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UniProtKB - P11234 (RALB_HUMAN)

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Protein

Ras-related protein Ral-B

Gene

RALB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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
View the complete GO annotation on QuickGO ...

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
View the complete GO annotation on QuickGO ...

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000144118.13
HGNCiHGNC:9840 RALB
MIMi179551 gene
neXtProtiNX_P11234

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

Chemistry databases

ChEMBLiCHEMBL3879851

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
ProteomicsDBi52727

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

Binary interactionsi

Show more details

GO - Molecular functioni

  • ATPase binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi111835, 35 interactors
IntActiP11234, 27 interactors
MINTiP11234
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

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
GeneTreeiENSGT00860000133672
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-type
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: July 18, 2018
This is version 192 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

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