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Entry version 118 (16 Oct 2019)
Sequence version 2 (30 May 2000)
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Protein

Kinesin-like protein KIF2C

Gene

KIF2C

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
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

In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells (By similarity). Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis (PubMed:14960279). Plays a role in chromosome congression and is required for the lateral to end-on conversion of the chromosome-microtubule attachment (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei258ATPBy similarity1

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 bindingi342 – 349ATPPROSITE-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

Biological processCell cycle, Cell division, Chromosome partition, Mitosis
LigandATP-binding, Nucleotide-binding

<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:
Kinesin-like protein KIF2C
Alternative name(s):
Kinesin-like protein 6
Mitotic centromere-associated kinesin
Short name:
MCAK
<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:KIF2C
Synonyms:KNSL6
<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>OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
<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 identifieri10029 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaCricetidaeCricetinaeCricetulus

<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, Microtubule, Nucleus

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi92S → A: Increased frequency of metaphase figures; when associated with A-106; A-108; A-112 and A-186. 2 Publications1
Mutagenesisi92S → E: Altered interaction with MTUS2/TIP150 and association with microtubules. Altered localization, reduced microtubule depolymerizing activity and increased frequency of prometaphase figures; when associated with E-106; E-108; E-112 and E-186. 2 Publications1
Mutagenesisi106S → A: Increased frequency of metaphase figures; when associated with A-92; A-108; A-112 and A-186. 1 Publication1
Mutagenesisi106S → E: Altered localization, reduced microtubule depolymerizing activity and increased frequency of prometaphase figures; when associated with E-92; E-108; E-112 and E-186. 1 Publication1
Mutagenesisi108S → A: Increased frequency of metaphase figures; when associated with A-92; A-106; A-112 and A-186. 1 Publication1
Mutagenesisi108S → E: Altered localization, reduced microtubule depolymerizing activity and increased frequency of prometaphase figures; when associated with E-92; E-106; E-112 and E-186. 1 Publication1
Mutagenesisi112S → A: Increased frequency of metaphase figures; when associated with A-92; A-106; A-108 and A-186. 1 Publication1
Mutagenesisi112S → E: Altered localization, reduced microtubule depolymerizing activity and increased frequency of prometaphase figures; when associated with E-92; E-106; E-108 and E-186. 1 Publication1
Mutagenesisi186S → A: Increased frequency of metaphase figures; when associated with A-92; A-106; A-108 and A-112. 1 Publication1
Mutagenesisi186S → E: Altered localization, reduced microtubule depolymerizing activity and increased frequency of prometaphase figures; when associated with E-92; E-106; E-108 and E-112. 1 Publication1
Mutagenesisi489G → A: No effect on microtubule depolymerization but unable to release tubulin dimers to recycle catalytically. 1 Publication1
Mutagenesisi491E → A: No effect on microtubule depolymerization but unable to release tubulin dimers to recycle catalytically. 1 Publication1

<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_00001254171 – 718Kinesin-like protein KIF2CAdd BLAST718

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 residuei3PhosphoserineBy similarity1
Modified residuei19PhosphoserineBy similarity1
Modified residuei92Phosphoserine; by AURKBBy similarity1
Modified residuei106Phosphoserine1 Publication1
Modified residuei108Phosphoserine1 Publication1
Modified residuei112Phosphoserine1 Publication1
Modified residuei163PhosphoserineBy similarity1
Modified residuei186Phosphoserine1 Publication1
Modified residuei513PhosphoserineBy similarity1
Modified residuei626PhosphoserineBy 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

Phosphorylation by AURKB, regulates association with centromeres and kinetochores and the microtubule depolymerization activity.1 Publication
Ubiquitinated.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P70096

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P70096

<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

Interacts with CENPH (By similarity).

Interacts with MTUS2/TIP150; the interaction is direct (PubMed:19543227).

Interacts with MAPRE1; the interaction is direct, regulated by phosphorylation and is probably required for targeting to growing microtubule plus ends (PubMed:19543227).

Interacts with KIF18B at microtubule tips; this interaction increases the affinity of both partners for microtubule plus ends and is required for robust microtubule depolymerization. Phosphorylation by AURKA or AURKB strongly reduces KIF18B-binding (By similarity).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
1613894, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10029.XP_007608905.1

<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
P70096

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>Domaini252 – 582Kinesin motorPROSITE-ProRule annotationAdd BLAST331

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>Regioni1 – 248GlobularSequence analysisAdd BLAST248
Regioni201 – 232Negative regulator of microtubule-bindingBy similarityAdd BLAST32

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 coili613 – 651Sequence analysisAdd BLAST39
Coiled coili689 – 716Sequence analysisAdd BLAST28

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi95 – 98Microtubule tip localization signal4
Motifi409 – 412Nuclear localization signalSequence analysis4

<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 microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.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. MCAK/KIF2 subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K10393

Identification of Orthologs from Complete Genome Data

More...
OMAi
RTTLECH

Database of Orthologous Groups

More...
OrthoDBi
418348at2759

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, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00225 Kinesin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00380 KINESINHEAVY

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00129 KISc, 1 hit

Superfamily database of structural and functional annotation

More...
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>Sequencei

<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.

P70096-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MESLPARLFP GLSIKIQRSN GLIHSANIST VNVEKSCVSV EWIEGGNTKG
60 70 80 90 100
KEIDFDDVAA INPELLQLLP LHPKDNLPLQ ENVTVPKQKR RSVNSKIPAP
110 120 130 140 150
KEGLRSRSTR MSTVPEVRIA TQENEMEVEL PVATNSRKQF SVATGLPRPS
160 170 180 190 200
CPAMTELPLS MVSEEAEEQV HPTRSTSSAN PARRKSCIVK EMEKMKNKRE
210 220 230 240 250
EKRAQNSEIR IKRAQEYDSS FPNWEFARMI KEFRVTIECH PLTLTDPTEE
260 270 280 290 300
HRICVCVRKR PLNKQELAKK EIDVISVPSK CLLFVHEPKL KVDLTKYLEN
310 320 330 340 350
QAFCFDFAFD ETASNEVVYR FTARPLVQTI FEGGKATCFA YGQTGSGKTH
360 370 380 390 400
TMGGDLSGKS QNTSKGIYAM ASRDVFLLKS QPRYRNLNLE VYVTFFEIYN
410 420 430 440 450
GKVFDLLNKK AKLRVLEDSK QQVQVVGLQE YLVNCADDVI KMLNMGSACR
460 470 480 490 500
TSGQTFANSN SSRSHACFQI LLRAKGRLHG KFSLVDLAGN ERGADTSSAD
510 520 530 540 550
RQTRMEGAEI NKSLLALKEC IRALGQNKAH TPFRESKLTQ VLRDSFIGEN
560 570 580 590 600
SRTCMIAMIS PGISSCEYTL NTLRYADRVK ELSPHSGLSG EQPIQMETEE
610 620 630 640 650
MEASSNGTSL AVNFKEEEEL SSQMSSFNEA MSQIRELEER AMEELREIIQ
660 670 680 690 700
QGPGWLELSE MTDQPDYDLE TFVNKAESAL TQQTKHFSAL REVIKALRVA
710
MQLEEQASKQ MNSKKRHQ
Length:718
Mass (Da):80,918
Last modified:May 30, 2000 - 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:i16ABD8BC66AD11B2
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U11790 mRNA Translation: AAB17358.2

NCBI Reference Sequences

More...
RefSeqi
NP_001233671.1, NM_001246742.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSCGRT00015041056; ENSCGRP00015033641; ENSCGRG00015025354

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100689309

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cge:100689309

<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
U11790 mRNA Translation: AAB17358.2
RefSeqiNP_001233671.1, NM_001246742.1

3D structure databases

SMRiP70096
ModBaseiSearch...

Protein-protein interaction databases

BioGridi1613894, 1 interactor
STRINGi10029.XP_007608905.1

PTM databases

iPTMnetiP70096

Proteomic databases

PRIDEiP70096

Genome annotation databases

EnsembliENSCGRT00015041056; ENSCGRP00015033641; ENSCGRG00015025354
GeneIDi100689309
KEGGicge:100689309

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
11004

Phylogenomic databases

KOiK10393
OMAiRTTLECH
OrthoDBi418348at2759

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, 1 hit
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...

MobiDB: a database of protein disorder and mobility annotations

More...
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 nameiKIF2C_CRIGR
<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: P70096
<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: November 1, 1997
Last sequence update: May 30, 2000
Last modified: October 16, 2019
This is version 118 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

<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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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