O95295 (SNAPN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SNARE-associated protein Snapin

Alternative name(s):
Biogenesis of lysosome-related organelles complex 1 subunit 7
Short name=BLOC-1 subunit 7
Synaptosomal-associated protein 25-binding protein
Short name=SNAP-associated protein

Gene names

Name:	SNAPIN
Synonyms:	BLOC1S7, SNAP25BP, SNAPAP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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	Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking. May modulate a step between vesicle priming, fusion and calcium-dependent neurotransmitter release through its ability to potentiate the interaction of synaptotagmin 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. Ref.10
Subunit structure	Interacts with CSNK1D, SNAP23 and STX4A but not with STX1A, VAMP2 and SYT1. Interacts with SNAP25; the interaction with SNAP25 is increased by its phosphorylation By similarity. Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos. Associates with the SNARE complex. Interacts with CEP110, NANOS1, PUM2 and RGS7. Interacts with human cytomegalovirus/HHV-5 protein UL70. Ref.7 Ref.8 Ref.9 Ref.12 Ref.16 Ref.17
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.12
Tissue specificity	Expressed in male germ cells of adult testis (at protein level). Ref.12
Developmental stage	Expressed in germ cells of 22-week prenatal testis. Ref.12
Post-translational modification	Phosphorylated by CSNK1D/CK1 By similarity.
Sequence similarities	Belongs to the SNAPIN family.

Ontologies

Keywords
Biological process	Exocytosis Host-virus interaction
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	anterograde axon cargo transport Inferred from sequence or structural similarity. Source: UniProtKB anterograde synaptic vesicle transport Inferred from sequence or structural similarity. Source: UniProtKB intracellular protein transport Traceable author statement Ref.1. Source: ProtInc melanosome organization Non-traceable author statement Ref.17. Source: UniProtKB neuron projection development Inferred from sequence or structural similarity. Source: UniProtKB synaptic vesicle exocytosis Inferred from direct assay Ref.1. Source: MGI synaptic vesicle fusion to presynaptic membrane Inferred from electronic annotation. Source: Compara synaptic vesicle maturation Inferred from electronic annotation. Source: Compara terminal button organization Inferred from electronic annotation. Source: Compara virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	BLOC-1 complex Inferred from direct assay Ref.8Ref.17. Source: UniProtKB Golgi apparatus Inferred from direct assay. Source: HPA Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell junction Inferred from electronic annotation. Source: UniProtKB-KW neuron projection Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay. Source: HPA perinuclear region of cytoplasm Inferred from direct assay Ref.12. Source: UniProtKB synaptic vesicle Traceable author statement Ref.1. Source: ProtInc synaptic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	SNARE binding Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BLOC1S2	Q6QNY1	7	EBI-296723,EBI-465872
BLOC1S6	Q9UL45	2	EBI-296723,EBI-465781
DTNBP1	Q96EV8	4	EBI-296723,EBI-465804
DYSF	O75923	3	EBI-296723,EBI-2799016
SLC14A2	Q15849-1	5	EBI-296723,EBI-1633392
Slc14a2	Q62668-1	6	EBI-296723,EBI-1635608	From a different organism.
SPTB	P11277	3	EBI-296723,EBI-514908

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.14
	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.14
	Modified residue	10	1	Phosphoserine Ref.14
	Modified residue	14	1	Phosphothreonine Ref.14
	Modified residue	50	1	Phosphoserine; by PKA By similarity
	Modified residue	129	1	Phosphotyrosine Ref.13
	Modified residue	133	1	Phosphoserine Ref.11 Ref.13 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE BLOC-1 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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CEP110.
[10]	"BLOC-1 is required for cargo-specific sorting from vacuolar early endosomes toward lysosome-related organelles." Setty S.R., Tenza D., Truschel S.T., Chou E., Sviderskaya E.V., Theos A.C., Lamoreux M.L., Di Pietro S.M., Starcevic M., Bennett D.C., Dell'Angelica E.C., Raposo G., Marks M.S. Mol. Biol. Cell 18:768-780(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PUM2 AND NANOS1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[13]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129 AND SER-133, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; THR-14 AND SER-133, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"Human cytomegalovirus primase UL70 specifically interacts with cellular factor Snapin." Shen A., Lei J., Yang E., Pei Y., Chen Y.C., Gong H., Xiao G., Liu F. J. Virol. 85:11732-11741(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HHV-5 PROTEIN UL70.
[17]	"Assembly and architecture of biogenesis of lysosome-related organelles complex-1 (BLOC-1)." Lee H.H., Nemecek D., Schindler C., Smith W.J., Ghirlando R., Steven A.C., Bonifacino J.S., Hurley J.H. J. Biol. Chem. 287:5882-5890(2012) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE BLOC-1 COMPLEX, COMPOSITION OF THE BLOC-1 COMPLEX.
+	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_012437.5.
UniGene	Hs.32018.
3D structure databases
ProteinModelPortal	O95295.
ModBase	Search...
Protein-protein interaction databases
IntAct	O95295. 63 interactions.
MINT	MINT-5002303.
STRING	9606.ENSP00000357674.
Protein family/group databases
TCDB	1.F.1.1.1. synaptosomal vesicle fusion pore (SVF-Pore) family.
PTM databases
PhosphoSite	O95295.
Proteomic databases
PaxDb	O95295.
PeptideAtlas	O95295.
PRIDE	O95295.
Protocols and materials databases
DNASU	23557.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000368685; ENSP00000357674; ENSG00000143553.
GeneID	23557.
KEGG	hsa:23557.
UCSC	uc001fcq.3. human.
Organism-specific databases
CTD	23557.
GeneCards	GC01P153631.
HGNC	HGNC:17145. SNAPIN.
HPA	HPA046974.
MIM	607007. gene.
neXtProt	NX_O95295.
PharmGKB	PA162404012.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG83669.
HOGENOM	HOG000253926.
HOVERGEN	HBG056744.
InParanoid	O95295.
OMA	ENTENFC.
OrthoDB	EOG4X6C9S.
PhylomeDB	O95295.
Enzyme and pathway databases
Reactome	REACT_11123. Membrane Trafficking.
Gene expression databases
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
GenomeRNAi	23557.
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:	April 3, 2013
This is version 106 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.