CDC42_MOUSE - dbPTM
CDC42_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDC42_MOUSE
UniProt AC P60766
Protein Name Cell division control protein 42 homolog
Gene Name Cdc42
Organism Mus musculus (Mouse).
Sequence Length 191
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side . Midbody . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle . Cytoplasm . Cell projection, lamellipodium membrane
Peripheral membrane protein
Cytopla
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 (By similarity). Required for DOCK10-mediated spine formation in Purkinje cells and hippocampal neurons. [PubMed: 25851601 Facilitates filopodia formation upon DOCK11-activation]
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
5Acetylation---MQTIKCVVVGDG
---CCEEEEEEECCC
25.1022826441
6S-nitrosocysteine--MQTIKCVVVGDGA
--CCEEEEEEECCCC
2.19-
6S-nitrosylation--MQTIKCVVVGDGA
--CCEEEEEEECCCC
2.1920925432
6Glutathionylation--MQTIKCVVVGDGA
--CCEEEEEEECCCC
2.1924333276
17PhosphorylationGDGAVGKTCLLISYT
CCCCCCCEEEEEEEE
11.4922802335
22PhosphorylationGKTCLLISYTTNKFP
CCEEEEEEEECCCCC
19.1822802335
23PhosphorylationKTCLLISYTTNKFPS
CEEEEEEEECCCCCH
15.5822802335
24PhosphorylationTCLLISYTTNKFPSE
EEEEEEEECCCCCHH
19.6622802335
25PhosphorylationCLLISYTTNKFPSEY
EEEEEEECCCCCHHH
28.3322802335
30PhosphorylationYTTNKFPSEYVPTVF
EECCCCCHHHCCCEE
44.7022802335
32PhosphorylationTNKFPSEYVPTVFDN
CCCCCHHHCCCEECC
18.9622802335
35PhosphorylationFPSEYVPTVFDNYAV
CCHHHCCCEECCEEE
24.6222802335
40PhosphorylationVPTVFDNYAVTVMIG
CCCEECCEEEEEEEC
12.3222802335
43PhosphorylationVFDNYAVTVMIGGEP
EECCEEEEEEECCEE
9.0022802335
51PhosphorylationVMIGGEPYTLGLFDT
EEECCEEEEEEEECC
15.4222802335
52PhosphorylationMIGGEPYTLGLFDTA
EECCEEEEEEEECCC
25.6822802335
58PhosphorylationYTLGLFDTAGQEDYD
EEEEEECCCCCCCHH
25.9222802335
64PhosphorylationDTAGQEDYDRLRPLS
CCCCCCCHHHCCCCC
11.3822802335
88PhosphorylationCFSVVSPSSFENVKE
EEEECCHHHHHCHHH
39.9022802335
89PhosphorylationFSVVSPSSFENVKEK
EEECCHHHHHCHHHH
39.7122802335
96UbiquitinationSFENVKEKWVPEITH
HHHCHHHHCCCCHHC
48.0122790023
105S-nitrosocysteineVPEITHHCPKTPFLL
CCCHHCCCCCCCEEE
2.61-
105GlutathionylationVPEITHHCPKTPFLL
CCCHHCCCCCCCEEE
2.6124333276
105S-nitrosylationVPEITHHCPKTPFLL
CCCHHCCCCCCCEEE
2.6120925432
128UbiquitinationDDPSTIEKLAKNKQK
CCHHHHHHHHHCCCC
50.3122790023
133UbiquitinationIEKLAKNKQKPITPE
HHHHHHCCCCCCCHH
60.0222790023
135UbiquitinationKLAKNKQKPITPETA
HHHHCCCCCCCHHHH
39.7427667366
135AcetylationKLAKNKQKPITPETA
HHHHCCCCCCCHHHH
39.7423201123
135MalonylationKLAKNKQKPITPETA
HHHHCCCCCCCHHHH
39.7426320211
141PhosphorylationQKPITPETAEKLARD
CCCCCHHHHHHHHHH
41.1228464351
144UbiquitinationITPETAEKLARDLKA
CCHHHHHHHHHHHHH
45.0122790023
144AcetylationITPETAEKLARDLKA
CCHHHHHHHHHHHHH
45.0123201123
150UbiquitinationEKLARDLKAVKYVEC
HHHHHHHHHCCEEEC
56.2627667366
153UbiquitinationARDLKAVKYVECSAL
HHHHHHCCEEECHHH
48.7322790023
153AcetylationARDLKAVKYVECSAL
HHHHHHCCEEECHHH
48.7322826441
153 (in isoform 1)Ubiquitination-48.7322790023
157S-nitrosylationKAVKYVECSALTQKG
HHCCEEECHHHCHHH
1.7420925432
157S-nitrosocysteineKAVKYVECSALTQKG
HHCCEEECHHHCHHH
1.74-
158PhosphorylationAVKYVECSALTQKGL
HCCEEECHHHCHHHH
16.89-
163SuccinylationECSALTQKGLKNVFD
ECHHHCHHHHHHHHC
62.06-
163AcetylationECSALTQKGLKNVFD
ECHHHCHHHHHHHHC
62.0623806337
163MalonylationECSALTQKGLKNVFD
ECHHHCHHHHHHHHC
62.0626320211
163UbiquitinationECSALTQKGLKNVFD
ECHHHCHHHHHHHHC
62.06-
183UbiquitinationALEPPEPKKSRRCVL
HHCCCCCCCCCCEEE
62.8122790023
184UbiquitinationLEPPEPKKSRRCVLL
HCCCCCCCCCCEEEC
60.9722790023
185 (in isoform 1)Ubiquitination-30.96-
188GeranylgeranylationEPKKSRRCVLL----
CCCCCCCEEEC----
2.16-
188MethylationEPKKSRRCVLL----
CCCCCCCEEEC----
2.16-
188S-palmitoylationEPKKSRRCVLL----
CCCCCCCEEEC----
2.1624059268
189S-palmitoylationPKKSRRCVLL-----
CCCCCCEEEC-----
6.0624059268

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
64YPhosphorylationKinaseSRCP05480
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDC42_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DOC11_MOUSEDock11physical
15710388
LIS1_MOUSEPafah1b1physical
16369480
IQGA1_MOUSEIqgap1physical
16369480
SRGP1_MOUSESrgap1physical
11672528

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CDC42_MOUSE

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Related Literatures of Post-Translational Modification

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