Tamalin trafficking regulator and scaffold protein tamalin [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Tamalinprovided by MGI
Official Full Name: trafficking regulator and scaffold protein tamalinprovided by MGI
Primary source: MGI:MGI:1860303
See related: Ensembl:ENSMUSG00000000531 AllianceGenome:MGI:1860303
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Grasp
Summary: Predicted to enable PDZ domain binding activity; identical protein binding activity; and small GTPase binding activity. Involved in regulation of postsynaptic neurotransmitter receptor internalization. Acts upstream of or within signal transduction. Located in plasma membrane. Is active in glutamatergic synapse. Orthologous to human TAMALIN (trafficking regulator and scaffold protein tamalin). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Broad expression in adrenal adult (RPKM 19.3), ovary adult (RPKM 17.4) and 22 other tissues See more
Orthologs: human all
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Genomic context

Location:: 15 F1; 15 56.57 cM

Exon count:: 9

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	15	NC_000081.7 (101122088..101130637)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	15	NC_000081.6 (101224207..101232756)

Chromosome 15 - NC_000081.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Tamalin Function Is Required for the Survival of Neurons and Oligodendrocytes in the CNS.
Title: Tamalin Function Is Required for the Survival of Neurons and Oligodendrocytes in the CNS.
Study results indicate a potential role of Grasp in the p53-mediated response of skin to UVB exposure
Title: Grp1-associated scaffold protein regulates skin homeostasis after ultraviolet irradiation.
A major mechanism by which insulin regulates glut4 recycling was uncovered. A general receptor for 3-phosphoinositides 1 was identified as a guanine nucleotide exchange factor for ADP-ribosylation factor 6 that promotes glut4 vesicle formation.
Title: Grp1 plays a key role in linking insulin signaling to glut4 recycling.
An upregulation of scaffold protein tamalin is found selectively in the hippocampus of animals subjected to electroconvulsive shock.
Title: Tamalin is a critical mediator of electroconvulsive shock-induced adult neuroplasticity.
plays a role in metabotropic glutamate receptor transport and forms its autoinhibitory state.[review]
Title: [Metabotropic glutamate receptor trafficking mechanism--autoinhibitory role of a scaffold protein tamalin].
Caspase cleavage of GRASP-1 occurs in specific brain regions in a time-dependent manner during development and ischemia.
Title: Physiological and pathological caspase cleavage of the neuronal RasGEF GRASP-1 as detected using a cleavage site-specific antibody.
tamalin is a novel signaling molecule that possesses a PDZ domain and a PDZ binding motif and mediates Syk signaling in an ITAM-based fashion
Title: Phosphorylation and recruitment of Syk by immunoreceptor tyrosine-based activation motif-based phosphorylation of tamalin.

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Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (2)
Targeted (3) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables PDZ domain binding	IEA Inferred from Electronic Annotation more info
enables PDZ domain binding	ISO Inferred from Sequence Orthology more info
enables identical protein binding	IEA Inferred from Electronic Annotation more info
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables small GTPase binding	IEA Inferred from Electronic Annotation more info
enables small GTPase binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
acts_upstream_of_or_within intracellular protein transport	ISO Inferred from Sequence Orthology more info	PubMed
involved_in regulation of postsynaptic neurotransmitter receptor internalization	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of postsynaptic neurotransmitter receptor internalization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in signal transduction	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within signal transduction	IPI Inferred from Physical Interaction more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	ISO Inferred from Sequence Orthology more info	PubMed
is_active_in glutamatergic synapse	IDA Inferred from Direct Assay more info	PubMed
is_active_in glutamatergic synapse	IMP Inferred from Mutant Phenotype more info	PubMed
is_active_in glutamatergic synapse	ISO Inferred from Sequence Orthology more info
located_in nuclear envelope lumen	ISO Inferred from Sequence Orthology more info	PubMed
located_in perinuclear region of cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	ISO Inferred from Sequence Orthology more info	PubMed
located_in postsynaptic density	IEA Inferred from Electronic Annotation more info
is_active_in postsynaptic density	ISO Inferred from Sequence Orthology more info
located_in postsynaptic membrane	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: general receptor for phosphoinositides 1-associated scaffold protein

Names: GRP1 (general receptor for phosphoinositides 1)-associated scaffold protein; GRP1-associated scaffold 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_019518.3 → NP_062391.3 general receptor for phosphoinositides 1-associated scaffold protein

See identical proteins and their annotated locations for NP_062391.3

Status: VALIDATED

Source sequence(s)

BC046307, BY730445

Consensus CDS

CCDS27847.1

UniProtKB/Swiss-Prot

Q9JJA9, Q9JKL0

Related

ENSMUSP00000000543.5, ENSMUST00000000543.6

Conserved Domains (1) summary

cd00992
Location:99 → 184

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

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

Reference GRCm39 C57BL/6J

Genomic

NC_000081.7 Reference GRCm39 C57BL/6J

Range

101122088..101130637

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_006521196.5 → XP_006521259.1 general receptor for phosphoinositides 1-associated scaffold protein isoform X1

Conserved Domains (1) summary

cd00992
Location:13 → 98

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...