2643-2649(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KIF18A AND BUB1B.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "CENP-E kinesin interacts with SKAP protein to orchestrate accurate chromosome segregation in mitosis."
      Huang Y., Wang W., Yao P., Wang X., Liu X., Zhuang X., Yan F., Zhou J., Du J., Ward T., Zou H., Zhang J., Fang G., Ding X., Dou Z., Yao X.
      J. Biol. Chem. 287:1500-1509(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKAP.
    18. "Crystal structure of the motor domain of the human kinetochore protein CENP-E."
      Garcia-Saez I., Yen T., Wade R.H., Kozielski F.
      J. Mol. Biol. 340:1107-1116(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-342 IN COMPLEX WITH ADP, PROTEIN SEQUENCE OF 2-7, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.

    Entry informationi

    Entry nameiCENPE_HUMAN
    AccessioniPrimary (citable) accession number: Q02224
    Secondary accession number(s): A6NKY9, A8K2U7, Q4LE75
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: October 23, 2007
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3