Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ras-related C3 botulinum toxin substrate 2

Gene

RAC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. Augments the production of reactive oxygen species (ROS) by NADPH oxidase.1 Publication

Enzyme regulationi

Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP, GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity, and GDP dissociation inhibitors which inhibit the dissociation of the nucleotide from the GTPase.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 17GTPBy similarity8
Nucleotide bindingi57 – 61GTPBy similarity5
Nucleotide bindingi115 – 118GTPBy similarity4

GO - Molecular functioni

  • GTPase activity Source: ProtInc
  • GTP binding Source: UniProtKB
  • protein kinase regulator activity Source: Ensembl

GO - Biological processi

  • actin filament organization Source: UniProtKB
  • bone resorption Source: Ensembl
  • cell projection assembly Source: Ensembl
  • chemotaxis Source: Ensembl
  • G-protein coupled receptor signaling pathway Source: Ensembl
  • lymphocyte aggregation Source: UniProtKB
  • platelet activation Source: Reactome
  • positive regulation of cell proliferation Source: Ensembl
  • positive regulation of lamellipodium assembly Source: UniProtKB
  • positive regulation of neutrophil chemotaxis Source: UniProtKB
  • positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
  • regulation of cell-substrate adhesion Source: UniProtKB
  • regulation of hydrogen peroxide metabolic process Source: BHF-UCL
  • regulation of mast cell chemotaxis Source: Ensembl
  • regulation of mast cell degranulation Source: Ensembl
  • regulation of neutrophil migration Source: UniProtKB
  • regulation of respiratory burst Source: BHF-UCL
  • regulation of small GTPase mediated signal transduction Source: Reactome
  • regulation of T cell proliferation Source: Ensembl
  • signal transduction Source: ProtInc
  • small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000128340-MONOMER.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-194840. Rho GTPase cycle.
R-HSA-4086400. PCP/CE pathway.
R-HSA-416482. G alpha (12/13) signalling events.
R-HSA-416572. Sema4D induced cell migration and growth-cone collapse.
R-HSA-5668599. RHO GTPases Activate NADPH Oxidases.
SignaLinkiP15153.
SIGNORiP15153.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related C3 botulinum toxin substrate 2
Alternative name(s):
GX
Small G protein
p21-Rac2
Gene namesi
Name:RAC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:9802. RAC2.

Subcellular locationi

  • Cytoplasm

  • Note: Membrane-associated when activated.

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • nuclear envelope Source: Ensembl
  • phagocytic vesicle membrane Source: Reactome
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Neutrophil immunodeficiency syndrome (NEUID)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn immunodeficiency syndrome due to defective neutrophils. Affected individuals present with leukocytosis, neutrophilia, severe recurrent bacterial infections and poor wound healing.
See also OMIM:608203
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01745257D → N in NEUID; dominant-negative mutant; binds GDP, but not GTP; inhibits oxidase activation and superoxide anion production in vitro. 1 PublicationCorresponds to variant rs74315507dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi189C → W: Abolishes in vitro prenylation. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi5880.
MalaCardsiRAC2.
MIMi608203. phenotype.
OpenTargetsiENSG00000128340.
Orphaneti183707. Neutrophil immunodeficiency syndrome.
PharmGKBiPA34163.

Chemistry databases

ChEMBLiCHEMBL5581.
DrugBankiDB00514. Dextromethorphan.

Polymorphism and mutation databases

DMDMi131806.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000420461 – 189Ras-related C3 botulinum toxin substrate 2Add BLAST189
PropeptideiPRO_0000042047190 – 192Removed in mature formBy similarity3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi32O-linked (GlcNAc); by Photorhabdus PAU_022301 Publication1
Modified residuei39ADP-ribosylasparagine; by botulinum toxinBy similarity1
Modified residuei147N6-acetyllysineCombined sources1
Modified residuei189Cysteine methyl esterBy similarity1
Lipidationi189S-geranylgeranyl cysteine1 Publication1

Post-translational modificationi

(Microbial infection) Glycosylated at Tyr-32 by Photorhabdus asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits downstream signaling by an impaired interaction with diverse regulator and effector proteins of Rac and leads to actin disassembly.1 Publication

Keywords - PTMi

Acetylation, ADP-ribosylation, Glycoprotein, Lipoprotein, Methylation, Prenylation

Proteomic databases

EPDiP15153.
MaxQBiP15153.
PaxDbiP15153.
PeptideAtlasiP15153.
PRIDEiP15153.

PTM databases

iPTMnetiP15153.
PhosphoSitePlusiP15153.
SwissPalmiP15153.

Expressioni

Tissue specificityi

Hematopoietic specific.

Gene expression databases

BgeeiENSG00000128340.
CleanExiHS_RAC2.
ExpressionAtlasiP15153. baseline and differential.
GenevisibleiP15153. HS.

Organism-specific databases

HPAiCAB022946.
HPA047820.

Interactioni

Subunit structurei

Interacts with DOCK2, which may activate it. Interacts with S100A8 and calprotectin (S100A8/9).2 Publications

Protein-protein interaction databases

BioGridi111818. 22 interactors.
DIPiDIP-34291N.
IntActiP15153. 12 interactors.
MINTiMINT-1616362.
STRINGi9606.ENSP00000249071.

Structurei

Secondary structure

1192
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Helixi16 – 25Combined sources10
Beta strandi39 – 46Combined sources8
Beta strandi49 – 56Combined sources8
Helixi62 – 64Combined sources3
Turni65 – 67Combined sources3
Helixi68 – 71Combined sources4
Beta strandi77 – 83Combined sources7
Helixi87 – 95Combined sources9
Helixi97 – 104Combined sources8
Beta strandi106 – 108Combined sources3
Beta strandi110 – 115Combined sources6
Helixi117 – 119Combined sources3
Helixi123 – 130Combined sources8
Turni131 – 133Combined sources3
Helixi139 – 149Combined sources11
Beta strandi152 – 156Combined sources5
Turni159 – 161Combined sources3
Helixi165 – 175Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DS6X-ray2.35A1-192[»]
2W2TX-ray1.95A2-179[»]
2W2VX-ray2.00A/B/C/D1-177[»]
2W2XX-ray2.30A/B2-179[»]
ProteinModelPortaliP15153.
SMRiP15153.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15153.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi32 – 40Effector regionSequence analysis9

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000118978.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP15153.
KOiK07860.
OMAiSYENVHA.
OrthoDBiEOG091G0KCM.
PhylomeDBiP15153.
TreeFamiTF101109.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P15153-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDSKP
60 70 80 90 100
VNLGLWDTAG QEDYDRLRPL SYPQTDVFLI CFSLVSPASY ENVRAKWFPE
110 120 130 140 150
VRHHCPSTPI ILVGTKLDLR DDKDTIEKLK EKKLAPITYP QGLALAKEID
160 170 180 190
SVKYLECSAL TQRGLKTVFD EAIRAVLCPQ PTRQQKRACS LL
Length:192
Mass (Da):21,429
Last modified:April 1, 1990 - v1
Checksum:i2A1F1266B07C3210
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03656929P → L in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_01745257D → N in NEUID; dominant-negative mutant; binds GDP, but not GTP; inhibits oxidase activation and superoxide anion production in vitro. 1 PublicationCorresponds to variant rs74315507dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29871 mRNA. Translation: AAA36538.1.
AF498965 mRNA. Translation: AAM21112.1.
CR456555 mRNA. Translation: CAG30441.1.
BT006919 mRNA. Translation: AAP35565.1.
Z82188 Genomic DNA. Translation: CAB45265.1.
BC001485 mRNA. Translation: AAH01485.1.
M64595 mRNA. Translation: AAA35941.1.
CCDSiCCDS13945.1.
PIRiB34386.
RefSeqiNP_002863.1. NM_002872.4.
UniGeneiHs.517601.

Genome annotation databases

EnsembliENST00000249071; ENSP00000249071; ENSG00000128340.
GeneIDi5880.
KEGGihsa:5880.
UCSCiuc003arc.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
RAC2base

RAC2 mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29871 mRNA. Translation: AAA36538.1.
AF498965 mRNA. Translation: AAM21112.1.
CR456555 mRNA. Translation: CAG30441.1.
BT006919 mRNA. Translation: AAP35565.1.
Z82188 Genomic DNA. Translation: CAB45265.1.
BC001485 mRNA. Translation: AAH01485.1.
M64595 mRNA. Translation: AAA35941.1.
CCDSiCCDS13945.1.
PIRiB34386.
RefSeqiNP_002863.1. NM_002872.4.
UniGeneiHs.517601.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DS6X-ray2.35A1-192[»]
2W2TX-ray1.95A2-179[»]
2W2VX-ray2.00A/B/C/D1-177[»]
2W2XX-ray2.30A/B2-179[»]
ProteinModelPortaliP15153.
SMRiP15153.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111818. 22 interactors.
DIPiDIP-34291N.
IntActiP15153. 12 interactors.
MINTiMINT-1616362.
STRINGi9606.ENSP00000249071.

Chemistry databases

ChEMBLiCHEMBL5581.
DrugBankiDB00514. Dextromethorphan.

PTM databases

iPTMnetiP15153.
PhosphoSitePlusiP15153.
SwissPalmiP15153.

Polymorphism and mutation databases

DMDMi131806.

Proteomic databases

EPDiP15153.
MaxQBiP15153.
PaxDbiP15153.
PeptideAtlasiP15153.
PRIDEiP15153.

Protocols and materials databases

DNASUi5880.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000249071; ENSP00000249071; ENSG00000128340.
GeneIDi5880.
KEGGihsa:5880.
UCSCiuc003arc.5. human.

Organism-specific databases

CTDi5880.
DisGeNETi5880.
GeneCardsiRAC2.
HGNCiHGNC:9802. RAC2.
HPAiCAB022946.
HPA047820.
MalaCardsiRAC2.
MIMi602049. gene.
608203. phenotype.
neXtProtiNX_P15153.
OpenTargetsiENSG00000128340.
Orphaneti183707. Neutrophil immunodeficiency syndrome.
PharmGKBiPA34163.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000118978.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP15153.
KOiK07860.
OMAiSYENVHA.
OrthoDBiEOG091G0KCM.
PhylomeDBiP15153.
TreeFamiTF101109.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000128340-MONOMER.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-194840. Rho GTPase cycle.
R-HSA-4086400. PCP/CE pathway.
R-HSA-416482. G alpha (12/13) signalling events.
R-HSA-416572. Sema4D induced cell migration and growth-cone collapse.
R-HSA-5668599. RHO GTPases Activate NADPH Oxidases.
SignaLinkiP15153.
SIGNORiP15153.

Miscellaneous databases

ChiTaRSiRAC2. human.
EvolutionaryTraceiP15153.
GeneWikiiRAC2.
GenomeRNAii5880.
PROiP15153.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000128340.
CleanExiHS_RAC2.
ExpressionAtlasiP15153. baseline and differential.
GenevisibleiP15153. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRAC2_HUMAN
AccessioniPrimary (citable) accession number: P15153
Secondary accession number(s): Q9UDJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 2, 2016
This is version 189 of the entry and version 1 of the sequence. [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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.