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Protein

Centromere-associated protein E

Gene

CENPE

Organism
Homo sapiens (Human)
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 (PubMed:7889940, PubMed:23891108, PubMed:25395579). The transport of pole-proximal chromosomes towards the spindle equator is favored by microtubule tracks that are detyrosinated (PubMed:25908662). Acts as a processive bi-directional tracker of dynamic microtubule tips; after chromosomes have congressed, continues to play an active role at kinetochores, enhancing their links with dynamic microtubule ends (PubMed:23955301). Suppresses chromosome congression in NDC80-depleted cells and contributes positively to congression only when microtubules are stabilized (PubMed:25743205). Plays an important role in the formation of stable attachments between kinetochores and spindle microtubules (PubMed:17535814) The stabilization of kinetochore-microtubule attachment also requires CENPE-dependent localization of other proteins to the kinetochore including BUB1B, MAD1 and MAD2. Plays a role in spindle assembly checkpoint activation (SAC) via its interaction with BUB1B resulting in the activation of its kinase activity, which is important for activating SAC. Necessary for the mitotic checkpoint signal at individual kinetochores to prevent aneuploidy due to single chromosome loss (By similarity).By similarity7 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 – 93ATP8

<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

  • ATPase activity Source: GO_Central
  • ATP binding Source: UniProtKB-KW
  • kinetochore binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • microtubule motor activity Source: UniProtKB

GO - Biological processi

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

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q02224

<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 E
Alternative name(s):
Centromere protein E
Short name:
CENP-E
Kinesin-71 Publication
Kinesin-related protein CENPE
<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:CENPE
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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: Chromosome 4

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000138778.11

Human Gene Nomenclature Database

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HGNCi
HGNC:1856 CENPE

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
117143 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q02224

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Microcephaly 13, primary, autosomal recessive (MCPH13)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age-related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small.
See also OMIM:616051
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072429933D → N in MCPH13; results in defective mitotic spindle formation and chromosome segregation; results in delayed mitotic progression. 1 PublicationCorresponds to variant dbSNP:rs144716013EnsemblClinVar.1
Natural variantiVAR_0724301355K → E in MCPH13; results in defective mitotic spindle formation and chromosome segregation; results in delayed mitotic progression. 1 PublicationCorresponds to variant dbSNP:rs141488085EnsemblClinVar.1

Keywords - Diseasei

Disease mutation, Primary microcephaly

Organism-specific databases

DisGeNET

More...
DisGeNETi
1062

MalaCards human disease database

More...
MalaCardsi
CENPE
MIMi616051 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000138778

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
808 Seckel syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA26400

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5870

Drug and drug target database

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DrugBanki
DB06097 GSK-923295

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CENPE

Domain mapping of disease mutations (DMDM)

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DMDMi
160358869

<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_00001254361 – 2698Centromere-associated protein EAdd BLAST2698
<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_00003967422699 – 2701Removed in mature formCurated3

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 residuei611PhosphoserineCombined sources1
Modified residuei2083PhosphoserineCombined sources1
Modified residuei2389PhosphoserineCombined sources1
Modified residuei2639PhosphoserineCombined sources1
Modified residuei2647PhosphoserineCombined sources1
Modified residuei2651PhosphoserineCombined sources1
Modified residuei2698Cysteine methyl esterCurated1
<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>Lipidationi2698S-farnesyl cysteine1 Publication1

<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.1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q02224

MaxQB - The MaxQuant DataBase

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MaxQBi
Q02224

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

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PaxDbi
Q02224

PeptideAtlas

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PeptideAtlasi
Q02224

PRoteomics IDEntifications database

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PRIDEi
Q02224

ProteomicsDB human proteome resource

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ProteomicsDBi
58063
58064 [Q02224-2]
58065 [Q02224-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q02224

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

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PhosphoSitePlusi
Q02224

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000138778 Expressed in 112 organ(s), highest expression level in oocyte

CleanEx database of gene expression profiles

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CleanExi
HS_CENPE

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q02224 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q02224 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA042294

<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 (PubMed:15236970). Interacts with CENPF (PubMed:9763420). Interacts with BUB1B (PubMed:9763420, PubMed:19625775). Interacts with SEPT7 (PubMed:18460473). Interacts with KIF18A (PubMed:19625775). Interacts with PRC1 (PubMed:15297875). Interacts with NUF2; this interaction determines kinetochore localization (PubMed:17535814). Interacts with SKAP; this interaction greatly favors SKAP binding to microtubules (PubMed:22110139). Interacts with TRAPPC12 (PubMed:25918224). Interacts with CTCF (PubMed:25395579).9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
107491, 41 interactors

Database of interacting proteins

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DIPi
DIP-38902N

Protein interaction database and analysis system

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IntActi
Q02224, 27 interactors

Molecular INTeraction database

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MINTi
Q02224

STRING: functional protein association networks

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STRINGi
9606.ENSP00000265148

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q02224

<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

Secondary structure

12701
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q02224

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

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SMRi
Q02224

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q02224

<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>Regioni2126 – 2476Kinetochore-binding domainAdd BLAST351
Regioni2510 – 2698Globular autoinhibitory domainBy similarityAdd BLAST189

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 coili336 – 2590Sequence analysisAdd BLAST2255

<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

More...
eggNOGi
KOG0242 Eukaryota
COG5059 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000160597

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000111540

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG097734

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q02224

KEGG Orthology (KO)

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KOi
K11498

Identification of Orthologs from Complete Genome Data

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OMAi
SVCRASW

Database of Orthologous Groups

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OrthoDBi
EOG091G0CFT

Database for complete collections of gene phylogenies

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PhylomeDBi
Q02224

TreeFam database of animal gene trees

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TreeFami
TF330343

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.850.10, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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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

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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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)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 describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q02224-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAEEGAVAVC VRVRPLNSRE ESLGETAQVY WKTDNNVIYQ VDGSKSFNFD
60 70 80 90 100
RVFHGNETTK NVYEEIAAPI IDSAIQGYNG TIFAYGQTAS GKTYTMMGSE
110 120 130 140 150
DHLGVIPRAI HDIFQKIKKF PDREFLLRVS YMEIYNETIT DLLCGTQKMK
160 170 180 190 200
PLIIREDVNR NVYVADLTEE VVYTSEMALK WITKGEKSRH YGETKMNQRS
210 220 230 240 250
SRSHTIFRMI LESREKGEPS NCEGSVKVSH LNLVDLAGSE RAAQTGAAGV
260 270 280 290 300
RLKEGCNINR SLFILGQVIK KLSDGQVGGF INYRDSKLTR ILQNSLGGNA
310 320 330 340 350
KTRIICTITP VSFDETLTAL QFASTAKYMK NTPYVNEVST DEALLKRYRK
360 370 380 390 400
EIMDLKKQLE EVSLETRAQA MEKDQLAQLL EEKDLLQKVQ NEKIENLTRM
410 420 430 440 450
LVTSSSLTLQ QELKAKRKRR VTWCLGKINK MKNSNYADQF NIPTNITTKT
460 470 480 490 500
HKLSINLLRE IDESVCSESD VFSNTLDTLS EIEWNPATKL LNQENIESEL
510 520 530 540 550
NSLRADYDNL VLDYEQLRTE KEEMELKLKE KNDLDEFEAL ERKTKKDQEM
560 570 580 590 600
QLIHEISNLK NLVKHAEVYN QDLENELSSK VELLREKEDQ IKKLQEYIDS
610 620 630 640 650
QKLENIKMDL SYSLESIEDP KQMKQTLFDA ETVALDAKRE SAFLRSENLE
660 670 680 690 700
LKEKMKELAT TYKQMENDIQ LYQSQLEAKK KMQVDLEKEL QSAFNEITKL
710 720 730 740 750
TSLIDGKVPK DLLCNLELEG KITDLQKELN KEVEENEALR EEVILLSELK
760 770 780 790 800
SLPSEVERLR KEIQDKSEEL HIITSEKDKL FSEVVHKESR VQGLLEEIGK
810 820 830 840 850
TKDDLATTQS NYKSTDQEFQ NFKTLHMDFE QKYKMVLEEN ERMNQEIVNL
860 870 880 890 900
SKEAQKFDSS LGALKTELSY KTQELQEKTR EVQERLNEME QLKEQLENRD
910 920 930 940 950
STLQTVEREK TLITEKLQQT LEEVKTLTQE KDDLKQLQES LQIERDQLKS
960 970 980 990 1000
DIHDTVNMNI DTQEQLRNAL ESLKQHQETI NTLKSKISEE VSRNLHMEEN
1010 1020 1030 1040 1050
TGETKDEFQQ KMVGIDKKQD LEAKNTQTLT ADVKDNEIIE QQRKIFSLIQ
1060 1070 1080 1090 1100
EKNELQQMLE SVIAEKEQLK TDLKENIEMT IENQEELRLL GDELKKQQEI
1110 1120 1130 1140 1150
VAQEKNHAIK KEGELSRTCD RLAEVEEKLK EKSQQLQEKQ QQLLNVQEEM
1160 1170 1180 1190 1200
SEMQKKINEI ENLKNELKNK ELTLEHMETE RLELAQKLNE NYEEVKSITK
1210 1220 1230 1240 1250
ERKVLKELQK SFETERDHLR GYIREIEATG LQTKEELKIA HIHLKEHQET
1260 1270 1280 1290 1300
IDELRRSVSE KTAQIINTQD LEKSHTKLQE EIPVLHEEQE LLPNVKEVSE
1310 1320 1330 1340 1350
TQETMNELEL LTEQSTTKDS TTLARIEMER LRLNEKFQES QEEIKSLTKE
1360 1370 1380 1390 1400
RDNLKTIKEA LEVKHDQLKE HIRETLAKIQ ESQSKQEQSL NMKEKDNETT
1410 1420 1430 1440 1450
KIVSEMEQFK PKDSALLRIE IEMLGLSKRL QESHDEMKSV AKEKDDLQRL
1460 1470 1480 1490 1500
QEVLQSESDQ LKENIKEIVA KHLETEEELK VAHCCLKEQE ETINELRVNL
1510 1520 1530 1540 1550
SEKETEISTI QKQLEAINDK LQNKIQEIYE KEEQFNIKQI SEVQEKVNEL
1560 1570 1580 1590 1600
KQFKEHRKAK DSALQSIESK MLELTNRLQE SQEEIQIMIK EKEEMKRVQE
1610 1620 1630 1640 1650
ALQIERDQLK ENTKEIVAKM KESQEKEYQF LKMTAVNETQ EKMCEIEHLK
1660 1670 1680 1690 1700
EQFETQKLNL ENIETENIRL TQILHENLEE MRSVTKERDD LRSVEETLKV
1710 1720 1730 1740 1750
ERDQLKENLR ETITRDLEKQ EELKIVHMHL KEHQETIDKL RGIVSEKTNE
1760 1770 1780 1790 1800
ISNMQKDLEH SNDALKAQDL KIQEELRIAH MHLKEQQETI DKLRGIVSEK
1810 1820 1830 1840 1850
TDKLSNMQKD LENSNAKLQE KIQELKANEH QLITLKKDVN ETQKKVSEME
1860 1870 1880 1890 1900
QLKKQIKDQS LTLSKLEIEN LNLAQKLHEN LEEMKSVMKE RDNLRRVEET
1910 1920 1930 1940 1950
LKLERDQLKE SLQETKARDL EIQQELKTAR MLSKEHKETV DKLREKISEK
1960 1970 1980 1990 2000
TIQISDIQKD LDKSKDELQK KIQELQKKEL QLLRVKEDVN MSHKKINEME
2010 2020 2030 2040 2050
QLKKQFEAQN LSMQSVRMDN FQLTKKLHES LEEIRIVAKE RDELRRIKES
2060 2070 2080 2090 2100
LKMERDQFIA TLREMIARDR QNHQVKPEKR LLSDGQQHLT ESLREKCSRI
2110 2120 2130 2140 2150
KELLKRYSEM DDHYECLNRL SLDLEKEIEF QKELSMRVKA NLSLPYLQTK
2160 2170 2180 2190 2200
HIEKLFTANQ RCSMEFHRIM KKLKYVLSYV TKIKEEQHES INKFEMDFID
2210 2220 2230 2240 2250
EVEKQKELLI KIQHLQQDCD VPSRELRDLK LNQNMDLHIE EILKDFSESE
2260 2270 2280 2290 2300
FPSIKTEFQQ VLSNRKEMTQ FLEEWLNTRF DIEKLKNGIQ KENDRICQVN
2310 2320 2330 2340 2350
NFFNNRIIAI MNESTEFEER SATISKEWEQ DLKSLKEKNE KLFKNYQTLK
2360 2370 2380 2390 2400
TSLASGAQVN PTTQDNKNPH VTSRATQLTT EKIRELENSL HEAKESAMHK
2410 2420 2430 2440 2450
ESKIIKMQKE LEVTNDIIAK LQAKVHESNK CLEKTKETIQ VLQDKVALGA
2460 2470 2480 2490 2500
KPYKEEIEDL KMKLVKIDLE KMKNAKEFEK EISATKATVE YQKEVIRLLR
2510 2520 2530 2540 2550
ENLRRSQQAQ DTSVISEHTD PQPSNKPLTC GGGSGIVQNT KALILKSEHI
2560 2570 2580 2590 2600
RLEKEISKLK QQNEQLIKQK NELLSNNQHL SNEVKTWKER TLKREAHKQV
2610 2620 2630 2640 2650
TCENSPKSPK VTGTASKKKQ ITPSQCKERN LQDPVPKESP KSCFFDSRSK
2660 2670 2680 2690 2700
SLPSPHPVRY FDNSSLGLCP EVQNAGAESV DSQPGPWHAS SGKDVPECKT

Q
Length:2,701
Mass (Da):316,415
Last modified:October 23, 2007 - v2
<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:i4BC59C2EF0B02D88
GO
Isoform 2 (identifier: Q02224-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2131-2166: Missing.

Show »
Length:2,665
Mass (Da):312,149
Checksum:iFD0951C16BECB82A
GO
Isoform 3 (identifier: Q02224-3) [UniParc]FASTAAdd to basket

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

Show »
Length:2,580
Mass (Da):301,789
Checksum:iC5EC35EE9A5E5524
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D6RBW0D6RBW0_HUMAN
Centromere-associated protein E
CENPE
1,126Annotation score:

Annotation score:2 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>
A0A087X0P0A0A087X0P0_HUMAN
Centromere-associated protein E
CENPE
2,664Annotation score:

Annotation score:2 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>
D6RHK2D6RHK2_HUMAN
Centromere-associated protein E
CENPE
183Annotation 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 BAE06078 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.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 conflicti51R → H in BAF83051 (PubMed:14702039).Curated1
Sequence conflicti300A → P in CAA78727 (PubMed:1406971).Curated1
Sequence conflicti440F → S in BAE06078 (Ref. 2) Curated1
Sequence conflicti566A → R in CAA78727 (PubMed:1406971).Curated1
Sequence conflicti902T → P in CAA78727 (PubMed:1406971).Curated1
Sequence conflicti1297E → K in CAA78727 (PubMed:1406971).Curated1
Sequence conflicti1546K → N in CAA78727 (PubMed:1406971).Curated1
Sequence conflicti1876K → E in CAA78727 (PubMed:1406971).Curated1
Sequence conflicti2008 – 2017AQNLSMQSVR → PNYLCKCE in CAA78727 (PubMed:1406971).Curated10
Sequence conflicti2190S → C in CAA78727 (PubMed:1406971).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_072429933D → N in MCPH13; results in defective mitotic spindle formation and chromosome segregation; results in delayed mitotic progression. 1 PublicationCorresponds to variant dbSNP:rs144716013EnsemblClinVar.1
Natural variantiVAR_0724301355K → E in MCPH13; results in defective mitotic spindle formation and chromosome segregation; results in delayed mitotic progression. 1 PublicationCorresponds to variant dbSNP:rs141488085EnsemblClinVar.1
Natural variantiVAR_0496891535F → L2 PublicationsCorresponds to variant dbSNP:rs2615542Ensembl.1
Natural variantiVAR_0496901581S → R. Corresponds to variant dbSNP:rs35100664Ensembl.1
Natural variantiVAR_0593701911S → T. Corresponds to variant dbSNP:rs1381657Ensembl.1
Natural variantiVAR_0496911925E → D. Corresponds to variant dbSNP:rs2306106Ensembl.1
Natural variantiVAR_0496922090T → M2 PublicationsCorresponds to variant dbSNP:rs2243682Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_028820549 – 573Missing in isoform 3. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_0288211972 – 2068IQELQ…EMIAR → Q in isoform 3. 1 PublicationAdd BLAST97
Alternative sequenceiVSP_0288222131 – 2166Missing in isoform 2. 1 PublicationAdd BLAST36

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z15005 mRNA Translation: CAA78727.1
AB209996 mRNA Translation: BAE06078.1 Different initiation.
AC079919 Genomic DNA No translation available.
CH471057 Genomic DNA Translation: EAX06171.1
AK290362 mRNA Translation: BAF83051.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS34042.1 [Q02224-1]
CCDS68768.1 [Q02224-3]

Protein sequence database of the Protein Information Resource

More...
PIRi
S28261

NCBI Reference Sequences

More...
RefSeqi
NP_001273663.1, NM_001286734.1 [Q02224-3]
NP_001804.2, NM_001813.2 [Q02224-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.75573

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000265148; ENSP00000265148; ENSG00000138778 [Q02224-1]
ENST00000380026; ENSP00000369365; ENSG00000138778 [Q02224-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1062

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:1062

UCSC genome browser

More...
UCSCi
uc003hxb.1 human [Q02224-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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
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
CCDSiCCDS34042.1 [Q02224-1]
CCDS68768.1 [Q02224-3]
PIRiS28261
RefSeqiNP_001273663.1, NM_001286734.1 [Q02224-3]
NP_001804.2, NM_001813.2 [Q02224-1]
UniGeneiHs.75573

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T5CX-ray2.50A/B2-342[»]
5JVPX-ray2.10A/B/C/D/E/F336-371[»]
ProteinModelPortaliQ02224
SMRiQ02224
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107491, 41 interactors
DIPiDIP-38902N
IntActiQ02224, 27 interactors
MINTiQ02224
STRINGi9606.ENSP00000265148

Chemistry databases

BindingDBiQ02224
ChEMBLiCHEMBL5870
DrugBankiDB06097 GSK-923295

PTM databases

iPTMnetiQ02224
PhosphoSitePlusiQ02224

Polymorphism and mutation databases

BioMutaiCENPE
DMDMi160358869

Proteomic databases

EPDiQ02224
MaxQBiQ02224
PaxDbiQ02224
PeptideAtlasiQ02224
PRIDEiQ02224
ProteomicsDBi58063
58064 [Q02224-2]
58065 [Q02224-3]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265148; ENSP00000265148; ENSG00000138778 [Q02224-1]
ENST00000380026; ENSP00000369365; ENSG00000138778 [Q02224-3]
GeneIDi1062
KEGGihsa:1062
UCSCiuc003hxb.1 human [Q02224-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1062
DisGeNETi1062
EuPathDBiHostDB:ENSG00000138778.11

GeneCards: human genes, protein and diseases

More...
GeneCardsi
CENPE

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0031416
HGNCiHGNC:1856 CENPE
HPAiHPA042294
MalaCardsiCENPE
MIMi117143 gene
616051 phenotype
neXtProtiNX_Q02224
OpenTargetsiENSG00000138778
Orphaneti808 Seckel syndrome
PharmGKBiPA26400

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0242 Eukaryota
COG5059 LUCA
GeneTreeiENSGT00940000160597
HOGENOMiHOG000111540
HOVERGENiHBG097734
InParanoidiQ02224
KOiK11498
OMAiSVCRASW
OrthoDBiEOG091G0CFT
PhylomeDBiQ02224
TreeFamiTF330343

Enzyme and pathway databases

ReactomeiR-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-HSA-2132295 MHC class II antigen presentation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-HSA-68877 Mitotic Prometaphase
R-HSA-983189 Kinesins
SIGNORiQ02224

Miscellaneous databases

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

More...
ChiTaRSi
CENPE human
EvolutionaryTraceiQ02224

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Centromere_protein_E

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
1062

Protein Ontology

More...
PROi
PR:Q02224

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000138778 Expressed in 112 organ(s), highest expression level in oocyte
CleanExiHS_CENPE
ExpressionAtlasiQ02224 baseline and differential
GenevisibleiQ02224 HS

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

More...
ProtoNeti
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_HUMAN
<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: Q02224
Secondary accession number(s): A6NKY9, A8K2U7, Q4LE75
<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: July 1, 1993
Last sequence update: October 23, 2007
Last modified: December 5, 2018
This is version 191 of the entry and version 2 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
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.

<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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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