Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Cell division control protein 42 homolog  

UniProtKB / Swiss-Prot ID :  CDC42_HUMAN

Gene Name (Synonyms) : 
CDC42  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell membrane; Lipid-anchor; Cytoplasmic side (Potential). Cytoplasm, cytoskeleton, centrosome. Cytoplasm, cytoskeleton, spindle. Midbody. Note=Localizes to spindle during prometaphase cells. Moves to the central spindle as cells progressed through anaph 

Protein Function :  Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Regulates the bipolar attachment of spindle microtubules to kinetochores before chromosome congression in metaphase. Plays a role in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. Mediates CDC42-dependent cell migration. 

Protein Sequence MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPL...
Predicted Secondary Structure CCEEEEEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEECCEEEEEEEEECCCCHHHHHHHHH...
Protein Variant -
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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
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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
32O-AMP-tyrosine; by Haemophilus IbpA.FPSEYVPTV
CCCCCCCCE
18.96UniProtKB
Link
35O-AMP-threonine; by Vibrio VopS.EYVPTVFDN
CCCCCEEEE
24.62UniProtKB
Link
64Phosphotyrosine (SRC)GQEDYDRLR
CCHHHHHHH
11.38PhosphoELM
Link
118noneGTQIDLRDD
EECCCCCCC
26.32HPRD
Link
118noneGTQIDLRDD
EECCCCCCC
26.32HPRD
Link
121noneIDLRDDPST
CCCCCCHHH
78.46HPRD
Link
121noneIDLRDDPST
CCCCCCHHH
78.46HPRD
Link
135N6-acetyllysineKNKQKPITP
HHCCCCCCH
39.74HPRD
Link
135N6-acetyllysine.KNKQKPITP
HHCCCCCCH
39.74UniProtKB
Link
144N6-acetyllysineETAEKLARD
HHHHHHHHH
45.01HPRD
Link
144N6-acetyllysine.ETAEKLARD
HHHHHHHHH
45.01UniProtKB
Link
153Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LKAVKYVEC
HCCCEEEEE
48.73Phosphositeplus
Link
163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ALTQKGLKN
ECCCCCHHH
62.06Phosphositeplus
Link
166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QKGLKNVFD
CCCHHHHHH
60.79Phosphositeplus
Link
183Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PPEPKKSRR
CCCCCCCCC
62.81Phosphositeplus
Link
184Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PEPKKSRRC
CCCCCCCCC
60.97Phosphositeplus
Link
188S-farnesyl cysteineKSRRCVLL
CCCCCCCC
2.16HPRD
Link
188S-methylcysteineKSRRCVLL
CCCCCCCC
2.16HPRD
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
WASL_HUMANphysical interactionMINT-72703MINT15834156
P85A_HUMANphysical interactionMINT-15428MINT7629060
P85A_HUMANphysical interactionMINT-19009MINT8034624
P85A_HUMANphysical interactionMINT-15429MINT7629060
WASP_HUMANphysical interactionMINT-13944MINT8625410
WASP_HUMANphysical interactionMINT-25018MINT10360578
WASP_HUMANphysical interactionMINT-13945MINT8625410
IQGA1_HUMANphysical interactionMINT-18639MINT8670801
IQGA1_HUMANphysical interactionMINT-14956MINT8798539
IQGA1_HUMANphysical interactionMINT-18637MINT8670801
IQGA1_HUMANphysical interactionMINT-14954MINT8798539
IQGA1_HUMANphysical interactionMINT-18638MINT8670801
IQGA1_HUMANphysical interactionMINT-14955MINT8798539
PAK1_HUMANphysical interactionMINT-14490MINT7744004
ARHG7_HUMANphysical interactionMINT-3372015MINT16983070
CIP4_HUMANphysical interactionMINT-50937MINT12456510
CIP4_HUMANphysical interactionMINT-15379MINT10713100
RHG01_HUMANphysical interactionDIP:10965EDIP9262406
RHG01_HUMANphysical interactionDIP:11034EDIP9846874
ITSN1_HUMANdirect interaction
physical interaction
EBI-602095
EBI-602112
intact12006984
12006984
MRCKA_HUMANphysical interaction
direct interaction
direct interaction
colocalization
EBI-689161
EBI-692745
EBI-692
intact15194684
9418861
9418861
9418861
RIF1_HUMANphysical interactionEBI-728820
intact16169070
P53_HUMANphysical interactionEBI-728823
intact16169070
EF1G_HUMANphysical interactionEBI-728465
intact16169070
UN119_HUMANphysical interactionEBI-728468
intact16169070
Q6P986_HUMANphysical interactionEBI-736460
intact16169070
ERG28_HUMANphysical interactionEBI-729735
intact16169070
PDE6D_HUMANphysical interactionEBI-729738
intact16169070
UBR1_HUMANphysical interactionEBI-729741
intact16169070
TIP60_HUMANphysical interactionEBI-731524
intact16169070
BORG5_HUMANphysical interactionEBI-754756
intact16189514
RHG01_HUMANdirect interaction
direct interaction
EBI-602776
EBI-1026599
intact9338791
9262406
LCK_HUMANphosphorylationEBI-984865
intact16293614
WASL_HUMANphosphorylation
phosphorylation
EBI-984865
EBI-985019
intact16293614
16293614
PTN2_HUMANphosphorylationEBI-985019
intact16293614
RHG24_HUMANphysical interactionEBI-989043
intact16862148
PAR6A_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical interaction
EBI-81907
EBI-81888
EBI-29546
intact10934474
10934474
11260256
11260256
14676191
14676191
KPCI_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
EBI-295488
EBI-295530
EBI-295
intact11260256
11260256
11260256
14676191
14676191
PAR6G_HUMANphysical interaction
physical interaction
EBI-295480
EBI-295504
intact11260256
11260256
PAR6B_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
EBI-295472
EBI-295499
EBI-295
intact11260256
11260256
11260256
14676191
14676191
IQGA1_HUMANphysical interaction
physical interaction
EBI-457807
EBI-457815
intact12745076
12745076
WASP_HUMANin vitro
in vivo
HPRD:00309HPRD8625410
10724160
15361624
12235133
10068673
12769846
9742969
10360578
MCF2L_HUMANin vitroHPRD:00309HPRD11889037
12006984
14701795
PAR6B_HUMANin vitro
in vivo
HPRD:00309HPRD14676191
11260256
10934474
ARHG6_HUMANin vitroHPRD:00309HPRD15649357
ARHG7_HUMANin vitroHPRD:00309HPRD15649357
P53_HUMANyeast 2-hybridHPRD:00309HPRD16169070
PDE6D_HUMANyeast 2-hybridHPRD:00309HPRD16169070
UN119_HUMANyeast 2-hybridHPRD:00309HPRD16169070
ERG28_HUMANyeast 2-hybridHPRD:00309HPRD16169070
BORG5_HUMANyeast 2-hybridHPRD:00309HPRD16189514
UBR1_HUMANyeast 2-hybridHPRD:00309HPRD16169070
EF1G_HUMANyeast 2-hybridHPRD:00309HPRD16169070
CA103_HUMANyeast 2-hybridHPRD:00309HPRD16169070
BORG2_HUMANin vitro
yeast 2-hybrid
HPRD:00309HPRD10490598
FNBP1_HUMANyeast 2-hybridHPRD:00309HPRD12421766
AKT1_HUMANin vivoHPRD:00309HPRD15824104
MK08_HUMANin vivoHPRD:00309HPRD15824104
MK09_HUMANin vivoHPRD:00309HPRD15824104
RBP1_HUMANENSP00000314458STRING
GMIP_HUMANENSP00000314458STRING
PKHG2_HUMANENSP00000314458STRING
PKHG2_HUMANENSP00000314458STRING
PKHG2_HUMANENSP00000314458STRING
RHG05_HUMANENSP00000314458STRING
PAR6A_HUMANENSP00000314458STRING
PDIA2_HUMANENSP00000314458STRING
CHIO_HUMANENSP00000314458STRING
WASL_HUMANENSP00000314458STRING
KS6B1_HUMANENSP00000314458STRING
CCND1_HUMANENSP00000314458STRING
GDIR2_HUMANENSP00000314458STRING
ECT2_HUMANENSP00000314458STRING
PLEK_HUMANENSP00000314458STRING
GNA13_HUMANENSP00000314458STRING
CEND3_HUMANENSP00000314458STRING
KALRN_HUMANENSP00000314458STRING
BORG5_HUMANENSP00000314458STRING
RAF1_HUMANENSP00000314458STRING
SNX9_HUMANENSP00000314458STRING
ARHG9_HUMANENSP00000314458STRING
FHOD1_HUMANENSP00000314458STRING
PAK6_HUMANENSP00000314458STRING
RGRF1_HUMANENSP00000314458STRING
RICH2_HUMANENSP00000314458STRING
PAK3_HUMANENSP00000314458STRING
ARP3_HUMANENSP00000314458STRING
NGEF_HUMANENSP00000314458STRING
CDGAP_HUMANENSP00000314458STRING
CDGAP_HUMANENSP00000314458STRING
M3K4_HUMANENSP00000314458STRING
S2A4R_HUMANENSP00000314458STRING
FGD4_HUMANENSP00000314458STRING
BNIP2_HUMANENSP00000314458STRING
IQGA1_HUMANENSP00000314458STRING
GDIR1_HUMANENSP00000314458STRING
AKT1_HUMANENSP00000314458STRING
P85A_HUMANENSP00000314458STRING
IQGA2_HUMANENSP00000314458STRING
RASA1_HUMANENSP00000314458STRING
RHG26_HUMANENSP00000314458STRING
FGD2_HUMANENSP00000314458STRING
TIAM2_HUMANENSP00000314458STRING
TIAM2_HUMANENSP00000314458STRING
BORG1_HUMANENSP00000314458STRING
KPCA_HUMANENSP00000314458STRING
TIAM1_HUMANENSP00000314458STRING
TIAM1_HUMANENSP00000314458STRING
KALRN_HUMANENSP00000314458STRING
M4K2_HUMANENSP00000314458STRING
RHG15_HUMANENSP00000314458STRING
RHG15_HUMANENSP00000314458STRING
RHG15_HUMANENSP00000314458STRING
RHG15_HUMANENSP00000314458STRING
RHG15_HUMANENSP00000314458STRING
RHG15_HUMANENSP00000314458STRING
RHG15_HUMANENSP00000314458STRING
RHG15_HUMANENSP00000314458STRING
RHG15_HUMANENSP00000314458STRING
RHG15_HUMANENSP00000314458STRING
RHG15_HUMANENSP00000314458STRING
RHG15_HUMANENSP00000314458STRING
BORG2_HUMANENSP00000314458STRING
FNBP2_HUMANENSP00000314458STRING
BORG3_HUMANENSP00000314458STRING
SRC8_HUMANENSP00000314458STRING
VAV_HUMANENSP00000314458STRING
CEND1_HUMANENSP00000314458STRING
BCR_HUMANENSP00000314458STRING
ABR_HUMANENSP00000314458STRING
M3K11_HUMANENSP00000314458STRING
RHG01_HUMANENSP00000314458STRING
MYO9B_HUMANENSP00000314458STRING
PAK2_HUMANENSP00000314458STRING
RHG24_HUMANENSP00000314458STRING
BAIP2_HUMANENSP00000314458STRING
CIP4_HUMANENSP00000314458STRING
GRLF1_HUMANENSP00000314458STRING
ACK1_HUMANENSP00000314458STRING
RHG10_HUMANENSP00000314458STRING
RHG10_HUMANENSP00000314458STRING
RHG10_HUMANENSP00000314458STRING
RHG10_HUMANENSP00000314458STRING
RHG10_HUMANENSP00000314458STRING
RHG10_HUMANENSP00000314458STRING
PRR5_HUMANENSP00000314458STRING
RHG08_HUMANENSP00000314458STRING
BORG4_HUMANENSP00000314458STRING
STA13_HUMANENSP00000314458STRING
STA13_HUMANENSP00000314458STRING
RHG06_HUMANENSP00000314458STRING
TRIO_HUMANENSP00000314458STRING
ARHG3_HUMANENSP00000314458STRING
FAK1_HUMANENSP00000314458STRING
PLD1_HUMANENSP00000314458STRING
RHG12_HUMANENSP00000314458STRING
SRGP1_HUMANENSP00000314458STRING
RHG09_HUMANENSP00000314458STRING
3BP1_HUMANENSP00000314458STRING
3BP1_HUMANENSP00000314458STRING
PAK4_HUMANENSP00000314458STRING
CLIP1_HUMANENSP00000314458STRING
MK08_HUMANENSP00000314458STRING
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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
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-135 AND LYS-144, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures