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P60879

- SNP25_MOUSE

UniProt

P60879 - SNP25_MOUSE

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Protein

Synaptosomal-associated protein 25

Gene

Snap25

Organism
Mus musculus (Mouse)
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.1 Publication

Sites

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

GO - Molecular functioni

  1. calcium-dependent protein binding Source: ParkinsonsUK-UCL
  2. SNARE binding Source: MGI
  3. syntaxin-1 binding Source: MGI

GO - Biological processi

  1. long-term synaptic potentiation Source: MGI
  2. neurotransmitter secretion Source: MGI
  3. regulation of establishment of protein localization Source: MGI
  4. regulation of neuron projection development Source: ParkinsonsUK-UCL
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_205038. Acetylcholine Neurotransmitter Release Cycle.
REACT_229514. Glutamate Neurotransmitter Release Cycle.
REACT_242222. Norepinephrine Neurotransmitter Release Cycle.
REACT_245631. GABA synthesis, release, reuptake and degradation.
REACT_263148. Regulation of insulin secretion.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:98331. Snap25.

Subcellular locationi

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

GO - Cellular componenti

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

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi85 – 851C → S: 91% reduction in palmitoylation level. 14% membrane association. No palmitoylation and less than 8% membrane association; when associated with S-88 or A-88. 1 Publication
Mutagenesisi88 – 881C → S: 79% reduction in palmitoylation level. 18% membrane association. No palmitoylation and less than 8% membrane association; when associated with S-85 or A-85. 1 Publication
Mutagenesisi90 – 901C → S: 58% reduction in palmitoylation level. 28% membrane association. Very little palmitoylation and less than 8% membrane association; when associated with S-92 or A-92. 1 Publication
Mutagenesisi92 – 921C → S: 65% reduction in palmitoylation level. 29% membrane association. No palmitoylation and less than 8% membrane association; when associated with S-90 or A-90. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 206206Synaptosomal-associated protein 25PRO_0000213589Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi85 – 851S-palmitoyl cysteine1 Publication
Lipidationi88 – 881S-palmitoyl cysteine1 Publication
Lipidationi90 – 901S-palmitoyl cysteine1 Publication
Lipidationi92 – 921S-palmitoyl cysteine1 Publication
Modified residuei138 – 1381Phosphothreonine; by PKC and PKA1 Publication
Modified residuei187 – 1871Phosphoserine; by PKC1 Publication

Post-translational modificationi

Palmitoylated. Cys-85 appears to be the main site, and palmitoylation is required for membrane association.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP60879.
PaxDbiP60879.
PRIDEiP60879.

PTM databases

PhosphoSiteiP60879.

Expressioni

Gene expression databases

BgeeiP60879.
CleanExiMM_SNAP25.
GenevestigatoriP60879.

Interactioni

Subunit structurei

Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A. This complex binds CPLX1. Interacts with TRIM9, RIMS1, SNAPIN and HGS. Binds STXBP6. Found in a ternary complex with STX1A and VAMP8 (By similarity). Found in a complex containing SYT1, SV2B and syntaxin-1. Interacts with CENPF and OTOF. Associates with the BLOC-1 complex. Isoform 1 and isoform 2 interact with BLOC1S6. Interacts with EQTN.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CenpfQ155P713EBI-445270,EBI-2211248
Vamp2P630445EBI-445270,EBI-521920

Protein-protein interaction databases

BioGridi203362. 15 interactions.
DIPiDIP-29066N.
IntActiP60879. 37 interactions.
MINTiMINT-2411221.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BU0model-C18-82[»]
D139-206[»]
ProteinModelPortaliP60879.
SMRiP60879. Positions 10-78, 141-204.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 7575Interaction with CENPFAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Belongs to the SNAP-25 family.Curated
Contains 2 t-SNARE coiled-coil homology domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG259235.
GeneTreeiENSGT00390000012186.
HOVERGENiHBG056971.
InParanoidiP60879.
KOiK18211.
OMAiESADAYQ.
OrthoDBiEOG75F4F5.
PhylomeDBiP60879.
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: P60879-1) [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

        10         20         30         40         50
MAEDADMRNE LEEMQRRADQ LADESLESTR RMLQLVEESK DAGIRTLVML
60 70 80 90 100
DEQGEQLERI EEGMDQINKD MKEAEKNLTD LGKFCGLCVC PCNKLKSSDA
110 120 130 140 150
YKKAWGNNQD GVVASQPARV VDEREQMAIS GGFIRRVTND ARENEMDENL
160 170 180 190 200
EQVSGIIGNL RHMALDMGNE IDTQNRQIDR IMEKADSNKT RIDEANQRAT

KMLGSG
Length:206
Mass (Da):23,315
Last modified:April 13, 2004 - v1
Checksum:iFBED2B082A4CB6A6
GO
Isoform 2 (identifier: P60879-2) [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. 3 PublicationsVSP_010019Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22012 mRNA. Translation: AAA61741.1.
AF483516 mRNA. Translation: AAL90790.1.
AF483517 mRNA. Translation: AAL90791.1.
AK078038 mRNA. Translation: BAC37105.1.
AL732447 Genomic DNA. Translation: CAM15064.1.
AL732447 Genomic DNA. Translation: CAM15065.1.
CH466519 Genomic DNA. Translation: EDL28390.1.
BC018249 mRNA. Translation: AAH18249.1.
CCDSiCCDS16793.1.
CCDS71153.1. [P60879-2]
PIRiA33623.
RefSeqiNP_001277985.1. NM_001291056.1. [P60879-2]
NP_035558.1. NM_011428.3. [P60879-1]
UniGeneiMm.45953.

Genome annotation databases

EnsembliENSMUST00000028727; ENSMUSP00000028727; ENSMUSG00000027273. [P60879-1]
ENSMUST00000110098; ENSMUSP00000105725; ENSMUSG00000027273. [P60879-2]
GeneIDi20614.
KEGGimmu:20614.
UCSCiuc008mop.1. mouse.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22012 mRNA. Translation: AAA61741.1 .
AF483516 mRNA. Translation: AAL90790.1 .
AF483517 mRNA. Translation: AAL90791.1 .
AK078038 mRNA. Translation: BAC37105.1 .
AL732447 Genomic DNA. Translation: CAM15064.1 .
AL732447 Genomic DNA. Translation: CAM15065.1 .
CH466519 Genomic DNA. Translation: EDL28390.1 .
BC018249 mRNA. Translation: AAH18249.1 .
CCDSi CCDS16793.1.
CCDS71153.1. [P60879-2 ]
PIRi A33623.
RefSeqi NP_001277985.1. NM_001291056.1. [P60879-2 ]
NP_035558.1. NM_011428.3. [P60879-1 ]
UniGenei Mm.45953.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BU0 model - C 18-82 [» ]
D 139-206 [» ]
ProteinModelPortali P60879.
SMRi P60879. Positions 10-78, 141-204.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203362. 15 interactions.
DIPi DIP-29066N.
IntActi P60879. 37 interactions.
MINTi MINT-2411221.

PTM databases

PhosphoSitei P60879.

Proteomic databases

MaxQBi P60879.
PaxDbi P60879.
PRIDEi P60879.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028727 ; ENSMUSP00000028727 ; ENSMUSG00000027273 . [P60879-1 ]
ENSMUST00000110098 ; ENSMUSP00000105725 ; ENSMUSG00000027273 . [P60879-2 ]
GeneIDi 20614.
KEGGi mmu:20614.
UCSCi uc008mop.1. mouse.

Organism-specific databases

CTDi 6616.
MGIi MGI:98331. Snap25.

Phylogenomic databases

eggNOGi NOG259235.
GeneTreei ENSGT00390000012186.
HOVERGENi HBG056971.
InParanoidi P60879.
KOi K18211.
OMAi ESADAYQ.
OrthoDBi EOG75F4F5.
PhylomeDBi P60879.
TreeFami TF315125.

Enzyme and pathway databases

Reactomei REACT_205038. Acetylcholine Neurotransmitter Release Cycle.
REACT_229514. Glutamate Neurotransmitter Release Cycle.
REACT_242222. Norepinephrine Neurotransmitter Release Cycle.
REACT_245631. GABA synthesis, release, reuptake and degradation.
REACT_263148. Regulation of insulin secretion.

Miscellaneous databases

ChiTaRSi Snap25. mouse.
NextBioi 298983.
PROi P60879.
SOURCEi Search...

Gene expression databases

Bgeei P60879.
CleanExi MM_SNAP25.
Genevestigatori P60879.

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. "The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations."
    Oyler G.A., Higgins G.A., Hart R.A., Battenberg E., Billingsley M., Bloom F.E., Wilson M.C.
    J. Cell Biol. 109:3039-3052(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION.
    Strain: BALB/c.
  2. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
    Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
    Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: ILS and ISS.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Medulla oblongata.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-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] (ISOFORM 2).
    Strain: C57BL/6.
    Tissue: Eye.
  7. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 18-31; 60-72; 125-135 AND 143-176, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  8. "Characterization of the palmitoylation domain of SNAP-25."
    Lane S.R., Liu Y.
    J. Neurochem. 69:1864-1869(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-85; CYS-88; CYS-90 AND CYS-92, MUTAGENESIS OF CYS-85; CYS-88; CYS-90 AND CYS-92.
  9. "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: INTERACTION WITH SNAPIN.
  10. "Differential phosphorylation of SNAP-25 in vivo by protein kinase C and protein kinase A."
    Hepp R., Cabaniols J.-P., Roche P.A.
    FEBS Lett. 532:52-56(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-138 AND SER-187.
  11. Cited for: INTERACTION WITH SYT1; SV2B AND SYNTAXIN-1.
  12. "Otoferlin, defective in a human deafness form, is essential for exocytosis at the auditory ribbon synapse."
    Roux I., Safieddine S., Nouvian R., Grati M., Simmler M.-C., Bahloul A., Perfettini I., Le Gall M., Rostaing P., Hamard G., Triller A., Avan P., Moser T., Petit C.
    Cell 127:277-289(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OTOF.
    Strain: BALB/c.
    Tissue: Cochlea.
  13. "CytLEK1 is a regulator of plasma membrane recycling through its interaction with SNAP-25."
    Pooley R.D., Reddy S., Soukoulis V., Roland J.T., Goldenring J.R., Bader D.M.
    Mol. Biol. Cell 17:3176-3186(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CENPF.
  14. "Acrosome formation-associated factor is involved in fertilization."
    Hu X.Q., Ji S.Y., Li Y.C., Fan C.H., Cai H., Yang J.L., Zhang C.P., Chen M., Pan Z.F., Hu Z.Y., Gao F., Liu Y.X.
    Fertil. Steril. 93:1482-1492(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EQTN.
  15. "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) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH THE BLOC-1 COMPLEX, SUBCELLULAR LOCATION, INTERACTION WITH BLOC1S6.
  16. "The synaptic SNARE complex is a parallel four-stranded helical bundle."
    Poirier M.A., Xiao W., Macosko J.C., Chan C., Shin Y.K., Bennett M.K.
    Nat. Struct. Biol. 5:765-769(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 18-206 IN COMPLEX WITH VAMP2 AND STX1A.

Entry informationi

Entry nameiSNP25_MOUSE
AccessioniPrimary (citable) accession number: P60879
Secondary accession number(s): A2AIC2
, A2AIC3, P13795, P36974, P70557, P70558, Q8IXK3, Q96FM2, Q9BR45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: November 26, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3