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Entry version 104 (13 Nov 2019)
Sequence version 1 (05 Jul 2004)
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Protein

Centromere-associated protein E

Gene

Cenpe

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. The transport of pole-proximal chromosomes towards the spindle equator is favored by microtubule tracks that are detyrosinated. 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. Suppresses chromosome congression in NDC80-depleted cells and contributes positively to congression only when microtubules are stabilized (By similarity). Plays an important role in the formation of stable attachments between kinetochores and spindle microtubules (PubMed:12925705). 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 (PubMed:12361599). Necessary for the mitotic checkpoint signal at individual kinetochores to prevent aneuploidy due to single chromosome loss (PubMed:12925705).By similarity2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi86 – 93ATPPROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-MMU-2132295 MHC class II antigen presentation
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-MMU-68877 Mitotic Prometaphase
R-MMU-983189 Kinesins

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CenpeImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1098230 Cenpe

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003651061 – 2471Centromere-associated protein EAdd BLAST2471
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00003967432472 – 2474Removed in mature formBy similarity3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei614PhosphoserineBy similarity1
Modified residuei2414PhosphoserineBy similarity1
Modified residuei2426PhosphoserineBy similarity1
Modified residuei2471Cysteine methyl esterBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2471S-farnesyl cysteineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q6RT24

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q6RT24

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q6RT24

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q6RT24

PRoteomics IDEntifications database

More...
PRIDEi
Q6RT24

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q6RT24

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q6RT24

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

Interacts with CENPF, SEPT7 KIF18A and PRC1 (By similarity).

Interacts with BUB1B (PubMed:12925705).

Interacts with SKAP; this interaction greatly favors SKAP binding to microtubules.

Interacts with TRAPPC12 and CTCF (By similarity).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
230907, 85 interactors

Protein interaction database and analysis system

More...
IntActi
Q6RT24, 4 interactors

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000057938

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q6RT24

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini6 – 329Kinesin motorPROSITE-ProRule annotationAdd BLAST324

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1962 – 2252Kinetochore binding domainBy similarityAdd BLAST291
Regioni2286 – 2471Globular autoinhibitory domainBy similarityAdd BLAST186

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili334 – 2366Sequence analysisAdd BLAST2033

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0242 Eukaryota
COG5059 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q6RT24

KEGG Orthology (KO)

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KOi
K11498

Database of Orthologous Groups

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OrthoDBi
21522at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q6RT24

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.850.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

The PANTHER Classification System

More...
PANTHERi
PTHR24115 PTHR24115, 2 hits

Pfam protein domain database

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Pfami
View protein in Pfam
PF00225 Kinesin, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00380 KINESINHEAVY

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00129 KISc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52540 SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00411 KINESIN_MOTOR_1, 1 hit
PS50067 KINESIN_MOTOR_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBAF52DD6068A2903
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9QKK1E9QKK1_MOUSE
Centromere-associated protein E
Cenpe
2,471Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0G2JG58A0A0G2JG58_MOUSE
Centromere-associated protein E
Cenpe
194Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH52843 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAI06097 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAC33868 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti231 – 241LNLVDLAGSER → IKLIDTVDLEG in BAA22386 (PubMed:9275178).CuratedAdd BLAST11
Sequence conflicti1760T → A in BAC33868 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
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

NCBI Reference Sequences

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RefSeqi
NP_776123.3, NM_173762.4

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
229841

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:229841

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

3D structure databases

SMRiQ6RT24
ModBaseiSearch...

Protein-protein interaction databases

BioGridi230907, 85 interactors
IntActiQ6RT24, 4 interactors
STRINGi10090.ENSMUSP00000057938

PTM databases

iPTMnetiQ6RT24
PhosphoSitePlusiQ6RT24

Proteomic databases

EPDiQ6RT24
jPOSTiQ6RT24
MaxQBiQ6RT24
PaxDbiQ6RT24
PRIDEiQ6RT24

Genome annotation databases

GeneIDi229841
KEGGimmu:229841

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
1062
MGIiMGI:1098230 Cenpe

Phylogenomic databases

eggNOGiKOG0242 Eukaryota
COG5059 LUCA
InParanoidiQ6RT24
KOiK11498
OrthoDBi21522at2759
PhylomeDBiQ6RT24

Enzyme and pathway databases

ReactomeiR-MMU-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-MMU-2132295 MHC class II antigen presentation
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-MMU-68877 Mitotic Prometaphase
R-MMU-983189 Kinesins

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Cenpe mouse

Protein Ontology

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PROi
PR:Q6RT24

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Family and domain databases

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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCENPE_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q6RT24
Secondary accession number(s): O35059
, Q3KQQ6, Q3V044, Q6PD00, Q7TPX4, Q80YB4, Q8BWX6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: July 5, 2004
Last modified: November 13, 2019
This is version 104 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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