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Q6RT24

- CENPE_MOUSE

UniProt

Q6RT24 - CENPE_MOUSE

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Protein

Centromere-associated protein E

Gene

Cenpe

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi86 – 938ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATPase activity Source: RefGenome
  2. ATP binding Source: UniProtKB-KW
  3. kinetochore binding Source: UniProtKB
  4. microtubule motor activity Source: RefGenome
  5. protein kinase binding Source: UniProtKB

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. attachment of spindle microtubules to kinetochore Source: UniProtKB
  3. establishment of protein localization Source: UniProtKB
  4. metabolic process Source: GOC
  5. microtubule-based movement Source: RefGenome
  6. mitotic nuclear division Source: UniProtKB-KW
  7. mitotic spindle assembly checkpoint Source: UniProtKB
  8. multicellular organismal development Source: UniProtKB-KW
  9. positive regulation of attachment of spindle microtubules to kinetochore Source: UniProtKB
  10. positive regulation of chromosome segregation Source: UniProtKB
  11. positive regulation of mitotic metaphase/anaphase transition Source: UniProtKB
  12. positive regulation of protein kinase activity Source: UniProtKB
  13. regulation of developmental process Source: UniProtKB
  14. regulation of mitosis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Motor protein

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Centromere-associated protein EImported
Alternative name(s):
Centromere protein E
Short name:
CENP-EBy similarity
Kinesin superfamily protein 101 Publication
Short name:
KIF101 Publication
Motor domain of KIF10Imported
Gene namesi
Name:CenpeImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1098230. Cenpe.

Subcellular locationi

Cytoplasmcytoskeletonspindle 2 Publications. Chromosomecentromerekinetochore 2 Publications
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.2 Publications

GO - Cellular componenti

  1. chromosome, centromeric region Source: MGI
  2. condensed chromosome outer kinetochore Source: MGI
  3. condensed nuclear chromosome kinetochore Source: MGI
  4. cytoplasm Source: UniProtKB-KW
  5. kinesin complex Source: RefGenome
  6. kinetochore Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24712471Centromere-associated protein EPRO_0000365106Add
BLAST
Propeptidei2472 – 24743Removed in mature formBy similarityPRO_0000396743

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2471 – 24711Cysteine methyl esterBy similarity
Lipidationi2471 – 24711S-farnesyl cysteineBy similarity

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 (By similarity).By similarity

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

Proteomic databases

MaxQBiQ6RT24.
PaxDbiQ6RT24.
PRIDEiQ6RT24.

PTM databases

PhosphoSiteiQ6RT24.

Expressioni

Tissue specificityi

Expressed in hippocampus. Also detected in liver and fibroblasts (at protein level).2 Publications

Gene expression databases

GenevestigatoriQ6RT24.

Interactioni

Subunit structurei

Monomer. Interacts with CENPF, SEPT7 KIF18A and PRC1 (By similarity). Interacts with BUBR1 kinase. Interacts with SKAP; this interaction greatly favors SKAP binding to microtubules (By similarity).By similarity

Protein-protein interaction databases

BioGridi230907. 4 interactions.
IntActiQ6RT24. 3 interactions.
STRINGi10090.ENSMUSP00000057938.

Structurei

3D structure databases

ProteinModelPortaliQ6RT24.
SMRiQ6RT24. Positions 4-339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 329324Kinesin motorPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1962 – 2252291Kinetochore binding domainBy similarityAdd
BLAST
Regioni2286 – 2471186Globular autoinhibitory domainBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili334 – 23662033Sequence AnalysisAdd
BLAST

Domaini

The protein is composed of a N-terminal kinesin-motor domain involved in the chromosome movements, a long coil-coiled region involved in the homodimerization and an inhibitory C-tail involved in autoinhibition of the N-terminal catalytic part.By similarity

Sequence similaritiesi

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.PROSITE-ProRule annotation
Contains 1 kinesin motor domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5059.
HOVERGENiHBG097734.
InParanoidiQ6RT24.
KOiK11498.
PhylomeDBiQ6RT24.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 1 hit.
PfamiPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6RT24-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEEASVAVC VRVRPLNSRE EELGEATHIY WKTDKNAIYQ SDGGKSFQFD
60 70 80 90 100
RVFDSNETTK NVYEEIAVPI ISSAIQGYNG TIFAYGQTAS GKTHTMMGSE
110 120 130 140 150
DCLGVIPRAI HDIFQRIKKF PEREFLLRVS YMEIYNETIT DLLCNAQKMK
160 170 180 190 200
PLIIREDTNR TVYVSDLTEE VVYTAEMALK WLATGEKNRH YGITKMNQRS
210 220 230 240 250
SRSHTIFRMI LESREKAEPS NCDGSVKVSH LNLVDLAGSE RAAQTGAEGV
260 270 280 290 300
RLKEGCFINR NLFILGQVIK KLSDGQVGGF INYRDSKLTR ILQNSLGGNA
310 320 330 340 350
KTRIICTITP ASLDETLTTL QFASTAKYMK NTPYVNEVSN DEALLKRYRR
360 370 380 390 400
EIADLRKQLE EVNTKTRAQE MEKDQLAQLL DEKDLLQKVQ DEKINNLKRM
410 420 430 440 450
LVTSSSIALQ QELEIKRKRR VTWCYGKMKD SNYEKEFKVP TSITTRKRKT
460 470 480 490 500
SVTSLRENSL MKFGESAASS EFEMLNNTLE SLAEVEWSSA TTLLSEENVE
510 520 530 540 550
SELNSLNAQY NDLVLDYEQL RRENEDLKLK LKEKNELEEF ELLEQKEERD
560 570 580 590 600
QEMQLMHEVS NLKNLIKHAE EYNQDLENDL SSKVKLLKEK EEQIKNLQEY
610 620 630 640 650
IDAQKSEKMK IDLSYTSDAT EDLKQAMRTL SDLDTVALDA KKESAFLRSE
660 670 680 690 700
NLELKEKINE LSDSRKQMES DIQMYQRQLE AKKKMQTDLD KELQLAFQEI
710 720 730 740 750
SKLSALVDGK GLLSNLELEK RITDLQKELN KEAEEKQTLQ EEVNLLSELK
760 770 780 790 800
SLPSEVETLR RELYEKSEEL HIITTEREKL FSEMAHKDSR IQGLLEEIGN
810 820 830 840 850
TRDDLATSQL SRRGSDGEWQ ALESLHAELE HRHAGVLEER ERLKQEIGAL
860 870 880 890 900
SKEAESLAFS LDSVKAELSH KTQELEQKTV EGQERLNKME ALREELESRD
910 920 930 940 950
SSLQSVEKEK VLLTEKLQQA LKEVKALTQE KKNLKQLQES LQTERDQLRS
960 970 980 990 1000
DIQDTVNMNI DTQEQLLNAL ESLKQHQETI NMLKMKAAEE LSDNLHVKDR
1010 1020 1030 1040 1050
GGARDEAQQK MDGIDEQNES AHTLLGGGKD NEVTEEQRKI DSLMQENSGL
1060 1070 1080 1090 1100
QQTLESVRAE KEQLKMDLKE NIEMSIENQE ELRILRDELK RQQEVAAQEK
1110 1120 1130 1140 1150
DHATEKTQEL SRTQERLAKT EEKLEEKNQK LQETQQQLLS TQEAMSKLQA
1160 1170 1180 1190 1200
KVIDMESLQN EFRNQGLALE RVETEKLELA QRLHESYEEV KSITKERNDL
1210 1220 1230 1240 1250
KELQESFEIE KKQLKEYARE IEAEGLQAKE ELNIAHANLK EYQEIITELR
1260 1270 1280 1290 1300
GSISENEAQG ASTQDTAKSA PELQGEVPEL LEQELLPVVK EARHSAEKVN
1310 1320 1330 1340 1350
GLEPVGAHSR TVHSMTMEGI EIGNLRLTKK LEESQMEISC LTREREDLRR
1360 1370 1380 1390 1400
TQETLQVECT QLKEDARRTL ANHLETEEEL NLARCCLKEQ ENKIDTLITS
1410 1420 1430 1440 1450
LSQRETELSS VRGQLALTTA ELERKVQELC EKQEELTRKE TSEAQGKMSE
1460 1470 1480 1490 1500
LEQLRELLLA QASALQNAES DRLRLNTQLE ESQEEMKTLR EEREELRRMQ
1510 1520 1530 1540 1550
EALHVESEQQ KESMKEISSK LQELQNKEYE CLAMKTINET QGSRCEMDHL
1560 1570 1580 1590 1600
NQQLEAQKST LEKVEMENVN LTQRLHETLE EMRSVAKERD ELWSMEERLT
1610 1620 1630 1640 1650
VERDQLKKSL EETVTKGMEK EEELRVAHVH LEEHQETINK LRKMVSDYTD
1660 1670 1680 1690 1700
EISHTQGDLK HTNAVVEAQN QDLREKEHQL SQVKADLRET VDQMEQLKKK
1710 1720 1730 1740 1750
LEAQSSTLES REIEKLELTQ QLNENLKKIT LVTKENDSLK IMDEALREER
1760 1770 1780 1790 1800
DQLRKSLQQT EARDLENQEK LRIAHMNLKE HQETIDRLME TMSEKTEEIS
1810 1820 1830 1840 1850
NMKMELENVN MKLQEKVQEL KTSERQRVKL KADASEAKKE LKEQGLTLSK
1860 1870 1880 1890 1900
IEMENLNLAQ KIHENLEEMK SVRKERDDLK KLEEILRMER DQLKDNLREA
1910 1920 1930 1940 1950
MLKAHQNHEE TMKCGKGLLC AGEYCTGRLR EKCFRIEKLL KRYSEMANDY
1960 1970 1980 1990 2000
ECLNKVSLDL ERETKTQKEL SVTVRTKLSL PHTQTKEMEK LLTANQRCSL
2010 2020 2030 2040 2050
EFHRALKRLK YVLSSIARIK EEQHESINKR EMAFIQEVEK QNELQIQIQS
2060 2070 2080 2090 2100
LSQTYRIPAR DLQIKLSQEM DLHIEEMLKD FSENDFLTIK TEVQQVLNNR
2110 2120 2130 2140 2150
KEITEFLGKW LNTLFDTENL KSTIQKENKS IGLVNNFYHS RITAMINEST
2160 2170 2180 2190 2200
EFEERSATRS KDLDQYLKSL KETTEQLSEV YQTLTASQSV VHLHPTVQPS
2210 2220 2230 2240 2250
TRDSERPQAA SGAEQLTSKN KIALGAVPYK EEIEDLKMQL VKSDLEKKAT
2260 2270 2280 2290 2300
AKEFDKKILS LKATVEHQEE MIRLLRENLR GHQQAQDTSM ISEQDSQLLS
2310 2320 2330 2340 2350
KPLTCGGGSG IVQSTKALIL KSEYKRMGSE ISKLKQQNEQ LRKQNNQLLS
2360 2370 2380 2390 2400
DNSQLSNEVK TWEERTLKRD SYRETTCENS PKSPKVTRTD SKRRQNTTSQ
2410 2420 2430 2440 2450
CRAQNLQDPV PKDSPKSWFF DNRSKSLPAP HPIRYFDNSS LGLCPEPDDV
2460 2470
ENVEPKTDLC QASLEKDVSQ CKTQ
Length:2,474
Mass (Da):286,525
Last modified:July 5, 2004 - v1
Checksum:iBAF52DD6068A2903
GO

Sequence cautioni

The sequence AAH52843.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAI06097.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence BAC33868.1 differs from that shown. Reason: Frameshift at position 1759.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti231 – 24111LNLVDLAGSER → IKLIDTVDLEG in BAA22386. (PubMed:9275178)CuratedAdd
BLAST
Sequence conflicti1760 – 17601T → A in BAC33868. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY493378 mRNA. Translation: AAR85498.1.
BC049989 mRNA. Translation: AAH49989.1.
BC052843 mRNA. Translation: AAH52843.1. Sequence problems.
BC059032 mRNA. Translation: AAH59032.1.
BC106096 mRNA. Translation: AAI06097.1. Sequence problems.
AK049676 mRNA. Translation: BAC33868.1. Frameshift.
AK133445 mRNA. Translation: BAE21661.1.
AB001426 mRNA. Translation: BAA22386.1.
RefSeqiNP_776123.3. NM_173762.4.
UniGeneiMm.161470.

Genome annotation databases

GeneIDi229841.
KEGGimmu:229841.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY493378 mRNA. Translation: AAR85498.1 .
BC049989 mRNA. Translation: AAH49989.1 .
BC052843 mRNA. Translation: AAH52843.1 . Sequence problems.
BC059032 mRNA. Translation: AAH59032.1 .
BC106096 mRNA. Translation: AAI06097.1 . Sequence problems.
AK049676 mRNA. Translation: BAC33868.1 . Frameshift.
AK133445 mRNA. Translation: BAE21661.1 .
AB001426 mRNA. Translation: BAA22386.1 .
RefSeqi NP_776123.3. NM_173762.4.
UniGenei Mm.161470.

3D structure databases

ProteinModelPortali Q6RT24.
SMRi Q6RT24. Positions 4-339.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 230907. 4 interactions.
IntActi Q6RT24. 3 interactions.
STRINGi 10090.ENSMUSP00000057938.

PTM databases

PhosphoSitei Q6RT24.

Proteomic databases

MaxQBi Q6RT24.
PaxDbi Q6RT24.
PRIDEi Q6RT24.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 229841.
KEGGi mmu:229841.

Organism-specific databases

CTDi 1062.
MGIi MGI:1098230. Cenpe.

Phylogenomic databases

eggNOGi COG5059.
HOVERGENi HBG097734.
InParanoidi Q6RT24.
KOi K11498.
PhylomeDBi Q6RT24.

Miscellaneous databases

NextBioi 379688.
PROi Q6RT24.
SOURCEi Search...

Gene expression databases

Genevestigatori Q6RT24.

Family and domain databases

Gene3Di 3.40.850.10. 1 hit.
InterProi IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR24115. PTHR24115. 1 hit.
Pfami PF00225. Kinesin. 1 hit.
[Graphical view ]
PRINTSi PR00380. KINESINHEAVY.
SMARTi SM00129. KISc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Centromere-associated protein-E is essential for the mammalian mitotic checkpoint to prevent aneuploidy due to single chromosome loss."
    Weaver B.A., Bonday Z.Q., Putkey F.R., Kops G.J., Silk A.D., Cleveland D.W.
    J. Cell Biol. 162:551-563(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH BUBR1, SUBCELLULAR LOCATION.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-546 AND 1652-2474.
    Strain: C57BL/6JImported and Czech IIImported.
    Tissue: BrainImported, EggImported, Mammary tumorImported and Olfactory epitheliumImported.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-520 AND 1705-2474.
    Strain: C57BL/6JImported.
    Tissue: Spinal cordImported and TestisImported.
  4. "Identification and classification of 16 new kinesin superfamily (KIF) proteins in mouse genome."
    Nakagawa T., Tanaka Y., Matsuoka E., Kondo S., Okada Y., Noda Y., Kanai Y., Hirokawa N.
    Proc. Natl. Acad. Sci. U.S.A. 94:9654-9659(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 82-241, TISSUE SPECIFICITY.
    Strain: ICRImported.
    Tissue: Hippocampus1 Publication.
  5. "Unstable kinetochore-microtubule capture and chromosomal instability following deletion of CENP-E."
    Putkey F.R., Cramer T., Morphew M.K., Silk A.D., Johnson R.S., McIntosh J.R., Cleveland D.W.
    Dev. Cell 3:351-365(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiCENPE_MOUSE
AccessioniPrimary (citable) accession number: Q6RT24
Secondary accession number(s): O35059
, Q3KQQ6, Q3V044, Q6PD00, Q7TPX4, Q80YB4, Q8BWX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3