Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peptidyl-prolyl cis-trans isomerase D

Gene

Ppid

Organism
Rattus norvegicus (Rat)
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

PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity region. Involved in regulation of UV radiation-induced apoptosis.By similarity

Caution

This protein should not be confused with mitochondrial peptidyl-prolyl cis-trans isomerase F (PPIF) which is often referred to as cyclophilin D or CypD.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Less sensitive to inhibition by cyclosporin A than is CYP-18.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

  • cyclosporin A binding Source: RGD
  • enzyme binding Source: RGD
  • estrogen receptor binding Source: UniProtKB
  • Hsp70 protein binding Source: UniProtKB
  • Hsp90 protein binding Source: UniProtKB
  • peptidyl-prolyl cis-trans isomerase activity Source: RGD
  • transcription factor binding Source: UniProtKB
  • unfolded protein binding Source: GO_Central

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 functionChaperone, Isomerase, Rotamase
Biological processApoptosis, Protein transport, Transport

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-8939211 ESR-mediated signaling

<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:
Peptidyl-prolyl cis-trans isomerase DBy similarity (EC:5.2.1.8By similarity)
Short name:
PPIase DBy similarity
Alternative name(s):
40 kDa peptidyl-prolyl cis-trans isomerase
Cyclophilin-40By similarity
Short name:
CYP-40By similarity
Rotamase DBy similarity
<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:PpidImported
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 2

Organism-specific databases

Rat genome database

More...
RGDi
1303174 Ppid

<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

Cytoplasm, 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000641551 – 370Peptidyl-prolyl cis-trans isomerase DAdd BLAST370

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 residuei5PhosphoserineBy similarity1
Modified residuei171N6-acetyllysineBy similarity1
Modified residuei198PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q6DGG0

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

More...
PaxDbi
Q6DGG0

PRoteomics IDEntifications database

More...
PRIDEi
Q6DGG0

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q6DGG0

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

More...
PhosphoSitePlusi
Q6DGG0

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q6DGG0

<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

More...
Bgeei
ENSRNOG00000027408 Expressed in 10 organ(s), highest expression level in brain

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q6DGG0 RN

<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

Identified in ESR1 or NR3C1/GCR steroid receptor-chaperone complexes. Found in HSP90 chaperone complexes with kinase clients LCK or EIF2AK1. Two monomers associate with one HSP90 homodimer. Interacts with HSP90AA1. Interacts with HSP90AB1; PPID and FKBP4 compete for binding to HSP90AB1 and the interaction is mutually exclusive with the PPID:HSPA8 interaction. Interacts with HSPA8; PPID and STIP1 but not FKBP4 compete for binding to HSPA8 and the interaction is mutually exclusive with the PPID:HSP90AB1 interaction. Interacts with S100A1 and S100A2; the interactions dissociate the PPID:HSP90AA1 interaction. Interacts with S100A6. Interacts with MYB, ILF2, XRCC6, RACK1 and RPS3. Interacts with cytoplasmic dynein 1 intermediate chain (DYNC1I1 or DYNC1I2) (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000035797

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q6DGG0

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

More...
SMRi
Q6DGG0

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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>Domaini19 – 183PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST165
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati223 – 256TPR 1Add BLAST34
Repeati273 – 306TPR 2Add BLAST34
Repeati308 – 340TPR 3Add BLAST33

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>Regioni185 – 215Chaperone activityBy similarityAdd BLAST31
Regioni214 – 370Interaction with HSP90AB1By similarityAdd BLAST157

<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

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0546 Eukaryota
COG0652 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154672

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000065980

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG053654

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q6DGG0

KEGG Orthology (KO)

More...
KOi
K05864

Identification of Orthologs from Complete Genome Data

More...
OMAi
AMCAIKL

Database of Orthologous Groups

More...
OrthoDBi
1403619at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q6DGG0

TreeFam database of animal gene trees

More...
TreeFami
TF324493

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.40.10, 1 hit
2.40.100.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029000 Cyclophilin-like_dom_sf
IPR024936 Cyclophilin-type_PPIase
IPR020892 Cyclophilin-type_PPIase_CS
IPR002130 Cyclophilin-type_PPIase_dom
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_repeat

The PANTHER Classification System

More...
PANTHERi
PTHR11071 PTHR11071, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00160 Pro_isomerase, 1 hit
PF13176 TPR_7, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00153 CSAPPISMRASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00028 TPR, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48452 SSF48452, 1 hit
SSF50891 SSF50891, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00170 CSA_PPIASE_1, 1 hit
PS50072 CSA_PPIASE_2, 1 hit
PS50005 TPR, 3 hits
PS50293 TPR_REGION, 2 hits

<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>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.

Q6DGG0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSHPSPAGKP SNSKNPRVFF DVDIGGERVG RIVLELFADI VPKTAENFRA
60 70 80 90 100
LCTGEKGTGP TTGKPLHFKG CPFHRIIKKF MIQGGDFSNQ NGTGGESIYG
110 120 130 140 150
EKFEDENFHY KHDREGLLSM ANAGPNTNGS QFFITTVPTP HLDGKHVVFG
160 170 180 190 200
QVIKGLGVAR MLENVEVNGE KPAKLCVIAE CGELKEGDEW GIFPKDGSGD
210 220 230 240 250
SHPDFPEDAD IDLKDVDKIL LISEDLKNIG NTFFKSQNWE MAIKKYAKVL
260 270 280 290 300
RYLDSSKAVI EKADVSRLQP IALSCVLNIG ACKLKMSNWQ GAIDSCLEAL
310 320 330 340 350
EMDPSNTKAL YRKAQGWQGL KEYDQALADL KKAQEIAPGD KAIQAELLKV
360 370
KQMIKAQKDK EKAVYAKMFA
Length:370
Mass (Da):40,766
Last modified:January 23, 2007 - v3
<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:i47E3001A73F3B175
GO

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
BC076386 mRNA Translation: AAH76386.1

NCBI Reference Sequences

More...
RefSeqi
NP_001004279.1, NM_001004279.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Rn.136915

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000037890; ENSRNOP00000035797; ENSRNOG00000027408

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
361967

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:361967

UCSC genome browser

More...
UCSCi
RGD:1303174 rat

<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
BC076386 mRNA Translation: AAH76386.1
RefSeqiNP_001004279.1, NM_001004279.1
UniGeneiRn.136915

3D structure databases

ProteinModelPortaliQ6DGG0
SMRiQ6DGG0
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000035797

PTM databases

iPTMnetiQ6DGG0
PhosphoSitePlusiQ6DGG0
SwissPalmiQ6DGG0

Proteomic databases

jPOSTiQ6DGG0
PaxDbiQ6DGG0
PRIDEiQ6DGG0

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000037890; ENSRNOP00000035797; ENSRNOG00000027408
GeneIDi361967
KEGGirno:361967
UCSCiRGD:1303174 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5481
RGDi1303174 Ppid

Phylogenomic databases

eggNOGiKOG0546 Eukaryota
COG0652 LUCA
GeneTreeiENSGT00940000154672
HOGENOMiHOG000065980
HOVERGENiHBG053654
InParanoidiQ6DGG0
KOiK05864
OMAiAMCAIKL
OrthoDBi1403619at2759
PhylomeDBiQ6DGG0
TreeFamiTF324493

Enzyme and pathway databases

ReactomeiR-RNO-8939211 ESR-mediated signaling

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q6DGG0

Gene expression databases

BgeeiENSRNOG00000027408 Expressed in 10 organ(s), highest expression level in brain
GenevisibleiQ6DGG0 RN

Family and domain databases

Gene3Di1.25.40.10, 1 hit
2.40.100.10, 1 hit
InterProiView protein in InterPro
IPR029000 Cyclophilin-like_dom_sf
IPR024936 Cyclophilin-type_PPIase
IPR020892 Cyclophilin-type_PPIase_CS
IPR002130 Cyclophilin-type_PPIase_dom
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_repeat
PANTHERiPTHR11071 PTHR11071, 1 hit
PfamiView protein in Pfam
PF00160 Pro_isomerase, 1 hit
PF13176 TPR_7, 1 hit
PRINTSiPR00153 CSAPPISMRASE
SMARTiView protein in SMART
SM00028 TPR, 3 hits
SUPFAMiSSF48452 SSF48452, 1 hit
SSF50891 SSF50891, 1 hit
PROSITEiView protein in PROSITE
PS00170 CSA_PPIASE_1, 1 hit
PS50072 CSA_PPIASE_2, 1 hit
PS50005 TPR, 3 hits
PS50293 TPR_REGION, 2 hits

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 nameiPPID_RAT
<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: Q6DGG0
<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: May 24, 2005
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 127 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again