RHG42_HUMAN - dbPTM
RHG42_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHG42_HUMAN
UniProt AC A6NI28
Protein Name Rho GTPase-activating protein 42
Gene Name ARHGAP42
Organism Homo sapiens (Human).
Sequence Length 874
Subcellular Localization
Protein Description May influence blood pressure by functioning as a GTPase-activating protein for RHOA in vascular smooth muscle..
Protein Sequence MGLPTLEFSDSYLDSPDFRERLQCHEIELERTNKFIKELIKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAETDDEISIAQSLKEFARLLIAVEEERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILEKHLNLSAKKKESHLQEADTQIDREHQNFYEASLEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPYKQQLQFNLQNTRNNFESTRQEVERLMQRMKSANQDYRPPSQWTMEGYLYVQEKRPLGFTWIKHYCTYDKGSKTFTMSVSEMKSSGKMNGLVTSSPEMFKLKSCIRRKTDSIDKRFCFDIEVVERHGIITLQAFSEANRKLWLEAMDGKEPIYTLPAIISKKEEMYLNEAGFNFVRKCIQAVETRGITILGLYRIGGVNSKVQKLMNTTFSPKSPPDIDIDIELWDNKTITSGLKNYLRCLAEPLMTYKLHKDFIIAVKSDDQNYRVEAVHALVHKLPEKNREMLDILIKHLVKVSLHSQQNLMTVSNLGVIFGPTLMRAQEETVAAMMNIKFQNIVVEILIEHYEKIFHTAPDPSIPLPQPQSRSGSRRTRAICLSTGSRKPRGRYTPCLAEPDSDSYSSSPDSTPMGSIESLSSHSSEQNSTTKSASCQPREKSGGIPWIATPSSSNGQKSLGLWTTSPESSSREDATKTDAESDCQSVASVTSPGDVSPPIDLVKKEPYGLSGLKRASASSLRSISAAEGNKSYSGSIQSLTSVGSKETPKASPNPDLPPKMCRRLRLDTASSNGYQRPGSVVAAKAQLFENVGSPKPVSSGRQAKAMYSCKAEHSHELSFPQGAIFSNVYPSVEPGWLKATYEGKTGLVPENYVVFL
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
32PhosphorylationHEIELERTNKFIKEL
CCCCHHHHHHHHHHH		33.13-
128AcetylationKEQIGAAKDGKKKFD
HHHHCCCCCCCCCCC		67.497469409
131AcetylationIGAAKDGKKKFDKES
HCCCCCCCCCCCHHH		64.027226489
138PhosphorylationKKKFDKESEKYYSIL
CCCCCHHHHHHHHHH		45.1629507054
142PhosphorylationDKESEKYYSILEKHL
CHHHHHHHHHHHHHH		10.58-
143PhosphorylationKESEKYYSILEKHLN
HHHHHHHHHHHHHHC		20.0124719451
154UbiquitinationKHLNLSAKKKESHLQ
HHHCCCHHHHHHHHH		62.0929967540
316PhosphorylationGKMNGLVTSSPEMFK
CCCCCCCCCCHHHHH		28.6424114839
332PhosphorylationKSCIRRKTDSIDKRF
HHHHHCCCCCCCCCC		32.92-
376PhosphorylationMDGKEPIYTLPAIIS
HCCCCCEEEHHHHHC		16.9729255136
377PhosphorylationDGKEPIYTLPAIISK
CCCCCEEEHHHHHCC		27.3029255136
424UbiquitinationRIGGVNSKVQKLMNT
EECCCCHHHHHHHCC		43.4029967540
434PhosphorylationKLMNTTFSPKSPPDI
HHHCCCCCCCCCCCC		29.3524719451
579PhosphorylationFHTAPDPSIPLPQPQ
HCCCCCCCCCCCCCC		44.1927251275
587PhosphorylationIPLPQPQSRSGSRRT
CCCCCCCCCCCCCCC		34.7926657352
600PhosphorylationRTRAICLSTGSRKPR
CCEEEEEECCCCCCC		26.7228857561
601PhosphorylationTRAICLSTGSRKPRG
CEEEEEECCCCCCCC		26.6521712546
603PhosphorylationAICLSTGSRKPRGRY
EEEEECCCCCCCCCC		36.9021712546
621PhosphorylationLAEPDSDSYSSSPDS
CCCCCCCCCCCCCCC		30.7622468782
628PhosphorylationSYSSSPDSTPMGSIE
CCCCCCCCCCCCCHH		37.4822468782
638PhosphorylationMGSIESLSSHSSEQN
CCCHHHHHCCCCCCC		34.97-
641PhosphorylationIESLSSHSSEQNSTT
HHHHHCCCCCCCCCC		37.20-
681PhosphorylationQKSLGLWTTSPESSS
CEEEEEEECCCCCCC		23.5727732954
682PhosphorylationKSLGLWTTSPESSSR
EEEEEEECCCCCCCC		30.6027732954
683PhosphorylationSLGLWTTSPESSSRE
EEEEEECCCCCCCCC		21.2121815630
686PhosphorylationLWTTSPESSSREDAT
EEECCCCCCCCCCCC		36.6827732954
687PhosphorylationWTTSPESSSREDATK
EECCCCCCCCCCCCC		31.5827732954
714PhosphorylationVTSPGDVSPPIDLVK
CCCCCCCCCCCCCCC		29.6929888752
728PhosphorylationKKEPYGLSGLKRASA
CCCCCCCCHHCCCCH		37.4028555341
731MethylationPYGLSGLKRASASSL
CCCCCHHCCCCHHHH		49.82-
734PhosphorylationLSGLKRASASSLRSI
CCHHCCCCHHHHHCC		32.4922798277
736PhosphorylationGLKRASASSLRSISA
HHCCCCHHHHHCCHH		27.6628102081
737PhosphorylationLKRASASSLRSISAA
HCCCCHHHHHCCHHH		27.7628102081
740PhosphorylationASASSLRSISAAEGN
CCHHHHHCCHHHCCC		26.6222210691
742PhosphorylationASSLRSISAAEGNKS
HHHHHCCHHHCCCCC		23.7522210691
749PhosphorylationSAAEGNKSYSGSIQS
HHHCCCCCCCCCCEE		28.6522199227
750PhosphorylationAAEGNKSYSGSIQSL
HHCCCCCCCCCCEEC		20.7522199227
751PhosphorylationAEGNKSYSGSIQSLT
HCCCCCCCCCCEECE		32.9122199227
753PhosphorylationGNKSYSGSIQSLTSV
CCCCCCCCCEECEEC		16.1222199227
756PhosphorylationSYSGSIQSLTSVGSK
CCCCCCEECEECCCC		31.7622199227
758PhosphorylationSGSIQSLTSVGSKET
CCCCEECEECCCCCC		26.9822199227
759PhosphorylationGSIQSLTSVGSKETP
CCCEECEECCCCCCC		29.7627251275
769PhosphorylationSKETPKASPNPDLPP
CCCCCCCCCCCCCCH		31.1928674419
786PhosphorylationCRRLRLDTASSNGYQ
HHHHCCCCCCCCCCC		32.7928152594
788PhosphorylationRLRLDTASSNGYQRP
HHCCCCCCCCCCCCC		26.8228152594
789PhosphorylationLRLDTASSNGYQRPG
HCCCCCCCCCCCCCC		31.6328152594
792PhosphorylationDTASSNGYQRPGSVV
CCCCCCCCCCCCCHH		12.9527273156
797PhosphorylationNGYQRPGSVVAAKAQ
CCCCCCCCHHHHHHH		18.9928152594
811PhosphorylationQLFENVGSPKPVSSG
HHHHHCCCCCCCCCC		26.0129496963
858PhosphorylationEPGWLKATYEGKTGL
CCCEEEEEEECCCCC		22.1018669648
870PhosphorylationTGLVPENYVVFL---
CCCCCCCEEEEC---		9.0618669648
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

Oops, there are no upstream regulatory protein records of RHG42_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHG42_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 RHG42_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RHG42_HUMAN !!
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 RHG42_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-858; SER-811 ANDTYR-870, AND MASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-376, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-376, AND MASSSPECTROMETRY.

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