dbPTM

RND3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RND3_HUMAN
UniProt AC	P61587
Protein Name	Rho-related GTP-binding protein RhoE
Gene Name	RND3
Organism	Homo sapiens (Human).
Sequence Length	244
Subcellular Localization	Golgi apparatus membrane Peripheral membrane protein.
Protein Description	Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins..
Protein Sequence	MKERRASQKLSSKSIMDPNQNVKCKIVVVGDSQCGKTALLHVFAKDCFPENYVPTVFENYTASFEIDTQRIELSLWDTSGSPYYDNVRPLSYPDSDAVLICFDISRPETLDSVLKKWKGEIQEFCPNTKMLLVGCKSDLRTDVSTLVELSNHRQTPVSYDQGANMAKQIGAATYIECSALQSENSVRDIFHVATLACVNKTNKNVKRNKSQRATKRISHMPSRPELSAVATDLRKDKAKSCTVM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MKERRASQKLSSKS -CCHHHHHHHCCCCC	26.49	22817900
9	Ubiquitination	KERRASQKLSSKSIM CHHHHHHHCCCCCCC	48.09	-
11	Phosphorylation	RRASQKLSSKSIMDP HHHHHHCCCCCCCCC	42.63	22817900
12	Phosphorylation	RASQKLSSKSIMDPN HHHHHCCCCCCCCCC	40.64	21712546
13	Ubiquitination	ASQKLSSKSIMDPNQ HHHHCCCCCCCCCCC	40.40	-
14	Phosphorylation	SQKLSSKSIMDPNQN HHHCCCCCCCCCCCC	25.70	29255136
144	Phosphorylation	SDLRTDVSTLVELSN HHCCCCHHHHHHHCC	20.87	28555341
145	Phosphorylation	DLRTDVSTLVELSNH HCCCCHHHHHHHCCC	34.37	28555341
167	Ubiquitination	DQGANMAKQIGAATY HHHHHHHHHHCCCEE	31.51	-
173	Phosphorylation	AKQIGAATYIECSAL HHHHCCCEEEEHHHH	25.21	22210691
174	Phosphorylation	KQIGAATYIECSALQ HHHCCCEEEEHHHHC	7.04	22210691
178	Phosphorylation	AATYIECSALQSENS CCEEEEHHHHCCCCC	21.15	22210691
210	Phosphorylation	KNVKRNKSQRATKRI CCHHCCHHHHHHHHH	28.57	-
218	Phosphorylation	QRATKRISHMPSRPE HHHHHHHHCCCCCHH	20.12	29255136
222	Phosphorylation	KRISHMPSRPELSAV HHHHCCCCCHHHHHH	53.55	29255136
227	Phosphorylation	MPSRPELSAVATDLR CCCCHHHHHHHHHHH	21.02	29214152
231	Phosphorylation	PELSAVATDLRKDKA HHHHHHHHHHHHHHH	29.03	-
240	Phosphorylation	LRKDKAKSCTVM--- HHHHHHHCCCCC---	21.63	-
241	Methylation	RKDKAKSCTVM---- HHHHHHCCCCC----	3.07	-
241	Farnesylation	RKDKAKSCTVM---- HHHHHHCCCCC----	3.07	8649376
241	Farnesylation	RKDKAKSCTVM---- HHHHHHCCCCC----	3.07	8649376

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
7	S	Phosphorylation	Kinase	ROCK1	Q13464	PSP
11	S	Phosphorylation	Kinase	ROCK1	Q13464	PSP
210	S	Phosphorylation	Kinase	PRKCZ	Q05513	GPS
218	S	Phosphorylation	Kinase	ROCK1	Q13464	PSP
240	S	Phosphorylation	Kinase	ROCK1	Q13464	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	SKP2	Q13309	PMID:24045951

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RND3_HUMAN !!

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 RND3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RHG05_HUMAN	ARHGAP5	physical	12842009
ROCK1_HUMAN	ROCK1	physical	12773565
CTRO_HUMAN	CIT	physical	12773565
UBX11_HUMAN	UBXN11	physical	11940653
PKHG5_HUMAN	PLEKHG5	physical	22807448
PLXB1_HUMAN	PLXNB1	physical	22807448
RGS14_HUMAN	RGS14	physical	22807448
RHG35_HUMAN	ARHGAP35	physical	22807448
SKP2_HUMAN	SKP2	physical	24045951
NOTC1_HUMAN	NOTCH1	physical	26108681
SUH_HUMAN	RBPJ	physical	26108681
MAML1_HUMAN	MAML1	physical	26108681

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 RND3_HUMAN

Related Literatures of Post-Translational Modification

Prenylation
Reference	PubMed
"Identification of a novel human Rho protein with unusual properties:GTPase deficiency and in vivo farnesylation."; Foster R., Hu K.-Q., Lu Y., Nolan K.M., Thissen J., Settleman J.; Mol. Cell. Biol. 16:2689-2699(1996). Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-244, CHARACTERIZATION, ANDISOPRENYLATION AT CYS-241.	8649376 [Abstract]