Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Ras-related C3 botulinum toxin substrate 1  

UniProtKB / Swiss-Prot ID :  RAC1_HUMAN

Gene Name (Synonyms) : 
RAC1, TC25 MIG5  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell membrane; Lipid-anchor; Cytoplasmic side (By similarity). Melanosome. Cytoplasm (By similarity). Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine (By similarity). Identified by mass spec 

Protein Function :  Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages (By similarity). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. Isoform B has an accelerated GEF-independent GDP/GTP exchange and an impaired GTP hydrolysis, which is restored partially by GTPase-activating proteins. It is able to bind to the GTPase-binding domain of PAK but not full-length PAK in a GTP- dependent manner, suggesting that the insertion does not completely abolish effector interaction. 

Protein Sequence MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPL...
Predicted Secondary Structure CCEEEEEEEECCCCCHHHHHHHHHCCCCCCCCCCCCEEEEEEEEEECCEEEEEEEEECCCCCHHHHHHHH...
Protein Variant
LocationDescription
26N -> D (in dbSNP:rs5830). VAR_014540
28F -> L (in dbSNP:rs5832). VAR_014541
59A -> T (in dbSNP:rs5837). VAR_014542
63D -> G (in dbSNP:rs5831). VAR_014543
93V -> G (in dbSNP:rs5826). VAR_014545
93V -> I (in dbSNP:rs5825). VAR_014544
108T -> I (in dbSNP:rs5838). VAR_014546
130K -> R (in dbSNP:rs5828). VAR_014547
133K -> E (in dbSNP:rs5835). VAR_014548
135T -> I (in dbSNP:rs11540455). VAR_033303
180P -> S (in dbSNP:rs16063). VAR_014549
182V -> E (in dbSNP:rs5836). VAR_014550
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
32N-acetyltyrosineFPGEYIPTV
CCCCCCCCC
20.37Phosphositeplus
Link
32O-AMP-tyrosine; by Haemophilus IbpA.FPGEYIPTV
CCCCCCCCC
20.37UniProtKB
Link
35O-AMP-threonine; by Vibrio VopS.EYIPTVFDN
CCCCCCEEE
25.01UniProtKB
Link
64PhosphotyrosineGQEDYDRLR
CCCHHHHHH
11.38Phosphositeplus
Link
71PhosphoserineLRPLSYPQT
HHHHHHCCC
37.13Phosphositeplus
Link
71Phosphoserine (AKT1)LRPLSYPQT
HHHHHHCCC
37.13HPRD
Link
71Phosphoserine (AKT1)LRPLSYPQT
HHHHHHCCC
37.13HPRD
Link
71Phosphoserine (PKB_group)LRPLSYPQT
HHHHHHCCC
37.13PhosphoELM
Link
71Phosphoserine.LRPLSYPQT
HHHHHHCCC
37.13UniProtKB
Link
96Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NVRAKWYPE
HHHHHHHHH
36.37Phosphositeplus
Link
116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LVGTKLDLR
EEEECCCCC
33.79Phosphositeplus
Link
123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LRDDKDTIE
CCCCCHHHH
62.15Phosphositeplus
Link
133Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LKEKKLTPI
HHHCCCCCC
59.70Phosphositeplus
Link
147Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LAMAKEIGA
HHHHHHHCC
36.46Phosphositeplus
Link
147Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).LAMAKEIGA
HHHHHHHCC
36.46UniProtKB
Link
153Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IGAVKYLEC
HCCEEEEEE
43.51Phosphositeplus
Link
166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QRGLKTVFD
CCCHHHHHH
45.53Phosphositeplus
Link
167PhosphothreonineRGLKTVFDE
CCHHHHHHH
31.29PhosphoELM
Link
167PhosphothreonineRGLKTVFDE
CCHHHHHHH
31.29Phosphositeplus
Link
178S-nitrosocysteineRAVLCPPPV
HHHHCCCCC
3.70dbSNO
Link-
183Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PPPVKKRKR
CCCCCCCCC
53.27Phosphositeplus
Link-
189Cysteine methyl ester.RKRKCLLL
CCCCCCCC
3.62UniProtKB
Link-
189S-geranylgeranyl cysteine.RKRKCLLL
CCCCCCCC
3.62UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
FRK_HUMANphysical interactionMINT-4507979MINT17318185
GDIR1_HUMANphysical interactionMINT-4298452MINT17245428
SET_HUMANphysical interactionMINT-4298480MINT17245428
SET_HUMANphysical interactionMINT-4298508MINT17245428
SET_HUMANphysical interactionMINT-4298550MINT17245428
SET_HUMANdirect interactionMINT-4298434MINT17245428
SET_HUMANphysical interactionMINT-4298402MINT17245428
SET_HUMANphysical interactionMINT-4298417MINT17245428
SET_HUMANcolocalizationMINT-4298526MINT17245428
PAK1_HUMANphysical interactionMINT-4298496MINT17245428
PAK1_HUMANphysical interactionMINT-49675MINT11950930
RHG15_HUMANphysical interactionMINT-19392MINT12650940
Q86WP1_HUMANphysical interactionMINT-19392MINT12650940
RHG15_HUMANphysical interactionMINT-19382MINT12650940
Q86WP1_HUMANphysical interactionMINT-19382MINT12650940
FHOD1_HUMANphysical interactionMINT-51615MINT15642356
NCF2_HUMANphysical interaction
direct interaction
EBI-489636
EBI-489678
intact11090627
11090627
GDIR1_HUMANdirect interaction
physical interaction
EBI-1031753
EBI-1061382
intact11513578
17353931
KPCI_HUMANphysical interaction
physical interaction
physical interaction
EBI-295484
EBI-295524
EBI-295
intact11260256
11260256
11260256
PAR6G_HUMANphysical interaction
physical interaction
EBI-295476
EBI-295519
intact11260256
11260256
PAR6B_HUMANphysical interaction
physical interaction
physical interaction
EBI-295468
EBI-295514
EBI-295
intact11260256
11260256
11260256
PAR6A_HUMANphysical interaction
physical interaction
EBI-295457
EBI-295509
intact11260256
11260256
DOCK1_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical int
EBI-457747
EBI-457738
EBI-448
intact12134158
12134158
12134158
12134158
12134158
12134158
15247908
15247908
DOCK2_HUMANphysical interactionEBI-448768
intact12134158
ELMO1_HUMANphysical interaction
physical interaction
EBI-446898
EBI-446978
intact15247908
15247908
STAT3_HUMANin vivo
yeast 2-hybrid
HPRD:03627HPRD11021801
ACTB_HUMANin vitro
in vivo
HPRD:03627HPRD11027608
ACTS_HUMANin vivoHPRD:03627HPRD11027608
CHIN_HUMANin vitroHPRD:03627HPRD8496137
NOS2A_HUMANin vitro
yeast 2-hybrid
HPRD:03627HPRD11457725
11422783
E2AK2_HUMANin vitroHPRD:03627HPRD7738010
P85A_HUMANin vitroHPRD:03627HPRD12086876
8034624
7629060
KPCA_HUMANin vivoHPRD:03627HPRD11284700
FLNA_HUMANin vivoHPRD:03627HPRD10051605
TBA4A_HUMANin vivoHPRD:03627HPRD8631991
KPCI_HUMANin vivoHPRD:03627HPRD11260256
M3K11_HUMANin vitroHPRD:03627HPRD9427749
OPHN1_HUMANin vitroHPRD:03627HPRD11998687
9582072
WASP_HUMANin vivoHPRD:03627HPRD8643625
CY24A_HUMANin vitroHPRD:03627HPRD10486263
NCF2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:03627HPRD11090627
11896062
9624165
9255350
8036496
7738010
NCK1_HUMANin vivoHPRD:03627HPRD10766742
STAT1_HUMANin vivoHPRD:03627HPRD15494521
PLXB1_HUMANin vitro
in vivo
HPRD:03627HPRD12123608
TIAM1_HUMANin vitro
in vivo
HPRD:03627HPRD11595749
11130063
KTN1_HUMANyeast 2-hybridHPRD:03627HPRD8769096
STAU1_HUMANin vitroHPRD:03627HPRD15121898
CAV1_HUMANin vivoHPRD:03627HPRD15976327
AMPM2_HUMANin vitroHPRD:03627HPRD7738010
TRIO_HUMANin vitro
in vivo
HPRD:03627HPRD11595749
GDIR1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:03627HPRD11513579
10673424
10346909
RAC1_HUMANin vitro
in vivo
HPRD:03627HPRD11134022
9857026
PAR6B_HUMANin vitro
yeast 2-hybrid
HPRD:03627HPRD11260256
RGRF1_HUMANin vitro
in vivo
HPRD:03627HPRD10220378
DVL2_HUMANin vivoHPRD:03627HPRD12533515
M3K4_HUMANin vitroHPRD:03627HPRD9305638
TLR2_HUMANin vivoHPRD:03627HPRD11101877
ARHG7_HUMANin vitroHPRD:03627HPRD14557270
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND MASSSPECTROMETRY.
Prenylation
ReferencePubMed
"Carboxyl-terminal isoprenylation of ras-related GTP-binding proteinsencoded by rac1, rac2, and ralA.";
Kinsella B.T., Erdman R.A., Maltese W.A.;
J. Biol. Chem. 266:9786-9794(1991).
Cited for: ISOPRENYLATION AT CYS-189.
Ubiquitylation
ReferencePubMed
"Activated Rac1, but not the tumorigenic variant Rac1b, isubiquitinated on Lys 147 through a JNK-regulated process.";
Visvikis O., Lores P., Boyer L., Chardin P., Lemichez E., Gacon G.;
FEBS J. 275:386-396(2008).
Cited for: UBIQUITINATION AT LYS-147.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures