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Entry version 85 (07 Apr 2021)
Sequence version 1 (14 Nov 2006)
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Protein

Segment polarity protein dishevelled homolog DVL-2

Gene

dvl2

Organism
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
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 transcript 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

Involved in at least 2 independent signaling cascades, controlling cell fate via canonical Wnt signaling and cell polarity via a planar cell polarity (PCP) cascade. Acts synergistically with dal/dapple-like to activate Wnt signaling, stabilizing ctnnb1/beta-catenin and leading to dorsal axis formation. Also prevents degradation of ctnnb1/beta-catenin by displacing gsk3 from a complex with ARP/Axin-related protein. Has an additional role in anterior-posterior (A/P) axis formation, specifying different neuroectodermal cell fates along the A/P axis in a dose-dependent manner by activating several early patterning genes. In the PCP pathway, required at the cell membrane for PCP-mediated neural and mesodermal convergent extension during gastrulation and subsequent neural tube closure, acting to activate jnk. Also involved in blastopore closure and archenteron elongation during early, but not late, gastrulation. Associates with ephrin receptors and ligands and acts as part of a downstream PCP pathway to mediate ephrin-mediated cell repulsion via activation of rhoa. Required for efnb1/ephrin-B1-driven movement of non-retinal progenitor cells into the retina during eye field formation. Patterns the hindbrain. Required for ciliogenesis. Controls the docking of basal bodies to the apical plasma membrane; mediates the activation, but not localization of rhoa at the apical surface of ciliated cells during basal body docking. Furthermore, required for the association of basal bodies with membrane-bound vesicles and the vesicle-trafficking protein exoc4/sec8, and this association is in turn required for basal body docking. Once basal bodies are docked, required for the planar polarization of basal bodies that underlies ciliary beating and the directional fluid flow across ciliated epithelia (By similarity).By similarity

<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
Biological processCilium biogenesis/degradation, Gastrulation, Wnt signaling pathway

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-XTR-201688, WNT mediated activation of DVL
R-XTR-2028269, Signaling by Hippo
R-XTR-4086400, PCP/CE pathway
R-XTR-4641258, Degradation of DVL
R-XTR-4641262, Disassembly of the destruction complex and recruitment of AXIN to the membrane
R-XTR-5099900, WNT5A-dependent internalization of FZD4
R-XTR-5663220, RHO GTPases Activate Formins

<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%5Fand%5Ftaxonomy%5Fsection">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:
Segment polarity protein dishevelled homolog DVL-2By similarity
Short name:
Dishevelled-2By similarity
Alternative name(s):
DSH homolog 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:dvl2Imported
Synonyms:dshBy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiXenopus tropicalis (Western clawed frog) (Silurana tropicalis)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri8364 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000008143 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Unassembled WGS sequence

Organism-specific databases

Xenopus laevis and tropicalis biology and genomics resource

More...
Xenbasei
XB-GENE-1017461, dvl2

<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

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003546651 – 732Segment polarity protein dishevelled homolog DVL-2Add BLAST732

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Phosphorylated. Phosphorylation is controlled by frizzled proteins, correlates with the onset of embryo dorsalizing events and is higher in the dorsal half of early cleavage embryos. Phosphorylated on tyrosine residues in response to association with efnb1/ephrin-B1 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...
PaxDbi
Q05AS8

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Can form homomultimers.

Interacts with prickle1.

Interacts (via the PDZ domain) with ccdc88c/dal and dact1-B/dpr.

Interacts (via the DIX domain) with ARP/Axin-related protein and dact1-A/frodo.

Interacts with sdc4, possibly via fz7.

Interacts directly (via the DEP domain) with efnb1/ephrin-B1. May interact indirectly with the phosphorylated ephrin receptors ephb1 and ephb2 via SH domain-containing adapters (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
8364.ENSXETP00000037494

<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
Q05AS8

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%5Fand%5Fdomains%5Fsection">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>Domaini1 – 82DIXPROSITE-ProRule annotationAdd BLAST82
Domaini250 – 335PDZPROSITE-ProRule annotationAdd BLAST86
Domaini424 – 498DEPPROSITE-ProRule annotationAdd BLAST75

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi90 – 127Pro-richSequence analysisAdd BLAST38
Compositional biasi218 – 223Poly-ArgSequence analysis6
Compositional biasi637 – 708Pro-richSequence analysisAdd BLAST72

<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 C-terminal region containing the DEP domain is required for membrane accumulation and phosphorylation. Wnt signaling and axis induction requires the DIX domain. The C-terminus contributes to the localization at the cilia base (By similarity).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 DSH family.Sequence analysis

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3571, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q05AS8

Identification of Orthologs from Complete Genome Data

More...
OMAi
TPWPLLH

Database of Orthologous Groups

More...
OrthoDBi
474724at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.10, 1 hit
2.30.42.10, 1 hit
3.10.20.380, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000591, DEP_dom
IPR024580, Dishevelled_C-dom
IPR008339, Dishevelled_fam
IPR003351, Dishevelled_protein_dom
IPR001158, DIX
IPR038207, DIX_dom_sf
IPR015506, Dsh/Dvl-rel
IPR008341, DVL2
IPR001478, PDZ
IPR036034, PDZ_sf
IPR029071, Ubiquitin-like_domsf
IPR036388, WH-like_DNA-bd_sf
IPR036390, WH_DNA-bd_sf

The PANTHER Classification System

More...
PANTHERi
PTHR10878, PTHR10878, 1 hit
PTHR10878:SF8, PTHR10878:SF8, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00610, DEP, 1 hit
PF02377, Dishevelled, 1 hit
PF00778, DIX, 1 hit
PF12316, Dsh_C, 1 hit
PF00595, PDZ, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01760, DISHEVELLED
PR01762, DISHEVELLED2

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00021, DAX, 1 hit
SM00049, DEP, 1 hit
SM00228, PDZ, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46785, SSF46785, 1 hit
SSF50156, SSF50156, 1 hit
SSF54236, SSF54236, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50186, DEP, 1 hit
PS50841, DIX, 1 hit
PS50106, PDZ, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q05AS8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAETKVIYHL DEEETPYLVK VPVPANEIRL RDFKAALGRG HAKYFFKAMD
60 70 80 90 100
QDFGVVKEEI SDDNAKLPCF NGRVVSWLVS SETSQTDSAP PAAEVRPDPP
110 120 130 140 150
PVPPPVPPPP AERTSGIGDS RPPSFHPNVS GSTEQLDQDN ESVISMRRDR
160 170 180 190 200
VRRRDSTEQG VARGVNGRAE RHLSGYESSS TLLTSEIETS ICDSEEDDAM
210 220 230 240 250
SRFSSSTEQS SASRLLKRHR RRRKQRPPRL ERTSSFSSVT DSTMSLNIIT
260 270 280 290 300
VTLNMEKYNF LGISIVGQSN ERGDGGIYIG SIMKGGAVAA DGRIEPGDML
310 320 330 340 350
LQVNDINFEN MSNDDAVRVL RDIVHKPGPI ILTVAKCWDP SPQGYFTLPR
360 370 380 390 400
NEPIQPIDPA AWVSHSAALS GSFPVYPGSA SMSSMTSSTS VTETELSHAL
410 420 430 440 450
PPVSLFSLSV HTDLASVAKV MASPESGLEV RDRMWLKITI PNAFLGSDMV
460 470 480 490 500
DWLYHHVEGF QDRREARKFA SNLLKAGLIR HTVNKITFSE QCYYIFGDLT
510 520 530 540 550
GCENYMANLS LNDNDGSSGA SDQDTLAPLP LPGASPWPLL PTFSYQYPAP
560 570 580 590 600
HPYSTQPPAY HELSSYSYGM GSAGSQHSEG SRSSGSNRSD GGRGTQKDER
610 620 630 640 650
SGVVGVGGGE SKSGSGSESE YSTRSSIRRI GGGEAGPPSE RSTSSRPPLH
660 670 680 690 700
HPPSVHSYAA PGVPLSYNPM MLMMMPPPPL PPPGACPPSS SVPPGAPPLV
710 720 730
RDLASVPPEL TASRQSFHMA MGNPSEFFVD VM
Length:732
Mass (Da):79,277
Last modified:November 14, 2006 - 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:i2683B15F9FAA5841
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F7EL55F7EL55_XENTR
Segment polarity protein dishevelle...
dvl2
316Annotation 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>

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
BC123948 mRNA Translation: AAI23949.1

NCBI Reference Sequences

More...
RefSeqi
NP_001072660.1, NM_001079192.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
780117

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
xtr:780117

<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
BC123948 mRNA Translation: AAI23949.1
RefSeqiNP_001072660.1, NM_001079192.1

3D structure databases

SMRiQ05AS8
ModBaseiSearch...

Protein-protein interaction databases

STRINGi8364.ENSXETP00000037494

Proteomic databases

PaxDbiQ05AS8

Genome annotation databases

GeneIDi780117
KEGGixtr:780117

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1856
XenbaseiXB-GENE-1017461, dvl2

Phylogenomic databases

eggNOGiKOG3571, Eukaryota
InParanoidiQ05AS8
OMAiTPWPLLH
OrthoDBi474724at2759

Enzyme and pathway databases

ReactomeiR-XTR-201688, WNT mediated activation of DVL
R-XTR-2028269, Signaling by Hippo
R-XTR-4086400, PCP/CE pathway
R-XTR-4641258, Degradation of DVL
R-XTR-4641262, Disassembly of the destruction complex and recruitment of AXIN to the membrane
R-XTR-5099900, WNT5A-dependent internalization of FZD4
R-XTR-5663220, RHO GTPases Activate Formins

Family and domain databases

Gene3Di1.10.10.10, 1 hit
2.30.42.10, 1 hit
3.10.20.380, 1 hit
InterProiView protein in InterPro
IPR000591, DEP_dom
IPR024580, Dishevelled_C-dom
IPR008339, Dishevelled_fam
IPR003351, Dishevelled_protein_dom
IPR001158, DIX
IPR038207, DIX_dom_sf
IPR015506, Dsh/Dvl-rel
IPR008341, DVL2
IPR001478, PDZ
IPR036034, PDZ_sf
IPR029071, Ubiquitin-like_domsf
IPR036388, WH-like_DNA-bd_sf
IPR036390, WH_DNA-bd_sf
PANTHERiPTHR10878, PTHR10878, 1 hit
PTHR10878:SF8, PTHR10878:SF8, 1 hit
PfamiView protein in Pfam
PF00610, DEP, 1 hit
PF02377, Dishevelled, 1 hit
PF00778, DIX, 1 hit
PF12316, Dsh_C, 1 hit
PF00595, PDZ, 1 hit
PRINTSiPR01760, DISHEVELLED
PR01762, DISHEVELLED2
SMARTiView protein in SMART
SM00021, DAX, 1 hit
SM00049, DEP, 1 hit
SM00228, PDZ, 1 hit
SUPFAMiSSF46785, SSF46785, 1 hit
SSF50156, SSF50156, 1 hit
SSF54236, SSF54236, 1 hit
PROSITEiView protein in PROSITE
PS50186, DEP, 1 hit
PS50841, DIX, 1 hit
PS50106, PDZ, 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 nameiDVL2_XENTR
<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: Q05AS8
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 14, 2006
Last modified: April 7, 2021
This is version 85 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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