PIN1 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 [Homo sapiens (human)] - Gene

Summary

Official Symbol: PIN1provided by HGNC
Official Full Name: peptidylprolyl cis/trans isomerase, NIMA-interacting 1provided by HGNC
Primary source: HGNC:HGNC:8988
See related: Ensembl:ENSG00000127445 MIM:601052; AllianceGenome:HGNC:8988
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: DOD; UBL5
Summary: Peptidyl-prolyl cis/trans isomerases (PPIases) catalyze the cis/trans isomerization of peptidyl-prolyl peptide bonds. This gene encodes one of the PPIases, which specifically binds to phosphorylated ser/thr-pro motifs to catalytically regulate the post-phosphorylation conformation of its substrates. The conformational regulation catalyzed by this PPIase has a profound impact on key proteins involved in the regulation of cell growth, genotoxic and other stress responses, the immune response, induction and maintenance of pluripotency, germ cell development, neuronal differentiation, and survival. This enzyme also plays a key role in the pathogenesis of Alzheimer's disease and many cancers. Multiple alternatively spliced transcript variants have been found for this gene.[provided by RefSeq, Jun 2011]
Expression: Ubiquitous expression in brain (RPKM 30.9), testis (RPKM 25.2) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 19p13.2

Exon count:: 6

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	19	NC_000019.10 (9835318..9849689)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	19	NC_060943.1 (9961482..9975854)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	19	NC_000019.9 (9945994..9960365)

Chromosome 19 - NC_000019.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

PIN1 promotes the metastasis of cholangiocarcinoma cells by RACK1-mediated phosphorylation of ANXA2.
Title: PIN1 promotes the metastasis of cholangiocarcinoma cells by RACK1-mediated phosphorylation of ANXA2.
The peptidyl-prolyl isomerase Pin1 controls GM-CSF-induced priming of NADPH oxidase in human neutrophils and priming at inflammatory sites.
Title: The peptidyl-prolyl isomerase Pin1 controls GM-CSF-induced priming of NADPH oxidase in human neutrophils and priming at inflammatory sites.
Stereospecific NANOG PEST Stabilization by Pin1.
Title: Stereospecific NANOG PEST Stabilization by Pin1.
Nuclear Phosphoproteome Reveals Prolyl Isomerase PIN1 as a Modulator of Oncogene-Induced Senescence.
Title: Nuclear Phosphoproteome Reveals Prolyl Isomerase PIN1 as a Modulator of Oncogene-Induced Senescence.
PIN1P1 is activated by CREB1 and promotes gastric cancer progression via interacting with YBX1 and upregulating PIN1.
Title: PIN1P1 is activated by CREB1 and promotes gastric cancer progression via interacting with YBX1 and upregulating PIN1.
The PIN1-YTHDF1 axis promotes breast tumorigenesis via the m[6]A-dependent stabilization of AURKA mRNA.
Title: The PIN1-YTHDF1 axis promotes breast tumorigenesis via the m(6)A-dependent stabilization of AURKA mRNA.
Stabilization of Pin1 by USP34 promotes Ubc9 isomerization and protein sumoylation in glioma stem cells.
Title: Stabilization of Pin1 by USP34 promotes Ubc9 isomerization and protein sumoylation in glioma stem cells.
Prolyl isomerase Pin1 promotes autophagy and cancer cell viability through activating FoxO3 signalling.
Title: Prolyl isomerase Pin1 promotes autophagy and cancer cell viability through activating FoxO3 signalling.
Oxygen-independent stabilization of HIF-2alpha in breast cancer through direct interaction with peptidyl-prolyl cis-trans isomerase NIMA-interacting 1.
Title: Oxygen-independent stabilization of HIF-2α in breast cancer through direct interaction with peptidyl-prolyl cis-trans isomerase NIMA-interacting 1.
The Peptidyl-Prolyl cis-trans isomerase, Pin1, associates with Protein Kinase C theta; via a critical Phospho-Thr-Pro motif in the V3 regulatory domain.
Title: The Peptidyl-Prolyl cis-trans isomerase, Pin1, associates with Protein Kinase C θ via a critical Phospho-Thr-Pro motif in the V3 regulatory domain.

Submit: New GeneRIF Correction See all GeneRIFs (380)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Protein interactions

Protein	Gene	Interaction	Pubs
Vif	vif	HIV-1 Vif(-) expression cooperates with Pin1 resulting in the reduction of A3G levels and the decreased incorporation of A3G into virions, suggesting the interaction between HIV-1 Vif and A3G	PubMed
capsid	gag	Phosphorylation of HIV-1 CA at serine residue 16 is involved in the HIV-1 core uncoating process. Interaction of PIN1 with the CA core within the target cells is required for the uncoating process	PubMed
integrase	gag-pol	HIV-1 IN is incapable of binding Pin1 Y23A mutant. The catalytically inactive Pin1 C113A mutant can bind HIV-1 IN, but completely ineffective at modifying IN sensitivity to subtilisin	PubMed
	gag-pol	Cellular Pin1 binds phosphorylated HIV-1 IN wild type and controls IN stability, but not S57A IN mutant	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

L17688 (e-PCR)
- UniSTS:74509

GDB:434012 (e-PCR)
- UniSTS:157204

A006W47 (e-PCR)
- UniSTS:53037

D8S2279 (e-PCR)
- UniSTS:473907

GDB:314949 (e-PCR)
- UniSTS:156503

L17796 (e-PCR)
- UniSTS:12896

D1S1423 (e-PCR)
- UniSTS:149619

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables GTPase activating protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables RNA polymerase II CTD heptapeptide repeat P3 isomerase activity	IEA Inferred from Electronic Annotation more info
enables RNA polymerase II CTD heptapeptide repeat P6 isomerase activity	IEA Inferred from Electronic Annotation more info
enables beta-catenin binding	IPI Inferred from Physical Interaction more info	PubMed
enables beta-catenin binding	ISS Inferred from Sequence or Structural Similarity more info
enables cis-trans isomerase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables cytoskeletal motor activity	ISS Inferred from Sequence or Structural Similarity more info
enables mitogen-activated protein kinase kinase binding	IPI Inferred from Physical Interaction more info	PubMed
enables peptidyl-prolyl cis-trans isomerase activity	EXP Inferred from Experiment more info	PubMed
enables peptidyl-prolyl cis-trans isomerase activity	IBA Inferred from Biological aspect of Ancestor more info
enables peptidyl-prolyl cis-trans isomerase activity	IDA Inferred from Direct Assay more info	PubMed
enables peptidyl-prolyl cis-trans isomerase activity	NAS Non-traceable Author Statement more info	PubMed
enables peptidyl-prolyl cis-trans isomerase activity	TAS Traceable Author Statement more info	PubMed
enables phosphoprotein binding	ISS Inferred from Sequence or Structural Similarity more info	PubMed
enables phosphoserine residue binding	IDA Inferred from Direct Assay more info	PubMed
enables phosphothreonine residue binding	IDA Inferred from Direct Assay more info	PubMed
enables phosphothreonine residue binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables tau protein binding	NAS Non-traceable Author Statement more info	PubMed
enables ubiquitin ligase activator activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in cellular response to hypoxia	IMP Inferred from Mutant Phenotype more info	PubMed
NOT involved_in microtubule polymerization	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of ERK1 and ERK2 cascade	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of SMAD protein signal transduction	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of amyloid-beta formation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of amyloid-beta formation	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of cell motility	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of protein binding	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of protein catabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of transforming growth factor beta receptor signaling pathway	IDA Inferred from Direct Assay more info	PubMed
involved_in neuron differentiation	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of GTPase activity	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of canonical Wnt signaling pathway	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of protein binding	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within positive regulation of protein phosphorylation	IGI Inferred from Genetic Interaction more info	PubMed
involved_in positive regulation of transcription by RNA polymerase II	IDA Inferred from Direct Assay more info	PubMed
involved_in protein peptidyl-prolyl isomerization	IDA Inferred from Direct Assay more info	PubMed
involved_in protein peptidyl-prolyl isomerization	TAS Traceable Author Statement more info	PubMed
involved_in protein stabilization	IDA Inferred from Direct Assay more info	PubMed
involved_in protein stabilization	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein targeting to mitochondrion	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within regulation of cytokinesis	IGI Inferred from Genetic Interaction more info	PubMed
acts_upstream_of_or_within regulation of cytokinesis	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of gene expression	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of mitotic nuclear division	TAS Traceable Author Statement more info	PubMed
involved_in regulation of protein localization to nucleus	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of protein phosphorylation	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of protein stability	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in response to hypoxia	IDA Inferred from Direct Assay more info	PubMed
involved_in synapse organization	ISS Inferred from Sequence or Structural Similarity more info

Component	Evidence Code	Pubs
located_in ciliary basal body	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info
located_in cytosol	ISS Inferred from Sequence or Structural Similarity more info
located_in cytosol	TAS Traceable Author Statement more info
is_active_in glutamatergic synapse	IDA Inferred from Direct Assay more info	PubMed
located_in midbody	IDA Inferred from Direct Assay more info	PubMed
located_in nuclear speck	IEA Inferred from Electronic Annotation more info
located_in nucleoplasm	IDA Inferred from Direct Assay more info
located_in nucleoplasm	TAS Traceable Author Statement more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	TAS Traceable Author Statement more info	PubMed
is_active_in postsynaptic cytosol	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

Names: PPIase Pin1; parvulin PIN1; protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1; protein interacting with never in mitosis A1; rotamase Pin1

NP_006212.1

EC 5.2.1.8

XP_011526370.1

EC 5.2.1.8

XP_054177179.1

EC 5.2.1.8

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

NG_029167.1 RefSeqGene

Range

5001..19483

Download

GenBank, FASTA, Sequence Viewer (Graphics), LRG_847

mRNA and Protein(s)

NM_006221.4 → NP_006212.1 peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

Status: REVIEWED

Description

Transcript Variant: This variant (1) represents the predominant transcript and encodes the functional protein.

Source sequence(s)

AK291074, BI827672, CA439440

Consensus CDS

CCDS12220.1

UniProtKB/Swiss-Prot

A8K4V9, Q13526, Q53X75

Related

ENSP00000247970.5, ENST00000247970.9

Conserved Domains (2) summary

pfam00397
Location:7 → 37

WW; WW domain

cl29122
Location:51 → 162

Rotamase_2; PPIC-type PPIASE domain

RNA

NR_038422.3 RNA Sequence

Status: REVIEWED

Description

Transcript Variant: This variant (2) includes an alternate exon, compared to variant 1, resulting in a premature stop codon. The transcript is predicted to be subject to nonsense-mediated decay (NMD).

Source sequence(s)

BC002899, BI827672, CA439440, CD675162
NR_038830.2 RNA Sequence

Status: REVIEWED

Description

Transcript Variant: This variant (3) includes an alternate exon in the 5' region, resulting in a premature stop codon, and lacks a segment in the 3' region, compared to variant 1. The transcript is predicted to be subject to nonsense-mediated decay (NMD).

Source sequence(s)

BC031971, BG912418, BI827672, CA439440, CD675162

Related

ENST00000590540.5

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p14 Primary Assembly

Genomic

NC_000019.10 Reference GRCh38.p14 Primary Assembly

Range

9835318..9849689

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_011528068.3 → XP_011526370.1 peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 isoform X1

Conserved Domains (3) summary

COG0760
Location:58 → 164

SurA; Parvulin-like peptidyl-prolyl isomerase [Posttranslational modification, protein turnover, chaperones]

pfam00397
Location:25 → 42

WW; WW domain

cl08278
Location:56 → 167

Rotamase_2; PPIC-type PPIASE domain