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Q02224 (CENPE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centromere-associated protein E
Alternative name(s):
Centromere protein E
Short name=CENP-E
Kinesin-related protein CENPE
Gene names
Name:CENPE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2701 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.10

Subunit structure

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. Ref.7 Ref.9 Ref.10 Ref.12 Ref.15 Ref.17 Ref.18

Subcellular location

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. Ref.6 Ref.7 Ref.10 Ref.12 Ref.13

Domain

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.

Post-translational modification

The C-terminal inhibitory domain is phosphorylated. Phosphorylation relieves autoinhibition of the kinetochore motor By similarity.

Sumoylated with SUMO2 and SUMO3. The sumoylation mediates the association to the kinetochore. Ref.13

Sequence similarities

Belongs to the kinesin-like protein family.

Contains 1 kinesin-motor domain.

Sequence caution

The sequence BAE06078.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Kinetochore
Microtubule
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Motor protein
   PTMIsopeptide bond
Lipoprotein
Methylation
Phosphoprotein
Prenylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

kinetochore assembly

Non-traceable author statement Ref.7. Source: UniProtKB

metabolic process

Inferred from mutant phenotype Ref.6. Source: GOC

microtubule-based movement

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic chromosome movement towards spindle pole

Traceable author statement Ref.1. Source: ProtInc

mitotic metaphase

Traceable author statement PubMed 2022189. Source: ProtInc

mitotic metaphase plate congression

Traceable author statement PubMed 9363944. Source: ProtInc

mitotic spindle assembly checkpoint

Inferred from electronic annotation. Source: InterPro

multicellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of protein kinase activity

Inferred from mutant phenotype PubMed 12925705. Source: UniProtKB

   Cellular_componentchromosome, centromeric region

Inferred from direct assay PubMed 11084331. Source: MGI

condensed chromosome outer kinetochore

Inferred from electronic annotation. Source: Ensembl

condensed chromosome, centromeric region

Inferred from direct assay PubMed 19465021. Source: UniProtKB

condensed nuclear chromosome kinetochore

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

kinesin complex

Inferred from electronic annotation. Source: InterPro

kinetochore

Inferred from direct assay PubMed 12925705. Source: UniProtKB

microtubule

Inferred from direct assay Ref.6. Source: UniProtKB

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

nucleus

Inferred from mutant phenotype Ref.7. Source: UniProtKB

spindle midzone

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

kinetochore binding

Inferred from direct assay Ref.7. Source: UniProtKB

microtubule motor activity

Inferred from mutant phenotype Ref.6. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q02224-1)

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.
Isoform 2 (identifier: Q02224-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2131-2166: Missing.
Isoform 3 (identifier: Q02224-3)

The sequence of this isoform differs from the canonical sequence as follows:
     549-573: Missing.
     1972-2068: IQELQKKELQ...IATLREMIAR → Q

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 26982698Centromere-associated protein E
PRO_0000125436
Propeptide2699 – 27013Removed in mature form Probable
PRO_0000396742

Regions

Domain1 – 335335Kinesin-motor
Nucleotide binding86 – 938ATP
Region2126 – 2476351Kinetochore-binding domain
Region2510 – 2698189Globular autoinhibitory domain By similarity
Coiled coil336 – 25902255 Potential

Amino acid modifications

Modified residue26471Phosphoserine Ref.14
Modified residue26981Cysteine methyl ester Probable
Lipidation26981S-farnesyl cysteine Ref.8
Cross-link1937Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Natural variations

Alternative sequence549 – 57325Missing in isoform 3.
VSP_028820
Alternative sequence1972 – 206897IQELQ…EMIAR → Q in isoform 3.
VSP_028821
Alternative sequence2131 – 216636Missing in isoform 2.
VSP_028822
Natural variant15351F → L. Ref.1
Corresponds to variant rs2615542 [ dbSNP | Ensembl ].
VAR_049689
Natural variant15811S → R.
Corresponds to variant rs35100664 [ dbSNP | Ensembl ].
VAR_049690
Natural variant19111S → T.
Corresponds to variant rs1381657 [ dbSNP | Ensembl ].
VAR_059370
Natural variant19251E → D.
Corresponds to variant rs2306106 [ dbSNP | Ensembl ].
VAR_049691
Natural variant20901T → M. Ref.1
Corresponds to variant rs2243682 [ dbSNP | Ensembl ].
VAR_049692

Experimental info

Sequence conflict511R → H in BAF83051. Ref.5
Sequence conflict3001A → P in CAA78727. Ref.1
Sequence conflict4401F → S in BAE06078. Ref.2
Sequence conflict5661A → R in CAA78727. Ref.1
Sequence conflict9021T → P in CAA78727. Ref.1
Sequence conflict12971E → K in CAA78727. Ref.1
Sequence conflict15461K → N in CAA78727. Ref.1
Sequence conflict18761K → E in CAA78727. Ref.1
Sequence conflict2008 – 201710AQNLSMQSVR → PNYLCKCE in CAA78727. Ref.1
Sequence conflict21901S → C in CAA78727. Ref.1

Secondary structure

........................................................ 2701
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 23, 2007. Version 2.
Checksum: 4BC59C2EF0B02D88

FASTA2,701316,415
        10         20         30         40         50         60 
MAEEGAVAVC VRVRPLNSRE ESLGETAQVY WKTDNNVIYQ VDGSKSFNFD RVFHGNETTK 

        70         80         90        100        110        120 
NVYEEIAAPI IDSAIQGYNG TIFAYGQTAS GKTYTMMGSE DHLGVIPRAI HDIFQKIKKF 

       130        140        150        160        170        180 
PDREFLLRVS YMEIYNETIT DLLCGTQKMK PLIIREDVNR NVYVADLTEE VVYTSEMALK 

       190        200        210        220        230        240 
WITKGEKSRH YGETKMNQRS SRSHTIFRMI LESREKGEPS NCEGSVKVSH LNLVDLAGSE 

       250        260        270        280        290        300 
RAAQTGAAGV RLKEGCNINR SLFILGQVIK KLSDGQVGGF INYRDSKLTR ILQNSLGGNA 

       310        320        330        340        350        360 
KTRIICTITP VSFDETLTAL QFASTAKYMK NTPYVNEVST DEALLKRYRK EIMDLKKQLE 

       370        380        390        400        410        420 
EVSLETRAQA MEKDQLAQLL EEKDLLQKVQ NEKIENLTRM LVTSSSLTLQ QELKAKRKRR 

       430        440        450        460        470        480 
VTWCLGKINK MKNSNYADQF NIPTNITTKT HKLSINLLRE IDESVCSESD VFSNTLDTLS 

       490        500        510        520        530        540 
EIEWNPATKL LNQENIESEL NSLRADYDNL VLDYEQLRTE KEEMELKLKE KNDLDEFEAL 

       550        560        570        580        590        600 
ERKTKKDQEM QLIHEISNLK NLVKHAEVYN QDLENELSSK VELLREKEDQ IKKLQEYIDS 

       610        620        630        640        650        660 
QKLENIKMDL SYSLESIEDP KQMKQTLFDA ETVALDAKRE SAFLRSENLE LKEKMKELAT 

       670        680        690        700        710        720 
TYKQMENDIQ LYQSQLEAKK KMQVDLEKEL QSAFNEITKL TSLIDGKVPK DLLCNLELEG 

       730        740        750        760        770        780 
KITDLQKELN KEVEENEALR EEVILLSELK SLPSEVERLR KEIQDKSEEL HIITSEKDKL 

       790        800        810        820        830        840 
FSEVVHKESR VQGLLEEIGK TKDDLATTQS NYKSTDQEFQ NFKTLHMDFE QKYKMVLEEN 

       850        860        870        880        890        900 
ERMNQEIVNL SKEAQKFDSS LGALKTELSY KTQELQEKTR EVQERLNEME QLKEQLENRD 

       910        920        930        940        950        960 
STLQTVEREK TLITEKLQQT LEEVKTLTQE KDDLKQLQES LQIERDQLKS DIHDTVNMNI 

       970        980        990       1000       1010       1020 
DTQEQLRNAL ESLKQHQETI NTLKSKISEE VSRNLHMEEN TGETKDEFQQ KMVGIDKKQD 

      1030       1040       1050       1060       1070       1080 
LEAKNTQTLT ADVKDNEIIE QQRKIFSLIQ EKNELQQMLE SVIAEKEQLK TDLKENIEMT 

      1090       1100       1110       1120       1130       1140 
IENQEELRLL GDELKKQQEI VAQEKNHAIK KEGELSRTCD RLAEVEEKLK EKSQQLQEKQ 

      1150       1160       1170       1180       1190       1200 
QQLLNVQEEM SEMQKKINEI ENLKNELKNK ELTLEHMETE RLELAQKLNE NYEEVKSITK 

      1210       1220       1230       1240       1250       1260 
ERKVLKELQK SFETERDHLR GYIREIEATG LQTKEELKIA HIHLKEHQET IDELRRSVSE 

      1270       1280       1290       1300       1310       1320 
KTAQIINTQD LEKSHTKLQE EIPVLHEEQE LLPNVKEVSE TQETMNELEL LTEQSTTKDS 

      1330       1340       1350       1360       1370       1380 
TTLARIEMER LRLNEKFQES QEEIKSLTKE RDNLKTIKEA LEVKHDQLKE HIRETLAKIQ 

      1390       1400       1410       1420       1430       1440 
ESQSKQEQSL NMKEKDNETT KIVSEMEQFK PKDSALLRIE IEMLGLSKRL QESHDEMKSV 

      1450       1460       1470       1480       1490       1500 
AKEKDDLQRL QEVLQSESDQ LKENIKEIVA KHLETEEELK VAHCCLKEQE ETINELRVNL 

      1510       1520       1530       1540       1550       1560 
SEKETEISTI QKQLEAINDK LQNKIQEIYE KEEQFNIKQI SEVQEKVNEL KQFKEHRKAK 

      1570       1580       1590       1600       1610       1620 
DSALQSIESK MLELTNRLQE SQEEIQIMIK EKEEMKRVQE ALQIERDQLK ENTKEIVAKM 

      1630       1640       1650       1660       1670       1680 
KESQEKEYQF LKMTAVNETQ EKMCEIEHLK EQFETQKLNL ENIETENIRL TQILHENLEE 

      1690       1700       1710       1720       1730       1740 
MRSVTKERDD LRSVEETLKV ERDQLKENLR ETITRDLEKQ EELKIVHMHL KEHQETIDKL 

      1750       1760       1770       1780       1790       1800 
RGIVSEKTNE ISNMQKDLEH SNDALKAQDL KIQEELRIAH MHLKEQQETI DKLRGIVSEK 

      1810       1820       1830       1840       1850       1860 
TDKLSNMQKD LENSNAKLQE KIQELKANEH QLITLKKDVN ETQKKVSEME QLKKQIKDQS 

      1870       1880       1890       1900       1910       1920 
LTLSKLEIEN LNLAQKLHEN LEEMKSVMKE RDNLRRVEET LKLERDQLKE SLQETKARDL 

      1930       1940       1950       1960       1970       1980 
EIQQELKTAR MLSKEHKETV DKLREKISEK TIQISDIQKD LDKSKDELQK KIQELQKKEL 

      1990       2000       2010       2020       2030       2040 
QLLRVKEDVN MSHKKINEME QLKKQFEAQN LSMQSVRMDN FQLTKKLHES LEEIRIVAKE 

      2050       2060       2070       2080       2090       2100 
RDELRRIKES LKMERDQFIA TLREMIARDR QNHQVKPEKR LLSDGQQHLT ESLREKCSRI 

      2110       2120       2130       2140       2150       2160 
KELLKRYSEM DDHYECLNRL SLDLEKEIEF QKELSMRVKA NLSLPYLQTK HIEKLFTANQ 

      2170       2180       2190       2200       2210       2220 
RCSMEFHRIM KKLKYVLSYV TKIKEEQHES INKFEMDFID EVEKQKELLI KIQHLQQDCD 

      2230       2240       2250       2260       2270       2280 
VPSRELRDLK LNQNMDLHIE EILKDFSESE FPSIKTEFQQ VLSNRKEMTQ FLEEWLNTRF 

      2290       2300       2310       2320       2330       2340 
DIEKLKNGIQ KENDRICQVN NFFNNRIIAI MNESTEFEER SATISKEWEQ DLKSLKEKNE 

      2350       2360       2370       2380       2390       2400 
KLFKNYQTLK TSLASGAQVN PTTQDNKNPH VTSRATQLTT EKIRELENSL HEAKESAMHK 

      2410       2420       2430       2440       2450       2460 
ESKIIKMQKE LEVTNDIIAK LQAKVHESNK CLEKTKETIQ VLQDKVALGA KPYKEEIEDL 

      2470       2480       2490       2500       2510       2520 
KMKLVKIDLE KMKNAKEFEK EISATKATVE YQKEVIRLLR ENLRRSQQAQ DTSVISEHTD 

      2530       2540       2550       2560       2570       2580 
PQPSNKPLTC GGGSGIVQNT KALILKSEHI RLEKEISKLK QQNEQLIKQK NELLSNNQHL 

      2590       2600       2610       2620       2630       2640 
SNEVKTWKER TLKREAHKQV TCENSPKSPK VTGTASKKKQ ITPSQCKERN LQDPVPKESP 

      2650       2660       2670       2680       2690       2700 
KSCFFDSRSK SLPSPHPVRY FDNSSLGLCP EVQNAGAESV DSQPGPWHAS SGKDVPECKT 


Q 

« Hide

Isoform 2 [UniParc].

Checksum: FD0951C16BECB82A
Show »

FASTA2,665312,149
Isoform 3 [UniParc].

Checksum: C5EC35EE9A5E5524
Show »

FASTA2,580301,789

References

« Hide 'large scale' references
[1]"CENP-E is a putative kinetochore motor that accumulates just before mitosis."
Yen T.J., Li G., Schaar B.T., Szilak I., Cleveland D.W.
Nature 359:536-539(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS LEU-1535 AND MET-2090.
[2]"Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1126 (ISOFORMS 1/2).
Tissue: Tongue.
[6]"Mitotic HeLa cells contain a CENP-E-associated minus end-directed microtubule motor."
Thrower D.A., Jordan M.A., Schaar B.T., Yen T.J., Wilson L.
EMBO J. 14:918-926(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]"Characterization of the kinetochore binding domain of CENP-E reveals interactions with the kinetochore proteins CENP-F and hBUBR1."
Chan G.K.T., Schaar B.T., Yen T.J.
J. Cell Biol. 143:49-63(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CENPF AND BUBR1, SUBCELLULAR LOCATION.
[8]"Farnesyl transferase inhibitors block the farnesylation of CENP-E and CENP-F and alter the association of CENP-E with the microtubules."
Ashar H.R., James L., Gray K., Carr D., Black S., Armstrong L., Bishop W.R., Kirschmeier P.
J. Biol. Chem. 275:30451-30457(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ISOPRENYLATION AT CYS-2698.
[9]"Essential roles of KIF4 and its binding partner PRC1 in organized central spindle midzone formation."
Kurasawa Y., Earnshaw W.C., Mochizuki Y., Dohmae N., Todokoro K.
EMBO J. 23:3237-3248(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRC1.
[10]"Human NUF2 interacts with centromere-associated protein E and is essential for a stable spindle microtubule-kinetochore attachment."
Liu D., Ding X., Du J., Cai X., Huang Y., Ward T., Shaw A., Yang Y., Hu R., Jin C., Yao X.
J. Biol. Chem. 282:21415-21424(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NUF2, SUBCELLULAR LOCATION.
[11]"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1937.
Tissue: Mammary cancer.
[12]"Septin 7 interacts with centromere-associated protein E and is required for its kinetochore localization."
Zhu M., Wang F., Yan F., Yao P.Y., Du J., Gao X., Wang X., Wu Q., Ward T., Li J., Kioko S., Hu R., Xie W., Ding X., Yao X.
J. Biol. Chem. 283:18916-18925(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SEPT7, SUBCELLULAR LOCATION.
[13]"SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis."
Zhang X.-D., Goeres J., Zhang H., Yen T.J., Porter A.C.G., Matunis M.J.
Mol. Cell 29:729-741(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION, SUBCELLULAR LOCATION.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2647, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Defects in chromosome congression and mitotic progression in KIF18A-deficient cells are partly mediated through impaired functions of CENP-E."
Huang Y., Yao Y., Xu H.-Z., Wang Z.-G., Lu L., Dai W.
Cell Cycle 8:2643-2649(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIF18A AND BUB1B.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"CENP-E kinesin interacts with SKAP protein to orchestrate accurate chromosome segregation in mitosis."
Huang Y., Wang W., Yao P., Wang X., Liu X., Zhuang X., Yan F., Zhou J., Du J., Ward T., Zou H., Zhang J., Fang G., Ding X., Dou Z., Yao X.
J. Biol. Chem. 287:1500-1509(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKAP.
[18]"Crystal structure of the motor domain of the human kinetochore protein CENP-E."
Garcia-Saez I., Yen T., Wade R.H., Kozielski F.
J. Mol. Biol. 340:1107-1116(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-342 IN COMPLEX WITH ADP, PROTEIN SEQUENCE OF 2-7, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS28261.
RefSeqNP_001273663.1. NM_001286734.1.
NP_001804.2. NM_001813.2.
UniGeneHs.75573.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T5CX-ray2.50A/B2-342[»]
ProteinModelPortalQ02224.
SMRQ02224. Positions 4-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107491. 18 interactions.
IntActQ02224. 9 interactions.
MINTMINT-5002721.
STRING9606.ENSP00000265148.

Chemistry

BindingDBQ02224.
ChEMBLCHEMBL5870.

PTM databases

PhosphoSiteQ02224.

Polymorphism databases

DMDM160358869.

Proteomic databases

PaxDbQ02224.
PRIDEQ02224.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265148; ENSP00000265148; ENSG00000138778. [Q02224-1]
ENST00000380026; ENSP00000369365; ENSG00000138778. [Q02224-3]
GeneID1062.
KEGGhsa:1062.
UCSCuc003hxb.1. human. [Q02224-1]
uc003hxc.1. human. [Q02224-3]

Organism-specific databases

CTD1062.
GeneCardsGC04M104027.
H-InvDBHIX0031416.
HGNCHGNC:1856. CENPE.
HPAHPA042294.
MIM117143. gene.
neXtProtNX_Q02224.
PharmGKBPA26400.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5059.
HOGENOMHOG000111540.
HOVERGENHBG097734.
InParanoidQ02224.
KOK11498.
OMAVKTWKER.
OrthoDBEOG7J9VNX.
PhylomeDBQ02224.
TreeFamTF330343.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ02224.
BgeeQ02224.
CleanExHS_CENPE.
GenevestigatorQ02224.

Family and domain databases

Gene3D3.40.850.10. 1 hit.
InterProIPR028368. CENPE.
IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR24115. PTHR24115. 1 hit.
PTHR24115:SF72. PTHR24115:SF72. 1 hit.
PfamPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSPR00380. KINESINHEAVY.
SMARTSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ02224.
GeneWikiCentromere_protein_E.
GenomeRNAi1062.
NextBio4442.
PROQ02224.
SOURCESearch...

Entry information

Entry nameCENPE_HUMAN
AccessionPrimary (citable) accession number: Q02224
Secondary accession number(s): A6NKY9, A8K2U7, Q4LE75
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 23, 2007
Last modified: April 16, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM