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O35166

- GOSR2_MOUSE

UniProt

O35166 - GOSR2_MOUSE

Protein

Golgi SNAP receptor complex member 2

Gene

Gosr2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (31 Aug 2004)
      Previous versions | rss
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    Functioni

    Involved in transport of proteins from the cis/medial-Golgi to the trans-Golgi network.

    GO - Biological processi

    1. protein transport Source: UniProtKB-KW
    2. vesicle-mediated transport Source: MGI

    Keywords - Biological processi

    Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_106572. XBP1(S) activates chaperone genes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Golgi SNAP receptor complex member 2
    Alternative name(s):
    27 kDa Golgi SNARE protein
    Membrin
    Gene namesi
    Name:Gosr2
    Synonyms:Gs27
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1927204. Gosr2.

    Subcellular locationi

    Golgi apparatuscis-Golgi network membrane By similarity; Single-pass type IV membrane protein By similarity. Golgi apparatus membrane By similarity
    Note: Concentrated most in the intermediate compartment/cis-Golgi network and the cis-Golgi cisternae 1 and 2. Greatly reduced in concentration at the trans end of the Golgi apparatus By similarity.By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: MGI
    2. Golgi membrane Source: MGI
    3. Golgi stack Source: InterPro
    4. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 212212Golgi SNAP receptor complex member 2PRO_0000212550Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO35166.
    PaxDbiO35166.
    PRIDEiO35166.

    PTM databases

    PhosphoSiteiO35166.

    Expressioni

    Gene expression databases

    ArrayExpressiO35166.
    BgeeiO35166.
    CleanExiMM_GOSR2.
    GenevestigatoriO35166.

    Interactioni

    Subunit structurei

    Identified in a unique SNARE complex composed of the Golgi SNAREs GOSR1, STX5 and YKT6.By similarity

    Protein-protein interaction databases

    IntActiO35166. 2 interactions.
    MINTiMINT-4096475.

    Structurei

    3D structure databases

    ProteinModelPortaliO35166.
    SMRiO35166. Positions 124-180.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 190190CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini212 – 2121VesicularSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei191 – 21121Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili60 – 9233Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the GOSR2 family.Curated

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG148687.
    GeneTreeiENSGT00490000043403.
    HOGENOMiHOG000231153.
    HOVERGENiHBG051765.
    InParanoidiO35166.
    KOiK08496.
    OMAiQNAHRGM.
    OrthoDBiEOG73RBCP.
    PhylomeDBiO35166.
    TreeFamiTF313702.

    Family and domain databases

    InterProiIPR027027. GOSR2/Membrin/Bos1.
    [Graphical view]
    PIRSFiPIRSF028865. Membrin-2. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O35166-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEPLYQQTNK QVQEIQSHMG RLERADKQSV HLVENEIQAS IEQIFSHLER    50
    LEILSSKEPL NRRQNAKLRV DQLKYDVQHL QTALRNFQHR RQVREQQERQ 100
    RDELLSRTFT TNDSDTTIPM DESLQFNSSL HNIHHGMDDL IGGGHSILEG 150
    LRAQRLTLKG TQKKILDIAN MLGLSNTVMR LIEKRAFQDK YFMIGGMLLT 200
    CAVMFLVVQY LT 212
    Length:212
    Mass (Da):24,725
    Last modified:August 31, 2004 - v2
    Checksum:i1622371B06090A6C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti99 – 991R → I in AAB82653. (PubMed:9349823)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF007550 mRNA. Translation: AAB82653.1.
    AK005697 mRNA. Translation: BAB24194.1.
    AK013052 mRNA. Translation: BAB28622.1.
    AK150004 mRNA. Translation: BAE29231.1.
    BC008525 mRNA. Translation: AAH08525.1.
    BC051253 mRNA. Translation: AAH51253.1.
    CCDSiCCDS25521.1.
    RefSeqiNP_062624.2. NM_019650.3.
    UniGeneiMm.195451.

    Genome annotation databases

    EnsembliENSMUST00000021329; ENSMUSP00000021329; ENSMUSG00000020946.
    GeneIDi56494.
    KEGGimmu:56494.
    UCSCiuc007lvo.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF007550 mRNA. Translation: AAB82653.1 .
    AK005697 mRNA. Translation: BAB24194.1 .
    AK013052 mRNA. Translation: BAB28622.1 .
    AK150004 mRNA. Translation: BAE29231.1 .
    BC008525 mRNA. Translation: AAH08525.1 .
    BC051253 mRNA. Translation: AAH51253.1 .
    CCDSi CCDS25521.1.
    RefSeqi NP_062624.2. NM_019650.3.
    UniGenei Mm.195451.

    3D structure databases

    ProteinModelPortali O35166.
    SMRi O35166. Positions 124-180.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O35166. 2 interactions.
    MINTi MINT-4096475.

    PTM databases

    PhosphoSitei O35166.

    Proteomic databases

    MaxQBi O35166.
    PaxDbi O35166.
    PRIDEi O35166.

    Protocols and materials databases

    DNASUi 56494.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000021329 ; ENSMUSP00000021329 ; ENSMUSG00000020946 .
    GeneIDi 56494.
    KEGGi mmu:56494.
    UCSCi uc007lvo.2. mouse.

    Organism-specific databases

    CTDi 9570.
    MGIi MGI:1927204. Gosr2.

    Phylogenomic databases

    eggNOGi NOG148687.
    GeneTreei ENSGT00490000043403.
    HOGENOMi HOG000231153.
    HOVERGENi HBG051765.
    InParanoidi O35166.
    KOi K08496.
    OMAi QNAHRGM.
    OrthoDBi EOG73RBCP.
    PhylomeDBi O35166.
    TreeFami TF313702.

    Enzyme and pathway databases

    Reactomei REACT_106572. XBP1(S) activates chaperone genes.

    Miscellaneous databases

    ChiTaRSi GOSR2. mouse.
    NextBioi 312782.
    PROi O35166.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O35166.
    Bgeei O35166.
    CleanExi MM_GOSR2.
    Genevestigatori O35166.

    Family and domain databases

    InterProi IPR027027. GOSR2/Membrin/Bos1.
    [Graphical view ]
    PIRSFi PIRSF028865. Membrin-2. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "A SNARE involved in protein transport through the Golgi apparatus."
      Lowe S.L., Peter F., Subramaniam V.N., Wong S.H., Hong W.
      Nature 389:881-884(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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].
      Strain: C57BL/6J.
      Tissue: Bone marrow, Embryo and Testis.
    3. "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].
      Strain: FVB/N and FVB/N-3.
      Tissue: Mammary gland.

    Entry informationi

    Entry nameiGOSR2_MOUSE
    AccessioniPrimary (citable) accession number: O35166
    Secondary accession number(s): Q3UDN0, Q9CR77
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: August 31, 2004
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3