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Protein

Centromere-associated protein E

Gene

CENPE

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. ATPase activity Source: GO_Central
  2. ATP binding Source: UniProtKB-KW
  3. kinetochore binding Source: UniProtKB
  4. microtubule motor activity Source: UniProtKB

GO - Biological processi

  1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  2. attachment of mitotic spindle microtubules to kinetochore Source: UniProtKB
  3. blood coagulation Source: Reactome
  4. cell division Source: UniProtKB-KW
  5. chromosome segregation Source: UniProtKB
  6. kinetochore assembly Source: UniProtKB
  7. metabolic process Source: GOC
  8. microtubule-based movement Source: GO_Central
  9. mitotic cell cycle Source: UniProtKB
  10. mitotic chromosome movement towards spindle pole Source: ProtInc
  11. mitotic metaphase plate congression Source: UniProtKB
  12. multicellular organismal development Source: UniProtKB-KW
  13. positive regulation of protein kinase activity Source: UniProtKB
  14. regulation of mitotic metaphase/anaphase transition 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 Componenti: 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 Source: UniProtKB
  2. chromosome, centromeric region Source: UniProtKB
  3. condensed chromosome, centromeric region Source: UniProtKB
  4. condensed chromosome outer kinetochore Source: Ensembl
  5. condensed nuclear chromosome kinetochore Source: Ensembl
  6. cytoplasm Source: HPA
  7. cytosol Source: Reactome
  8. kinesin complex Source: GO_Central
  9. kinetochore Source: UniProtKB
  10. membrane Source: UniProtKB
  11. microtubule Source: UniProtKB
  12. microtubule cytoskeleton Source: HPA
  13. midbody Source: UniProtKB
  14. mitotic spindle midzone Source: UniProtKB
  15. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule

Pathology & Biotechi

Involvement in diseasei

Microcephaly 13, primary, autosomal recessive (MCPH13)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age-related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small.

See also OMIM:616051
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti933 – 9331D → N in MCPH13; results in defective mitotic spindle formation and chromosome segregation; results in delayed mitotic progression. 1 Publication
Corresponds to variant rs144716013 [ dbSNP | Ensembl ].
VAR_072429
Natural varianti1355 – 13551K → E in MCPH13; results in defective mitotic spindle formation and chromosome segregation; results in delayed mitotic progression. 1 Publication
Corresponds to variant rs141488085 [ dbSNP | Ensembl ].
VAR_072430

Keywords - Diseasei

Disease mutation, Primary microcephaly

Organism-specific databases

MIMi616051. phenotype.
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

BgeeiQ02224.
CleanExiHS_CENPE.
ExpressionAtlasiQ02224. baseline and differential.
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 – 137Combined sources
Turni22 – 254Combined sources
Beta strandi31 – 344Combined sources
Beta strandi37 – 404Combined sources
Beta strandi46 – 483Combined sources
Helixi59 – 657Combined sources
Helixi68 – 758Combined sources
Beta strandi80 – 878Combined sources
Helixi92 – 965Combined sources
Beta strandi100 – 1034Combined sources
Helixi105 – 11612Combined sources
Helixi117 – 1193Combined sources
Beta strandi123 – 13513Combined sources
Beta strandi138 – 1469Combined sources
Turni157 – 1593Combined sources
Helixi175 – 18713Combined sources
Beta strandi190 – 1978Combined sources
Turni199 – 2024Combined sources
Beta strandi204 – 21512Combined sources
Beta strandi226 – 23510Combined sources
Helixi239 – 2413Combined sources
Beta strandi254 – 2563Combined sources
Helixi260 – 27415Combined sources
Helixi283 – 2853Combined sources
Helixi287 – 2915Combined sources
Helixi293 – 2953Combined sources
Beta strandi298 – 30811Combined sources
Helixi314 – 32613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00770000120453.
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. AlignAdd to basket

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

        10         20         30         40         50
MAEEGAVAVC VRVRPLNSRE ESLGETAQVY WKTDNNVIYQ VDGSKSFNFD
60 70 80 90 100
RVFHGNETTK NVYEEIAAPI IDSAIQGYNG TIFAYGQTAS GKTYTMMGSE
110 120 130 140 150
DHLGVIPRAI HDIFQKIKKF PDREFLLRVS YMEIYNETIT DLLCGTQKMK
160 170 180 190 200
PLIIREDVNR NVYVADLTEE VVYTSEMALK WITKGEKSRH YGETKMNQRS
210 220 230 240 250
SRSHTIFRMI LESREKGEPS NCEGSVKVSH LNLVDLAGSE RAAQTGAAGV
260 270 280 290 300
RLKEGCNINR SLFILGQVIK KLSDGQVGGF INYRDSKLTR ILQNSLGGNA
310 320 330 340 350
KTRIICTITP VSFDETLTAL QFASTAKYMK NTPYVNEVST DEALLKRYRK
360 370 380 390 400
EIMDLKKQLE EVSLETRAQA MEKDQLAQLL EEKDLLQKVQ NEKIENLTRM
410 420 430 440 450
LVTSSSLTLQ QELKAKRKRR VTWCLGKINK MKNSNYADQF NIPTNITTKT
460 470 480 490 500
HKLSINLLRE IDESVCSESD VFSNTLDTLS EIEWNPATKL LNQENIESEL
510 520 530 540 550
NSLRADYDNL VLDYEQLRTE KEEMELKLKE KNDLDEFEAL ERKTKKDQEM
560 570 580 590 600
QLIHEISNLK NLVKHAEVYN QDLENELSSK VELLREKEDQ IKKLQEYIDS
610 620 630 640 650
QKLENIKMDL SYSLESIEDP KQMKQTLFDA ETVALDAKRE SAFLRSENLE
660 670 680 690 700
LKEKMKELAT TYKQMENDIQ LYQSQLEAKK KMQVDLEKEL QSAFNEITKL
710 720 730 740 750
TSLIDGKVPK DLLCNLELEG KITDLQKELN KEVEENEALR EEVILLSELK
760 770 780 790 800
SLPSEVERLR KEIQDKSEEL HIITSEKDKL FSEVVHKESR VQGLLEEIGK
810 820 830 840 850
TKDDLATTQS NYKSTDQEFQ NFKTLHMDFE QKYKMVLEEN ERMNQEIVNL
860 870 880 890 900
SKEAQKFDSS LGALKTELSY KTQELQEKTR EVQERLNEME QLKEQLENRD
910 920 930 940 950
STLQTVEREK TLITEKLQQT LEEVKTLTQE KDDLKQLQES LQIERDQLKS
960 970 980 990 1000
DIHDTVNMNI DTQEQLRNAL ESLKQHQETI NTLKSKISEE VSRNLHMEEN
1010 1020 1030 1040 1050
TGETKDEFQQ KMVGIDKKQD LEAKNTQTLT ADVKDNEIIE QQRKIFSLIQ
1060 1070 1080 1090 1100
EKNELQQMLE SVIAEKEQLK TDLKENIEMT IENQEELRLL GDELKKQQEI
1110 1120 1130 1140 1150
VAQEKNHAIK KEGELSRTCD RLAEVEEKLK EKSQQLQEKQ QQLLNVQEEM
1160 1170 1180 1190 1200
SEMQKKINEI ENLKNELKNK ELTLEHMETE RLELAQKLNE NYEEVKSITK
1210 1220 1230 1240 1250
ERKVLKELQK SFETERDHLR GYIREIEATG LQTKEELKIA HIHLKEHQET
1260 1270 1280 1290 1300
IDELRRSVSE KTAQIINTQD LEKSHTKLQE EIPVLHEEQE LLPNVKEVSE
1310 1320 1330 1340 1350
TQETMNELEL LTEQSTTKDS TTLARIEMER LRLNEKFQES QEEIKSLTKE
1360 1370 1380 1390 1400
RDNLKTIKEA LEVKHDQLKE HIRETLAKIQ ESQSKQEQSL NMKEKDNETT
1410 1420 1430 1440 1450
KIVSEMEQFK PKDSALLRIE IEMLGLSKRL QESHDEMKSV AKEKDDLQRL
1460 1470 1480 1490 1500
QEVLQSESDQ LKENIKEIVA KHLETEEELK VAHCCLKEQE ETINELRVNL
1510 1520 1530 1540 1550
SEKETEISTI QKQLEAINDK LQNKIQEIYE KEEQFNIKQI SEVQEKVNEL
1560 1570 1580 1590 1600
KQFKEHRKAK DSALQSIESK MLELTNRLQE SQEEIQIMIK EKEEMKRVQE
1610 1620 1630 1640 1650
ALQIERDQLK ENTKEIVAKM KESQEKEYQF LKMTAVNETQ EKMCEIEHLK
1660 1670 1680 1690 1700
EQFETQKLNL ENIETENIRL TQILHENLEE MRSVTKERDD LRSVEETLKV
1710 1720 1730 1740 1750
ERDQLKENLR ETITRDLEKQ EELKIVHMHL KEHQETIDKL RGIVSEKTNE
1760 1770 1780 1790 1800
ISNMQKDLEH SNDALKAQDL KIQEELRIAH MHLKEQQETI DKLRGIVSEK
1810 1820 1830 1840 1850
TDKLSNMQKD LENSNAKLQE KIQELKANEH QLITLKKDVN ETQKKVSEME
1860 1870 1880 1890 1900
QLKKQIKDQS LTLSKLEIEN LNLAQKLHEN LEEMKSVMKE RDNLRRVEET
1910 1920 1930 1940 1950
LKLERDQLKE SLQETKARDL EIQQELKTAR MLSKEHKETV DKLREKISEK
1960 1970 1980 1990 2000
TIQISDIQKD LDKSKDELQK KIQELQKKEL QLLRVKEDVN MSHKKINEME
2010 2020 2030 2040 2050
QLKKQFEAQN LSMQSVRMDN FQLTKKLHES LEEIRIVAKE RDELRRIKES
2060 2070 2080 2090 2100
LKMERDQFIA TLREMIARDR QNHQVKPEKR LLSDGQQHLT ESLREKCSRI
2110 2120 2130 2140 2150
KELLKRYSEM DDHYECLNRL SLDLEKEIEF QKELSMRVKA NLSLPYLQTK
2160 2170 2180 2190 2200
HIEKLFTANQ RCSMEFHRIM KKLKYVLSYV TKIKEEQHES INKFEMDFID
2210 2220 2230 2240 2250
EVEKQKELLI KIQHLQQDCD VPSRELRDLK LNQNMDLHIE EILKDFSESE
2260 2270 2280 2290 2300
FPSIKTEFQQ VLSNRKEMTQ FLEEWLNTRF DIEKLKNGIQ KENDRICQVN
2310 2320 2330 2340 2350
NFFNNRIIAI MNESTEFEER SATISKEWEQ DLKSLKEKNE KLFKNYQTLK
2360 2370 2380 2390 2400
TSLASGAQVN PTTQDNKNPH VTSRATQLTT EKIRELENSL HEAKESAMHK
2410 2420 2430 2440 2450
ESKIIKMQKE LEVTNDIIAK LQAKVHESNK CLEKTKETIQ VLQDKVALGA
2460 2470 2480 2490 2500
KPYKEEIEDL KMKLVKIDLE KMKNAKEFEK EISATKATVE YQKEVIRLLR
2510 2520 2530 2540 2550
ENLRRSQQAQ DTSVISEHTD PQPSNKPLTC GGGSGIVQNT KALILKSEHI
2560 2570 2580 2590 2600
RLEKEISKLK QQNEQLIKQK NELLSNNQHL SNEVKTWKER TLKREAHKQV
2610 2620 2630 2640 2650
TCENSPKSPK VTGTASKKKQ ITPSQCKERN LQDPVPKESP KSCFFDSRSK
2660 2670 2680 2690 2700
SLPSPHPVRY FDNSSLGLCP EVQNAGAESV DSQPGPWHAS SGKDVPECKT

Q
Length:2,701
Mass (Da):316,415
Last modified:October 22, 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.Curated

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 (Ref. 2) Curated
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 varianti933 – 9331D → N in MCPH13; results in defective mitotic spindle formation and chromosome segregation; results in delayed mitotic progression. 1 Publication
Corresponds to variant rs144716013 [ dbSNP | Ensembl ].
VAR_072429
Natural varianti1355 – 13551K → E in MCPH13; results in defective mitotic spindle formation and chromosome segregation; results in delayed mitotic progression. 1 Publication
Corresponds to variant rs141488085 [ dbSNP | Ensembl ].
VAR_072430
Natural varianti1535 – 15351F → L.2 Publications
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.2 Publications
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

BindingDBiQ02224.
ChEMBLiCHEMBL5870.

PTM databases

PhosphoSiteiQ02224.

Polymorphism databases

DMDMi160358869.

Proteomic databases

MaxQBiQ02224.
PaxDbiQ02224.
PRIDEiQ02224.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi1062.
GeneCardsiGC04M104027.
H-InvDBHIX0031416.
HGNCiHGNC:1856. CENPE.
HPAiHPA042294.
MIMi117143. gene.
616051. phenotype.
neXtProtiNX_Q02224.
PharmGKBiPA26400.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5059.
GeneTreeiENSGT00770000120453.
HOGENOMiHOG000111540.
HOVERGENiHBG097734.
InParanoidiQ02224.
KOiK11498.
OMAiNERMNQE.
OrthoDBiEOG7J9VNX.
PhylomeDBiQ02224.
TreeFamiTF330343.

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.

Miscellaneous databases

ChiTaRSiCENPE. human.
EvolutionaryTraceiQ02224.
GeneWikiiCentromere_protein_E.
GenomeRNAii1062.
NextBioi4442.
PROiQ02224.
SOURCEiSearch...

Gene expression databases

BgeeiQ02224.
CleanExiHS_CENPE.
ExpressionAtlasiQ02224. baseline and differential.
GenevestigatoriQ02224.

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]
ProtoNetiSearch...

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(1991) [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 (FEB-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(2004) [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(2003) [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(1994) [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(1997) [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(1999) [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(2003) [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(2006) [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(2006) [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(2007) [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(2007) [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(2008) [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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SKAP.
  18. "Mutations in CENPE define a novel kinetochore-centromeric mechanism for microcephalic primordial dwarfism."
    Mirzaa G.M., Vitre B., Carpenter G., Abramowicz I., Gleeson J.G., Paciorkowski A.R., Cleveland D.W., Dobyns W.B., O'Driscoll M.
    Hum. Genet. 133:1023-1039(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MCPH13, VARIANTS MCPH13 ASN-933 AND GLU-1355, CHARACTERIZATION OF VARIANTS MCPH13 ASN-933 AND GLU-1355, VARIANTS LEU-1535 AND MET-2090.
  19. "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(2003) [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: June 30, 1993
Last sequence update: October 22, 2007
Last modified: March 3, 2015
This is version 153 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.