O95295 (SNAPN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SNARE-associated protein Snapin

Alternative name(s):
Synaptosomal-associated protein 25-binding protein
Short name=SNAP-associated protein

Gene names

Name:	SNAPIN
Synonyms:	SNAP25BP, SNAPAP

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	136 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May modulate a step between vesicle priming, fusion and calcium-dependent neurotransmitter release by potentiating the interaction of synaptotagmins with the SNAREs and the plasma-membrane-associated protein SNAP25. Its phosphorylation state influences exocytotic protein interactions and may regulate synaptic vesicle exocytosis. May also have a role in the mechanisms of SNARE-mediated membrane fusion in non-neuronal cells By similarity.
Subunit structure	Associates with the SNARE complex. Interacts with SNAP23, SNAP25 and STX4A but not with STX1A, VAMP2 and SYT1. Binds to CSNK1D. Phosphorylation increases its interaction with SNAP25 By similarity. Interacts with RGS7. Component of the biogenesis of lysosome-related organelles (BLOC-1) complex which is required for normal biogenesis of specialized organelles of the endosomal-lysosomal system. Interacts with CEP110, PUM2 and NANOS1. Ref.7 Ref.9 Ref.13
Subcellular location	Cytoplasm By similarity. Membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmic vesicle › secretory vesicle › synaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Cell junction › synapse › synaptosome. Cytoplasm › perinuclear region. Golgi apparatus membrane By similarity. Note: May be cytoplasmic and peripheral membrane bound or anchored to the vesicular membrane through an N-terminal signal anchor By similarity. Co-localizes with NANOS1 and PUM2 in the perinuclear region of germ cells. Ref.13
Tissue specificity	Expressed in male germ cells of adult testis (at protein level). Ref.13
Developmental stage	Expressed in germ cells of 22-week prenatal testis. Ref.13
Post-translational modification	Phosphorylated by CSNK1D/CK1 By similarity. Ref.10 Ref.11 Ref.12 Ref.14
Sequence similarities	Belongs to the SNAPIN family.

Ontologies

Keywords
Biological process	Exocytosis
Cellular component	Cell junction Cytoplasm Cytoplasmic vesicle Golgi apparatus Membrane Synapse Synaptosome
Coding sequence diversity	Polymorphism
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	intracellular protein transport Traceable author statement. Source: ProtInc
Cellular component	BLOC-1 complex Inferred from direct assay Ref.8. Source: UniProtKB cell junction Inferred from electronic annotation. Source: UniProtKB-KW perinuclear region of cytoplasm Inferred from direct assay Ref.13. Source: UniProtKB synaptic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell synaptosome Inferred from direct assay Ref.1. Source: MGI
Molecular function	SNARE binding Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BLOC1S2	Q6QNY1	3	EBI-296723,EBI-465872
DTNBP1	Q96EV8	2	EBI-296723,EBI-465804
SLC14A2	Q15849-1	5	EBI-296723,EBI-1633392
Slc14a2	Q62668-1	6	EBI-296723,EBI-1635608	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 136	135	SNARE-associated protein Snapin		PRO_0000097556
Regions
	Coiled coil	37 – 126	90	Potential
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.12
	Modified residue	14	1	Phosphothreonine Ref.12
	Modified residue	50	1	Phosphoserine; by PKA By similarity
	Modified residue	129	1	Phosphotyrosine Ref.14
	Modified residue	133	1	Phosphoserine Ref.10 Ref.11 Ref.12 Ref.14
Natural variations
	Natural variant	112	1	S → C. Corresponds to variant rs1802461 [ dbSNP | Ensembl ].		VAR_017423

Sequences

	Sequence		Length	Mass (Da)
	O95295 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 3EA402AC53C81FFF	FASTA	136	14,874
	10 20 30 40 50 60 MAGAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN 70 80 90 100 110 120 LATELCRINE DQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR 130 RAMLDSGIYP PGSPGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Snapin: a SNARE-associated protein implicated in synaptic transmission." Ilardi J.M., Mochida S., Sheng Z.-H. Nat. Neurosci. 2:119-124(1999) [PubMed: 10195194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Adipose tissue.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung carcinoma and Melanoma.
[7]	"Snapin interacts with the N-terminus of regulator of G protein signaling 7." Hunt R.A., Edris W., Chanda P.K., Nieuwenhuijsen B., Young K.H. Biochem. Biophys. Res. Commun. 303:594-599(2003) [PubMed: 12659861] [Abstract] Cited for: INTERACTION WITH RGS7.
[8]	"Identification of snapin and three novel proteins (BLOS1, BLOS2, and BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related organelles complex-1 (BLOC-1)." Starcevic M., Dell'Angelica E.C. J. Biol. Chem. 279:28393-28401(2004) [PubMed: 15102850] [Abstract] Cited for: IDENTIFICATION IN BLOC1 COMPLEX.
[9]	"Centriolin anchoring of exocyst and SNARE complexes at the midbody is required for secretory-vesicle-mediated abscission." Gromley A., Yeaman C., Rosa J., Redick S., Chen C.-T., Mirabelle S., Guha M., Sillibourne J., Doxsey S.J. Cell 123:75-87(2005) [PubMed: 16213214] [Abstract] Cited for: INTERACTION WITH CEP110.
[10]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND SER-133, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"The SNARE-associated component SNAPIN binds PUMILIO2 and NANOS1 proteins in human male germ cells." Ginter-Matuszewska B., Spik A., Rembiszewska A., Koyias C., Kupryjanczyk J., Jaruzelska J. Mol. Hum. Reprod. 15:173-179(2009) [PubMed: 19168546] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PUM2 AND NANOS1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[14]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129 AND SER-133, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF086837 mRNA. Translation: AAD11417.1. AK024555 mRNA. Translation: BAB14927.1. BT006753 mRNA. Translation: AAP35399.1. AL592150 Genomic DNA. Translation: CAI18797.1. CH471121 Genomic DNA. Translation: EAW53288.1. CH471121 Genomic DNA. Translation: EAW53289.1. BC000761 mRNA. Translation: AAH00761.1. BC004494 mRNA. Translation: AAH04494.1.
IPI	IPI00018331.
RefSeq	NP_036569.1. NM_012437.4.
UniGene	Hs.32018.
3D structure databases
ProteinModelPortal	O95295.
ModBase	Search...
Protein-protein interaction databases
IntAct	O95295. 30 interactions.
MINT	MINT-5002303.
STRING	O95295.
Protein family/group databases
TCDB	1.F.1.1.1. synaptosomal vesicle fusion pore (SVF-Pore) family.
PTM databases
PhosphoSite	O95295.
Proteomic databases
PeptideAtlas	O95295.
PRIDE	O95295.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000368685; ENSP00000357674; ENSG00000143553.
GeneID	23557.
KEGG	hsa:23557.
UCSC	uc001fcq.1. human.
Organism-specific databases
CTD	23557.
GeneCards	GC01P153631.
H-InvDB	HIX0001087.
HGNC	HGNC:17145. SNAPIN.
HPA	HPA046974.
MIM	607007. gene.
neXtProt	NX_O95295.
PharmGKB	PA162404012.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00390000008274.
HOGENOM	HBG717464.
HOVERGEN	HBG056744.
InParanoid	O95295.
OMA	ENTENFC.
OrthoDB	EOG4X6C9S.
PhylomeDB	O95295.
Enzyme and pathway databases
Reactome	REACT_11123. Membrane Trafficking.
Gene expression databases
ArrayExpress	O95295.
Bgee	O95295.
CleanEx	HS_SNAPIN.
Genevestigator	O95295.
GermOnline	ENSG00000143553. Homo sapiens.
Family and domain databases
InterPro	IPR017246. Snapin. [Graphical view]
PIRSF	PIRSF037631. Snapin. 1 hit.
ProtoNet	Search...
Other
NextBio	46130.
SOURCE	Search...

Entry information

Entry name

SNAPN_HUMAN

Accession

Primary (citable) accession number: O95295
Secondary accession number(s): D3DV56, Q5SXU8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	May 1, 1999
Last modified:	January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.