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Protein

Ras-related protein Ral-B

Gene

Ralb

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

Functioni

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).By similarity

Enzyme regulationi

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).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi21 – 299GTPBy similarity
Nucleotide bindingi68 – 725GTPBy similarity
Nucleotide bindingi128 – 1314GTPBy similarity
Nucleotide bindingi158 – 1603GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis, Cell cycle, Cell division

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_296095. p38MAPK events.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Ral-B
Gene namesi
Name:Ralb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1927244. Ralb.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 203203Ras-related protein Ral-BPRO_0000082699Add
BLAST
Propeptidei204 – 2063Removed in mature formBy similarityPRO_0000281351

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031Cysteine methyl esterBy similarity
Lipidationi203 – 2031S-geranylgeranyl cysteineBy similarity

Post-translational modificationi

Prenylation is essential for membrane localization.By similarity

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiQ9JIW9.
PaxDbiQ9JIW9.
PRIDEiQ9JIW9.

PTM databases

PhosphoSiteiQ9JIW9.

Expressioni

Gene expression databases

BgeeiQ9JIW9.
GenevisibleiQ9JIW9. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi211033. 1 interaction.
IntActiQ9JIW9. 3 interactions.
MINTiMINT-1866131.
STRINGi10090.ENSMUSP00000004565.

Structurei

3D structure databases

ProteinModelPortaliQ9JIW9.
SMRiQ9JIW9. Positions 12-185.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi43 – 519Effector region

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ras family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00780000121849.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiQ9JIW9.
KOiK07835.
OMAiRESHMAS.
OrthoDBiEOG7QVM41.
PhylomeDBiQ9JIW9.
TreeFamiTF312796.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR028412. Ral.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PTHR24070:SF199. PTHR24070:SF199. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9JIW9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAANKGKSQG SLVLHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS
60 70 80 90 100
YRKKVVLDGE EVQIDILDTA GQEDYAAIRD NYFRSGEGFL LVFSITEHES
110 120 130 140 150
FTATAEFREQ ILRVKSEEDK IPLLVVGNKS DLEERRQVPV DEARGKAEEW
160 170 180 190 200
GVQYVETSAK TRANVDKVFF DLMREIRAKK MSENKDKNGR KSSKSKKSFK

ERCCLL
Length:206
Mass (Da):23,349
Last modified:October 1, 2000 - v1
Checksum:i6CA5994C74221232
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF174296 mRNA. Translation: AAF89875.1.
AK017698 mRNA. Translation: BAB30881.1.
AK159993 mRNA. Translation: BAE35543.1.
BC006907 mRNA. Translation: AAH06907.1.
CCDSiCCDS15225.1.
RefSeqiNP_071722.1. NM_022327.5.
XP_006529845.1. XM_006529782.1.
UniGeneiMm.27832.

Genome annotation databases

EnsembliENSMUST00000004565; ENSMUSP00000004565; ENSMUSG00000004451.
GeneIDi64143.
KEGGimmu:64143.
UCSCiuc007cis.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF174296 mRNA. Translation: AAF89875.1.
AK017698 mRNA. Translation: BAB30881.1.
AK159993 mRNA. Translation: BAE35543.1.
BC006907 mRNA. Translation: AAH06907.1.
CCDSiCCDS15225.1.
RefSeqiNP_071722.1. NM_022327.5.
XP_006529845.1. XM_006529782.1.
UniGeneiMm.27832.

3D structure databases

ProteinModelPortaliQ9JIW9.
SMRiQ9JIW9. Positions 12-185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211033. 1 interaction.
IntActiQ9JIW9. 3 interactions.
MINTiMINT-1866131.
STRINGi10090.ENSMUSP00000004565.

PTM databases

PhosphoSiteiQ9JIW9.

Proteomic databases

MaxQBiQ9JIW9.
PaxDbiQ9JIW9.
PRIDEiQ9JIW9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004565; ENSMUSP00000004565; ENSMUSG00000004451.
GeneIDi64143.
KEGGimmu:64143.
UCSCiuc007cis.2. mouse.

Organism-specific databases

CTDi5899.
MGIiMGI:1927244. Ralb.

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00780000121849.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiQ9JIW9.
KOiK07835.
OMAiRESHMAS.
OrthoDBiEOG7QVM41.
PhylomeDBiQ9JIW9.
TreeFamiTF312796.

Enzyme and pathway databases

ReactomeiREACT_296095. p38MAPK events.

Miscellaneous databases

ChiTaRSiRalb. mouse.
NextBioi319935.
PROiQ9JIW9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JIW9.
GenevisibleiQ9JIW9. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR028412. Ral.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PTHR24070:SF199. PTHR24070:SF199. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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].

Entry informationi

Entry nameiRALB_MOUSE
AccessioniPrimary (citable) accession number: Q9JIW9
Secondary accession number(s): Q3TVS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: October 1, 2000
Last modified: June 24, 2015
This is version 133 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.