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FLASH GENE

Symbol

SNAPIN

contributors: mct/npt/pgu - updated : 16-04-2016

HGNC name	SNAP-associated protein
HGNC id	17145

FLASH GENE DNA RNA EXPRESSION PROTEIN DISORDER ANIMAL & CELL MODELS

EXPRESSION

Type

widely

expressed in	(based on citations)
organ(s)	System Organ level 1 Organ level 2 Organ level 3 Organ level 4 Level Pubmed Species Stage Rna symbol Cardiovascular heart         Lymphoid/Immune tonsils       highly Nervous brain       specific Reproductive male system prostate         male system testis       Skin/Tegument skin       highly

tissue

System Tissue Tissue level 1 Tissue level 2 Level Pubmed Species Stage Rna symbol Connective bone     highly

cells

System Cell Pubmed Species Stage Rna symbol Reproductive spermatocyte

cell lineage

cell lines

fluid/secretion

at STAGE

physiological period

fetal, perinatal, growth/childhood

PROTEIN

PHYSICAL PROPERTIES		globular
STRUCTURE

motifs/domains	a N-terminal hydrophobic segment characteristic of a transmembrane domain
	a coiled-coil C-terminal helical domain containing the SNAP23-binding site, responsible for protein-protein interaction and could enable SNAPIN to be an adaptor of PUM2 and NANOS1, binding other factors to regulate translation in the development of the human germ cells

HOMOLOGY

interspecies	homolog to rattus LOC295217
	homolog to murine Snapap

Homologene

FAMILY

CATEGORY

regulatory

SUBCELLULAR LOCALIZATION	plasma membrane
	intracellular
	intracellular,cytoplasm,organelle,membrane
	intracellular,cytoplasm,organelle,Golgi
	intracellular,cytoplasm,organelle,endosome
	intracellular,cytoplasm,organelle,lysosome
	intracellular,cytoplasm,cytosolic,vesicle
text	peripheral membrane-bound pools in adipocytes
	in human testis, SNAPIN co-localizes with PUM2 and NANOS1 in prenatal and also in spermatogenic germ cells of the adult

basic FUNCTION	SNARE binding activity
	playing a general role in SNARE-mediated vesicle fusion events in non-neuronal cells in addition to its participation in Ca2+-regulated neurosecretion
	functioning as a regulator of an important cAMP synthesis enzyme in the brain
	regulates dendrite number in developing neurons by modulating cypin-promoted microtubule assembly
	probable targets for the amplification mechanism and may therefore be involved, together or separately, in the development or progression of Hepatocellular carcinoma
	promote the maturation/priming of synaptic vesicles (SVs) by interacting with components of the SNARE complex
	plays likely an extra role in mammals which is germ cell specific

CELLULAR PROCESS

PHYSIOLOGICAL PROCESS

PATHWAY

metabolism

signaling

a component

biogenesis of lysosome-related organelles complex-1 (BLOC-1) is a ubiquitously expressed multisubunit protein complex required for the normal biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules

INTERACTION

DNA

RNA

small molecule

protein	interacting with SNAP25
	ADCY6 interacting protein
	binds to cypin's (GDA) CRMP homology domain, which is where tubulin binds (competes with tubulin for binding to cypin, resulting in decreased microtubule assembly)
	robust interaction with wild type and mutant torsinA (TOR1A)
	binding partner of dysbindin-1 in the brain (function of dysbindin-1 in presynaptic, postsynaptic and microtubule locations may all be related to known functions of snapin)
	interaction partner of CSNK1D (possible function for CKSNK1D in modulating snapin specific functions)
	interacting with PUM2 (interacts with SNAPIN, a modulator of SNARE complex assembly, which is involved in vesicle trafficking
	interacts additionally with NANOS1 protein
	interacting with the C terminus of ADRA1A (augments ADRA1A-operated calcium influx through TRPC6)
	EHD1 binds to the C terminus of SNAPIN via its C terminus EH domain
	ADCY6, an enzyme which catalyzes cAMP synthesis, regulates neurite outgrowth by direct interaction with a binding protein (SNAPIN) of SNAP25 at the N terminus of ADCY6 (AC6-N)
	specifically binds to SNAPIN and this interaction effectively facilitates endosomal maturation without affecting autophagic cargo degradation
	RNF13 directly interacted with SNAPIN, a SNAP-25-interacting protein
	SNAPIN, a SNAP25 interacting protein, interacts with LRRK2
	LRRK2 may regulate neurotransmitter release via control of SNAPIN function by inhibitory phosphorylation
	SNAPIN, a SNARE-associated protein implicated in synaptic transmission, is a new binding partner of the carboxyl terminal of SLC6A3
	SNAPIN/SLC6A3 interaction represents a direct link between exocytotic and reuptake mechanisms and is a potential target for DA (dopamine) transmission modulation

cell & other

REGULATION

ASSOCIATED DISORDERS

corresponding disease(s)

Other morbid association(s)

Type Gene Modification Chromosome rearrangement Protein expression Protein Function tumoral     --over   in hepatocellular carcinomas

Susceptibility

Variant & Polymorphism

Candidate gene

Marker

Therapy target

ANIMAL & CELL MODELS