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Q9CQC9

- SAR1B_MOUSE

UniProt

Q9CQC9 - SAR1B_MOUSE

Protein

GTP-binding protein SAR1b

Gene

Sar1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Involved in transport from the endoplasmic reticulum to the Golgi apparatus. Activated by the guanine nucleotide exchange factor PREB. Involved in the selection of the protein cargo and the assembly of the COPII coat complex.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi34 – 341MagnesiumBy similarity
    Metal bindingi75 – 751MagnesiumBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi32 – 398GTPBy similarity
    Nucleotide bindingi75 – 784GTPBy similarity
    Nucleotide bindingi134 – 1374GTPBy similarity

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

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

    Keywords - Biological processi

    ER-Golgi transport, Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_196550. MHC class II antigen presentation.
    REACT_198968. Regulation of cholesterol biosynthesis by SREBP (SREBF).
    REACT_205304. COPII (Coat Protein 2) Mediated Vesicle Transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GTP-binding protein SAR1b
    Gene namesi
    Name:Sar1b
    Synonyms:Sara1b, Sara2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1913647. Sar1b.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Peripheral membrane protein 1 Publication. Golgi apparatusGolgi stack membrane 1 Publication; Peripheral membrane protein 1 Publication
    Note: Associated with the endoplasmic reticulum and Golgi stacks, in particular in the juxta-nuclear Golgi region.

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. Golgi cisterna membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 198198GTP-binding protein SAR1bPRO_0000206262Add
    BLAST

    Proteomic databases

    MaxQBiQ9CQC9.
    PaxDbiQ9CQC9.
    PRIDEiQ9CQC9.

    PTM databases

    PhosphoSiteiQ9CQC9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9CQC9.
    BgeeiQ9CQC9.
    CleanExiMM_SAR1B.
    GenevestigatoriQ9CQC9.

    Interactioni

    Subunit structurei

    Homodimer. Part of the COPII coat complex. Binds to the cytoplasmic tails of target proteins in the endoplasmic reticulum By similarity. Binds PREB.By similarity

    Protein-protein interaction databases

    BioGridi211441. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CQC9.
    SMRiQ9CQC9. Positions 13-198.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. SAR1 family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    GeneTreeiENSGT00550000074696.
    HOGENOMiHOG000163690.
    HOVERGENiHBG104997.
    InParanoidiQ9CQC9.
    KOiK07953.
    OMAiDEQLANC.
    OrthoDBiEOG7W1550.
    PhylomeDBiQ9CQC9.
    TreeFamiTF312890.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR006689. Small_GTPase_ARF/SAR.
    IPR006687. Small_GTPase_SAR1.
    [Graphical view]
    PfamiPF00025. Arf. 1 hit.
    [Graphical view]
    PRINTSiPR00328. SAR1GTPBP.
    SMARTiSM00178. SAR. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51422. SAR1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9CQC9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFIFDWIYS GFSSVLQFLG LYKKSGKLVF LGLDNAGKTT LLHMLKDDRL    50
    GQHVPTLHPT SEELTIAGMT FTTFDLGGHV QARRVWKNYL PAINGIVFLV 100
    DCADHERLLE SKEELDSLMT DETIANVPIL ILGNKIDRPE AISEERLREM 150
    FGLYGQTTGK GSVSLKELNA RPLEVFMCSV LKRQGYGEGF RWMAQYID 198
    Length:198
    Mass (Da):22,382
    Last modified:June 1, 2001 - v1
    Checksum:i9D0173C53FCD7A6B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002327 mRNA. Translation: BAB22015.1.
    AK010187 mRNA. Translation: BAB26755.1.
    AK013559 mRNA. Translation: BAB28905.1.
    AK150906 mRNA. Translation: BAE29948.1.
    BC082550 mRNA. Translation: AAH82550.1.
    CCDSiCCDS24661.1.
    RefSeqiNP_079811.1. NM_025535.2.
    UniGeneiMm.196592.

    Genome annotation databases

    EnsembliENSMUST00000020653; ENSMUSP00000020653; ENSMUSG00000020386.
    GeneIDi66397.
    KEGGimmu:66397.
    UCSCiuc007iup.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002327 mRNA. Translation: BAB22015.1 .
    AK010187 mRNA. Translation: BAB26755.1 .
    AK013559 mRNA. Translation: BAB28905.1 .
    AK150906 mRNA. Translation: BAE29948.1 .
    BC082550 mRNA. Translation: AAH82550.1 .
    CCDSi CCDS24661.1.
    RefSeqi NP_079811.1. NM_025535.2.
    UniGenei Mm.196592.

    3D structure databases

    ProteinModelPortali Q9CQC9.
    SMRi Q9CQC9. Positions 13-198.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211441. 1 interaction.

    PTM databases

    PhosphoSitei Q9CQC9.

    Proteomic databases

    MaxQBi Q9CQC9.
    PaxDbi Q9CQC9.
    PRIDEi Q9CQC9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020653 ; ENSMUSP00000020653 ; ENSMUSG00000020386 .
    GeneIDi 66397.
    KEGGi mmu:66397.
    UCSCi uc007iup.2. mouse.

    Organism-specific databases

    CTDi 51128.
    MGIi MGI:1913647. Sar1b.

    Phylogenomic databases

    eggNOGi COG1100.
    GeneTreei ENSGT00550000074696.
    HOGENOMi HOG000163690.
    HOVERGENi HBG104997.
    InParanoidi Q9CQC9.
    KOi K07953.
    OMAi DEQLANC.
    OrthoDBi EOG7W1550.
    PhylomeDBi Q9CQC9.
    TreeFami TF312890.

    Enzyme and pathway databases

    Reactomei REACT_196550. MHC class II antigen presentation.
    REACT_198968. Regulation of cholesterol biosynthesis by SREBP (SREBF).
    REACT_205304. COPII (Coat Protein 2) Mediated Vesicle Transport.

    Miscellaneous databases

    NextBioi 321555.
    PROi Q9CQC9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9CQC9.
    Bgeei Q9CQC9.
    CleanExi MM_SAR1B.
    Genevestigatori Q9CQC9.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR006689. Small_GTPase_ARF/SAR.
    IPR006687. Small_GTPase_SAR1.
    [Graphical view ]
    Pfami PF00025. Arf. 1 hit.
    [Graphical view ]
    PRINTSi PR00328. SAR1GTPBP.
    SMARTi SM00178. SAR. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51422. SAR1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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, Hippocampus, Kidney and Tongue.
    2. "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: C57BL/6.
      Tissue: Brain.
    3. "The mammalian guanine nucleotide exchange factor mSec12 is essential for activation of the Sar1 GTPase directing endoplasmic reticulum export."
      Weissman J.T., Plutner H., Balch W.E.
      Traffic 2:465-475(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PREB, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiSAR1B_MOUSE
    AccessioniPrimary (citable) accession number: Q9CQC9
    Secondary accession number(s): Q3UBL6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 9, 2003
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 109 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

    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