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Protein

GTP-binding protein SAR1b

Gene

Sar1b

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 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
Complete GO annotation...

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.
REACT_246972. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

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
Complete GO annotation...

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

BgeeiQ9CQC9.
CleanExiMM_SAR1B.
ExpressionAtlasiQ9CQC9. baseline and differential.
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.
OMAiMKELNTR.
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

        10         20         30         40         50
MSFIFDWIYS GFSSVLQFLG LYKKSGKLVF LGLDNAGKTT LLHMLKDDRL
60 70 80 90 100
GQHVPTLHPT SEELTIAGMT FTTFDLGGHV QARRVWKNYL PAINGIVFLV
110 120 130 140 150
DCADHERLLE SKEELDSLMT DETIANVPIL ILGNKIDRPE AISEERLREM
160 170 180 190
FGLYGQTTGK GSVSLKELNA RPLEVFMCSV LKRQGYGEGF RWMAQYID
Length:198
Mass (Da):22,382
Last modified:June 1, 2001 - v1
Checksum:i9D0173C53FCD7A6B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi211441. 1 interaction.

PTM databases

PhosphoSiteiQ9CQC9.

Proteomic databases

MaxQBiQ9CQC9.
PaxDbiQ9CQC9.
PRIDEiQ9CQC9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi51128.
MGIiMGI:1913647. Sar1b.

Phylogenomic databases

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

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.
REACT_246972. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

NextBioi321555.
PROiQ9CQC9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQC9.
CleanExiMM_SAR1B.
ExpressionAtlasiQ9CQC9. baseline and differential.
GenevestigatoriQ9CQC9.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 112 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

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 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.