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Protein

Golgi SNAP receptor complex member 1

Gene

Gosr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. May play a protective role against hydrogen peroxide induced cytotoxicity under glutathione depleted conditions in neuronal cells by regulating the intracellular ROS levels via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14). Participates in docking and fusion stage of ER to cis-Golgi transport. Plays an important physiological role in VLDL-transport vesicle-Golgi fusion and thus in VLDL delivery to the hepatic cis-Golgi (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-6807878. COPI-mediated anterograde transport.
R-MMU-6811438. Intra-Golgi traffic.

Names & Taxonomyi

Protein namesi
Recommended name:
Golgi SNAP receptor complex member 1
Alternative name(s):
28 kDa Golgi SNARE protein
28 kDa cis-Golgi SNARE p28
Short name:
GOS-28
Gene namesi
Name:Gosr1
Synonyms:Gs28
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1858260. Gosr1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 229228CytoplasmicSequence analysisAdd
BLAST
Transmembranei230 – 25021Helical; Anchor for type IV membrane proteinSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 250249Golgi SNAP receptor complex member 1PRO_0000212543Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiO88630.
PaxDbiO88630.
PRIDEiO88630.

PTM databases

iPTMnetiO88630.
PhosphoSiteiO88630.
SwissPalmiO88630.

Expressioni

Inductioni

Decreased levels in 25-hydroxycholesterol treated melanocytes (at protein level).1 Publication

Gene expression databases

CleanExiMM_GOSR1.
GenevisibleiO88630. MM.

Interactioni

Subunit structurei

Component of several multiprotein Golgi SNARE complexes. Identified in a SNARE complex with BET1, STX5 and YKT6, in a SNARE complex with BET1L, STX5 and YKT6, in a SNARE complex with STX5, GOSR2, SEC22B and BET1, and in complex with STX5 and COG3. Interacts with GABARAPL2 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi207294. 1 interaction.
IntActiO88630. 2 interactions.
MINTiMINT-4121107.
STRINGi10090.ENSMUSP00000010536.

Structurei

3D structure databases

ProteinModelPortaliO88630.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili9 – 2719Sequence analysisAdd
BLAST
Coiled coili72 – 9322Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the GOSR1 family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3208. Eukaryota.
ENOG410YI1X. LUCA.
GeneTreeiENSGT00390000008688.
HOGENOMiHOG000207760.
HOVERGENiHBG051764.
InParanoidiO88630.
KOiK08495.
OMAiINDKMAE.
OrthoDBiEOG769ZM1.
TreeFamiTF105782.

Family and domain databases

InterProiIPR023601. Golgi_SNAP_su1.
[Graphical view]
PANTHERiPTHR21094. PTHR21094. 1 hit.
PIRSFiPIRSF027109. Golgi_SNARE. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O88630-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAGTSNYWE DLRKQARQLE NELDLKLVSF SKLCTSYSHS GSRDGGRDRY
60 70 80 90 100
SSDTTPLLNG SSQDRMFETM AIEIEQLLAR LTGVNDKMAE YTHSAGVPSL
110 120 130 140 150
NAALMHTLQR HRDILQDYTH EFHKTKANFT AIRERENLMG SVRKDIESYK
160 170 180 190 200
SGSGVNNRRT ELFLKEHDHL RNSDRLIEET ISIAMATKEN MTSQRGMLKS
210 220 230 240 250
IHSKMNTLAN RFPAVNSLIQ RINLRKRRDS LILGGVIGIC TILLLLYAFH
Length:250
Mass (Da):28,489
Last modified:October 3, 2012 - v2
Checksum:iACF7FF5CCA0C2D52
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301F → S in AAC32189 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079901 mRNA. Translation: AAC32189.1.
AK133836 mRNA. Translation: BAE21873.1.
AK134515 mRNA. Translation: BAE22167.1.
AK147799 mRNA. Translation: BAE28147.1.
AK154972 mRNA. Translation: BAE32964.1.
AK161386 mRNA. Translation: BAE36365.1.
BX000359 Genomic DNA. Translation: CAI25288.1.
CH466596 Genomic DNA. Translation: EDL12868.1.
BC008542 mRNA. Translation: AAH08542.1.
CCDSiCCDS25070.1.
RefSeqiNP_058090.2. NM_016810.3.
UniGeneiMm.20931.

Genome annotation databases

EnsembliENSMUST00000010536; ENSMUSP00000010536; ENSMUSG00000010392.
GeneIDi53334.
KEGGimmu:53334.
UCSCiuc007kfz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079901 mRNA. Translation: AAC32189.1.
AK133836 mRNA. Translation: BAE21873.1.
AK134515 mRNA. Translation: BAE22167.1.
AK147799 mRNA. Translation: BAE28147.1.
AK154972 mRNA. Translation: BAE32964.1.
AK161386 mRNA. Translation: BAE36365.1.
BX000359 Genomic DNA. Translation: CAI25288.1.
CH466596 Genomic DNA. Translation: EDL12868.1.
BC008542 mRNA. Translation: AAH08542.1.
CCDSiCCDS25070.1.
RefSeqiNP_058090.2. NM_016810.3.
UniGeneiMm.20931.

3D structure databases

ProteinModelPortaliO88630.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207294. 1 interaction.
IntActiO88630. 2 interactions.
MINTiMINT-4121107.
STRINGi10090.ENSMUSP00000010536.

PTM databases

iPTMnetiO88630.
PhosphoSiteiO88630.
SwissPalmiO88630.

Proteomic databases

EPDiO88630.
PaxDbiO88630.
PRIDEiO88630.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000010536; ENSMUSP00000010536; ENSMUSG00000010392.
GeneIDi53334.
KEGGimmu:53334.
UCSCiuc007kfz.1. mouse.

Organism-specific databases

CTDi9527.
MGIiMGI:1858260. Gosr1.

Phylogenomic databases

eggNOGiKOG3208. Eukaryota.
ENOG410YI1X. LUCA.
GeneTreeiENSGT00390000008688.
HOGENOMiHOG000207760.
HOVERGENiHBG051764.
InParanoidiO88630.
KOiK08495.
OMAiINDKMAE.
OrthoDBiEOG769ZM1.
TreeFamiTF105782.

Enzyme and pathway databases

ReactomeiR-MMU-6807878. COPI-mediated anterograde transport.
R-MMU-6811438. Intra-Golgi traffic.

Miscellaneous databases

PROiO88630.
SOURCEiSearch...

Gene expression databases

CleanExiMM_GOSR1.
GenevisibleiO88630. MM.

Family and domain databases

InterProiIPR023601. Golgi_SNAP_su1.
[Graphical view]
PANTHERiPTHR21094. PTHR21094. 1 hit.
PIRSFiPIRSF027109. Golgi_SNARE. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse cis-Golgi p28 (GS28) mRNA."
    Bui T.D., Subramaniam V.N., Hong W.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    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 and NOD.
    Tissue: Head and Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. 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].
  5. "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.
    Tissue: Mammary tumor.
  6. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 33-49, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  7. "25-hydroxycholesterol acts in the Golgi compartment to induce degradation of tyrosinase."
    Hall A.M., Krishnamoorthy L., Orlow S.J.
    Pigment Cell Res. 17:396-406(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INDUCTION BY 25-HYDROXYCHOLESTEROL.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiGOSR1_MOUSE
AccessioniPrimary (citable) accession number: O88630
Secondary accession number(s): Q91VU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 3, 2012
Last modified: June 8, 2016
This is version 112 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, Direct protein sequencing, 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

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 one 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.