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O95295 (SNAPN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length136 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 and synaptic vesicle recycling. 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 Ref.11

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. 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 CNTRL, NANOS1, PUM2 and RGS7. Interacts with TOR1A; the interaction is direct and associates SNAPIN with the CSN complex. Interacts with human cytomegalovirus/HHV-5 protein UL70. Ref.7 Ref.8 Ref.9 Ref.11 Ref.14 Ref.18 Ref.19 Ref.20

Subcellular location

Cytoplasm By similarity. Membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Cytoplasmperinuclear region. Golgi apparatus membrane By similarity. Cytoplasmic vesiclesecretory vesicle By similarity. Note: May be cytoplasmic and peripheral membrane bound or anchored to the vesicular membrane through an N-terminal signal anchor By similarity. Colocalizes with NANOS1 and PUM2 in the perinuclear region of germ cells. Ref.11 Ref.14 Ref.18

Tissue specificity

Expressed in male germ cells of adult testis (at protein level). Ref.14

Developmental stage

Expressed in germ cells of 22-week prenatal testis. Ref.14

Post-translational modification

Phosphorylated by CSNK1D/CK1 By similarity. Phosphorylated by PKD, phosphorylation controls SNAPIN protein stability. Ref.11 Ref.18

Sequence similarities

Belongs to the SNAPIN family.

Ontologies

Keywords
   Biological processExocytosis
Host-virus interaction
   Cellular componentCell junction
Cytoplasm
Cytoplasmic vesicle
Golgi apparatus
Membrane
Synapse
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterograde 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.20. Source: UniProtKB

neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

neurotransmitter secretion

Traceable author statement Ref.1. Source: ProtInc

positive regulation of late endosome to lysosome transport

Traceable author statement PubMed 23949442. Source: ParkinsonsUK-UCL

regulation of protein binding

Inferred from mutant phenotype PubMed 23949442. Source: ParkinsonsUK-UCL

synaptic vesicle exocytosis

Inferred from direct assay Ref.1. Source: MGI

synaptic vesicle fusion to presynaptic membrane

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle maturation

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle transport

Inferred from mutant phenotype Ref.11. Source: UniProtKB

terminal button organization

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentBLOC-1 complex

Inferred from direct assay Ref.8Ref.20. 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

nucleolus

Inferred from direct assay. Source: HPA

perinuclear region of cytoplasm

Inferred from direct assay Ref.14. Source: UniProtKB

secretory granule

Inferred from sequence or structural similarity. Source: UniProtKB

synapse

Inferred from direct assay Ref.1. Source: MGI

synaptic vesicle

Inferred from direct assay Ref.18. Source: UniProtKB

synaptic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

transport vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionSNARE binding

Inferred from direct assay Ref.1. Source: MGI

protein binding

Inferred from physical interaction PubMed 12809483Ref.11Ref.14Ref.18. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 136135SNARE-associated protein Snapin
PRO_0000097556

Regions

Region83 – 13654Interaction with TOR1A
Coiled coil37 – 12690 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.13 Ref.16 Ref.21
Modified residue101Phosphoserine Ref.16
Modified residue141Phosphothreonine Ref.16
Modified residue501Phosphoserine; by PKA By similarity
Modified residue1291Phosphotyrosine Ref.15
Modified residue1331Phosphoserine Ref.12 Ref.15 Ref.16

Natural variations

Natural variant1121S → C.
Corresponds to variant rs1802461 [ dbSNP | Ensembl ].
VAR_017423

Sequences

Sequence LengthMass (Da)Tools
O95295 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 3EA402AC53C81FFF

FASTA13614,874
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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 CNTRL.
[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]"The dystonia-associated protein torsinA modulates synaptic vesicle recycling."
Granata A., Watson R., Collinson L.M., Schiavo G., Warner T.T.
J. Biol. Chem. 283:7568-7579(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN VESICLE RECYCLING, INTERACTION WITH TOR1A, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[14]"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.
[15]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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].
[18]"CSN complex controls the stability of selected synaptic proteins via a torsinA-dependent process."
Granata A., Koo S.J., Haucke V., Schiavo G., Warner T.T.
EMBO J. 30:181-193(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TOR1A, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[19]"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.
[20]"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.
[21]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, 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.
CCDSCCDS1049.1.
RefSeqNP_036569.1. NM_012437.5.
UniGeneHs.32018.

3D structure databases

ProteinModelPortalO95295.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117101. 32 interactions.
IntActO95295. 66 interactions.
MINTMINT-5002303.
STRING9606.ENSP00000357674.

Protein family/group databases

TCDB1.F.1.1.1. the synaptosomal vesicle fusion pore (svf-pore) family.

PTM databases

PhosphoSiteO95295.

Proteomic databases

MaxQBO95295.
PaxDbO95295.
PeptideAtlasO95295.
PRIDEO95295.

Protocols and materials databases

DNASU23557.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368685; ENSP00000357674; ENSG00000143553.
GeneID23557.
KEGGhsa:23557.
UCSCuc001fcq.4. human.

Organism-specific databases

CTD23557.
GeneCardsGC01P153631.
HGNCHGNC:17145. SNAPIN.
HPAHPA046974.
MIM607007. gene.
neXtProtNX_O95295.
PharmGKBPA162404012.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG83669.
HOGENOMHOG000253926.
HOVERGENHBG056744.
InParanoidO95295.
OMAHVHSVRE.
OrthoDBEOG7SXW5D.
PhylomeDBO95295.
TreeFamTF319577.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

BgeeO95295.
CleanExHS_SNAPIN.
GenevestigatorO95295.

Family and domain databases

InterProIPR017246. Snapin.
IPR028119. Snapin/Pallidin/Snn1.
[Graphical view]
PANTHERPTHR31305. PTHR31305. 1 hit.
PfamPF14712. Snapin_Pallidin. 1 hit.
[Graphical view]
PIRSFPIRSF037631. Snapin. 1 hit.
ProtoNetSearch...

Other

GeneWikiSNAPAP.
GenomeRNAi23557.
NextBio46130.
PROO95295.
SOURCESearch...

Entry information

Entry nameSNAPN_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM