RHG08_HUMAN - dbPTM
RHG08_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHG08_HUMAN
UniProt AC P85298
Protein Name Rho GTPase-activating protein 8
Gene Name ARHGAP8
Organism Homo sapiens (Human).
Sequence Length 464
Subcellular Localization
Protein Description GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state..
Protein Sequence MAGQDPALSTSHPFYDVARHGILQVAGDDRFGRRVVTFSCCRMPPSHELDHQRLLEYLKYTLDQYVENDYTIVYFHYGLNSRNKPSLGWLQSAYKEFDRKDGDLTMWPRLVSNSKLKRSSHLSLPKYWDYRYKKNLKALYVVHPTSFIKVLWNILKPLISHKFGKKVIYFNYLSELHEHLKYDQLVIPPEVLRYDEKLQSLHEGRTPPPTKTPPPRPPLPTQQFGVSLQYLKDKNQGELIPPVLRFTVTYLREKGLRTEGLFRRSASVQTVREIQRLYNQGKPVNFDDYGDIHIPAVILKTFLRELPQPLLTFQAYEQILGITCVESSLRVTGCRQILRSLPEHNYVVLRYLMGFLHAVSRESIFNKMNSSNLACVFGLNLIWPSQGVSSLSALVPLNMFTELLIEYYEKIFSTPEAPGEHGLAPWEQGSRAAPLQEAVPRTQATGLTKPTLPPSPLMAARRRL
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
2Acetylation------MAGQDPALS
------CCCCCCCCC		25.10-
39PhosphorylationGRRVVTFSCCRMPPS
CCEEEEEECCCCCCC		11.71-
60PhosphorylationRLLEYLKYTLDQYVE
HHHHHHHHHHHHHHH		15.22-
65PhosphorylationLKYTLDQYVENDYTI
HHHHHHHHHHCCEEE		14.92-
70PhosphorylationDQYVENDYTIVYFHY
HHHHHCCEEEEEEEE		15.22-
95 (in isoform 4)Ubiquitination-52.1821890473
95UbiquitinationGWLQSAYKEFDRKDG
HHHHHHHHHHCCCCC		52.1821890473
95 (in isoform 2)Ubiquitination-52.1821890473
95UbiquitinationGWLQSAYKEFDRKDG
HHHHHHHHHHCCCCC		52.1821890473
146PhosphorylationLYVVHPTSFIKVLWN
EEEECCHHHHHHHHH		29.4424719451
166UbiquitinationISHKFGKKVIYFNYL
HHHCCCCEEEEEEHH		33.9521890473
166 (in isoform 2)Ubiquitination-33.9521890473
192 (in isoform 3)Ubiquitination-3.9121906983
197 (in isoform 1)Ubiquitination-49.2621906983
197UbiquitinationEVLRYDEKLQSLHEG
HHHHCHHHHHHHHCC		49.2621906983
200PhosphorylationRYDEKLQSLHEGRTP
HCHHHHHHHHCCCCC		41.9723312004
201 (in isoform 2)Ubiquitination-2.4821890473
201UbiquitinationYDEKLQSLHEGRTPP
CHHHHHHHHCCCCCC		2.4821890473
206PhosphorylationQSLHEGRTPPPTKTP
HHHHCCCCCCCCCCC		51.5128985074
210PhosphorylationEGRTPPPTKTPPPRP
CCCCCCCCCCCCCCC		54.0129449344
212PhosphorylationRTPPPTKTPPPRPPL
CCCCCCCCCCCCCCC		43.4328348404
227 (in isoform 3)Ubiquitination-15.3321906983
232 (in isoform 1)Ubiquitination-62.8221906983
232UbiquitinationGVSLQYLKDKNQGEL
CEEHHHHHCCCCCCC		62.8221906983
251 (in isoform 2)Ubiquitination-4.1021890473
251UbiquitinationLRFTVTYLREKGLRT
HHHHHHHHHHCCCCC		4.10-
258PhosphorylationLREKGLRTEGLFRRS
HHHCCCCCCCHHHCC		39.1722210691
265PhosphorylationTEGLFRRSASVQTVR
CCCHHHCCCCHHHHH		22.1922210691
267PhosphorylationGLFRRSASVQTVREI
CHHHCCCCHHHHHHH		18.9228857561
270PhosphorylationRRSASVQTVREIQRL
HCCCCHHHHHHHHHH		21.2622210691
277 (in isoform 3)Ubiquitination-2.4221906983
278PhosphorylationVREIQRLYNQGKPVN
HHHHHHHHHCCCCCC		13.9729496907
282UbiquitinationQRLYNQGKPVNFDDY
HHHHHCCCCCCCCCC		35.7121906983
282 (in isoform 1)Ubiquitination-35.7121906983
289PhosphorylationKPVNFDDYGDIHIPA
CCCCCCCCCCCCHHH		20.6729496907
442PhosphorylationLQEAVPRTQATGLTK
HHHCCCCCCCCCCCC		19.2423312004
445PhosphorylationAVPRTQATGLTKPTL
CCCCCCCCCCCCCCC		23.9423312004
448PhosphorylationRTQATGLTKPTLPPS
CCCCCCCCCCCCCCC		36.0017192257
451PhosphorylationATGLTKPTLPPSPLM
CCCCCCCCCCCCHHH		54.1523312004
455PhosphorylationTKPTLPPSPLMAARR
CCCCCCCCHHHHHHH		28.8228188228
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
455SPhosphorylationKinaseMAPK8P45983
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHG08_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 RHG08_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SH3G3_HUMANSH3GL3physical
26186194
SH3G2_HUMANSH3GL2physical
26186194
SH3G1_HUMANSH3GL1physical
26186194
5HT3C_HUMANHTR3Cphysical
26186194
SH3G3_HUMANSH3GL3physical
28514442
SH3G2_HUMANSH3GL2physical
28514442
SH3G1_HUMANSH3GL1physical
28514442
5HT3C_HUMANHTR3Cphysical
28514442
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 RHG08_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-448, AND MASSSPECTROMETRY.

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