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Protein

SNARE-associated protein Snapin

Gene

SNAPIN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  • SNARE binding Source: MGI

GO - Biological processi

  • anterograde axon cargo transport Source: UniProtKB
  • anterograde synaptic vesicle transport Source: UniProtKB
  • autophagic vacuole maturation Source: Ensembl
  • endosome to lysosome transport Source: MGI
  • intracellular protein transport Source: ProtInc
  • melanosome organization Source: UniProtKB
  • negative regulation of neuron projection development Source: Ensembl
  • neuron projection development Source: UniProtKB
  • neurotransmitter secretion Source: ProtInc
  • positive regulation of late endosome to lysosome transport Source: ParkinsonsUK-UCL
  • regulation of protein binding Source: ParkinsonsUK-UCL
  • synaptic vesicle exocytosis Source: MGI
  • synaptic vesicle fusion to presynaptic membrane Source: Ensembl
  • synaptic vesicle maturation Source: Ensembl
  • synaptic vesicle transport Source: UniProtKB
  • terminal button organization Source: Ensembl
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Exocytosis, Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.

Protein family/group databases

TCDBi1.F.1.1.1. the synaptosomal vesicle fusion pore (svf-pore) family.

Names & Taxonomyi

Protein namesi
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 namesi
Name:SNAPIN
Synonyms:BLOC1S7, SNAP25BP, SNAPAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:17145. SNAPIN.

Subcellular locationi

GO - Cellular componenti

  • BLOC-1 complex Source: UniProtKB
  • cell junction Source: UniProtKB-KW
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • Golgi apparatus Source: HPA
  • Golgi membrane Source: UniProtKB-SubCell
  • nucleolus Source: HPA
  • perinuclear region of cytoplasm Source: UniProtKB
  • secretory granule Source: UniProtKB
  • synapse Source: MGI
  • synaptic vesicle Source: UniProtKB
  • synaptic vesicle membrane Source: UniProtKB-SubCell
  • transport vesicle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162404012.

Polymorphism and mutation databases

BioMutaiSNAPIN.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 136135SNARE-associated protein SnapinPRO_0000097556Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei10 – 101Phosphoserine1 Publication
Modified residuei14 – 141Phosphothreonine1 Publication
Modified residuei50 – 501Phosphoserine; by PKABy similarity
Modified residuei129 – 1291Phosphotyrosine1 Publication
Modified residuei133 – 1331Phosphoserine3 Publications

Post-translational modificationi

Phosphorylated by CSNK1D/CK1 (By similarity). Phosphorylated by PKD, phosphorylation controls SNAPIN protein stability.By similarity2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO95295.
PaxDbiO95295.
PeptideAtlasiO95295.
PRIDEiO95295.

PTM databases

PhosphoSiteiO95295.

Expressioni

Tissue specificityi

Expressed in male germ cells of adult testis (at protein level).1 Publication

Developmental stagei

Expressed in germ cells of 22-week prenatal testis.1 Publication

Gene expression databases

BgeeiO95295.
CleanExiHS_SNAPIN.
GenevestigatoriO95295.

Organism-specific databases

HPAiHPA046974.

Interactioni

Subunit structurei

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 UL70.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BLOC1S2Q6QNY17EBI-296723,EBI-465872
BLOC1S6Q9UL452EBI-296723,EBI-465781
DTNBP1Q96EV84EBI-296723,EBI-465804
DYSFO759233EBI-296723,EBI-2799016
LRRK2Q5S0075EBI-296723,EBI-5323863
SLC14A2Q15849-15EBI-296723,EBI-1633392
Slc14a2Q62668-16EBI-296723,EBI-1635608From a different organism.
SPTBP112773EBI-296723,EBI-514908

Protein-protein interaction databases

BioGridi117101. 41 interactions.
IntActiO95295. 66 interactions.
MINTiMINT-5002303.
STRINGi9606.ENSP00000357674.

Structurei

3D structure databases

ProteinModelPortaliO95295.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni83 – 13654Interaction with TOR1AAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili37 – 12690Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the SNAPIN family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG83669.
GeneTreeiENSGT00390000008274.
HOGENOMiHOG000253926.
HOVERGENiHBG056744.
InParanoidiO95295.
OMAiINEHQKV.
OrthoDBiEOG7SXW5D.
PhylomeDBiO95295.
TreeFamiTF319577.

Family and domain databases

InterProiIPR017246. Snapin.
IPR028119. Snapin/Pallidin/Snn1.
[Graphical view]
PANTHERiPTHR31305. PTHR31305. 1 hit.
PfamiPF14712. Snapin_Pallidin. 1 hit.
[Graphical view]
PIRSFiPIRSF037631. Snapin. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O95295-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES
60 70 80 90 100
QVELREQIDN LATELCRINE DQKVALDLDP YVKKLLNARR RVVLVNNILQ
110 120 130
NAQERLRRLN HSVAKETARR RAMLDSGIYP PGSPGK
Length:136
Mass (Da):14,874
Last modified:May 1, 1999 - v1
Checksum:i3EA402AC53C81FFF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121S → C.
Corresponds to variant rs1802461 [ dbSNP | Ensembl ].
VAR_017423

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1049.1.
RefSeqiNP_036569.1. NM_012437.5.
UniGeneiHs.32018.

Genome annotation databases

EnsembliENST00000368685; ENSP00000357674; ENSG00000143553.
GeneIDi23557.
KEGGihsa:23557.
UCSCiuc001fcq.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1049.1.
RefSeqiNP_036569.1. NM_012437.5.
UniGeneiHs.32018.

3D structure databases

ProteinModelPortaliO95295.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117101. 41 interactions.
IntActiO95295. 66 interactions.
MINTiMINT-5002303.
STRINGi9606.ENSP00000357674.

Protein family/group databases

TCDBi1.F.1.1.1. the synaptosomal vesicle fusion pore (svf-pore) family.

PTM databases

PhosphoSiteiO95295.

Polymorphism and mutation databases

BioMutaiSNAPIN.

Proteomic databases

MaxQBiO95295.
PaxDbiO95295.
PeptideAtlasiO95295.
PRIDEiO95295.

Protocols and materials databases

DNASUi23557.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368685; ENSP00000357674; ENSG00000143553.
GeneIDi23557.
KEGGihsa:23557.
UCSCiuc001fcq.4. human.

Organism-specific databases

CTDi23557.
GeneCardsiGC01P153631.
HGNCiHGNC:17145. SNAPIN.
HPAiHPA046974.
MIMi607007. gene.
neXtProtiNX_O95295.
PharmGKBiPA162404012.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG83669.
GeneTreeiENSGT00390000008274.
HOGENOMiHOG000253926.
HOVERGENiHBG056744.
InParanoidiO95295.
OMAiINEHQKV.
OrthoDBiEOG7SXW5D.
PhylomeDBiO95295.
TreeFamiTF319577.

Enzyme and pathway databases

ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

GeneWikiiSNAPAP.
GenomeRNAii23557.
NextBioi46130.
PROiO95295.
SOURCEiSearch...

Gene expression databases

BgeeiO95295.
CleanExiHS_SNAPIN.
GenevestigatoriO95295.

Family and domain databases

InterProiIPR017246. Snapin.
IPR028119. Snapin/Pallidin/Snn1.
[Graphical view]
PANTHERiPTHR31305. PTHR31305. 1 hit.
PfamiPF14712. Snapin_Pallidin. 1 hit.
[Graphical view]
PIRSFiPIRSF037631. Snapin. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSNAPN_HUMAN
AccessioniPrimary (citable) accession number: O95295
Secondary accession number(s): D3DV56, Q5SXU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: May 1, 1999
Last modified: April 29, 2015
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.