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Q02224

- CENPE_HUMAN

UniProt

Q02224 - CENPE_HUMAN

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Protein

Centromere-associated protein E

Gene
CENPE
Organism
Homo sapiens (Human)
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

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
Complete GO annotation...

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.5 Publications

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. microtubule Source: UniProtKB
  10. microtubule cytoskeleton Source: HPA
  11. nucleus Source: UniProtKB
  12. spindle Source: UniProtKB-SubCell
Complete GO annotation...

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 form InferredPRO_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 ester Inferred
Lipidationi2698 – 26981S-farnesyl cysteine1 Publication

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.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.

Miscellaneous databases

EvolutionaryTraceiQ02224.

Family & Domainsi

Domains and Repeats

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

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili336 – 25902255 Reviewed predictionAdd
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.
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.

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. VSP_028820Add
BLAST
Alternative sequencei1972 – 206897IQELQ…EMIAR → Q in isoform 3. VSP_028821Add
BLAST
Alternative sequencei2131 – 216636Missing in isoform 2. VSP_028822Add
BLAST

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 147 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

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