St13 ST13, Hsp70 interacting protein [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: St13provided by RGD
Official Full Name: ST13, Hsp70 interacting proteinprovided by RGD
Primary source: RGD:621312
See related: EnsemblRapid:ENSRNOG00000018920 AllianceGenome:RGD:621312
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Summary: Enables several functions, including Hsp70 protein binding activity; dATP binding activity; and unfolded protein binding activity. Involved in chaperone cofactor-dependent protein refolding and negative regulation of protein refolding. Part of protein-containing complex. Orthologous to several human genes including ST13 (ST13 Hsp70 interacting protein) and ST13P5 (ST13, Hsp70 interacting protein pseudogene 5). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in Kidney (RPKM 684.5), Liver (RPKM 640.3) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 7q34

Exon count:: 13

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	7	NC_086025.1 (114769758..114805877, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	7	NC_051342.1 (112891007..112925727, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	7	NC_005106.4 (122585770..122635731, complement)

Chromosome 7 - NC_086025.1 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?

The tetratricopeptide repeat domain of rat Hip with the Hsp70 ATPase domain through an extensive interface, to form a bracket that locks ADP in the binding cleft.
Title: Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle.
The co-aggregation phenomenon of heat shock protein 70 with alpha-synuclein can be prevented in vitro by co-chaperone Hip (ST13), which can facilitate depletion of Hsc70 by amyloidogenic polypeptides, impairing chaperone proteostasis.
Title: Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by Hip.
HIP was cleaved by granzyme B; the granzyme B-mediated cleavage site was mapped to the BID loop-like region of HIP; data implicate HIP in the proteolytic cascade of some apoptotic pathways
Title: Proteolysis of HIP during apoptosis occurs within a region similar to the BID loop.

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General gene information

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Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables Hsp70 protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables Hsp70 protein binding	IDA Inferred from Direct Assay more info	PubMed
enables Hsp70 protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables dATP binding	IDA Inferred from Direct Assay more info	PubMed
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein dimerization activity	IEA Inferred from Electronic Annotation more info
enables protein domain specific binding	IDA Inferred from Direct Assay more info	PubMed
enables protein domain specific binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-containing complex binding	IDA Inferred from Direct Assay more info	PubMed
enables protein-folding chaperone binding	IPI Inferred from Physical Interaction more info	PubMed
enables unfolded protein binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in ADP transport	IEA Inferred from Electronic Annotation more info
involved_in AMP transport	IEA Inferred from Electronic Annotation more info
involved_in FAD transmembrane transport	IEA Inferred from Electronic Annotation more info
involved_in NAD transmembrane transport	IEA Inferred from Electronic Annotation more info
involved_in chaperone cofactor-dependent protein refolding	IBA Inferred from Biological aspect of Ancestor more info
involved_in chaperone cofactor-dependent protein refolding	IDA Inferred from Direct Assay more info	PubMed
involved_in coenzyme A transmembrane transport	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of protein refolding	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within response to bacterium	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
part_of protein-containing complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: hsc70-interacting protein

Names: hip; protein ST13 homolog; suppression of tumorigenicity 13 (colon carcinoma) Hsp70-interacting protein

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_031122.2 → NP_112384.1 hsc70-interacting protein

See identical proteins and their annotated locations for NP_112384.1

Status: PROVISIONAL

Source sequence(s)

JAXUCZ010000007

UniProtKB/Swiss-Prot

P50503

UniProtKB/TrEMBL

A0A8I5ZYX0, A6HSZ6

Related

ENSRNOP00000084383.1, ENSRNOT00000107864.2

Conserved Domains (5) summary

smart00727
Location:318 → 357

STI1; Heat shock chaperonin-binding motif

cd14438
Location:3 → 43

Hip_N; N-terminal dimerization domain of the Hsp70-interacting protein (Hip) and similar proteins

sd00006
Location:113 → 141

TPR; TPR repeat [structural motif]

pfam00515
Location:147 → 179

TPR_1; Tetratricopeptide repeat

pfam13414
Location:112 → 178

TPR_11; TPR repeat