PPIAL4G peptidylprolyl isomerase A like 4G [Homo sapiens (human)] - Gene

Summary

Official Symbol: PPIAL4Gprovided by HGNC
Official Full Name: peptidylprolyl isomerase A like 4Gprovided by HGNC
Primary source: HGNC:HGNC:33996
See related: Ensembl:ENSG00000236334 AllianceGenome:HGNC:33996
Gene type: protein coding
RefSeq status: INFERRED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: COAS-2
Summary: Predicted to enable cyclosporin A binding activity and peptidyl-prolyl cis-trans isomerase activity. Predicted to be involved in protein folding and protein peptidyl-prolyl isomerization. Predicted to be active in cytoplasm and intracellular membrane-bounded organelle. [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

Location:: 1q21.2

Exon count:: 1

Annotation release	Status	Assembly	Chr	Location
RS_2023_10	current	GRCh38.p14 (GCF_000001405.40)	1	NC_000001.11 (148482548..148483302, complement)
RS_2023_10	current	T2T-CHM13v2.0 (GCF_009914755.1)	1	NC_060925.1 (146324062..146324816)
105.20220307	previous assembly	GRCh37.p13 (GCF_000001405.25)	1	NC_000001.10 (147954635..147955394, complement)

Chromosome 1 - NC_000001.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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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)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

G16257 (e-PCR)
- UniSTS:51476

PMC262691P6 (e-PCR)
- UniSTS:272328

NoName (e-PCR)
- UniSTS:483537

Clone Names

FLJ16804, MGC163248, MGC163250, BX284650.5

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables cyclosporin A binding	IBA Inferred from Biological aspect of Ancestor more info
enables peptidyl-prolyl cis-trans isomerase activity	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein peptidyl-prolyl isomerization	IBA Inferred from Biological aspect of Ancestor more info

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: peptidyl-prolyl cis-trans isomerase A-like 4G

Names: PPIase A-like 4A; PPIase A-like 4G; chromosome 1-amplified sequence 2; peptidylprolyl cis-trans isomerase A-like 4; peptidylprolyl cis-trans isomerase A-like 4A; peptidylprolyl cis-trans isomerase A-like 4G; peptidylprolyl isomerase A (cyclophilin A)-like 4G

NP_001116540.1

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.

mRNA and Protein(s)

NM_001123068.3 → NP_001116540.1 peptidyl-prolyl cis-trans isomerase A-like 4G

See identical proteins and their annotated locations for NP_001116540.1

Status: INFERRED

Source sequence(s)

AC239811

Consensus CDS

CCDS41375.2

UniProtKB/Swiss-Prot

A1L431, A2BFH1, P0DN37

UniProtKB/TrEMBL

A0A0H2UH34

Related

ENSP00000393845.1, ENST00000419275.3

Conserved Domains (1) summary

cl00197
Location:4 → 162

cyclophilin; cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the ...