UniProtKB - Q02224 (CENPE_HUMAN)
Protein
Centromere-associated protein E
Gene
CENPE
Organism
Homo sapiens (Human)
Status
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 86 – 93 | ATP | 8 |
GO - Molecular functioni
- ATPase activity Source: GO_Central
- ATP binding Source: UniProtKB-KW
- kinetochore binding Source: UniProtKB
- microtubule 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: GO_Central
- microtubule plus-end directed mitotic chromosome migration Source: UniProtKB
- mitotic cell cycle Source: UniProtKB
- mitotic chromosome movement towards spindle pole Source: UniProtKB
- mitotic metaphase plate congression Source: UniProtKB
- mitotic spindle organization 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 endoplasmic reticulum Source: Reactome
Keywordsi
Molecular function | Developmental protein, Motor protein |
Biological process | Cell cycle, Cell division, Mitosis |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactomei | R-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 |
SIGNORi | Q02224 |
Names & Taxonomyi
Protein namesi | Recommended name: Centromere-associated protein EAlternative name(s): Centromere protein E Short name: CENP-E Kinesin-71 Publication Kinesin-related protein CENPE |
Gene namesi | Name:CENPE |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000138778.11 |
HGNCi | HGNC:1856 CENPE |
MIMi | 117143 gene |
neXtProti | NX_Q02224 |
Subcellular locationi
Cytoskeleton
- spindle 1 Publication
Other locations
- kinetochore 6 Publications
- centromere 1 Publication
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 (By similarity). Recruited to the kinetochore in a SEPT7, CENPQ and TRAPPC12-dependent manner (PubMed:18460473, PubMed:25918224, PubMed:25395579). Recruited to the pericentromeric/centromeric regions of the chromosome in a CTCF-dependent manner (PubMed:26321640).By similarity4 Publications
Cytoskeleton
- kinesin complex Source: GO_Central
- kinetochore microtubule Source: UniProtKB
- microtubule Source: UniProtKB
- microtubule cytoskeleton Source: HPA
- mitotic spindle midzone Source: UniProtKB
- spindle midzone Source: UniProtKB
Cytosol
- cytosol Source: HPA
Nucleus
- nucleoplasm Source: HPA
- nucleus Source: UniProtKB
Other locations
- chromosome Source: UniProtKB
- chromosome, centromeric region Source: UniProtKB
- condensed chromosome kinetochore Source: UniProtKB-SubCell
- condensed chromosome, centromeric region Source: UniProtKB
- kinetochore Source: UniProtKB
- membrane Source: UniProtKB
- midbody Source: UniProtKB
Keywords - Cellular componenti
Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, MicrotubulePathology & 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:616051Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_072429 | 933 | D → 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_072430 | 1355 | K → 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 microcephalyOrganism-specific databases
DisGeNETi | 1062 |
MalaCardsi | CENPE |
MIMi | 616051 phenotype |
OpenTargetsi | ENSG00000138778 |
Orphaneti | 808 Seckel syndrome |
PharmGKBi | PA26400 |
Chemistry databases
ChEMBLi | CHEMBL5870 |
DrugBanki | DB06097 GSK-923295 |
Polymorphism and mutation databases
BioMutai | CENPE |
DMDMi | 160358869 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000125436 | 1 – 2698 | Centromere-associated protein EAdd BLAST | 2698 | |
PropeptideiPRO_0000396742 | 2699 – 2701 | Removed in mature formCurated | 3 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 611 | PhosphoserineCombined sources | 1 | |
Modified residuei | 2083 | PhosphoserineCombined sources | 1 | |
Modified residuei | 2389 | PhosphoserineCombined sources | 1 | |
Modified residuei | 2639 | PhosphoserineCombined sources | 1 | |
Modified residuei | 2647 | PhosphoserineCombined sources | 1 | |
Modified residuei | 2651 | PhosphoserineCombined sources | 1 | |
Modified residuei | 2698 | Cysteine methyl esterCurated | 1 | |
Lipidationi | 2698 | S-farnesyl cysteine1 Publication | 1 |
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 conjugationProteomic databases
EPDi | Q02224 |
jPOSTi | Q02224 |
MaxQBi | Q02224 |
PaxDbi | Q02224 |
PeptideAtlasi | Q02224 |
PRIDEi | Q02224 |
ProteomicsDBi | 58063 58064 [Q02224-2] 58065 [Q02224-3] |
PTM databases
iPTMneti | Q02224 |
PhosphoSitePlusi | Q02224 |
Expressioni
Gene expression databases
Bgeei | ENSG00000138778 Expressed in 112 organ(s), highest expression level in oocyte |
ExpressionAtlasi | Q02224 baseline and differential |
Genevisiblei | Q02224 HS |
Organism-specific databases
HPAi | HPA042294 |
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
- microtubule binding Source: UniProtKB
Protein-protein interaction databases
BioGridi | 107491, 42 interactors |
DIPi | DIP-38902N |
IntActi | Q02224, 29 interactors |
MINTi | Q02224 |
STRINGi | 9606.ENSP00000265148 |
Chemistry databases
BindingDBi | Q02224 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1T5C | X-ray | 2.50 | A/B | 2-342 | [»] | |
5JVP | X-ray | 2.10 | A/B/C/D/E/F | 336-371 | [»] | |
ProteinModelPortali | Q02224 | |||||
SMRi | Q02224 | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q02224 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 6 – 329 | Kinesin motorPROSITE-ProRule annotationAdd BLAST | 324 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2126 – 2476 | Kinetochore-binding domainAdd BLAST | 351 | |
Regioni | 2510 – 2698 | Globular autoinhibitory domainBy similarityAdd BLAST | 189 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 336 – 2590 | Sequence analysisAdd BLAST | 2255 |
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 coilPhylogenomic databases
eggNOGi | KOG0242 Eukaryota COG5059 LUCA |
GeneTreei | ENSGT00940000160597 |
HOGENOMi | HOG000111540 |
HOVERGENi | HBG097734 |
InParanoidi | Q02224 |
KOi | K11498 |
OMAi | SVCRASW |
OrthoDBi | 1528613at2759 |
PhylomeDBi | Q02224 |
TreeFami | TF330343 |
Family and domain databases
Gene3Di | 3.40.850.10, 1 hit |
InterProi | View protein in InterPro IPR027640 Kinesin-like_fam IPR019821 Kinesin_motor_CS IPR001752 Kinesin_motor_dom IPR036961 Kinesin_motor_dom_sf IPR027417 P-loop_NTPase |
PANTHERi | PTHR24115 PTHR24115, 2 hits |
Pfami | View protein in Pfam PF00225 Kinesin, 1 hit |
PRINTSi | PR00380 KINESINHEAVY |
SMARTi | View protein in SMART SM00129 KISc, 1 hit |
SUPFAMi | SSF52540 SSF52540, 1 hit |
PROSITEi | View protein in PROSITE PS00411 KINESIN_MOTOR_1, 1 hit PS50067 KINESIN_MOTOR_2, 1 hit |
s (3+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 3 produced by isoformsialternative splicing. AlignAdd to basketThis 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.
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
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketD6RBW0 | D6RBW0_HUMAN | Centromere-associated protein E | CENPE | 1,126 | Annotation score: | ||
A0A087X0P0 | A0A087X0P0_HUMAN | Centromere-associated protein E | CENPE | 2,664 | Annotation score: | ||
D6RHK2 | D6RHK2_HUMAN | Centromere-associated protein E | CENPE | 183 | Annotation score: |
Sequence cautioni
The sequence BAE06078 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 51 | R → H in BAF83051 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 300 | A → P in CAA78727 (PubMed:1406971).Curated | 1 | |
Sequence conflicti | 440 | F → S in BAE06078 (Ref. 2) Curated | 1 | |
Sequence conflicti | 566 | A → R in CAA78727 (PubMed:1406971).Curated | 1 | |
Sequence conflicti | 902 | T → P in CAA78727 (PubMed:1406971).Curated | 1 | |
Sequence conflicti | 1297 | E → K in CAA78727 (PubMed:1406971).Curated | 1 | |
Sequence conflicti | 1546 | K → N in CAA78727 (PubMed:1406971).Curated | 1 | |
Sequence conflicti | 1876 | K → E in CAA78727 (PubMed:1406971).Curated | 1 | |
Sequence conflicti | 2008 – 2017 | AQNLSMQSVR → PNYLCKCE in CAA78727 (PubMed:1406971).Curated | 10 | |
Sequence conflicti | 2190 | S → C in CAA78727 (PubMed:1406971).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_072429 | 933 | D → 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_072430 | 1355 | K → 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_049689 | 1535 | F → L2 PublicationsCorresponds to variant dbSNP:rs2615542Ensembl. | 1 | |
Natural variantiVAR_049690 | 1581 | S → R. Corresponds to variant dbSNP:rs35100664Ensembl. | 1 | |
Natural variantiVAR_059370 | 1911 | S → T. Corresponds to variant dbSNP:rs1381657Ensembl. | 1 | |
Natural variantiVAR_049691 | 1925 | E → D. Corresponds to variant dbSNP:rs2306106Ensembl. | 1 | |
Natural variantiVAR_049692 | 2090 | T → M2 PublicationsCorresponds to variant dbSNP:rs2243682Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_028820 | 549 – 573 | Missing in isoform 3. 1 PublicationAdd BLAST | 25 | |
Alternative sequenceiVSP_028821 | 1972 – 2068 | IQELQ…EMIAR → Q in isoform 3. 1 PublicationAdd BLAST | 97 | |
Alternative sequenceiVSP_028822 | 2131 – 2166 | Missing in isoform 2. 1 PublicationAdd BLAST | 36 |
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 |
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 |
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] |
Keywords - Coding sequence diversityi
Alternative splicing, PolymorphismSimilar 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 |
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: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1T5C | X-ray | 2.50 | A/B | 2-342 | [»] | |
5JVP | X-ray | 2.10 | A/B/C/D/E/F | 336-371 | [»] | |
ProteinModelPortali | Q02224 | |||||
SMRi | Q02224 | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Protein-protein interaction databases
BioGridi | 107491, 42 interactors |
DIPi | DIP-38902N |
IntActi | Q02224, 29 interactors |
MINTi | Q02224 |
STRINGi | 9606.ENSP00000265148 |
Chemistry databases
BindingDBi | Q02224 |
ChEMBLi | CHEMBL5870 |
DrugBanki | DB06097 GSK-923295 |
PTM databases
iPTMneti | Q02224 |
PhosphoSitePlusi | Q02224 |
Polymorphism and mutation databases
BioMutai | CENPE |
DMDMi | 160358869 |
Proteomic databases
EPDi | Q02224 |
jPOSTi | Q02224 |
MaxQBi | Q02224 |
PaxDbi | Q02224 |
PeptideAtlasi | Q02224 |
PRIDEi | Q02224 |
ProteomicsDBi | 58063 58064 [Q02224-2] 58065 [Q02224-3] |
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] |
Organism-specific databases
CTDi | 1062 |
DisGeNETi | 1062 |
EuPathDBi | HostDB:ENSG00000138778.11 |
GeneCardsi | CENPE |
H-InvDBi | HIX0031416 |
HGNCi | HGNC:1856 CENPE |
HPAi | HPA042294 |
MalaCardsi | CENPE |
MIMi | 117143 gene 616051 phenotype |
neXtProti | NX_Q02224 |
OpenTargetsi | ENSG00000138778 |
Orphaneti | 808 Seckel syndrome |
PharmGKBi | PA26400 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0242 Eukaryota COG5059 LUCA |
GeneTreei | ENSGT00940000160597 |
HOGENOMi | HOG000111540 |
HOVERGENi | HBG097734 |
InParanoidi | Q02224 |
KOi | K11498 |
OMAi | SVCRASW |
OrthoDBi | 1528613at2759 |
PhylomeDBi | Q02224 |
TreeFami | TF330343 |
Enzyme and pathway databases
Reactomei | R-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 |
SIGNORi | Q02224 |
Miscellaneous databases
ChiTaRSi | CENPE human |
EvolutionaryTracei | Q02224 |
GeneWikii | Centromere_protein_E |
GenomeRNAii | 1062 |
PROi | PR:Q02224 |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000138778 Expressed in 112 organ(s), highest expression level in oocyte |
ExpressionAtlasi | Q02224 baseline and differential |
Genevisiblei | Q02224 HS |
Family and domain databases
Gene3Di | 3.40.850.10, 1 hit |
InterProi | View protein in InterPro IPR027640 Kinesin-like_fam IPR019821 Kinesin_motor_CS IPR001752 Kinesin_motor_dom IPR036961 Kinesin_motor_dom_sf IPR027417 P-loop_NTPase |
PANTHERi | PTHR24115 PTHR24115, 2 hits |
Pfami | View protein in Pfam PF00225 Kinesin, 1 hit |
PRINTSi | PR00380 KINESINHEAVY |
SMARTi | View protein in SMART SM00129 KISc, 1 hit |
SUPFAMi | SSF52540 SSF52540, 1 hit |
PROSITEi | View protein in PROSITE PS00411 KINESIN_MOTOR_1, 1 hit PS50067 KINESIN_MOTOR_2, 1 hit |
ProtoNeti | Search... |
Entry informationi
Entry namei | CENPE_HUMAN | |
Accessioni | Q02224Primary (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: | February 13, 2019 | |
This is version 193 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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 proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - Human chromosome 4
Human chromosome 4: entries, gene names and cross-references to MIM - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations