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Q921E2 (RAB31_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-31
Gene names
Name:Rab31
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Required for the integrity and for normal function of the Golgi apparatus and the trans-Golgi network. Plays a role in insulin-stimulated translocation of GLUT4 to the cell membrane. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and Mycobacterium By similarity. Plays a role in M6PR transport from the trans-Golgi network to endosomes. Plays a role in the internalization of EGFR from the cell membrane into endosomes. Ref.3 Ref.6

Subunit structure

Interacts with OCRL. Interacts (in GDP-bound form) with RIN3 and GAPVD1, which function as guanine exchange factors (GEF). Interacts with EGFR By similarity. Interacts with NGFR. Interacts (in GTP-bound form) with EEA1. Ref.6

Subcellular location

Golgi apparatustrans-Golgi network By similarity. Golgi apparatustrans-Golgi network membrane; Lipid-anchor; Cytoplasmic side By similarity. Early endosome By similarity. Cytoplasmic vesiclephagosome By similarity. Cytoplasmic vesiclephagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Note: Rapidly recruited to phagosomes containing S.aureus or Mycobacterium By similarity.

Tissue specificity

Detected in brain astrocytes (at protein level). Ref.5

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Sequence caution

The sequence BAC34585.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 194194Ras-related protein Rab-31
PRO_0000121233

Regions

Nucleotide binding12 – 198GTP By similarity
Nucleotide binding60 – 645GTP By similarity
Nucleotide binding118 – 1214GTP By similarity
Motif34 – 429Effector region By similarity

Amino acid modifications

Modified residue351Phosphoserine Ref.4
Lipidation1931S-geranylgeranyl cysteine By similarity
Lipidation1941S-geranylgeranyl cysteine By similarity

Experimental info

Sequence conflict491C → W in BAC34585. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q921E2 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 4EBCAF6E2431AD02

FASTA19421,331
        10         20         30         40         50         60 
MAIRELKVCL LGDTGVGKSS IVCRFVQDHF DHNISPTIGA SFMTKTVPCG NELHKFLIWD 

        70         80         90        100        110        120 
TAGQERFHSL APMYYRGSAA AVIVYDITKQ DSFHTLKKWV KELKEHGPEN IVMAIAGNKC 

       130        140        150        160        170        180 
DLSDIREVPL KDAKEYAESI GAIVVETSAK NAINIEELFQ GISRQIPPLG PQENGNSGGI 

       190 
KLGNQSLQAS RRCC 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: Spinal ganglion.
[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: FVB/N.
Tissue: Mammary tumor.
[3]"Transport of mannose-6-phosphate receptors from the trans-Golgi network to endosomes requires Rab31."
Rodriguez-Gabin A.G., Yin X., Si Q., Larocca J.N.
Exp. Cell Res. 315:2215-2230(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"Rab22B is expressed in the CNS astroglia lineage and plays a role in epidermal growth factor receptor trafficking in A431 cells."
Ng E.L., Ng J.J., Liang F., Tang B.L.
J. Cell. Physiol. 221:716-728(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"p75 neurotrophin receptor regulates glucose homeostasis and insulin sensitivity."
Baeza-Raja B., Li P., Le Moan N., Sachs B.D., Schachtrup C., Davalos D., Vagena E., Bridges D., Kim C., Saltiel A.R., Olefsky J.M., Akassoglou K.
Proc. Natl. Acad. Sci. U.S.A. 109:5838-5843(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EEA1 AND NGFR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK051270 mRNA. Translation: BAC34585.1. Different initiation.
BC013063 mRNA. Translation: AAH13063.1.
RefSeqNP_598446.2. NM_133685.2.
UniGeneMm.29274.

3D structure databases

ProteinModelPortalQ921E2.
SMRQ921E2. Positions 3-167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid223081. 1 interaction.
IntActQ921E2. 4 interactions.
MINTMINT-4997919.

PTM databases

PhosphoSiteQ921E2.

Proteomic databases

MaxQBQ921E2.
PaxDbQ921E2.
PRIDEQ921E2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID106572.
KEGGmmu:106572.

Organism-specific databases

CTD11031.
MGIMGI:1914603. Rab31.

Phylogenomic databases

eggNOGCOG1100.
HOVERGENHBG009351.
InParanoidQ921E2.
KOK07891.
OMAIANSCER.
PhylomeDBQ921E2.

Gene expression databases

ArrayExpressQ921E2.
BgeeQ921E2.
CleanExMM_RAB31.
GenevestigatorQ921E2.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio358266.
PROQ921E2.
SOURCESearch...

Entry information

Entry nameRAB31_MOUSE
AccessionPrimary (citable) accession number: Q921E2
Secondary accession number(s): Q8BKP0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot