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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

Microtubule plus-end-directed kinetochore motor which plays an important role in chromosome congression, microtubule-kinetochore conjugation and spindle assembly checkpoint activation. Drives chromosome congression (alignment of chromosomes at the spindle equator resulting in the formation of the metaphase plate) by mediating the lateral sliding of polar chromosomes along spindle microtubules towards the spindle equator and by aiding the establishment and maintenance of connections between kinetochores and spindle microtubules (PubMed:7889940, PubMed:23891108, PubMed:25395579). The transport of pole-proximal chromosomes towards the spindle equator is favored by microtubule tracks that are detyrosinated (PubMed:25908662). Acts as a processive bi-directional tracker of dynamic microtubule tips; after chromosomes have congressed, continues to play an active role at kinetochores, enhancing their links with dynamic microtubule ends (PubMed:23955301). Suppresses chromosome congression in NDC80-depleted cells and contributes positively to congression only when microtubules are stabilized (PubMed:25743205). Plays an important role in the formation of stable attachments between kinetochores and spindle microtubules (PubMed:17535814) The stabilization of kinetochore-microtubule attachment also requires CENPE-dependent localization of other proteins to the kinetochore including BUB1B, MAD1 and MAD2. Plays a role in spindle assembly checkpoint activation (SAC) via its interaction with BUB1B resulting in the activation of its kinase activity, which is important for activating SAC. Necessary for the mitotic checkpoint signal at individual kinetochores to prevent aneuploidy due to single chromosome loss (By similarity).By similarity7 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi86 – 93ATP8

GO - Molecular functioni

  • ATPase activity Source: GO_Central
  • ATP binding Source: UniProtKB-KW
  • kinetochore binding Source: UniProtKB
  • microtubule motor activity Source: UniProtKB

GO - Biological processi

  • antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  • attachment of mitotic spindle microtubules to kinetochore Source: UniProtKB
  • cell division Source: UniProtKB-KW
  • chromosome segregation Source: UniProtKB
  • kinetochore assembly Source: UniProtKB
  • lateral attachment of mitotic spindle microtubules to kinetochore Source: UniProtKB
  • metaphase plate congression Source: UniProtKB
  • microtubule-based movement Source: Reactome
  • mitotic cell cycle Source: UniProtKB
  • mitotic chromosome movement towards spindle pole Source: ProtInc
  • mitotic metaphase plate congression Source: UniProtKB
  • multicellular organism development Source: UniProtKB-KW
  • positive regulation of protein kinase activity Source: UniProtKB
  • regulation of mitotic metaphase/anaphase transition Source: UniProtKB
  • retrograde vesicle-mediated transport, Golgi to ER Source: Reactome
  • sister chromatid cohesion Source: Reactome
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

BioCyciZFISH:ENSG00000138778-MONOMER.
ReactomeiR-HSA-2132295. MHC class II antigen presentation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-983189. Kinesins.

Names & Taxonomyi

Protein namesi
Recommended name:
Centromere-associated protein E
Alternative name(s):
Centromere protein E
Short name:
CENP-E
Kinesin-71 Publication
Kinesin-related protein CENPE
Gene namesi
Name:CENPE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:1856. CENPE.

Subcellular locationi

GO - Cellular componenti

  • chromosome Source: UniProtKB
  • chromosome, centromeric region Source: UniProtKB
  • condensed chromosome, centromeric region Source: UniProtKB
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • kinesin complex Source: GO_Central
  • kinetochore Source: UniProtKB
  • membrane Source: UniProtKB
  • microtubule Source: UniProtKB
  • microtubule cytoskeleton Source: HPA
  • midbody Source: UniProtKB
  • mitotic spindle midzone Source: UniProtKB
  • 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)DescriptionActionsGraphical viewLength
Natural variantiVAR_072429933D → N in MCPH13; results in defective mitotic spindle formation and chromosome segregation; results in delayed mitotic progression. 1 PublicationCorresponds to variant rs144716013dbSNPEnsembl.1
Natural variantiVAR_0724301355K → E in MCPH13; results in defective mitotic spindle formation and chromosome segregation; results in delayed mitotic progression. 1 PublicationCorresponds to variant rs141488085dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Primary microcephaly

Organism-specific databases

DisGeNETi1062.
MalaCardsiCENPE.
MIMi616051. phenotype.
OpenTargetsiENSG00000138778.
PharmGKBiPA26400.

Chemistry databases

ChEMBLiCHEMBL5870.

Polymorphism and mutation databases

BioMutaiCENPE.
DMDMi160358869.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001254361 – 2698Centromere-associated protein EAdd BLAST2698
PropeptideiPRO_00003967422699 – 2701Removed in mature formCurated3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei611PhosphoserineCombined sources1
Modified residuei2083PhosphoserineCombined sources1
Modified residuei2389PhosphoserineCombined sources1
Modified residuei2639PhosphoserineCombined sources1
Modified residuei2647PhosphoserineCombined sources1
Modified residuei2651PhosphoserineCombined sources1
Modified residuei2698Cysteine methyl esterCurated1
Lipidationi2698S-farnesyl cysteine1 Publication1

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

EPDiQ02224.
MaxQBiQ02224.
PaxDbiQ02224.
PeptideAtlasiQ02224.
PRIDEiQ02224.

PTM databases

iPTMnetiQ02224.
PhosphoSitePlusiQ02224.

Expressioni

Gene expression databases

BgeeiENSG00000138778.
CleanExiHS_CENPE.
ExpressionAtlasiQ02224. baseline and differential.
GenevisibleiQ02224. HS.

Organism-specific databases

HPAiHPA042294.

Interactioni

Subunit structurei

Monomer (PubMed:15236970). Interacts with CENPF (PubMed:9763420). Interacts with BUB1B (PubMed:9763420, PubMed:19625775). Interacts with SEPT7 (PubMed:18460473). Interacts with KIF18A (PubMed:19625775). Interacts with PRC1 (PubMed:15297875). Interacts with NUF2; this interaction determines kinetochore localization (PubMed:17535814). Interacts with SKAP; this interaction greatly favors SKAP binding to microtubules (PubMed:22110139). Interacts with TRAPPC12 (PubMed:25918224). Interacts with CTCF (PubMed:25395579).9 Publications

Binary interactionsi

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

GO - Molecular functioni

  • kinetochore binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107491. 38 interactors.
DIPiDIP-38902N.
IntActiQ02224. 23 interactors.
MINTiMINT-5002721.
STRINGi9606.ENSP00000265148.

Chemistry databases

BindingDBiQ02224.

Structurei

Secondary structure

12701
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 13Combined sources7
Turni22 – 25Combined sources4
Beta strandi31 – 34Combined sources4
Beta strandi37 – 40Combined sources4
Beta strandi46 – 48Combined sources3
Helixi59 – 65Combined sources7
Helixi68 – 75Combined sources8
Beta strandi80 – 87Combined sources8
Helixi92 – 96Combined sources5
Beta strandi100 – 103Combined sources4
Helixi105 – 116Combined sources12
Helixi117 – 119Combined sources3
Beta strandi123 – 135Combined sources13
Beta strandi138 – 146Combined sources9
Turni157 – 159Combined sources3
Helixi175 – 187Combined sources13
Beta strandi190 – 197Combined sources8
Turni199 – 202Combined sources4
Beta strandi204 – 215Combined sources12
Beta strandi226 – 235Combined sources10
Helixi239 – 241Combined sources3
Beta strandi254 – 256Combined sources3
Helixi260 – 274Combined sources15
Helixi283 – 285Combined sources3
Helixi287 – 291Combined sources5
Helixi293 – 295Combined sources3
Beta strandi298 – 308Combined sources11
Helixi314 – 326Combined sources13
Helixi341 – 375Combined sources35

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T5CX-ray2.50A/B2-342[»]
5JVPX-ray2.10A/B/C/D/E/F336-375[»]
A/B/C/D/E/F391-440[»]
A/B/C/D/E/F417-443[»]
ProteinModelPortaliQ02224.
SMRiQ02224.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02224.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 329Kinesin motorPROSITE-ProRule annotationAdd BLAST324

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2126 – 2476Kinetochore-binding domainAdd BLAST351
Regioni2510 – 2698Globular autoinhibitory domainBy similarityAdd BLAST189

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili336 – 2590Sequence analysisAdd BLAST2255

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

eggNOGiKOG0242. Eukaryota.
COG5059. LUCA.
GeneTreeiENSGT00860000133684.
HOGENOMiHOG000111540.
HOVERGENiHBG097734.
InParanoidiQ02224.
KOiK11498.
OMAiMKNSNYA.
OrthoDBiEOG091G0CFT.
PhylomeDBiQ02224.
TreeFamiTF330343.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR033066. CENP-E.
IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 6 hits.
PTHR24115:SF459. PTHR24115:SF459. 6 hits.
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 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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti51R → H in BAF83051 (PubMed:14702039).Curated1
Sequence conflicti300A → P in CAA78727 (PubMed:1406971).Curated1
Sequence conflicti440F → S in BAE06078 (Ref. 2) Curated1
Sequence conflicti566A → R in CAA78727 (PubMed:1406971).Curated1
Sequence conflicti902T → P in CAA78727 (PubMed:1406971).Curated1
Sequence conflicti1297E → K in CAA78727 (PubMed:1406971).Curated1
Sequence conflicti1546K → N in CAA78727 (PubMed:1406971).Curated1
Sequence conflicti1876K → E in CAA78727 (PubMed:1406971).Curated1
Sequence conflicti2008 – 2017AQNLSMQSVR → PNYLCKCE in CAA78727 (PubMed:1406971).Curated10
Sequence conflicti2190S → C in CAA78727 (PubMed:1406971).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_072429933D → N in MCPH13; results in defective mitotic spindle formation and chromosome segregation; results in delayed mitotic progression. 1 PublicationCorresponds to variant rs144716013dbSNPEnsembl.1
Natural variantiVAR_0724301355K → E in MCPH13; results in defective mitotic spindle formation and chromosome segregation; results in delayed mitotic progression. 1 PublicationCorresponds to variant rs141488085dbSNPEnsembl.1
Natural variantiVAR_0496891535F → L.2 PublicationsCorresponds to variant rs2615542dbSNPEnsembl.1
Natural variantiVAR_0496901581S → R.Corresponds to variant rs35100664dbSNPEnsembl.1
Natural variantiVAR_0593701911S → T.Corresponds to variant rs1381657dbSNPEnsembl.1
Natural variantiVAR_0496911925E → D.Corresponds to variant rs2306106dbSNPEnsembl.1
Natural variantiVAR_0496922090T → M.2 PublicationsCorresponds to variant rs2243682dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_028820549 – 573Missing in isoform 3. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_0288211972 – 2068IQELQ…EMIAR → Q in isoform 3. 1 PublicationAdd BLAST97
Alternative sequenceiVSP_0288222131 – 2166Missing in isoform 2. 1 PublicationAdd BLAST36

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]

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T5CX-ray2.50A/B2-342[»]
5JVPX-ray2.10A/B/C/D/E/F336-375[»]
A/B/C/D/E/F391-440[»]
A/B/C/D/E/F417-443[»]
ProteinModelPortaliQ02224.
SMRiQ02224.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107491. 38 interactors.
DIPiDIP-38902N.
IntActiQ02224. 23 interactors.
MINTiMINT-5002721.
STRINGi9606.ENSP00000265148.

Chemistry databases

BindingDBiQ02224.
ChEMBLiCHEMBL5870.

PTM databases

iPTMnetiQ02224.
PhosphoSitePlusiQ02224.

Polymorphism and mutation databases

BioMutaiCENPE.
DMDMi160358869.

Proteomic databases

EPDiQ02224.
MaxQBiQ02224.
PaxDbiQ02224.
PeptideAtlasiQ02224.
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]

Organism-specific databases

CTDi1062.
DisGeNETi1062.
GeneCardsiCENPE.
H-InvDBHIX0031416.
HGNCiHGNC:1856. CENPE.
HPAiHPA042294.
MalaCardsiCENPE.
MIMi117143. gene.
616051. phenotype.
neXtProtiNX_Q02224.
OpenTargetsiENSG00000138778.
PharmGKBiPA26400.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0242. Eukaryota.
COG5059. LUCA.
GeneTreeiENSGT00860000133684.
HOGENOMiHOG000111540.
HOVERGENiHBG097734.
InParanoidiQ02224.
KOiK11498.
OMAiMKNSNYA.
OrthoDBiEOG091G0CFT.
PhylomeDBiQ02224.
TreeFamiTF330343.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000138778-MONOMER.
ReactomeiR-HSA-2132295. MHC class II antigen presentation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-983189. Kinesins.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000138778.
CleanExiHS_CENPE.
ExpressionAtlasiQ02224. baseline and differential.
GenevisibleiQ02224. HS.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR033066. CENP-E.
IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 6 hits.
PTHR24115:SF459. PTHR24115:SF459. 6 hits.
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...

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: November 30, 2016
This is version 172 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

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 one 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.