CDC42_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CDC42_RAT
• UniProt AC: Q8CFN2
• Protein Name: Cell division control protein 42 homolog
• Gene Name: Cdc42
• Organism: Rattus norvegicus (Rat).
• 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. Required for DOCK10-mediated spine formation in Purkinje cells and hippocampal neurons. Facilitates filopodia formation upon DOCK11-activation. 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
64	Phosphorylation	DTAGQEDYDRLRPLS CCCCCCCHHHCCCCC	11.38	-
124	Phosphorylation	IDLRDDPSTIEKLAK EECCCCHHHHHHHHH	49.35	30181290
125	Phosphorylation	DLRDDPSTIEKLAKN ECCCCHHHHHHHHHC	38.25	30181290
128	Acetylation	DDPSTIEKLAKNKQK CCHHHHHHHHHCCCC	50.31	22902405
133	Ubiquitination	IEKLAKNKQKPITPE HHHHHHCCCCCCCHH	60.02	-
135	Acetylation	KLAKNKQKPITPETA HHHHCCCCCCCHHHH	39.74	22902405
135	Ubiquitination	KLAKNKQKPITPETA HHHHCCCCCCCHHHH	39.74	-
144	Acetylation	ITPETAEKLARDLKA CCHHHHHHHHHHHHH	45.01	22902405
144	Ubiquitination	ITPETAEKLARDLKA CCHHHHHHHHHHHHH	45.01	-
150	Acetylation	EKLARDLKAVKYVEC HHHHHHHHHCCEEEC	56.26	22902405
153	Acetylation	ARDLKAVKYVECSAL HHHHHHCCEEECHHH	48.73	22902405
166	Acetylation	ALTQKGLKNVFDEAI HHCHHHHHHHHCHHH	60.79	22902405
188	Methylation	EPKKSRRCVLL---- CCCCCCCEEEC----	2.16	-
188	Geranylgeranylation	EPKKSRRCVLL---- CCCCCCCEEEC----	2.16	-
188	S-palmitoylation	EPKKSRRCVLL---- CCCCCCCEEEC----	2.16	19092927
189	S-palmitoylation	PKKSRRCVLL----- CCCCCCEEEC-----	6.06	19092927

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
64	Y	Phosphorylation	Kinase	SRC	Q9WUD9	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CDC42_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CDC42_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PAK2_RAT	Pak2	physical	7592896

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.