Q02224 (CENPE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Centromere-associated protein E

Alternative name(s):
Centromere protein E
Short name=CENP-E
Kinesin-related protein CENPE

Gene names

Name:

CENPE

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2701 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Chromosome › centromere › kinetochore. Cytoplasm › cytoskeleton › spindle. 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 process	Cell cycle Cell division Mitosis
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Kinetochore Microtubule
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Motor protein
PTM	Isopeptide bond Lipoprotein Methylation Phosphoprotein Prenylation Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class II Traceable author statement. Source: Reactome blood coagulation Traceable author statement. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW kinetochore assembly Non-traceable author statement Ref.7. Source: UniProtKB 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 prometaphase Traceable author statement. Source: Reactome 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_component	condensed chromosome outer kinetochore Inferred from electronic annotation. Source: Compara condensed chromosome, centromeric region Inferred from direct assay PubMed 19465021. Source: UniProtKB condensed nuclear chromosome kinetochore Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome kinetochore Inferred from direct assay PubMed 12925705. Source: UniProtKB microtubule Inferred from direct assay Ref.6. Source: UniProtKB microtubule associated complex Inferred from electronic annotation. Source: InterPro nucleus Inferred from mutant phenotype Ref.7. Source: UniProtKB spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP 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

With	Entry	#Exp.	IntAct	Notes
BUB1B	O60566	4	EBI-1375040,EBI-1001438
NUF2	Q9BZD4	9	EBI-1375040,EBI-724102

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2698

2698

Centromere-associated protein E

PRO_0000125436

Propeptide

2699 – 2701

3

Removed in mature form Probable

PRO_0000396742

Regions

Domain

1 – 335

335

Kinesin-motor

Nucleotide binding

86 – 93

8

ATP

Region

2126 – 2476

351

Kinetochore-binding domain

Region

2510 – 2698

189

Globular autoinhibitory domain By similarity

Coiled coil

336 – 2590

2255

Potential

Amino acid modifications

Modified residue

2647

1

Phosphoserine Ref.14

Modified residue

2698

1

Cysteine methyl ester Probable

Lipidation

2698

1

S-farnesyl cysteine Ref.8

Cross-link

1937

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Natural variations

Alternative sequence

549 – 573

25

Missing in isoform 3.

VSP_028820

Alternative sequence

1972 – 2068

97

IQELQ…EMIAR → Q in isoform 3.

VSP_028821

Alternative sequence

2131 – 2166

36

Missing in isoform 2.

VSP_028822

Natural variant

1535

1

F → L. Ref.1
Corresponds to variant rs2615542 [ dbSNP | Ensembl ].

VAR_049689

Natural variant

1581

1

S → R.
Corresponds to variant rs35100664 [ dbSNP | Ensembl ].

VAR_049690

Natural variant

1911

1

S → T.
Corresponds to variant rs1381657 [ dbSNP | Ensembl ].

VAR_059370

Natural variant

1925

1

E → D.
Corresponds to variant rs2306106 [ dbSNP | Ensembl ].

VAR_049691

Natural variant

2090

1

T → M. Ref.1
Corresponds to variant rs2243682 [ dbSNP | Ensembl ].

VAR_049692

Experimental info

Sequence conflict

51

1

R → H in BAF83051. Ref.5

Sequence conflict

300

1

A → P in CAA78727. Ref.1

Sequence conflict

440

1

F → S in BAE06078. Ref.2

Sequence conflict

566

1

A → R in CAA78727. Ref.1

Sequence conflict

902

1

T → P in CAA78727. Ref.1

Sequence conflict

1297

1

E → K in CAA78727. Ref.1

Sequence conflict

1546

1

K → N in CAA78727. Ref.1

Sequence conflict

1876

1

K → E in CAA78727. Ref.1

Sequence conflict

2008 – 2017

10

AQNLSMQSVR → PNYLCKCE in CAA78727. Ref.1

Sequence conflict

2190

1

S → C in CAA78727. Ref.1

Secondary structure

1

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2701

Helix Strand Turn

Details...

Beta strand

7 – 13

7

Turn

22 – 25

4

Beta strand

31 – 34

4

Beta strand

37 – 40

4

Beta strand

46 – 48

3

Helix

59 – 65

7

Helix

68 – 75

8

Beta strand

80 – 87

8

Helix

92 – 96

5

Beta strand

100 – 103

4

Helix

105 – 116

12

Helix

117 – 119

3

Beta strand

123 – 135

13

Beta strand

138 – 146

9

Turn

157 – 159

3

Helix

175 – 187

13

Beta strand

190 – 197

8

Turn

199 – 202

4

Beta strand

204 – 215

12

Beta strand

226 – 235

10

Helix

239 – 241

3

Beta strand

254 – 256

3

Helix

260 – 274

15

Helix

283 – 285

3

Helix

287 – 291

5

Helix

293 – 295

3

Beta strand

298 – 308

11

Helix

314 – 326

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 23, 2007. Version 2. Checksum: 4BC59C2EF0B02D88	FASTA	2,701	316,415
	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
	Isoform 2 [UniParc]. Checksum: FD0951C16BECB82A	FASTA	2,665	312,149
	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 HRIMKKLKYV LSYVTKIKEE QHESINKFEM 2170 2180 2190 2200 2210 2220 DFIDEVEKQK ELLIKIQHLQ QDCDVPSREL RDLKLNQNMD LHIEEILKDF SESEFPSIKT 2230 2240 2250 2260 2270 2280 EFQQVLSNRK EMTQFLEEWL NTRFDIEKLK NGIQKENDRI CQVNNFFNNR IIAIMNESTE 2290 2300 2310 2320 2330 2340 FEERSATISK EWEQDLKSLK EKNEKLFKNY QTLKTSLASG AQVNPTTQDN KNPHVTSRAT 2350 2360 2370 2380 2390 2400 QLTTEKIREL ENSLHEAKES AMHKESKIIK MQKELEVTND IIAKLQAKVH ESNKCLEKTK 2410 2420 2430 2440 2450 2460 ETIQVLQDKV ALGAKPYKEE IEDLKMKLVK IDLEKMKNAK EFEKEISATK ATVEYQKEVI 2470 2480 2490 2500 2510 2520 RLLRENLRRS QQAQDTSVIS EHTDPQPSNK PLTCGGGSGI VQNTKALILK SEHIRLEKEI 2530 2540 2550 2560 2570 2580 SKLKQQNEQL IKQKNELLSN NQHLSNEVKT WKERTLKREA HKQVTCENSP KSPKVTGTAS 2590 2600 2610 2620 2630 2640 KKKQITPSQC KERNLQDPVP KESPKSCFFD SRSKSLPSPH PVRYFDNSSL GLCPEVQNAG 2650 2660 AESVDSQPGP WHASSGKDVP ECKTQ
	Isoform 3 [UniParc]. Checksum: C5EC35EE9A5E5524	FASTA	2,580	301,789
	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 ERKTKKDQEN ELSSKVELLR EKEDQIKKLQ EYIDSQKLEN IKMDLSYSLE SIEDPKQMKQ 610 620 630 640 650 660 TLFDAETVAL DAKRESAFLR SENLELKEKM KELATTYKQM ENDIQLYQSQ LEAKKKMQVD 670 680 690 700 710 720 LEKELQSAFN EITKLTSLID GKVPKDLLCN LELEGKITDL QKELNKEVEE NEALREEVIL 730 740 750 760 770 780 LSELKSLPSE VERLRKEIQD KSEELHIITS EKDKLFSEVV HKESRVQGLL EEIGKTKDDL 790 800 810 820 830 840 ATTQSNYKST DQEFQNFKTL HMDFEQKYKM VLEENERMNQ EIVNLSKEAQ KFDSSLGALK 850 860 870 880 890 900 TELSYKTQEL QEKTREVQER LNEMEQLKEQ LENRDSTLQT VEREKTLITE KLQQTLEEVK 910 920 930 940 950 960 TLTQEKDDLK QLQESLQIER DQLKSDIHDT VNMNIDTQEQ LRNALESLKQ HQETINTLKS 970 980 990 1000 1010 1020 KISEEVSRNL HMEENTGETK DEFQQKMVGI DKKQDLEAKN TQTLTADVKD NEIIEQQRKI 1030 1040 1050 1060 1070 1080 FSLIQEKNEL QQMLESVIAE KEQLKTDLKE NIEMTIENQE ELRLLGDELK KQQEIVAQEK 1090 1100 1110 1120 1130 1140 NHAIKKEGEL SRTCDRLAEV EEKLKEKSQQ LQEKQQQLLN VQEEMSEMQK KINEIENLKN 1150 1160 1170 1180 1190 1200 ELKNKELTLE HMETERLELA QKLNENYEEV KSITKERKVL KELQKSFETE RDHLRGYIRE 1210 1220 1230 1240 1250 1260 IEATGLQTKE ELKIAHIHLK EHQETIDELR RSVSEKTAQI INTQDLEKSH TKLQEEIPVL 1270 1280 1290 1300 1310 1320 HEEQELLPNV KEVSETQETM NELELLTEQS TTKDSTTLAR IEMERLRLNE KFQESQEEIK 1330 1340 1350 1360 1370 1380 SLTKERDNLK TIKEALEVKH DQLKEHIRET LAKIQESQSK QEQSLNMKEK DNETTKIVSE 1390 1400 1410 1420 1430 1440 MEQFKPKDSA LLRIEIEMLG LSKRLQESHD EMKSVAKEKD DLQRLQEVLQ SESDQLKENI 1450 1460 1470 1480 1490 1500 KEIVAKHLET EEELKVAHCC LKEQEETINE LRVNLSEKET EISTIQKQLE AINDKLQNKI 1510 1520 1530 1540 1550 1560 QEIYEKEEQF NIKQISEVQE KVNELKQFKE HRKAKDSALQ SIESKMLELT NRLQESQEEI 1570 1580 1590 1600 1610 1620 QIMIKEKEEM KRVQEALQIE RDQLKENTKE IVAKMKESQE KEYQFLKMTA VNETQEKMCE 1630 1640 1650 1660 1670 1680 IEHLKEQFET QKLNLENIET ENIRLTQILH ENLEEMRSVT KERDDLRSVE ETLKVERDQL 1690 1700 1710 1720 1730 1740 KENLRETITR DLEKQEELKI VHMHLKEHQE TIDKLRGIVS EKTNEISNMQ KDLEHSNDAL 1750 1760 1770 1780 1790 1800 KAQDLKIQEE LRIAHMHLKE QQETIDKLRG IVSEKTDKLS NMQKDLENSN AKLQEKIQEL 1810 1820 1830 1840 1850 1860 KANEHQLITL KKDVNETQKK VSEMEQLKKQ IKDQSLTLSK LEIENLNLAQ KLHENLEEMK 1870 1880 1890 1900 1910 1920 SVMKERDNLR RVEETLKLER DQLKESLQET KARDLEIQQE LKTARMLSKE HKETVDKLRE 1930 1940 1950 1960 1970 1980 KISEKTIQIS DIQKDLDKSK DELQKKQDRQ NHQVKPEKRL LSDGQQHLTE SLREKCSRIK 1990 2000 2010 2020 2030 2040 ELLKRYSEMD DHYECLNRLS LDLEKEIEFQ KELSMRVKAN LSLPYLQTKH IEKLFTANQR 2050 2060 2070 2080 2090 2100 CSMEFHRIMK KLKYVLSYVT KIKEEQHESI NKFEMDFIDE VEKQKELLIK IQHLQQDCDV 2110 2120 2130 2140 2150 2160 PSRELRDLKL NQNMDLHIEE ILKDFSESEF PSIKTEFQQV LSNRKEMTQF LEEWLNTRFD 2170 2180 2190 2200 2210 2220 IEKLKNGIQK ENDRICQVNN FFNNRIIAIM NESTEFEERS ATISKEWEQD LKSLKEKNEK 2230 2240 2250 2260 2270 2280 LFKNYQTLKT SLASGAQVNP TTQDNKNPHV TSRATQLTTE KIRELENSLH EAKESAMHKE 2290 2300 2310 2320 2330 2340 SKIIKMQKEL EVTNDIIAKL QAKVHESNKC LEKTKETIQV LQDKVALGAK PYKEEIEDLK 2350 2360 2370 2380 2390 2400 MKLVKIDLEK MKNAKEFEKE ISATKATVEY QKEVIRLLRE NLRRSQQAQD TSVISEHTDP 2410 2420 2430 2440 2450 2460 QPSNKPLTCG GGSGIVQNTK ALILKSEHIR LEKEISKLKQ QNEQLIKQKN ELLSNNQHLS 2470 2480 2490 2500 2510 2520 NEVKTWKERT LKREAHKQVT CENSPKSPKV TGTASKKKQI TPSQCKERNL QDPVPKESPK 2530 2540 2550 2560 2570 2580 SCFFDSRSKS LPSPHPVRYF DNSSLGLCPE VQNAGAESVD SQPGPWHASS GKDVPECKTQ

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, 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.

IPI

IPI00296365.
IPI00619925.
IPI00868715.

PIR

S28261.

RefSeq

NP_001804.2. NM_001813.2.

UniGene

Hs.75573.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1T5C	X-ray	2.50	A/B	2-342	[»]

ProteinModelPortal

Q02224.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q02224. 8 interactions.

MINT

MINT-5002721.

STRING

9606.ENSP00000265148.

PTM databases

PhosphoSite

Q02224.

Polymorphism databases

DMDM

160358869.

Proteomic databases

PaxDb

Q02224.

PRIDE

Q02224.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265148; ENSP00000265148; ENSG00000138778.
ENST00000380026; ENSP00000369365; ENSG00000138778.

GeneID

1062.

KEGG

hsa:1062.

UCSC

uc003hxb.1. human.
uc003hxc.1. human.

Organism-specific databases

CTD

1062.

GeneCards

GC04M104027.

H-InvDB

HIX0031416.

HGNC

HGNC:1856. CENPE.

HPA

HPA042294.

MIM

117143. gene.

neXtProt

NX_Q02224.

PharmGKB

PA26400.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5059.

HOGENOM

HOG000111540.

HOVERGEN

HBG097734.

InParanoid

Q02224.

KO

K11498.

OMA

VKTWKER.

Enzyme and pathway databases

Reactome

REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q02224.

Bgee

Q02224.

CleanEx

HS_CENPE.

Genevestigator

Q02224.

Family and domain databases

Gene3D

3.40.850.10. 1 hit.

InterPro

IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
[Graphical view]

Pfam

PF00225. Kinesin. 1 hit.
[Graphical view]

PRINTS

PR00380. KINESINHEAVY.

SMART

SM00129. KISc. 1 hit.
[Graphical view]

PROSITE

PS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q02224.

ChEMBL

CHEMBL5870.

EvolutionaryTrace

Q02224.

GenomeRNAi

1062.

NextBio

4442.

SOURCE

Search...

Entry information

Entry name

CENPE_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

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.