dbPTM

RHG29_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RHG29_MOUSE
UniProt AC	Q8CGF1
Protein Name	Rho GTPase-activating protein 29
Gene Name	Arhgap29
Organism	Mus musculus (Mouse).
Sequence Length	1266
Subcellular Localization
Protein Description	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. May act as a specific effector of RAP2A to regulate Rho (By similarity). In concert with RASIP1, suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis..
Protein Sequence	MIAHKQKKAKKKRVWASGQPSAAITTSEMGLKSVSSSSSFDPEYIKELVNDVRKFSHMLLYLKEAILSDCFKEVIHIRLDELLRVLKSILSKHQNLSSVDLQSAAEVLTAKVKAVNFTEVNEENKNDIFREVFSSIETLAFTFGNILTNFLMGDVGSDSILRLPISRESKSFENISVDSVDLPHEKGNFSPIELDNLLLKNTDSIELALSYAKTWSKYTKNIVSWVEKKLNLELESTRNIVKLAEATRSSIGIQEFMPLQSLFTNALLSDIHSSHLLQQTIAALQANKFVQPLLGRKNEMEKQRKEIKDLWKQQQNKLLETETALKKAKLLCMQRQDEYEKAKSSMFRAEEEQLSSSVGLAKNLNKQLEKRRRLEEEALQKVEEANEHYKVCVTNVEERRNDLENTKREILTQLRTLVFQCDLTLKAVTVNLFHMQQLQAASLANSLQSLCDSAKLYDPGQEYSEFVKATSSSELEEKVDGNVNKQMTNSPQTSGYEPADSLEDVARLPDSCHKLEEDRCSNSADMTGPSFVRSWKFGMFSDSESTGGSSESRSLDSESISPGDFHRKLPRTPSSGTMSSADDLDEREPPSPSEAGPNSLGAFKKTLMSKAALTHKFRKLRSPTKCRDCDGIVMFPGVECEECLLVCHRKCLENLVIICGHQKLQGKMHIFGAEFIQVAKKEPDGIPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSSHDICDVLKLYLRQLPEPFILFRLYKEFIDLAKEIQHVNEEQEAKKDSPEDKKHPHVSIEVNRILLKSKDLLRQLPASHFNSLHYLIAHLRRVVDHAEENKMNSKNLGVIFGPTLIRPRPTTAPVTISSLAEYSNQARLVEFLITYSQKIFDGSLQPQAVVISNTGAVAPQVDQGYLPKPLLSPDERDTDHSMKPLFFSSKEDIRSSDCESKSFELTTSFEESERRQNALGKCDAPLLDNKVHLLFDQEHESASQKMEDVCKSPKLLLLKSNRAANSVQRHTPRTKMRPVSLPVDRLLLLASSPTERSSRDVGNVDSDKFGKNPAFEGLHRKDNSNTTRSKVNGFDQQNVQKSWDTQYVRNNFTAKTTMIVPSAYPEKGLTVNTGNNRDHPGSKAHAEPARAAGDVSERRSSDSCPATAVRAPRTLQPQHWTTFYKPPNPTFSVRGTEEKTALPSIAVPPVLVHAPQIHVTKSDPDSEATLACPVQTSGQPKESSEEPALPEGTPTCQRPRLKRMQQFEDLEDEIPQFV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
33	Phosphorylation	TSEMGLKSVSSSSSF CCHHCCCCCCCCCCC	32.07	23984901
35	Phosphorylation	EMGLKSVSSSSSFDP HHCCCCCCCCCCCCH	31.43	26239621
36	Phosphorylation	MGLKSVSSSSSFDPE HCCCCCCCCCCCCHH	31.89	26239621
37	Phosphorylation	GLKSVSSSSSFDPEY CCCCCCCCCCCCHHH	23.61	23984901
38	Phosphorylation	LKSVSSSSSFDPEYI CCCCCCCCCCCHHHH	36.65	23984901
39	Phosphorylation	KSVSSSSSFDPEYIK CCCCCCCCCCHHHHH	35.30	26239621
44	Phosphorylation	SSSFDPEYIKELVND CCCCCHHHHHHHHHH	23.76	23984901
46	Ubiquitination	SFDPEYIKELVNDVR CCCHHHHHHHHHHHH	44.06	22790023
88	Phosphorylation	ELLRVLKSILSKHQN HHHHHHHHHHHHCCC	25.30	24719451
166	Phosphorylation	SILRLPISRESKSFE CEECCCCCCCCCCCC	28.23	29472430
169	Phosphorylation	RLPISRESKSFENIS CCCCCCCCCCCCCEE	32.27	26239621
171	Phosphorylation	PISRESKSFENISVD CCCCCCCCCCCEECC	47.26	25521595
176	Phosphorylation	SKSFENISVDSVDLP CCCCCCEECCEECCC	31.30	25521595
179	Phosphorylation	FENISVDSVDLPHEK CCCEECCEECCCCCC	18.51	21082442
190	Phosphorylation	PHEKGNFSPIELDNL CCCCCCCCCHHHHHE	29.03	26239621
355	Phosphorylation	RAEEEQLSSSVGLAK HHHHHHHHHHHHHHH	21.91	23984901
356	Phosphorylation	AEEEQLSSSVGLAKN HHHHHHHHHHHHHHH	37.32	23984901
357	Phosphorylation	EEEQLSSSVGLAKNL HHHHHHHHHHHHHHH	19.48	25521595
464	Phosphorylation	YDPGQEYSEFVKATS CCCCHHHHHHHHHCC	24.65	25338131
488	Phosphorylation	GNVNKQMTNSPQTSG CCCCHHHCCCCCCCC	30.01	25293948
490	Phosphorylation	VNKQMTNSPQTSGYE CCHHHCCCCCCCCCC	14.82	25293948
493	Phosphorylation	QMTNSPQTSGYEPAD HHCCCCCCCCCCCCC	27.74	25293948
494	Phosphorylation	MTNSPQTSGYEPADS HCCCCCCCCCCCCCC	33.84	25293948
496	Phosphorylation	NSPQTSGYEPADSLE CCCCCCCCCCCCCHH	20.64	25293948
501	Phosphorylation	SGYEPADSLEDVARL CCCCCCCCHHHHHCC	35.45	28973931
521	Phosphorylation	KLEEDRCSNSADMTG HCCCCCCCCCCCCCC	34.41	27087446
523	Phosphorylation	EEDRCSNSADMTGPS CCCCCCCCCCCCCCH	14.89	27742792
527	Phosphorylation	CSNSADMTGPSFVRS CCCCCCCCCCHHHHH	46.63	29472430
554	Phosphorylation	GGSSESRSLDSESIS CCCCCCCCCCCCCCC	45.89	26239621
557	Phosphorylation	SESRSLDSESISPGD CCCCCCCCCCCCCCC	38.24	26239621
559	Phosphorylation	SRSLDSESISPGDFH CCCCCCCCCCCCCHH	32.11	26239621
561	Phosphorylation	SLDSESISPGDFHRK CCCCCCCCCCCHHHC	31.91	26239621
572	Phosphorylation	FHRKLPRTPSSGTMS HHHCCCCCCCCCCCC	26.11	26643407
574	Phosphorylation	RKLPRTPSSGTMSSA HCCCCCCCCCCCCCC	40.56	25521595
575	Phosphorylation	KLPRTPSSGTMSSAD CCCCCCCCCCCCCCH	39.21	25521595
577	Phosphorylation	PRTPSSGTMSSADDL CCCCCCCCCCCCHHC	18.81	25521595
579	Phosphorylation	TPSSGTMSSADDLDE CCCCCCCCCCHHCCC	23.39	25293948
580	Phosphorylation	PSSGTMSSADDLDER CCCCCCCCCHHCCCC	25.54	25293948
591	Phosphorylation	LDEREPPSPSEAGPN CCCCCCCCCCCCCCC	52.34	25521595
593	Phosphorylation	EREPPSPSEAGPNSL CCCCCCCCCCCCCCH	44.40	25293948
785	Phosphorylation	EQEAKKDSPEDKKHP HHHHHCCCCCHHCCC	38.78	23684622
920	Phosphorylation	YLPKPLLSPDERDTD CCCCCCCCCCCCCCC	37.68	28418008
936	Phosphorylation	SMKPLFFSSKEDIRS CCCCCCCCCHHHHCC	32.92	27742792
937	Phosphorylation	MKPLFFSSKEDIRSS CCCCCCCCHHHHCCC	34.60	26824392
943	Phosphorylation	SSKEDIRSSDCESKS CCHHHHCCCCCCCCC	30.75	23684622
944	Phosphorylation	SKEDIRSSDCESKSF CHHHHCCCCCCCCCE	36.11	23684622
950	Phosphorylation	SSDCESKSFELTTSF CCCCCCCCEEEECCH	32.98	28973931
956	Phosphorylation	KSFELTTSFEESERR CCEEEECCHHHHHHH	25.98	28973931
1000	Phosphorylation	KMEDVCKSPKLLLLK HHHHHHHCHHEEHHC	23.34	26824392
1028	Phosphorylation	RTKMRPVSLPVDRLL CCCCCCCCCCHHHHH	29.64	26239621
1039	Phosphorylation	DRLLLLASSPTERSS HHHHHHHCCCCCCCC	36.50	26239621
1040	Phosphorylation	RLLLLASSPTERSSR HHHHHHCCCCCCCCC	30.18	26824392
1042	Phosphorylation	LLLASSPTERSSRDV HHHHCCCCCCCCCCC	46.08	26239621
1090	Phosphorylation	DQQNVQKSWDTQYVR CHHHCHHHCCHHHHH	17.06	29514104
1095	Phosphorylation	QKSWDTQYVRNNFTA HHHCCHHHHHCCCEE	11.94	29514104
1148	Phosphorylation	GDVSERRSSDSCPAT CCCCHHCCCCCCCCC	44.72	23684622
1149	Phosphorylation	DVSERRSSDSCPATA CCCHHCCCCCCCCCE	31.56	25521595
1151	Phosphorylation	SERRSSDSCPATAVR CHHCCCCCCCCCEEE	24.77	23684622
1210	Phosphorylation	PQIHVTKSDPDSEAT CEEEEECCCCCCCCE	45.04	25293948
1214	Phosphorylation	VTKSDPDSEATLACP EECCCCCCCCEEECE	34.22	25293948
1241	Phosphorylation	EPALPEGTPTCQRPR CCCCCCCCCCCCCHH	17.48	26824392
1243	Phosphorylation	ALPEGTPTCQRPRLK CCCCCCCCCCCHHHH	22.55	26643407

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
1040	S	Phosphorylation	Kinase	MTOR	Q9JLN9	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RHG29_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 RHG29_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of RHG29_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of RHG29_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176 AND SER-179, ANDMASS SPECTROMETRY.	17242355 [Abstract]