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UniProtKB - Q02224 (CENPE_HUMAN)

Protein

Centromere-associated protein E

Gene

CENPE

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionDevelopmental protein, Motor protein
Biological processCell cycle, Cell division, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-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
SIGNORiQ02224

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000138778.11
HGNCiHGNC:1856 CENPE
MIMi117143 gene
neXtProtiNX_Q02224

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 dbSNP:rs144716013EnsemblClinVar.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 dbSNP:rs141488085EnsemblClinVar.1

Keywords - Diseasei

Disease mutation, Primary microcephaly

Organism-specific databases

DisGeNETi1062
MalaCardsiCENPE
MIMi616051 phenotype
OpenTargetsiENSG00000138778
PharmGKBiPA26400

Chemistry databases

ChEMBLiCHEMBL5870
DrugBankiDB06097 GSK-923295

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

Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

Proteomic databases

EPDiQ02224
MaxQBiQ02224
PaxDbiQ02224
PeptideAtlasiQ02224
PRIDEiQ02224
ProteomicsDBi58063
58064 [Q02224-2]
58065 [Q02224-3]

PTM databases

iPTMnetiQ02224
PhosphoSitePlusiQ02224

Expressioni

Gene expression databases

BgeeiENSG00000138778 Expressed in 112 organ(s), highest expression level in oocyte
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

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi107491, 41 interactors
DIPiDIP-38902N
IntActiQ02224, 26 interactors
MINTiQ02224
STRINGi9606.ENSP00000265148

Chemistry databases

BindingDBiQ02224

Structurei

Secondary structure

12701
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0242 Eukaryota
COG5059 LUCA
GeneTreeiENSGT00910000143992
HOGENOMiHOG000111540
HOVERGENiHBG097734
InParanoidiQ02224
KOiK11498
OMAiSVCRASW
OrthoDBiEOG091G0CFT
PhylomeDBiQ02224
TreeFamiTF330343

Family and domain databases

Gene3Di3.40.850.10, 1 hit
InterProiView protein in InterPro
IPR027640 Kinesin-like_fam
IPR019821 Kinesin_motor_CS
IPR001752 Kinesin_motor_dom
IPR036961 Kinesin_motor_dom_sf
IPR027417 P-loop_NTPase
PANTHERiPTHR24115 PTHR24115, 2 hits
PfamiView protein in Pfam
PF00225 Kinesin, 1 hit
PRINTSiPR00380 KINESINHEAVY
SMARTiView protein in SMART
SM00129 KISc, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00411 KINESIN_MOTOR_1, 1 hit
PS50067 KINESIN_MOTOR_2, 1 hit

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

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D6RBW0D6RBW0_HUMAN
Centromere-associated protein E
CENPE
1,126Annotation score:
A0A087X0P0A0A087X0P0_HUMAN
Centromere-associated protein E
CENPE
2,664Annotation score:
D6RHK2D6RHK2_HUMAN
Centromere-associated protein E
CENPE
183Annotation score:

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 dbSNP:rs144716013EnsemblClinVar.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 dbSNP:rs141488085EnsemblClinVar.1
Natural variantiVAR_0496891535F → L2 PublicationsCorresponds to variant dbSNP:rs2615542Ensembl.1
Natural variantiVAR_0496901581S → R. Corresponds to variant dbSNP:rs35100664Ensembl.1
Natural variantiVAR_0593701911S → T. Corresponds to variant dbSNP:rs1381657Ensembl.1
Natural variantiVAR_0496911925E → D. Corresponds to variant dbSNP:rs2306106Ensembl.1
Natural variantiVAR_0496922090T → M2 PublicationsCorresponds to variant dbSNP:rs2243682Ensembl.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

Similar proteinsi

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/F336-371[»]
ProteinModelPortaliQ02224
SMRiQ02224
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107491, 41 interactors
DIPiDIP-38902N
IntActiQ02224, 26 interactors
MINTiQ02224
STRINGi9606.ENSP00000265148

Chemistry databases

BindingDBiQ02224
ChEMBLiCHEMBL5870
DrugBankiDB06097 GSK-923295

PTM databases

iPTMnetiQ02224
PhosphoSitePlusiQ02224

Polymorphism and mutation databases

BioMutaiCENPE
DMDMi160358869

Proteomic databases

EPDiQ02224
MaxQBiQ02224
PaxDbiQ02224
PeptideAtlasiQ02224
PRIDEiQ02224
ProteomicsDBi58063
58064 [Q02224-2]
58065 [Q02224-3]

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
EuPathDBiHostDB:ENSG00000138778.11
GeneCardsiCENPE
H-InvDBiHIX0031416
HGNCiHGNC:1856 CENPE
HPAiHPA042294
MalaCardsiCENPE
MIMi117143 gene
616051 phenotype
neXtProtiNX_Q02224
OpenTargetsiENSG00000138778
PharmGKBiPA26400
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0242 Eukaryota
COG5059 LUCA
GeneTreeiENSGT00910000143992
HOGENOMiHOG000111540
HOVERGENiHBG097734
InParanoidiQ02224
KOiK11498
OMAiSVCRASW
OrthoDBiEOG091G0CFT
PhylomeDBiQ02224
TreeFamiTF330343

Enzyme and pathway databases

ReactomeiR-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-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
SIGNORiQ02224

Miscellaneous databases

ChiTaRSiCENPE human
EvolutionaryTraceiQ02224
GeneWikiiCentromere_protein_E
GenomeRNAii1062
PROiPR:Q02224
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000138778 Expressed in 112 organ(s), highest expression level in oocyte
CleanExiHS_CENPE
ExpressionAtlasiQ02224 baseline and differential
GenevisibleiQ02224 HS

Family and domain databases

Gene3Di3.40.850.10, 1 hit
InterProiView protein in InterPro
IPR027640 Kinesin-like_fam
IPR019821 Kinesin_motor_CS
IPR001752 Kinesin_motor_dom
IPR036961 Kinesin_motor_dom_sf
IPR027417 P-loop_NTPase
PANTHERiPTHR24115 PTHR24115, 2 hits
PfamiView protein in Pfam
PF00225 Kinesin, 1 hit
PRINTSiPR00380 KINESINHEAVY
SMARTiView protein in SMART
SM00129 KISc, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00411 KINESIN_MOTOR_1, 1 hit
PS50067 KINESIN_MOTOR_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCENPE_HUMAN
AccessioniPrimary (citable) accession number: Q02224
Secondary accession number(s): A6NKY9, A8K2U7, Q4LE75
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 23, 2007
Last modified: September 12, 2018
This is version 189 of the entry and version 2 of the sequence. See 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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