CDC42_HUMAN - dbPTM
CDC42_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDC42_HUMAN
UniProt AC P60953
Protein Name Cell division control protein 42 homolog
Gene Name CDC42
Organism Homo sapiens (Human).
Sequence Length 191
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle . Midbody . Localizes to spindle during prometaphase cells. Moves to the central spindle as cells
Protein Description 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. Required for DOCK10-mediated spine formation in Purkinje cells and hippocampal neurons. Facilitates filopodia formation upon DOCK11-activation (By similarity). Also plays a role in phagocytosis through organization of the F-actin cytoskeleton associated with forming phagocytic cups..
Protein Sequence MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPPEPKKSRRCVLL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
5Ubiquitination---MQTIKCVVVGDG
---CCEEEEEEECCC
25.10-
6S-palmitoylation--MQTIKCVVVGDGA
--CCEEEEEEECCCC
2.1929575903
30PhosphorylationYTTNKFPSEYVPTVF
EECCCCCHHHCCCEE
44.70-
32O-AMP-tyrosineTNKFPSEYVPTVFDN
CCCCCHHHCCCEECC
18.96-
32PhosphorylationTNKFPSEYVPTVFDN
CCCCCHHHCCCEECC
18.96-
32O-linked_GlycosylationTNKFPSEYVPTVFDN
CCCCCHHHCCCEECC
18.9624141704
32AMPylationTNKFPSEYVPTVFDN
CCCCCHHHCCCEECC
18.9619362538
35O-AMP-threonineFPSEYVPTVFDNYAV
CCHHHCCCEECCEEE
24.62-
35PhosphorylationFPSEYVPTVFDNYAV
CCHHHCCCEECCEEE
24.62-
35O-linked_GlycosylationFPSEYVPTVFDNYAV
CCHHHCCCEECCEEE
24.627775453
35AMPylationFPSEYVPTVFDNYAV
CCHHHCCCEECCEEE
24.6219039103
64PhosphorylationDTAGQEDYDRLRPLS
CCCCCCCHHHCCCCC
11.3820736484
71PhosphorylationYDRLRPLSYPQTDVF
HHHCCCCCCCCCCEE
37.1318669648
107 (in isoform 1)Ubiquitination-74.3821890473
107 (in isoform 2)Ubiquitination-74.3821890473
107UbiquitinationEITHHCPKTPFLLVG
CHHCCCCCCCEEEEE
74.38-
128AcetylationDDPSTIEKLAKNKQK
CCHHHHHHHHHCCCC
50.3126051181
128 (in isoform 1)Ubiquitination-50.3121890473
128UbiquitinationDDPSTIEKLAKNKQK
CCHHHHHHHHHCCCC
50.31-
128 (in isoform 2)Ubiquitination-50.3121890473
133 (in isoform 1)Ubiquitination-60.0221890473
133 (in isoform 2)Ubiquitination-60.0221890473
133UbiquitinationIEKLAKNKQKPITPE
HHHHHHCCCCCCCHH
60.02-
135AcetylationKLAKNKQKPITPETA
HHHHCCCCCCCHHHH
39.7419608861
135 (in isoform 2)Ubiquitination-39.7421890473
135UbiquitinationKLAKNKQKPITPETA
HHHHCCCCCCCHHHH
39.74-
135 (in isoform 1)Ubiquitination-39.7421890473
138PhosphorylationKNKQKPITPETAEKL
HCCCCCCCHHHHHHH
24.4928060719
141PhosphorylationQKPITPETAEKLARD
CCCCCHHHHHHHHHH
41.1228985074
144 (in isoform 2)Ubiquitination-45.0121890473
144AcetylationITPETAEKLARDLKA
CCHHHHHHHHHHHHH
45.0123749302
144 (in isoform 1)Ubiquitination-45.0121890473
144UbiquitinationITPETAEKLARDLKA
CCHHHHHHHHHHHHH
45.01-
153 (in isoform 2)Ubiquitination-48.7321890473
153AcetylationARDLKAVKYVECSAL
HHHHHHCCEEECHHH
48.7325953088
153UbiquitinationARDLKAVKYVECSAL
HHHHHHCCEEECHHH
48.7322053931
154PhosphorylationRDLKAVKYVECSALT
HHHHHCCEEECHHHC
8.5528152594
157S-palmitoylationKAVKYVECSALTQKG
HHCCEEECHHHCHHH
1.7429575903
161PhosphorylationYVECSALTQKGLKNV
EEECHHHCHHHHHHH
28.1425159151
163AcetylationECSALTQKGLKNVFD
ECHHHCHHHHHHHHC
62.0626051181
163 (in isoform 2)Ubiquitination-62.0621890473
163UbiquitinationECSALTQKGLKNVFD
ECHHHCHHHHHHHHC
62.0621890473
166UbiquitinationALTQKGLKNVFDEAI
HHCHHHHHHHHCHHH
60.7921906983
166 (in isoform 2)Ubiquitination-60.7921890473
182 (in isoform 1)Phosphorylation-55.97-
183UbiquitinationALEPPEPKKSRRCVL
HHCCCCCCCCCCEEE
62.8122053931
183 (in isoform 2)Ubiquitination-62.8121890473
184UbiquitinationLEPPEPKKSRRCVLL
HCCCCCCCCCCEEEC
60.9722053931
184 (in isoform 2)Ubiquitination-60.9721890473
188GeranylgeranylationEPKKSRRCVLL----
CCCCCCCEEEC----
2.1610676816
188MethylationEPKKSRRCVLL----
CCCCCCCEEEC----
2.1610676816
188GeranylgeranylationEPKKSRRCVLL----
CCCCCCCEEEC----
2.1610676816

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
64YPhosphorylationKinaseSRCP12931
Uniprot
64YPhosphorylationKinaseSRCP12931
PSP
64YPhosphorylationKinaseSRC-FAMILY-GPS
64YPhosphorylationKinaseSRC64-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
35TGlycosylation

7777059

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CDC42_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BORG5_HUMANCDC42EP1physical
16189514
FBP1L_HUMANFNBP1Lphysical
15260990
KAT5_HUMANKAT5physical
16169070
ERG28_HUMANC14orf1physical
16169070
PDE6D_HUMANPDE6Dphysical
16169070
UBR1_HUMANUBR1physical
16169070
LRIF1_HUMANLRIF1physical
16169070
P53_HUMANTP53physical
16169070
EF1G_HUMANEEF1Gphysical
16169070
U119A_HUMANUNC119physical
16169070
BNIP2_HUMANBNIP2physical
10799524
ARHG8_MOUSENet1physical
9535835
DIAP3_MOUSEDiap3physical
9535835
ROCK1_MOUSERock1physical
9535835
BORG2_HUMANCDC42EP3physical
9535835
VAV_HUMANVAV1physical
11287617
M3K10_HUMANMAP3K10physical
9427749
RHG01_HUMANARHGAP1physical
9427749
M3K11_HUMANMAP3K11physical
9427749
C42S1_HUMANCDC42SE1physical
10816584
C42S2_HUMANCDC42SE2physical
10816584
CDC42_HUMANCDC42physical
10211824
IQGA2_HUMANIQGAP2physical
8756646
M3K11_HUMANMAP3K11physical
10799501
M3K4_HUMANMAP3K4physical
9079650
BAIP2_HUMANBAIAP2physical
11696321
ERRFI_HUMANERRFI1physical
10749885
PAK6_HUMANPAK6physical
11773441
IQGA1_HUMANIQGAP1physical
8798539
PAR6B_HUMANPARD6Bphysical
10934474
WASP_HUMANWASphysical
10713100
MCF2_HUMANMCF2physical
10854437
DOCK9_HUMANDOCK9physical
12172552
BORG3_HUMANCDC42EP5physical
11035016
BORG1_HUMANCDC42EP2physical
11035016
PKHG2_HUMANPLEKHG2physical
11839748
PAK4_HUMANPAK4physical
9822598
PAK2_HUMANPAK2physical
9822598
RHG01_HUMANARHGAP1physical
10551883
BNIP2_HUMANBNIP2physical
10551883
FGD1_HUMANFGD1physical
8969170
ARHGP_HUMANARHGEF25physical
12547822
WASL_HUMANWASLphysical
9422512
PAK5_HUMANPAK7physical
12032833
PLD1_HUMANPLD1physical
10747870
IQGA1_HUMANIQGAP1physical
8670801
IQGA1_HUMANIQGAP1physical
9182573
PAK1_HUMANPAK1physical
9535855
PAK2_HUMANPAK2physical
9535855
IQGA1_HUMANIQGAP1physical
9535855
GDIR1_HUMANARHGDIAphysical
20936779
ARRB1_HUMANARRB1physical
20936779
ARRB2_HUMANARRB2physical
20936779
CASB_HUMANCSN2physical
20936779
DIAP2_HUMANDIAPH2physical
20936779
COX1_HUMANCOX1physical
20936779
MYO6_HUMANMYO6physical
20936779
MYO9A_HUMANMYO9Aphysical
20936779
PAK1_HUMANPAK1physical
20936779
PAK2_HUMANPAK2physical
20936779
PAK3_HUMANPAK3physical
20936779
GDS1_HUMANRAP1GDS1physical
20936779
RL22_HUMANRPL22physical
20936779
S10A9_HUMANS100A9physical
20936779
F10A1_HUMANST13physical
20936779
UBC_HUMANUBCphysical
20936779
VRK2_HUMANVRK2physical
20936779
WASP_HUMANWASphysical
20936779
ZN175_HUMANZNF175physical
20936779
MRCKA_HUMANCDC42BPAphysical
20936779
GANP_HUMANMCM3APphysical
20936779
HERC2_HUMANHERC2physical
20936779
WASL_HUMANWASLphysical
20936779
RL23_HUMANRPL23physical
20936779
MRCKB_HUMANCDC42BPBphysical
20936779
RHG32_HUMANARHGAP32physical
20936779
ARHGB_HUMANARHGEF11physical
20936779
ACK1_HUMANTNK2physical
20936779
PAK4_HUMANPAK4physical
20936779
BORG1_HUMANCDC42EP2physical
20936779
BAIP2_HUMANBAIAP2physical
20936779
BORG2_HUMANCDC42EP3physical
20936779
BORG5_HUMANCDC42EP1physical
20936779
SYNE1_HUMANSYNE1physical
20936779
BORG4_HUMANCDC42EP4physical
20936779
C42S1_HUMANCDC42SE1physical
20936779
PAK6_HUMANPAK6physical
20936779
PAK5_HUMANPAK7physical
20936779
PAR6B_HUMANPARD6Bphysical
20936779
FMNL2_HUMANFMNL2physical
20936779
SH319_HUMANSH3D19physical
20936779
K2026_HUMANKIAA2026physical
20936779
MUC12_HUMANMUC12physical
20936779
CBL_HUMANCBLphysical
14505571
ARHG7_HUMANARHGEF7physical
14505571
ARHG7_MOUSEArhgef7physical
14505571
PAK3_MOUSEPak3physical
14505571
HAKAI_HUMANCBLL1physical
18057010
CADH1_HUMANCDH1physical
18057010
A2MG_HUMANA2Mphysical
18624398
FETUA_HUMANAHSGphysical
18624398
APOH_HUMANAPOHphysical
18624398
CBPN_HUMANCPN1physical
18624398
ETFA_HUMANETFAphysical
18624398
FHR4_HUMANCFHR4physical
18624398
LEG1_HUMANLGALS1physical
18624398
ZN234_HUMANZNF234physical
18624398
GDIR1_HUMANARHGDIAphysical
21900206
CBL_HUMANCBLphysical
16356860
UBP6_HUMANUSP6physical
12612085
BCAR1_HUMANBCAR1physical
17038317
ACK1_HUMANTNK2physical
10360579
PAK1_HUMANPAK1physical
10360579
WASP_HUMANWASphysical
10360579
ACK1_HUMANTNK2physical
15123659
ACK1_HUMANTNK2physical
10684602
PAK1_HUMANPAK1physical
10684602
WASP_HUMANWASphysical
10684602
RHG01_HUMANARHGAP1physical
10684602
PAK1_HUMANPAK1physical
10802735
LRRK2_HUMANLRRK2physical
21048939
ARHG6_HUMANARHGEF6physical
15306850
FGD3_HUMANFGD3physical
18363964
TGFR1_HUMANTGFBR1physical
15761153
TGFR2_HUMANTGFBR2physical
15761153
RAP1A_HUMANRAP1Aphysical
22939629
PAK3_HUMANPAK3physical
11157984
ZN420_HUMANZNF420physical
11157984
ACK1_HUMANTNK2physical
11157984
BAIP2_HUMANBAIAP2physical
11157984
WIPF1_HUMANWIPF1physical
11331876
WASL_HUMANWASLphysical
11331876
RIOK3_HUMANRIOK3physical
21988832
BORG1_HUMANCDC42EP2physical
21988832
BORG5_HUMANCDC42EP1physical
21988832
ADIP_HUMANSSX2IPphysical
21988832
SYEP_HUMANEPRSphysical
22863883
SYLC_HUMANLARSphysical
22863883
RUVB1_HUMANRUVBL1physical
22863883
ELOB_HUMANTCEB2physical
22863883
BIRC2_HUMANBIRC2physical
24276241
PAK1_HUMANPAK1physical
24276241
TRAF2_HUMANTRAF2physical
24276241
GDIR1_HUMANARHGDIAphysical
24276241
PAR6B_HUMANPARD6Bphysical
23439680
PAK2_HUMANPAK2physical
25416956
BORG1_HUMANCDC42EP2physical
25416956
BORG5_HUMANCDC42EP1physical
25416956
PAR6B_HUMANPARD6Bphysical
25416956
ACK1_HUMANTNK2physical
16052498
AHNK_HUMANAHNAKphysical
26344197
GDIR1_HUMANARHGDIAphysical
26344197
GDIR3_HUMANARHGDIGphysical
26344197
DUT_HUMANDUTphysical
26344197
SYFA_HUMANFARSAphysical
26344197
NOTC2_HUMANNOTCH2physical
26344197
PAK4_HUMANPAK4physical
26344197
RB11B_HUMANRAB11Bphysical
26344197
RAB14_HUMANRAB14physical
26344197
RAB1A_HUMANRAB1Aphysical
26344197
RAB1B_HUMANRAB1Bphysical
26344197
STMN1_HUMANSTMN1physical
26344197
QCR2_HUMANUQCRC2physical
26344197
VAPA_HUMANVAPAphysical
26344197
KTN1_MOUSEKtn1physical
9535835
RHG01_HUMANARHGAP1physical
14749388
FACD2_HUMANFANCD2physical
26496610
KIFC3_HUMANKIFC3physical
26496610
MECP2_HUMANMECP2physical
26496610
MSH3_HUMANMSH3physical
26496610
MYH10_HUMANMYH10physical
26496610
NDUV3_HUMANNDUFV3physical
26496610
PRDX1_HUMANPRDX1physical
26496610
RAD51_HUMANRAD51physical
26496610
STX3_HUMANSTX3physical
26496610
SF01_HUMANSF1physical
26496610
IQGA1_HUMANIQGAP1physical
26496610
EI2BG_HUMANEIF2B3physical
26496610
SC24C_HUMANSEC24Cphysical
26496610
GOGA5_HUMANGOLGA5physical
26496610
ARPC5_HUMANARPC5physical
26496610
CEPT1_HUMANCEPT1physical
26496610
PRDX3_HUMANPRDX3physical
26496610
FKBP9_HUMANFKBP9physical
26496610
SCMH1_HUMANSCMH1physical
26496610
ZC3H4_HUMANZC3H4physical
26496610
PNISR_HUMANPNISRphysical
26496610
GOLI4_HUMANGOLIM4physical
26496610
ACAD9_HUMANACAD9physical
26496610
ASTE1_HUMANASTE1physical
26496610
5NT3A_HUMANNT5C3Aphysical
26496610
M3K20_HUMANZAKphysical
26496610
S38A2_HUMANSLC38A2physical
26496610
DJC10_HUMANDNAJC10physical
26496610
MID51_HUMANMIEF1physical
26496610
E41LB_HUMANEPB41L4Bphysical
26496610
RAIN_HUMANRASIP1physical
26496610
RABL6_HUMANRABL6physical
26496610
BBX_HUMANBBXphysical
26496610
C42S2_HUMANCDC42SE2physical
26496610
KIF17_HUMANKIF17physical
26496610
ZSWM5_HUMANZSWIM5physical
26496610
WNK1_HUMANWNK1physical
26496610
IQGA3_HUMANIQGAP3physical
26496610
M3K11_HUMANMAP3K11physical
25241761
MK09_HUMANMAPK9physical
25241761
MK08_HUMANMAPK8physical
25241761
M3K4_HUMANMAP3K4physical
25241761
ARHG6_HUMANARHGEF6physical
25241761
CASP3_HUMANCASP3physical
25241761

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CDC42_HUMAN

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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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