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Q9JIW9 (RALB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. 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 Ral-B
Gene names
Name:Ralb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length206 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells. Plays a role in the late stages of cytokinesis and is required for the abscission of the bridge joining the sister cells emerging from mitosis. Required for suppression of apoptosis By similarity.

Enzyme regulation

Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by a guanine nucleotide-exchange factor (GEF) and inactivated by a GTPase-activating protein (GAP).

Subunit structure

Interacts with EXOC8. Interacts with RALBP1 via its effector domain By similarity.

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side By similarity. Note: During late cytokinesis localizes at the midbody By similarity.

Post-translational modification

Prenylation is essential for membrane localization By similarity.

Sequence similarities

Belongs to the small GTPase superfamily. Ras family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 203203Ras-related protein Ral-B
PRO_0000082699
Propeptide204 – 2063Removed in mature form By similarity
PRO_0000281351

Regions

Nucleotide binding21 – 299GTP By similarity
Nucleotide binding68 – 725GTP By similarity
Nucleotide binding128 – 1314GTP By similarity
Nucleotide binding158 – 1603GTP By similarity
Motif43 – 519Effector region

Amino acid modifications

Modified residue2031Cysteine methyl ester By similarity
Lipidation2031S-geranylgeranyl cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9JIW9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 6CA5994C74221232

FASTA20623,349
        10         20         30         40         50         60 
MAANKGKSQG SLVLHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS YRKKVVLDGE 

        70         80         90        100        110        120 
EVQIDILDTA GQEDYAAIRD NYFRSGEGFL LVFSITEHES FTATAEFREQ ILRVKSEEDK 

       130        140        150        160        170        180 
IPLLVVGNKS DLEERRQVPV DEARGKAEEW GVQYVETSAK TRANVDKVFF DLMREIRAKK 

       190        200 
MSENKDKNGR KSSKSKKSFK ERCCLL 

« Hide

References

« Hide 'large scale' references
[1]"Tissue-specific expression of GTPas RalA and RalB during embryogenesis and regulation by epithelial-mesenchymal interaction."
Zhao Z., Rivkees S.A.
Mech. Dev. 97:201-204(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
[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. 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: Embryo.
[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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF174296 mRNA. Translation: AAF89875.1.
AK017698 mRNA. Translation: BAB30881.1.
AK159993 mRNA. Translation: BAE35543.1.
BC006907 mRNA. Translation: AAH06907.1.
RefSeqNP_071722.1. NM_022327.5.
XP_006529845.1. XM_006529782.1.
UniGeneMm.27832.

3D structure databases

ProteinModelPortalQ9JIW9.
SMRQ9JIW9. Positions 12-185.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211033. 1 interaction.
IntActQ9JIW9. 3 interactions.
MINTMINT-1866131.

PTM databases

PhosphoSiteQ9JIW9.

Proteomic databases

PaxDbQ9JIW9.
PRIDEQ9JIW9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000004565; ENSMUSP00000004565; ENSMUSG00000004451.
GeneID64143.
KEGGmmu:64143.
UCSCuc007cis.2. mouse.

Organism-specific databases

CTD5899.
MGIMGI:1927244. Ralb.

Phylogenomic databases

eggNOGCOG1100.
GeneTreeENSGT00750000117261.
HOGENOMHOG000233973.
HOVERGENHBG009351.
InParanoidQ9JIW9.
KOK07835.
OMAXFVEDYE.
OrthoDBEOG7QVM41.
PhylomeDBQ9JIW9.
TreeFamTF312796.

Gene expression databases

BgeeQ9JIW9.
GenevestigatorQ9JIW9.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR028412. Ral.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERPTHR24070. PTHR24070. 1 hit.
PTHR24070:SF3. PTHR24070:SF3. 1 hit.
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio319935.
PROQ9JIW9.
SOURCESearch...

Entry information

Entry nameRALB_MOUSE
AccessionPrimary (citable) accession number: Q9JIW9
Secondary accession number(s): Q3TVS5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 119 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