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Protein

Peptidyl-prolyl cis-trans isomerase A

Gene

PPIA

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

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.1 Publication

<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

Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.1 Publication

<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: UniProtKB
  • peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB
  • RNA binding Source: UniProtKB
  • unfolded protein binding Source: GO_Central
  • virion binding 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 functionIsomerase, Rotamase
Biological processHost-virus interaction

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
5.2.1.8 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-114608 Platelet degranulation
R-HSA-162585 Uncoating of the HIV Virion
R-HSA-162588 Budding and maturation of HIV virion
R-HSA-162592 Integration of provirus
R-HSA-162594 Early Phase of HIV Life Cycle
R-HSA-164516 Minus-strand DNA synthesis
R-HSA-164525 Plus-strand DNA synthesis
R-HSA-173107 Binding and entry of HIV virion
R-HSA-175474 Assembly Of The HIV Virion
R-HSA-180689 APOBEC3G mediated resistance to HIV-1 infection
R-HSA-2025928 Calcineurin activates NFAT
R-HSA-210991 Basigin interactions
R-HSA-6798695 Neutrophil degranulation
R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation

<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 A (EC:5.2.1.81 Publication)
Short name:
PPIase A
Alternative name(s):
Cyclophilin A
Cyclosporin A-binding protein
Rotamase A
Cleaved into the following chain:
<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:PPIA
Synonyms:CYPA
<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 7

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000196262.13

Human Gene Nomenclature Database

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HGNCi
HGNC:9253 PPIA

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
123840 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P62937

<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, Secreted

<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>Mutagenesisi121W → A: 200-fold decrease of sensitivity to CsA. 1 Publication1
Mutagenesisi121W → E: Loss of peptidyl-prolyl cis-trans isomerase activity. 1 Publication1
Mutagenesisi121W → F: 75-fold decrease of sensitivity to CsA. 1 Publication1
Mutagenesisi121W → H: No effect on peptidyl-prolyl cis-trans isomerase activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
5478

Open Targets

More...
OpenTargetsi
ENSG00000196262

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA33574

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1949

Drug and drug target database

More...
DrugBanki
DB01742 (3r)-1-Acetyl-3-Methylpiperidine
DB00091 Cyclosporine
DB02419 Ethyl Oxo(Piperidin-1-Yl)Acetate
DB00172 L-Proline

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
2751

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PPIA

Domain mapping of disease mutations (DMDM)

More...
DMDMi
51702775

<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_00004232401 – 165Peptidyl-prolyl cis-trans isomerase AAdd BLAST165
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; alternateCombined sources5 Publications
ChainiPRO_00000641152 – 165Peptidyl-prolyl cis-trans isomerase A, N-terminally processedAdd BLAST164

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 residuei1N-acetylmethionineCombined sources1
Modified residuei2N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processedCombined sources2 Publications1
Modified residuei28N6-acetyllysine; alternateCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residuei44N6-acetyllysineCombined sources1
Modified residuei76N6-acetyllysineCombined sources1
Modified residuei77PhosphoserineCombined sources1
Modified residuei82N6-acetyllysine; alternateCombined sources1
Cross-linki82Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei93PhosphothreonineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi108N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei125N6-acetyllysineCombined sources1 Publication1
Modified residuei131N6-acetyllysineCombined sources1
Modified residuei133N6-acetyllysineBy 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

Acetylation at Lys-125 markedly inhibits catalysis of cis to trans isomerization and stabilizes cis rather than trans forms of the HIV-1 capsid. PPIA acetylation also antagonizes the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition.2 Publications

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P62937

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

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PaxDbi
P62937

PeptideAtlas

More...
PeptideAtlasi
P62937

PRoteomics IDEntifications database

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PRIDEi
P62937

ProteomicsDB human proteome resource

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ProteomicsDBi
12696
57455

Consortium for Top Down Proteomics

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TopDownProteomicsi
P62937-1 [P62937-1]

2D gel databases

DOSAC-COBS 2D-PAGE database

More...
DOSAC-COBS-2DPAGEi
P62937

USC-OGP 2-DE database

More...
OGPi
P62937

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00419585
P62937

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P62937

University College Dublin 2-DE Proteome Database

More...
UCD-2DPAGEi
P62937

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P62937

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

More...
PhosphoSitePlusi
P62937

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P62937

<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
ENSG00000196262 Expressed in 206 organ(s), highest expression level in anterior cingulate cortex

CleanEx database of gene expression profiles

More...
CleanExi
HS_PPIA

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P62937 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P62937 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB004655
HPA058345

<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 protein phosphatase PPP3CA/calcineurin A (PubMed:12218175, PubMed:12357034).2 Publications
(Microbial infection) Interacts with HIV-1 capsid protein (PubMed:20364129, PubMed:8513493).2 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)

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BioGridi
111474, 124 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P62937

Database of interacting proteins

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DIPi
DIP-6080N

Protein interaction database and analysis system

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IntActi
P62937, 77 interactors

Molecular INTeraction database

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MINTi
P62937

STRING: functional protein association networks

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STRINGi
9606.ENSP00000419425

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P62937

<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

1165
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
P62937

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

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SMRi
P62937

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P62937

<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>Domaini7 – 163PPIase cyclophilin-typePROSITE-ProRule annotationAdd 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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0865 Eukaryota
COG0652 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153142

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000065981

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG001065

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P62937

KEGG Orthology (KO)

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KOi
K03767

Identification of Orthologs from Complete Genome Data

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OMAi
RFLDGQY

Database of Orthologous Groups

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OrthoDBi
EOG091G0BGL

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P62937

TreeFam database of animal gene trees

More...
TreeFami
TF316719

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.100.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR029000 Cyclophilin-like_dom_sf
IPR024936 Cyclophilin-type_PPIase
IPR020892 Cyclophilin-type_PPIase_CS
IPR002130 Cyclophilin-type_PPIase_dom

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

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001467 Peptidylpro_ismrse, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00153 CSAPPISMRASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
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

<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 (2+)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 2 <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 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P62937-1) [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
MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG
60 70 80 90 100
SCFHRIIPGF MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSM
110 120 130 140 150
ANAGPNTNGS QFFICTAKTE WLDGKHVVFG KVKEGMNIVE AMERFGSRNG
160
KTSKKITIAD CGQLE
Length:165
Mass (Da):18,012
Last modified:January 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:i9B2E637A555E4434
GO
Isoform 2 (identifier: P62937-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: Missing.

Show »
Length:105
Mass (Da):11,418
Checksum:i4629A635A48F744B
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
C9J5S7C9J5S7_HUMAN
Peptidyl-prolyl cis-trans isomerase
PPIA
121Annotation 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>
F8WE65F8WE65_HUMAN
Peptidyl-prolyl cis-trans isomerase
PPIA
120Annotation 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>
E5RIZ5E5RIZ5_HUMAN
Peptidyl-prolyl cis-trans isomerase...
PPIA
58Annotation 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>

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 conflicti89I → T in AAH05982 (PubMed:15489334).Curated1
Sequence conflicti106N → I in AAH07104 (PubMed:15489334).Curated1
Sequence conflicti165E → D in CAG32988 (Ref. 4) Curated1

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_0560501 – 60Missing in isoform 2. 2 PublicationsAdd BLAST60

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
Y00052 mRNA Translation: CAA68264.1
X52851 Genomic DNA Translation: CAA37039.1
AK290085 mRNA Translation: BAF82774.1
AK293003 mRNA Translation: BAF85692.1
CR456707 mRNA Translation: CAG32988.1
AB451307 mRNA Translation: BAG70121.1
AB451438 mRNA Translation: BAG70252.1
AY739283 Genomic DNA Translation: AAU13906.1
AC004854 Genomic DNA No translation available.
AC013436 Genomic DNA No translation available.
BC000689 mRNA Translation: AAH00689.1
BC003026 mRNA Translation: AAH03026.2
BC005320 mRNA Translation: AAH05320.1
BC005982 mRNA Translation: AAH05982.1
BC007104 mRNA Translation: AAH07104.1
BC013915 mRNA Translation: AAH13915.1
BC073992 mRNA Translation: AAH73992.1
BC093076 mRNA Translation: AAH93076.1
BC106030 mRNA Translation: AAI06031.1
BC137057 mRNA Translation: AAI37058.1
BC137058 mRNA Translation: AAI37059.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS5494.1 [P62937-1]
CCDS75592.1 [P62937-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
A94496 CSHUA

NCBI Reference Sequences

More...
RefSeqi
NP_001287910.1, NM_001300981.1 [P62937-2]
NP_066953.1, NM_021130.4 [P62937-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.356331

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000355968; ENSP00000430817; ENSG00000196262 [P62937-2]
ENST00000468812; ENSP00000419425; ENSG00000196262 [P62937-1]
ENST00000489459; ENSP00000427976; ENSG00000196262 [P62937-2]
ENST00000620047; ENSP00000479961; ENSG00000196262 [P62937-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5478

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5478

UCSC genome browser

More...
UCSCi
uc064djo.1 human [P62937-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs
Wikipedia

Cyclophilin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00052 mRNA Translation: CAA68264.1
X52851 Genomic DNA Translation: CAA37039.1
AK290085 mRNA Translation: BAF82774.1
AK293003 mRNA Translation: BAF85692.1
CR456707 mRNA Translation: CAG32988.1
AB451307 mRNA Translation: BAG70121.1
AB451438 mRNA Translation: BAG70252.1
AY739283 Genomic DNA Translation: AAU13906.1
AC004854 Genomic DNA No translation available.
AC013436 Genomic DNA No translation available.
BC000689 mRNA Translation: AAH00689.1
BC003026 mRNA Translation: AAH03026.2
BC005320 mRNA Translation: AAH05320.1
BC005982 mRNA Translation: AAH05982.1
BC007104 mRNA Translation: AAH07104.1
BC013915 mRNA Translation: AAH13915.1
BC073992 mRNA Translation: AAH73992.1
BC093076 mRNA Translation: AAH93076.1
BC106030 mRNA Translation: AAI06031.1
BC137057 mRNA Translation: AAI37058.1
BC137058 mRNA Translation: AAI37059.1
CCDSiCCDS5494.1 [P62937-1]
CCDS75592.1 [P62937-2]
PIRiA94496 CSHUA
RefSeqiNP_001287910.1, NM_001300981.1 [P62937-2]
NP_066953.1, NM_021130.4 [P62937-1]
UniGeneiHs.356331

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
1AK4X-ray2.36A/B1-165[»]
1AWQX-ray1.58A2-165[»]
1AWRX-ray1.58A/B/C/D/E/F2-165[»]
1AWSX-ray2.55A2-165[»]
1AWTX-ray2.55A/B/C/D/E/F2-165[»]
1AWUX-ray2.34A2-165[»]
1AWVX-ray2.34A/B/C/D/E/F2-165[»]
1BCKX-ray1.80A1-165[»]
1CWAX-ray2.10A1-165[»]
1CWBX-ray2.20A1-165[»]
1CWCX-ray1.86A1-165[»]
1CWFX-ray1.86A1-165[»]
1CWHX-ray1.86A1-165[»]
1CWIX-ray1.90A1-165[»]
1CWJX-ray1.80A1-165[»]
1CWKX-ray1.80A1-165[»]
1CWLX-ray1.80A1-165[»]
1CWMX-ray2.00A1-165[»]
1CWOX-ray1.86A1-165[»]
1FGLX-ray1.80A1-165[»]
1M63X-ray2.80C/G1-165[»]
1M9CX-ray2.00A/B1-165[»]
1M9DX-ray1.90A/B1-165[»]
1M9EX-ray1.72A/B1-164[»]
1M9FX-ray1.73A/B1-165[»]
1M9XX-ray1.70A/B/E/F1-165[»]
1M9YX-ray1.90A/B/E/F1-165[»]
1MF8X-ray3.10C1-165[»]
1MIKX-ray1.76A1-165[»]
1NMKX-ray2.10A/B1-165[»]
1OCANMR-A1-165[»]
1RMHX-ray2.40A/B2-165[»]
1VBSX-ray2.00A1-165[»]
1VBTX-ray2.30A/B1-165[»]
1W8LX-ray1.80A2-165[»]
1W8MX-ray1.65A2-165[»]
1W8VX-ray1.70A2-165[»]
1YNDX-ray1.60A/B1-165[»]
1ZKFX-ray2.55A/B1-165[»]
2ALFX-ray1.90A2-165[»]
2CPLX-ray1.63A1-165[»]
2CYHX-ray1.64A2-165[»]
2MS4NMR-A1-165[»]
2MZUNMR-A1-165[»]
2N0TNMR-A1-165[»]
2RMAX-ray2.10A/C/E/G/I/K/M/O/Q/S1-165[»]
2RMBX-ray2.10A/C/E/G/I/K/M/O/Q/S1-165[»]
2X25X-ray1.20B2-165[»]
2X2AX-ray1.40A/B1-165[»]
2X2CX-ray2.41K/M/O/Q/S1-165[»]
2X2DX-ray1.95B/C1-165[»]
2XGYX-ray1.80B1-165[»]
3CYHX-ray1.90A2-165[»]
3CYSNMR-A1-165[»]
3K0MX-ray1.25A1-165[»]
3K0NX-ray1.39A1-165[»]
3K0OX-ray1.55A1-165[»]
3K0PX-ray1.65A1-165[»]
3K0QX-ray2.32A1-165[»]
3K0RX-ray2.42A1-165[»]
3ODIX-ray2.20A/C/E/G/I/K/M/O/Q/S1-165[»]
3ODLX-ray2.31A/C/E/G/I/K/M/O/Q/S1-165[»]
3RDDX-ray2.14A1-165[»]
4CYHX-ray2.10A2-165[»]
4IPZX-ray1.67A1-165[»]
4N1MX-ray1.15A1-165[»]
4N1NX-ray1.50A1-165[»]
4N1OX-ray1.75A1-165[»]
4N1PX-ray1.90A1-165[»]
4N1QX-ray1.65A1-165[»]
4N1RX-ray1.80A1-165[»]
4N1SX-ray1.47A1-165[»]
4YUGX-ray1.48A1-165[»]
4YUHX-ray1.34A1-165[»]
4YUIX-ray1.38A1-165[»]
4YUJX-ray1.42A1-165[»]
4YUKX-ray1.48A1-165[»]
4YULX-ray1.42A1-165[»]
4YUMX-ray1.50A1-165[»]
4YUNX-ray1.58A1-165[»]
4YUOX-ray1.20A1-165[»]
4YUPX-ray1.75A1-165[»]
5CYHX-ray2.10A2-165[»]
5F66X-ray1.15A1-165[»]
5FJBelectron microscopy9.00C2-165[»]
5KULX-ray1.70A2-165[»]
5KUNX-ray1.70A2-165[»]
5KUOX-ray1.70A2-165[»]
5KUQX-ray1.70A2-165[»]
5KURX-ray1.70A2-165[»]
5KUSX-ray1.70A2-165[»]
5KUUX-ray1.70A2-165[»]
5KUVX-ray1.70A2-165[»]
5KUWX-ray1.70A2-165[»]
5KUZX-ray1.70A2-165[»]
5KV0X-ray1.70A2-165[»]
5KV1X-ray1.70A2-165[»]
5KV2X-ray1.70A2-165[»]
5KV3X-ray1.70A2-165[»]
5KV4X-ray1.70A2-165[»]
5KV5X-ray1.70A2-165[»]
5KV6X-ray1.70A2-165[»]
5KV7X-ray1.70A2-165[»]
5LUDX-ray1.25A1-165[»]
5NOQX-ray1.60A1-165[»]
5NORX-ray1.80A1-165[»]
5NOSX-ray1.35A1-165[»]
5NOTX-ray1.45A1-165[»]
5NOUX-ray1.30A1-165[»]
5NOVX-ray2.00A1-165[»]
5NOWX-ray1.48A1-165[»]
5NOXX-ray1.49A1-165[»]
5NOYX-ray1.43A1-165[»]
5NOZX-ray1.61A1-165[»]
5T9UX-ray2.30A/B/C/D1-164[»]
5T9WX-ray2.00A2-165[»]
5T9ZX-ray1.40A2-164[»]
5TA2X-ray1.48A2-164[»]
5TA4X-ray1.50A2-165[»]
5WC7X-ray1.43A1-165[»]
6BTAX-ray1.50A1-165[»]
ProteinModelPortaliP62937
SMRiP62937
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111474, 124 interactors
CORUMiP62937
DIPiDIP-6080N
IntActiP62937, 77 interactors
MINTiP62937
STRINGi9606.ENSP00000419425

Chemistry databases

BindingDBiP62937
ChEMBLiCHEMBL1949
DrugBankiDB01742 (3r)-1-Acetyl-3-Methylpiperidine
DB00091 Cyclosporine
DB02419 Ethyl Oxo(Piperidin-1-Yl)Acetate
DB00172 L-Proline
GuidetoPHARMACOLOGYi2751

PTM databases

iPTMnetiP62937
PhosphoSitePlusiP62937
SwissPalmiP62937

Polymorphism and mutation databases

BioMutaiPPIA
DMDMi51702775

2D gel databases

DOSAC-COBS-2DPAGEiP62937
OGPiP62937
REPRODUCTION-2DPAGEiIPI00419585
P62937
SWISS-2DPAGEiP62937
UCD-2DPAGEiP62937

Proteomic databases

EPDiP62937
PaxDbiP62937
PeptideAtlasiP62937
PRIDEiP62937
ProteomicsDBi12696
57455
TopDownProteomicsiP62937-1 [P62937-1]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5478
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355968; ENSP00000430817; ENSG00000196262 [P62937-2]
ENST00000468812; ENSP00000419425; ENSG00000196262 [P62937-1]
ENST00000489459; ENSP00000427976; ENSG00000196262 [P62937-2]
ENST00000620047; ENSP00000479961; ENSG00000196262 [P62937-2]
GeneIDi5478
KEGGihsa:5478
UCSCiuc064djo.1 human [P62937-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5478
DisGeNETi5478
EuPathDBiHostDB:ENSG00000196262.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PPIA
HGNCiHGNC:9253 PPIA
HPAiCAB004655
HPA058345
MIMi123840 gene
neXtProtiNX_P62937
OpenTargetsiENSG00000196262
PharmGKBiPA33574

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0865 Eukaryota
COG0652 LUCA
GeneTreeiENSGT00940000153142
HOGENOMiHOG000065981
HOVERGENiHBG001065
InParanoidiP62937
KOiK03767
OMAiRFLDGQY
OrthoDBiEOG091G0BGL
PhylomeDBiP62937
TreeFamiTF316719

Enzyme and pathway databases

BRENDAi5.2.1.8 2681
ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-162585 Uncoating of the HIV Virion
R-HSA-162588 Budding and maturation of HIV virion
R-HSA-162592 Integration of provirus
R-HSA-162594 Early Phase of HIV Life Cycle
R-HSA-164516 Minus-strand DNA synthesis
R-HSA-164525 Plus-strand DNA synthesis
R-HSA-173107 Binding and entry of HIV virion
R-HSA-175474 Assembly Of The HIV Virion
R-HSA-180689 APOBEC3G mediated resistance to HIV-1 infection
R-HSA-2025928 Calcineurin activates NFAT
R-HSA-210991 Basigin interactions
R-HSA-6798695 Neutrophil degranulation
R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation

Miscellaneous databases

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

More...
ChiTaRSi
PPIA human
EvolutionaryTraceiP62937

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Peptidylprolyl_isomerase_A

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

More...
GenomeRNAii
5478

Protein Ontology

More...
PROi
PR:P62937

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000196262 Expressed in 206 organ(s), highest expression level in anterior cingulate cortex
CleanExiHS_PPIA
ExpressionAtlasiP62937 baseline and differential
GenevisibleiP62937 HS

Family and domain databases

Gene3Di2.40.100.10, 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
PANTHERiPTHR11071 PTHR11071, 1 hit
PfamiView protein in Pfam
PF00160 Pro_isomerase, 1 hit
PIRSFiPIRSF001467 Peptidylpro_ismrse, 1 hit
PRINTSiPR00153 CSAPPISMRASE
SUPFAMiSSF50891 SSF50891, 1 hit
PROSITEiView protein in PROSITE
PS00170 CSA_PPIASE_1, 1 hit
PS50072 CSA_PPIASE_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 nameiPPIA_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: P62937
Secondary accession number(s): A8K220
, P05092, Q3KQW3, Q567Q0, Q6IBU5, Q96IX3, Q9BRU4, Q9BTY9, Q9UC61
<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: August 13, 1987
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 170 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. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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