Skip Header

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

P15153

- RAC2_HUMAN

UniProt

P15153 - RAC2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ras-related C3 botulinum toxin substrate 2

Gene

RAC2

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 178GTPBy similarity
Nucleotide bindingi57 – 615GTPBy similarity
Nucleotide bindingi115 – 1184GTPBy similarity

GO - Molecular functioni

  1. GTPase activity Source: ProtInc
  2. GTP binding Source: UniProtKB

GO - Biological processi

  1. actin filament organization Source: UniProtKB
  2. axon guidance Source: Reactome
  3. blood coagulation Source: Reactome
  4. bone resorption Source: Ensembl
  5. cell projection assembly Source: Ensembl
  6. G-protein coupled receptor signaling pathway Source: Ensembl
  7. lymphocyte aggregation Source: UniProtKB
  8. platelet activation Source: Reactome
  9. positive regulation of cell proliferation Source: Ensembl
  10. positive regulation of lamellipodium assembly Source: UniProtKB
  11. positive regulation of neutrophil chemotaxis Source: UniProtKB
  12. regulation of cell-substrate adhesion Source: UniProtKB
  13. regulation of hydrogen peroxide metabolic process Source: BHF-UCL
  14. regulation of neutrophil migration Source: UniProtKB
  15. regulation of respiratory burst Source: BHF-UCL
  16. regulation of small GTPase mediated signal transduction Source: Reactome
  17. signal transduction Source: ProtInc
  18. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_1695. GPVI-mediated activation cascade.
REACT_172581. PCP/CE pathway.
REACT_18407. G alpha (12/13) signalling events.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
SignaLinkiP15153.

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
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:9802. RAC2.

Subcellular locationi

Cytoplasm
Note: Membrane-associated when activated.

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
  3. focal adhesion Source: UniProtKB
  4. lamellipodium Source: UniProtKB
  5. nuclear envelope Source: Ensembl
  6. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Neutrophil immunodeficiency syndrome (NEUID) [MIM:608203]: An immunodeficiency syndrome due to defective neutrophils. Affected individuals present with leukocytosis, neutrophilia, severe recurrent bacterial infections and poor wound healing.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571D → N in NEUID; dominant-negative mutant; binds GDP, but not GTP; inhibits oxidase activation and superoxide anion production in vitro. 1 Publication
VAR_017452

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi189 – 1891C → W: Abolishes in vitro prenylation. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi608203. phenotype.
Orphaneti183707. Neutrophil immunodeficiency syndrome.
PharmGKBiPA34163.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 189189Ras-related C3 botulinum toxin substrate 2PRO_0000042046Add
BLAST
Propeptidei190 – 1923Removed in mature formBy similarityPRO_0000042047

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391ADP-ribosylasparagine; by botulinum toxinBy similarity
Modified residuei147 – 1471N6-acetyllysine1 Publication
Modified residuei189 – 1891Cysteine methyl esterBy similarity
Lipidationi189 – 1891S-geranylgeranyl cysteine1 Publication

Keywords - PTMi

Acetylation, ADP-ribosylation, Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiP15153.
PaxDbiP15153.
PeptideAtlasiP15153.
PRIDEiP15153.

PTM databases

PhosphoSiteiP15153.

Expressioni

Tissue specificityi

Hematopoietic specific.

Gene expression databases

BgeeiP15153.
CleanExiHS_RAC2.
ExpressionAtlasiP15153. baseline and differential.
GenevestigatoriP15153.

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. 19 interactions.
DIPiDIP-34291N.
IntActiP15153. 12 interactions.
MINTiMINT-1616362.
STRINGi9606.ENSP00000249071.

Structurei

Secondary structure

1
192
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119
Helixi16 – 2510
Beta strandi39 – 468
Beta strandi49 – 568
Helixi62 – 643
Turni65 – 673
Helixi68 – 714
Beta strandi77 – 837
Helixi87 – 959
Helixi97 – 1048
Beta strandi106 – 1083
Beta strandi110 – 1156
Helixi117 – 1193
Helixi123 – 1308
Turni131 – 1333
Helixi139 – 14911
Beta strandi152 – 1565
Turni159 – 1613
Helixi165 – 17511

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 1-181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15153.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi32 – 409Effector regionSequence Analysis

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118978.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP15153.
KOiK07860.
OMAiREDRSYL.
OrthoDBiEOG764747.
PhylomeDBiP15153.
TreeFamiTF101109.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00174. RHO. 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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291P → L in a breast cancer sample; somatic mutation. 1 Publication
VAR_036569
Natural varianti57 – 571D → N in NEUID; dominant-negative mutant; binds GDP, but not GTP; inhibits oxidase activation and superoxide anion production in vitro. 1 Publication
VAR_017452

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human.

Polymorphism databases

DMDMi131806.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS13945.1.
PIRi B34386.
RefSeqi NP_002863.1. NM_002872.4.
UniGenei Hs.517601.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DS6 X-ray 2.35 A 1-192 [» ]
2W2T X-ray 1.95 A 2-179 [» ]
2W2V X-ray 2.00 A/B/C/D 1-177 [» ]
2W2X X-ray 2.30 A/B 2-179 [» ]
ProteinModelPortali P15153.
SMRi P15153. Positions 1-181.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111818. 19 interactions.
DIPi DIP-34291N.
IntActi P15153. 12 interactions.
MINTi MINT-1616362.
STRINGi 9606.ENSP00000249071.

Chemistry

ChEMBLi CHEMBL5581.
DrugBanki DB00514. Dextromethorphan.

PTM databases

PhosphoSitei P15153.

Polymorphism databases

DMDMi 131806.

Proteomic databases

MaxQBi P15153.
PaxDbi P15153.
PeptideAtlasi P15153.
PRIDEi P15153.

Protocols and materials databases

DNASUi 5880.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000249071 ; ENSP00000249071 ; ENSG00000128340 .
GeneIDi 5880.
KEGGi hsa:5880.
UCSCi uc003arc.3. human.

Organism-specific databases

CTDi 5880.
GeneCardsi GC22M037621.
HGNCi HGNC:9802. RAC2.
HPAi CAB022946.
HPA047820.
MIMi 602049. gene.
608203. phenotype.
neXtProti NX_P15153.
Orphaneti 183707. Neutrophil immunodeficiency syndrome.
PharmGKBi PA34163.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
GeneTreei ENSGT00760000118978.
HOGENOMi HOG000233974.
HOVERGENi HBG009351.
InParanoidi P15153.
KOi K07860.
OMAi REDRSYL.
OrthoDBi EOG764747.
PhylomeDBi P15153.
TreeFami TF101109.

Enzyme and pathway databases

Reactomei REACT_11051. Rho GTPase cycle.
REACT_1695. GPVI-mediated activation cascade.
REACT_172581. PCP/CE pathway.
REACT_18407. G alpha (12/13) signalling events.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
SignaLinki P15153.

Miscellaneous databases

EvolutionaryTracei P15153.
GeneWikii RAC2.
GenomeRNAii 5880.
NextBioi 22854.
PROi P15153.
SOURCEi Search...

Gene expression databases

Bgeei P15153.
CleanExi HS_RAC2.
ExpressionAtlasi P15153. baseline and differential.
Genevestigatori P15153.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view ]
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00174. RHO. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51420. RHO. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Rac, a novel ras-related family of proteins that are botulinum toxin substrates."
    Didsbury J., Weber R.F., Bokoch G.M., Evans T., Snyderman R.
    J. Biol. Chem. 264:16378-16382(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Brain.
  7. "Regulation of the superoxide-generating NADPH oxidase by a small GTP-binding protein and its stimulatory and inhibitory GDP/GTP exchange proteins."
    Mizuno T., Kaibuchi K., Ando S., Musha T., Hiraoka K., Takaishi K., Asada M., Nunoi H., Matsuda I., Takai Y.
    J. Biol. Chem. 267:10215-10218(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 6-15; 97-107 AND 134-165.
  8. "Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2."
    Knaus U.G., Heyworth P.G., Evans T., Curnutte J.T., Bokoch G.M.
    Science 254:1512-1515(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 7-16; 19-49; 154-163 AND 175-183, FUNCTION.
    Tissue: Neutrophil.
  9. "A hemopoietic specific gene encoding a small GTP binding protein is overexpressed during T cell activation."
    Reibel L., Dorseuil O., Stancou R., Bertoglio J., Gacon G.
    Biochem. Biophys. Res. Commun. 175:451-458(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-192.
  10. "Regulation of the human neutrophil NADPH oxidase by rho-related G-proteins."
    Kwong C.H., Malech H.L., Rotrosen D., Leto T.L.
    Biochemistry 32:5711-5717(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 97-102 AND 167-174.
    Tissue: Neutrophil.
  11. "Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA."
    Kinsella B.T., Erdman R.A., Maltese W.A.
    J. Biol. Chem. 266:9786-9794(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-189, MUTAGENESIS OF CYS-189.
  12. "Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins."
    Nishihara H., Kobayashi S., Hashimoto Y., Ohba F., Mochizuki N., Kurata T., Nagashima K., Matsuda M.
    Biochim. Biophys. Acta 1452:179-187(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DOCK2.
  13. "The arachidonic acid-binding protein S100A8/A9 promotes NADPH oxidase activation by interaction with p67phox and Rac-2."
    Kerkhoff C., Nacken W., Benedyk M., Dagher M.C., Sopalla C., Doussiere J.
    FASEB J. 19:467-469(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH S100A8 AND CALPROTECTIN.
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI."
    Scheffzek K., Stephan I., Jensen O.N., Illenberger D., Gierschik P.
    Nat. Struct. Biol. 7:122-126(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF COMPLEX WITH ARHGDIB.
  17. Cited for: VARIANT NEUID ASN-57.
  18. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-29.

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: October 29, 2014
This is version 167 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

External Data

Dasty 3