ARHGG_HUMAN - dbPTM
ARHGG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARHGG_HUMAN
UniProt AC Q5VV41
Protein Name Rho guanine nucleotide exchange factor 16
Gene Name ARHGEF16
Organism Homo sapiens (Human).
Sequence Length 709
Subcellular Localization Cytoplasm .
Protein Description Guanyl-nucleotide exchange factor of the RHOG GTPase stimulating the exchange of RHOG-associated GDP for GTP. May play a role in chemotactic cell migration by mediating the activation of RAC1 by EPHA2. May also activate CDC42 and mediate activation of CDC42 by the viral protein HPV16 E6..
Protein Sequence MAQRHSDSSLEEKLLGHRFHSELRLDAGGNPASGLPMVRGSPRVRDDAAFQPQVPAPPQPRPPGHEEPWPIVLSTESPAALKLGTQQLIPKSLAVASKAKTPARHQSFGAAVLSREAARRDPKLLPAPSFSLDDMDVDKDPGGMLRRNLRNQSYRAAMKGLGKPGGQGDAIQLSPKLQALAEEPSQPHTRSPAKNKKTLGRKRGHKGSFKDDPQLYQEIQERGLNTSQESDDDILDESSSPEGTQKVDATIVVKSYRPAQVTWSQLPEVVELGILDQLSTEERKRQEAMFEILTSEFSYQHSLSILVEEFLQSKELRATVTQMEHHHLFSNILDVLGASQRFFEDLEQRHKAQVLVEDISDILEEHAEKHFHPYIAYCSNEVYQQRTLQKLISSNAAFREALREIERRPACGGLPMLSFLILPMQRVTRLPLLMDTLCLKTQGHSERYKAASRALKAISKLVRQCNEGAHRMERMEQMYTLHTQLDFSKVKSLPLISASRWLLKRGELFLVEETGLFRKIASRPTCYLFLFNDVLVVTKKKSEESYMVQDYAQMNHIQVEKIEPSELPLPGGGNRSSSVPHPFQVTLLRNSEGRQEQLLLSSDSASDRARWIVALTHSERQWQGLSSKGDLPQVEITKAFFAKQADEVTLQQADVVLVLQQEDGWLYGERLRDGETGWFPEDFARFITSRVAVEGNVRRMERLRVETDV
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------MAQRHSDSS
------CCCCCCCCC		18.3421406692
6Phosphorylation--MAQRHSDSSLEEK
--CCCCCCCCCHHHH		41.1828355574
8PhosphorylationMAQRHSDSSLEEKLL
CCCCCCCCCHHHHHH		39.5823927012
9PhosphorylationAQRHSDSSLEEKLLG
CCCCCCCCHHHHHHC		44.8025159151
21PhosphorylationLLGHRFHSELRLDAG
HHCCCCCCCEEECCC		35.3029496963
33PhosphorylationDAGGNPASGLPMVRG
CCCCCCCCCCCCCCC		41.9627251275
41PhosphorylationGLPMVRGSPRVRDDA
CCCCCCCCCCCCCCC		10.0422617229
74PhosphorylationEPWPIVLSTESPAAL
CCCCEEEECCCCHHH		21.1628348404
75PhosphorylationPWPIVLSTESPAALK
CCCEEEECCCCHHHC		36.0028348404
77PhosphorylationPIVLSTESPAALKLG
CEEEECCCCHHHCCC		21.6729496963
101PhosphorylationAVASKAKTPARHQSF
HHHHCCCCCHHHHHH		27.3429214152
107PhosphorylationKTPARHQSFGAAVLS
CCCHHHHHHHHHHHC		21.3722167270
114PhosphorylationSFGAAVLSREAARRD
HHHHHHHCHHHHHCC		22.8323927012
129PhosphorylationPKLLPAPSFSLDDMD
CCCCCCCCCCCCCCC		29.5826657352
131PhosphorylationLLPAPSFSLDDMDVD
CCCCCCCCCCCCCCC		34.9127251275
139UbiquitinationLDDMDVDKDPGGMLR
CCCCCCCCCCCCHHH		66.72-
153PhosphorylationRRNLRNQSYRAAMKG
HHHHHHHHHHHHHCC		21.8229496963
154PhosphorylationRNLRNQSYRAAMKGL
HHHHHHHHHHHHCCC		8.4330576142
159AcetylationQSYRAAMKGLGKPGG
HHHHHHHCCCCCCCC		46.3826051181
159MethylationQSYRAAMKGLGKPGG
HHHHHHHCCCCCCCC		46.38-
174PhosphorylationQGDAIQLSPKLQALA
CCCHHHCCHHHHHHH		12.0122167270
176UbiquitinationDAIQLSPKLQALAEE
CHHHCCHHHHHHHCC		50.27-
185PhosphorylationQALAEEPSQPHTRSP
HHHHCCCCCCCCCCC		60.6725159151
189PhosphorylationEEPSQPHTRSPAKNK
CCCCCCCCCCCCCCC		39.2523927012
191PhosphorylationPSQPHTRSPAKNKKT
CCCCCCCCCCCCCCC		30.3025159151
208PhosphorylationRKRGHKGSFKDDPQL
CCCCCCCCCCCCHHH		33.6525463755
210UbiquitinationRGHKGSFKDDPQLYQ
CCCCCCCCCCHHHHH		64.02-
216PhosphorylationFKDDPQLYQEIQERG
CCCCHHHHHHHHHCC		10.0025159151
226PhosphorylationIQERGLNTSQESDDD
HHHCCCCCCCCCCCC		36.5130278072
227PhosphorylationQERGLNTSQESDDDI
HHCCCCCCCCCCCCC		30.7730278072
230PhosphorylationGLNTSQESDDDILDE
CCCCCCCCCCCCCCC		38.4125159151
238PhosphorylationDDDILDESSSPEGTQ
CCCCCCCCCCCCCCC		35.4625159151
239PhosphorylationDDILDESSSPEGTQK
CCCCCCCCCCCCCCE		48.1125159151
240PhosphorylationDILDESSSPEGTQKV
CCCCCCCCCCCCCEE		35.9323927012
244PhosphorylationESSSPEGTQKVDATI
CCCCCCCCCEEEEEE		24.4523663014
280PhosphorylationGILDQLSTEERKRQE
CHHHHCCHHHHHHHH		50.9221815630
360PhosphorylationQVLVEDISDILEEHA
HHHHHCHHHHHHHHH		30.8125348772
394PhosphorylationTLQKLISSNAAFREA
HHHHHHHCCHHHHHH		24.40-
418PhosphorylationCGGLPMLSFLILPMQ
CCCCCHHHHHHHCHH		16.26-
492PhosphorylationLDFSKVKSLPLISAS
CCHHHCCCCCCCCHH		37.9029853039
497PhosphorylationVKSLPLISASRWLLK
CCCCCCCCHHHHHHH		28.0726434776
499PhosphorylationSLPLISASRWLLKRG
CCCCCCHHHHHHHCC		19.7326434776
565PhosphorylationQVEKIEPSELPLPGG
EEEECCHHCCCCCCC		38.6923312004
576PhosphorylationLPGGGNRSSSVPHPF
CCCCCCCCCCCCCCE		30.8522167270
577PhosphorylationPGGGNRSSSVPHPFQ
CCCCCCCCCCCCCEE		31.9225463755
578PhosphorylationGGGNRSSSVPHPFQV
CCCCCCCCCCCCEEE		40.7025463755
586PhosphorylationVPHPFQVTLLRNSEG
CCCCEEEEEEECCCC		14.8623927012
606PhosphorylationLLSSDSASDRARWIV
EEECCCHHHHHHHHH		31.4219690332
618PhosphorylationWIVALTHSERQWQGL
HHHEEECCHHHHCCC		29.2824114839
628UbiquitinationQWQGLSSKGDLPQVE
HHCCCCCCCCCCCCH		53.74-
638UbiquitinationLPQVEITKAFFAKQA
CCCCHHHHHHHHHCC		49.19-
688PhosphorylationEDFARFITSRVAVEG
HHHHHHHHHHHHHCC		14.0421601212
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 ARHGG_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARHGG_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 ARHGG_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MISSL_HUMANMAPK1IP1Lphysical
25416956
ELMO1_HUMANELMO1physical
26882976
AT1A2_HUMANATP1A2physical
28514442
DPP8_HUMANDPP8physical
28514442
UBAC1_HUMANUBAC1physical
28514442
KPCI_HUMANPRKCIphysical
28514442
IF122_HUMANIFT122physical
28514442
PML_HUMANPMLphysical
28514442
HSP7C_HUMANHSPA8physical
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 ARHGG_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 SER-41; SER-107; SER-174;SER-208; SER-227; SER-230; SER-240 AND SER-577, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND MASSSPECTROMETRY.

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