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Protein

Ras-related protein Ral-B

Gene

RALB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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 (By similarity). Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells (By similarity). Required for suppression of apoptosis (PubMed:17875936). In late stages of cytokinesis, upon completion of the bridge formation between dividing cells, mediates exocyst recruitment to the midbody to drive abscission (PubMed:18756269).By similarity2 Publications

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)DescriptionActionsGraphical viewLength
Nucleotide bindingi21 – 29GTP9
Nucleotide bindingi68 – 72GTP5
Nucleotide bindingi128 – 131GTP4
Nucleotide bindingi158 – 160GTP3

GO - Molecular functioni

  • ATPase binding Source: UniProtKB
  • GDP binding Source: UniProtKB
  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • cellular response to exogenous dsRNA Source: UniProtKB
  • cellular response to starvation Source: UniProtKB
  • negative regulation of protein binding Source: UniProtKB
  • positive regulation of autophagosome assembly Source: UniProtKB
  • positive regulation of protein binding Source: UniProtKB
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  • Ras protein signal transduction Source: InterPro
  • regulation of exocyst assembly Source: UniProtKB
  • regulation of exocyst localization Source: UniProtKB
  • signal transduction Source: ProtInc

Keywordsi

Biological processApoptosis, Cell cycle, Cell division
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-171007. p38MAPK events.
SIGNORiP11234.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Ral-B
Gene namesi
Name:RALB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000144118.13.
HGNCiHGNC:9840. RALB.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1 – 11Missing : No effect on cytokinesis. Impaired cytokinesis, as shown by increased number of binucleate cells; when associated with V-23. 1 PublicationAdd BLAST11
Mutagenesisi23G → V: Impaired cytokinesis, as shown by increased number of binucleate cells. Impaired cytokinesis; when associated with 1-M--S-11 or N-49. No effect on cytokinesis; when associated with R-38, W-48 or E-49. No effect on interaction with EXOC2 and EXOC8. Decreased interaction with EXOC2 and EXOC8; when associated with R-38 or W-48. 1 Publication1
Mutagenesisi38E → R: No effect on cytokinesis. No effect on cytokinesis; when associated with V-23. Decreased interaction with EXOC2 and EXOC8; when associated with V-23. 1 Publication1
Mutagenesisi46T → A: Reduces the binding affinity to EXOC2 effector. 1 Publication1
Mutagenesisi46T → S: Reduces the binding affinity to EXOC2 effector. 1 Publication1
Mutagenesisi48A → W: Impaired abscission, the last step of cytokinesis, as shown by the accumulation of bridged cells. No effect on cytokinesis; when associated with V-23. Decreased interaction with EXOC2 and EXOC8; when associated with V-23. 1 Publication1
Mutagenesisi49D → E: Impaired abscission, the last step of cytokinesis. No effect on cytokinesis; when associated with V-23. 1 Publication1
Mutagenesisi49D → N: No effect on cytokinesis. Impaired cytokinesis, as shown by increased number of binucleate cells; when associated with V-23. 1 Publication1
Mutagenesisi72Q → L: Loss of GTPase activity. 1 Publication1
Mutagenesisi203C → S: Loss of geranylgeranylation and membrane localization. 1 Publication1
Mutagenesisi206L → S: Converts geranyl-geranylation to farnesylation. No effect on membrane localization. Confers resistance to GGTI-induced pancreatic cancer cell apoptosis, but not to GGTI-dependent inhibition of anchorage-independent proliferation. 1 Publication1

Organism-specific databases

DisGeNETi5899.
OpenTargetsiENSG00000144118.
PharmGKBiPA34198.

Polymorphism and mutation databases

BioMutaiRALB.
DMDMi131835.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000826981 – 203Ras-related protein Ral-BAdd BLAST203
PropeptideiPRO_0000281349204 – 206Removed in mature formBy similarity3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei203Cysteine methyl esterBy similarity1
Lipidationi203S-geranylgeranyl cysteine1 Publication1

Post-translational modificationi

Prenylation is essential for membrane localization. The geranylgeranylated form and the farnesylated mutant does not undergo alternative prenylation in response to geranylgeranyltransferase I inhibitors (GGTIs) and farnesyltransferase I inhibitors (FTIs).1 Publication
The farnesylated form confers resistance to the proapoptotic and anti-anchorage-dependent growth effects of geranylgeranyltransferase I inhibitors, including GGTI-2417.1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

EPDiP11234.
PaxDbiP11234.
PeptideAtlasiP11234.
PRIDEiP11234.

PTM databases

iPTMnetiP11234.
PhosphoSitePlusiP11234.
SwissPalmiP11234.

Expressioni

Gene expression databases

BgeeiENSG00000144118.
CleanExiHS_RALB.
ExpressionAtlasiP11234. baseline and differential.
GenevisibleiP11234. HS.

Organism-specific databases

HPAiCAB026010.
HPA065232.

Interactioni

Subunit structurei

Interacts with EXOC2/Sec5 and EXOC8/Exo84 (PubMed:14525976, PubMed:18756269, PubMed:19166349). Interacts (via effector domain) with RALBP1 (PubMed:7673236, PubMed:20696399).5 Publications

GO - Molecular functioni

  • ATPase binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111835. 34 interactors.
IntActiP11234. 19 interactors.
MINTiMINT-5000915.
STRINGi9606.ENSP00000272519.

Structurei

Secondary structure

1206
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni10 – 12Combined sources3
Beta strandi14 – 25Combined sources12
Helixi27 – 36Combined sources10
Beta strandi51 – 56Combined sources6
Beta strandi61 – 68Combined sources8
Beta strandi74 – 77Combined sources4
Helixi78 – 84Combined sources7
Beta strandi87 – 96Combined sources10
Helixi98 – 114Combined sources17
Beta strandi117 – 119Combined sources3
Beta strandi123 – 128Combined sources6
Helixi140 – 148Combined sources9
Turni149 – 151Combined sources3
Beta strandi154 – 156Combined sources3
Turni159 – 161Combined sources3
Helixi165 – 179Combined sources15
Turni180 – 182Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KE5NMR-A12-185[»]
2KWINMR-A8-185[»]
ProteinModelPortaliP11234.
SMRiP11234.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11234.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi43 – 51Effector region9

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ras family.Curated

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00860000133678.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiP11234.
KOiK07835.
OMAiTSRMAAN.
OrthoDBiEOG091G0UAU.
PhylomeDBiP11234.
TreeFamiTF312796.

Family and domain databases

InterProiView protein in InterPro
IPR027417. P-loop_NTPase.
IPR028412. Ral.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
PANTHERiPTHR24070. PTHR24070. 1 hit.
PTHR24070:SF199. PTHR24070:SF199. 1 hit.
PfamiView protein in Pfam
PF00071. Ras. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiView protein in PROSITE
PS51421. RAS. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P11234-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAANKSKGQS SLALHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS
60 70 80 90 100
YRKKVVLDGE EVQIDILDTA GQEDYAAIRD NYFRSGEGFL LVFSITEHES
110 120 130 140 150
FTATAEFREQ ILRVKAEEDK IPLLVVGNKS DLEERRQVPV EEARSKAEEW
160 170 180 190 200
GVQYVETSAK TRANVDKVFF DLMREIRTKK MSENKDKNGK KSSKNKKSFK

ERCCLL
Length:206
Mass (Da):23,409
Last modified:July 1, 1989 - v1
Checksum:iE0AC95130FB6452C
GO
Isoform 2 (identifier: P11234-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MKQRQSALQWVICVSQPQKTSEM

Note: No experimental confirmation available.
Show »
Length:228
Mass (Da):25,967
Checksum:iB36FAF7D688B0861
GO
Isoform 3 (identifier: P11234-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     36-37: YD → NVSKSLAYDKKKYTANKKVEGIL

Note: No experimental confirmation available.
Show »
Length:227
Mass (Da):25,710
Checksum:i174A6FBCF109A103
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0558431M → MKQRQSALQWVICVSQPQKT SEM in isoform 2. 1 Publication1
Alternative sequenceiVSP_05584436 – 37YD → NVSKSLAYDKKKYTANKKVE GIL in isoform 3. 1 Publication2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15015 mRNA. Translation: CAA33119.1.
M35416 mRNA. Translation: AAA60250.1.
AF493911 mRNA. Translation: AAM12625.1.
BT006953 mRNA. Translation: AAP35599.1.
AK127675 mRNA. Translation: BAC87080.1.
AK303214 mRNA. Translation: BAG64302.1.
AK312453 mRNA. Translation: BAG35360.1.
AC012363 Genomic DNA. Translation: AAY14800.1.
CH471103 Genomic DNA. Translation: EAW95240.1.
CH471103 Genomic DNA. Translation: EAW95242.1.
BC018163 mRNA. Translation: AAH18163.1.
CCDSiCCDS2131.1. [P11234-1]
PIRiS04597. TVHUAB.
RefSeqiNP_002872.1. NM_002881.2. [P11234-1]
XP_005263781.1. XM_005263724.1. [P11234-2]
XP_005263784.1. XM_005263727.1. [P11234-1]
XP_005263785.1. XM_005263728.1. [P11234-1]
XP_005263786.1. XM_005263729.2. [P11234-1]
XP_016860111.1. XM_017004622.1. [P11234-1]
UniGeneiHs.469820.

Genome annotation databases

EnsembliENST00000272519; ENSP00000272519; ENSG00000144118. [P11234-1]
ENST00000420510; ENSP00000414224; ENSG00000144118. [P11234-1]
GeneIDi5899.
KEGGihsa:5899.
UCSCiuc002tmk.4. human. [P11234-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiRALB_HUMAN
AccessioniPrimary (citable) accession number: P11234
Secondary accession number(s): B4E040, Q53T32, Q6ZS74
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 25, 2017
This is version 187 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families