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P60880

- SNP25_HUMAN

UniProt

P60880 - SNP25_HUMAN

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Protein
Synaptosomal-associated protein 25
Gene
SNAP25, SNAP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei180 – 1812Cleavage; by BONT/E

GO - Molecular functioni

  1. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. energy reserve metabolic process Source: Reactome
  2. glutamate secretion Source: Reactome
  3. neurotransmitter secretion Source: Reactome
  4. neurotransmitter uptake Source: UniProtKB
  5. regulation of insulin secretion Source: UniProtKB
  6. small molecule metabolic process Source: Reactome
  7. synaptic transmission Source: UniProtKB
  8. synaptic vesicle docking involved in exocytosis Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_12591. Glutamate Neurotransmitter Release Cycle.
REACT_15293. Dopamine Neurotransmitter Release Cycle.
REACT_15309. Acetylcholine Neurotransmitter Release Cycle.
REACT_15418. Norepinephrine Neurotransmitter Release Cycle.
REACT_15425. Serotonin Neurotransmitter Release Cycle.
REACT_18325. Regulation of insulin secretion.
REACT_200616. Toxicity of botulinum toxin type E (BoNT/E).
REACT_200658. Toxicity of botulinum toxin type C (BoNT/C).
REACT_200737. Toxicity of botulinum toxin type A (BoNT/A).
REACT_23947. GABA synthesis, release, reuptake and degradation.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptosomal-associated protein 25
Short name:
SNAP-25
Alternative name(s):
Super protein
Short name:
SUP
Synaptosomal-associated 25 kDa protein
Gene namesi
Name:SNAP25
Synonyms:SNAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:11132. SNAP25.

Subcellular locationi

Cytoplasmperinuclear region By similarity. Cell membrane; Lipid-anchor. Cell junctionsynapsesynaptosome
Note: Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region By similarity.

GO - Cellular componenti

  1. SNARE complex Source: UniProtKB
  2. cell junction Source: UniProtKB-KW
  3. cytoplasm Source: UniProtKB
  4. growth cone Source: HGNC
  5. membrane Source: UniProtKB
  6. neuron projection Source: HGNC
  7. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  8. plasma membrane Source: Reactome
  9. synapse Source: UniProtKB-KW
  10. synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex Source: Ensembl
  11. trans-Golgi network Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35980.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 206206Synaptosomal-associated protein 25
PRO_0000213587Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi85 – 851S-palmitoyl cysteine By similarity
Lipidationi88 – 881S-palmitoyl cysteine By similarity
Lipidationi90 – 901S-palmitoyl cysteine By similarity
Lipidationi92 – 921S-palmitoyl cysteine By similarity
Modified residuei138 – 1381Phosphothreonine By similarity
Modified residuei187 – 1871Phosphoserine By similarity

Post-translational modificationi

Palmitoylated. Cys-85 appears to be the main site, and palmitoylation is required for membrane association By similarity.

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP60880.
PaxDbiP60880.
PRIDEiP60880.

PTM databases

PhosphoSiteiP60880.

Miscellaneous databases

PMAP-CutDBQ5U0B5.

Expressioni

Tissue specificityi

Neurons of the neocortex, hippocampus, piriform cortex, anterior thalamic nuclei, pontine nuclei, and granule cells of the cerebellum.

Gene expression databases

BgeeiP60880.
CleanExiHS_SNAP25.
GenevestigatoriP60880.

Organism-specific databases

HPAiCAB000360.
HPA001830.

Interactioni

Subunit structurei

Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A. This complex binds CPLX1. Interacts with CENPF, TRIM9, RIMS1, SNAPIN, OTOF and HGS. Binds STXBP6. Found in a ternary complex with STX1A and VAMP8. Found in a complex containing SYT1, SV2B and syntaxin-1 By similarity. Associates with the BLOC-1 complex. Isoform 1 and isoform 2 interact with BLOC1S6. Interacts with EQTN By similarity.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ZDHHC17Q8IUH53EBI-524785,EBI-524753

Protein-protein interaction databases

BioGridi112500. 28 interactions.
DIPiDIP-34554N.
IntActiP60880. 11 interactions.
MINTiMINT-1403389.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 8073
Helixi148 – 16720
Beta strandi191 – 1933

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KILX-ray2.30C10-81[»]
D139-204[»]
1XTGX-ray2.10B146-204[»]
3RK2X-ray2.20C/G7-82[»]
D/H141-203[»]
3RK3X-ray3.50C7-82[»]
D141-203[»]
3RL0X-ray3.80C/G/K/O/S/W/a/e7-82[»]
D/H/L/P/T/X/b/f141-203[»]
3ZURX-ray2.71A/B145-206[»]
ProteinModelPortaliP60880.
SMRiP60880. Positions 10-78, 141-204.

Miscellaneous databases

EvolutionaryTraceiP60880.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 8163t-SNARE coiled-coil homology 1
Add
BLAST
Domaini140 – 20263t-SNARE coiled-coil homology 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 7575Interaction with CENPF By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi85 – 928Cys-rich

Sequence similaritiesi

Belongs to the SNAP-25 family.

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG259235.
HOVERGENiHBG056971.
KOiK18211.
OMAiESADAYQ.
OrthoDBiEOG75F4F5.
PhylomeDBiP60880.
TreeFamiTF315125.

Family and domain databases

InterProiIPR000928. SNAP-25.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF00835. SNAP-25. 1 hit.
PF05739. SNARE. 1 hit.
[Graphical view]
SMARTiSM00397. t_SNARE. 2 hits.
[Graphical view]
PROSITEiPS50192. T_SNARE. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Note: Isoforms differ by the usage of two alternative homologous exons (5a and 5b) which code for positions 56 to 94 and differ only in 9 positions out of 39.

Isoform 1 (identifier: P60880-1) [UniParc]FASTAAdd to Basket

Also known as: SNAP-25b

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MAEDADMRNE LEEMQRRADQ LADESLESTR RMLQLVEESK DAGIRTLVML    50
DEQGEQLERI EEGMDQINKD MKEAEKNLTD LGKFCGLCVC PCNKLKSSDA 100
YKKAWGNNQD GVVASQPARV VDEREQMAIS GGFIRRVTND ARENEMDENL 150
EQVSGIIGNL RHMALDMGNE IDTQNRQIDR IMEKADSNKT RIDEANQRAT 200
KMLGSG 206
Length:206
Mass (Da):23,315
Last modified:April 13, 2004 - v1
Checksum:iFBED2B082A4CB6A6
GO
Isoform 2 (identifier: P60880-2) [UniParc] [UniParc]FASTAAdd to Basket

Also known as: SNAP-25a

The sequence of this isoform differs from the canonical sequence as follows:
     58-89: ERIEEGMDQINKDMKEAEKNLTDLGKFCGLCV → DRVEEGMNHINQDMKEAEKNLKDLGKCCGLFI

Show »
Length:206
Mass (Da):23,336
Checksum:iE272652C701EA984
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei58 – 8932ERIEE…CGLCV → DRVEEGMNHINQDMKEAEKN LKDLGKCCGLFI in isoform 2.
VSP_006186Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441I → V in BAD97337. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L19760 mRNA. Translation: AAC37545.1.
L19761 mRNA. Translation: AAC37546.1.
D21267 mRNA. Translation: BAA22370.1.
BT019684 mRNA. Translation: AAV38490.1.
AK223617 mRNA. Translation: BAD97337.1.
AK289647 mRNA. Translation: BAF82336.1.
AK314359 mRNA. Translation: BAG36991.1.
AL023913 Genomic DNA. Translation: CAB42860.1.
AL023913 Genomic DNA. Translation: CAC34534.1.
AL023913 Genomic DNA. Translation: CAD56158.1.
CH471133 Genomic DNA. Translation: EAX10346.1.
CH471133 Genomic DNA. Translation: EAX10349.1.
CH471133 Genomic DNA. Translation: EAX10350.1.
CH471133 Genomic DNA. Translation: EAX10352.1.
BC010647 mRNA. Translation: AAH10647.1.
CCDSiCCDS13109.1. [P60880-2]
CCDS13110.1.
PIRiI53735.
I67823.
RefSeqiNP_003072.2. NM_003081.3. [P60880-2]
NP_570824.1. NM_130811.2. [P60880-1]
XP_005260865.1. XM_005260808.2. [P60880-1]
XP_005260867.1. XM_005260810.2. [P60880-2]
UniGeneiHs.167317.

Genome annotation databases

EnsembliENST00000254976; ENSP00000254976; ENSG00000132639. [P60880-1]
ENST00000304886; ENSP00000307341; ENSG00000132639. [P60880-2]
GeneIDi6616.
KEGGihsa:6616.
UCSCiuc002wnq.2. human.
uc002wnr.2. human. [P60880-2]

Polymorphism databases

DMDMi46397726.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L19760 mRNA. Translation: AAC37545.1 .
L19761 mRNA. Translation: AAC37546.1 .
D21267 mRNA. Translation: BAA22370.1 .
BT019684 mRNA. Translation: AAV38490.1 .
AK223617 mRNA. Translation: BAD97337.1 .
AK289647 mRNA. Translation: BAF82336.1 .
AK314359 mRNA. Translation: BAG36991.1 .
AL023913 Genomic DNA. Translation: CAB42860.1 .
AL023913 Genomic DNA. Translation: CAC34534.1 .
AL023913 Genomic DNA. Translation: CAD56158.1 .
CH471133 Genomic DNA. Translation: EAX10346.1 .
CH471133 Genomic DNA. Translation: EAX10349.1 .
CH471133 Genomic DNA. Translation: EAX10350.1 .
CH471133 Genomic DNA. Translation: EAX10352.1 .
BC010647 mRNA. Translation: AAH10647.1 .
CCDSi CCDS13109.1. [P60880-2 ]
CCDS13110.1.
PIRi I53735.
I67823.
RefSeqi NP_003072.2. NM_003081.3. [P60880-2 ]
NP_570824.1. NM_130811.2. [P60880-1 ]
XP_005260865.1. XM_005260808.2. [P60880-1 ]
XP_005260867.1. XM_005260810.2. [P60880-2 ]
UniGenei Hs.167317.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KIL X-ray 2.30 C 10-81 [» ]
D 139-204 [» ]
1XTG X-ray 2.10 B 146-204 [» ]
3RK2 X-ray 2.20 C/G 7-82 [» ]
D/H 141-203 [» ]
3RK3 X-ray 3.50 C 7-82 [» ]
D 141-203 [» ]
3RL0 X-ray 3.80 C/G/K/O/S/W/a/e 7-82 [» ]
D/H/L/P/T/X/b/f 141-203 [» ]
3ZUR X-ray 2.71 A/B 145-206 [» ]
ProteinModelPortali P60880.
SMRi P60880. Positions 10-78, 141-204.
ModBasei Search...

Protein-protein interaction databases

BioGridi 112500. 28 interactions.
DIPi DIP-34554N.
IntActi P60880. 11 interactions.
MINTi MINT-1403389.

Chemistry

ChEMBLi CHEMBL2364159.
DrugBanki DB00083. Botulinum Toxin Type A.

Protein family/group databases

TCDBi 1.F.1.1.1. the synaptosomal vesicle fusion pore (svf-pore) family.

PTM databases

PhosphoSitei P60880.

Polymorphism databases

DMDMi 46397726.

Proteomic databases

MaxQBi P60880.
PaxDbi P60880.
PRIDEi P60880.

Protocols and materials databases

DNASUi 6616.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000254976 ; ENSP00000254976 ; ENSG00000132639 . [P60880-1 ]
ENST00000304886 ; ENSP00000307341 ; ENSG00000132639 . [P60880-2 ]
GeneIDi 6616.
KEGGi hsa:6616.
UCSCi uc002wnq.2. human.
uc002wnr.2. human. [P60880-2 ]

Organism-specific databases

CTDi 6616.
GeneCardsi GC20P010199.
HGNCi HGNC:11132. SNAP25.
HPAi CAB000360.
HPA001830.
MIMi 600322. gene.
neXtProti NX_P60880.
PharmGKBi PA35980.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG259235.
HOVERGENi HBG056971.
KOi K18211.
OMAi ESADAYQ.
OrthoDBi EOG75F4F5.
PhylomeDBi P60880.
TreeFami TF315125.

Enzyme and pathway databases

Reactomei REACT_12591. Glutamate Neurotransmitter Release Cycle.
REACT_15293. Dopamine Neurotransmitter Release Cycle.
REACT_15309. Acetylcholine Neurotransmitter Release Cycle.
REACT_15418. Norepinephrine Neurotransmitter Release Cycle.
REACT_15425. Serotonin Neurotransmitter Release Cycle.
REACT_18325. Regulation of insulin secretion.
REACT_200616. Toxicity of botulinum toxin type E (BoNT/E).
REACT_200658. Toxicity of botulinum toxin type C (BoNT/C).
REACT_200737. Toxicity of botulinum toxin type A (BoNT/A).
REACT_23947. GABA synthesis, release, reuptake and degradation.

Miscellaneous databases

ChiTaRSi SNAP25. human.
EvolutionaryTracei P60880.
GeneWikii SNAP25.
GenomeRNAii 6616.
NextBioi 25761.
PMAP-CutDB Q5U0B5.
PROi P60880.
SOURCEi Search...

Gene expression databases

Bgeei P60880.
CleanExi HS_SNAP25.
Genevestigatori P60880.

Family and domain databases

InterProi IPR000928. SNAP-25.
IPR000727. T_SNARE_dom.
[Graphical view ]
Pfami PF00835. SNAP-25. 1 hit.
PF05739. SNARE. 1 hit.
[Graphical view ]
SMARTi SM00397. t_SNARE. 2 hits.
[Graphical view ]
PROSITEi PS50192. T_SNARE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human cDNA clones encoding two different isoforms of the nerve terminal protein SNAP-25."
    Bark I.C., Wilson M.C.
    Gene 139:291-292(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Fetal brain and Temporal cortex.
  2. "Cloning and sequence analysis of the human SNAP25 cDNA."
    Zhao N., Hashida H., Takahashi N., Sakaki Y.
    Gene 145:313-314(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Frontal cortex.
  3. "Insulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2."
    Jagadish M.N., Fernandez C.S., Hewish D.R., Macaulay S.L., Gough K.H., Grusovin J., Verkuylen A., Cosgrove L., Alafaci A., Frenkel M.J., Ward C.W.
    Biochem. J. 317:945-954(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    Tissue: Skeletal muscle.
  4. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  5. "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] (ISOFORMS 1 AND 2).
    Tissue: Amygdala and Hippocampus.
  6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  7. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORM 2).
    Tissue: Eye.
  10. "SNAP-25 is also an iron-sulfur protein."
    Huang Q., Hong X., Hao Q.
    FEBS Lett. 582:1431-1436(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PUTATIVE IRON-SULFUR CLUSTER.
  11. "The dysbindin-containing complex (BLOC-1) in brain: developmental regulation, interaction with SNARE proteins and role in neurite outgrowth."
    Ghiani C.A., Starcevic M., Rodriguez-Fernandez I.A., Nazarian R., Cheli V.T., Chan L.N., Malvar J.S., de Vellis J., Sabatti C., Dell'Angelica E.C.
    Mol. Psychiatry 15:204-215(2010)
    Cited for: ASSOCIATION WITH THE BLOC-1 COMPLEX, INTERACTION WITH BLOC1S6.
  12. "Three-dimensional structure of the complexin/SNARE complex."
    Chen X., Tomchick D.R., Kovrigin E., Arac D., Machius M., Suedhof T.C., Rizo J.
    Neuron 33:397-409(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 11-81 AND 141-202 IN COMPLEX WITH STX1A; CPLX1 AND VAMP2, STRUCTURE BY NMR.

Entry informationi

Entry nameiSNP25_HUMAN
AccessioniPrimary (citable) accession number: P60880
Secondary accession number(s): B2RAU4
, D3DW16, D3DW17, P13795, P36974, P70557, P70558, Q53EM2, Q5U0B5, Q8IXK3, Q96FM2, Q9BR45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: September 3, 2014
This is version 121 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

Miscellaneous

When cloned and expressed in Eschericia coli, where protein palmitoylation does not occur, Cys-85, Cys-88, Cys-90 and Cys-92 in the protein sequence readily form an iron-sulfur cluster instead.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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