Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Rho guanine nucleotide exchange factor 16  

UniProtKB / Swiss-Prot ID :  ARHGG_HUMAN

Gene Name (Synonyms) : 
ARHGEF16, EPHEXIN4, NBR  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm (Probable). 

Protein Function :  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 MAQRHSDSSLEEKLLGHRFHSELRLDAGGNPASGLPMVRGSPRVRDDAAFQPQVPAPPQPRPPGHEEPWP...
Predicted Secondary Structure CCCCCCCCHHHHHHHHHHHCCCEEECCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
137V -> M (in dbSNP:rs3806164). VAR_059796
370H -> Y (in dbSNP:rs2185639). VAR_059797
681E -> K (in dbSNP:rs56309807). VAR_061796
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
6PhosphoserineAQRHSDSSL
CCCCCCCHH
41.18HPRD
Link
6PhosphoserineAQRHSDSSL
CCCCCCCHH
41.18Phosphositeplus
Link
41PhosphoserineMVRGSPRVR
CCCCCCCCC
10.04HPRD
Link
41PhosphoserineMVRGSPRVR
CCCCCCCCC
10.04PhosphoELM
Link
41PhosphoserineMVRGSPRVR
CCCCCCCCC
10.04Phosphositeplus
Link
41PhosphoserineMVRGSPRVR
CCCCCCCCC
10.04SysPTM
Link
41Phosphoserine.MVRGSPRVR
CCCCCCCCC
10.04UniProtKB
Link
107PhosphoserineARHQSFGAA
HHHHHHHHH
21.37HPRD
Link
107PhosphoserineARHQSFGAA
HHHHHHHHH
21.37PhosphoELM
Link
107PhosphoserineARHQSFGAA
HHHHHHHHH
21.37Phosphositeplus
Link
107PhosphoserineARHQSFGAA
HHHHHHHHH
21.37SysPTM
Link
107Phosphoserine.ARHQSFGAA
HHHHHHHHH
21.37UniProtKB
Link
174PhosphoserineAIQLSPKLQ
CCCCCCCCC
12.01HPRD
Link
174PhosphoserineAIQLSPKLQ
CCCCCCCCC
12.01PhosphoELM
Link
174PhosphoserineAIQLSPKLQ
CCCCCCCCC
12.01Phosphositeplus
Link
174PhosphoserineAIQLSPKLQ
CCCCCCCCC
12.01SysPTM
Link
174Phosphoserine.AIQLSPKLQ
CCCCCCCCC
12.01UniProtKB
Link
185PhosphoserineAEEPSQPHT
CCCCCCCCC
60.67HPRD
Link
191PhosphoserinePHTRSPAKN
CCCCCCCCC
30.30HPRD
Link
191PhosphoserinePHTRSPAKN
CCCCCCCCC
30.30PhosphoELM
Link
191PhosphoserinePHTRSPAKN
CCCCCCCCC
30.30Phosphositeplus
Link
208PhosphoserineGHKGSFKDD
CCCCCCCCC
33.65HPRD
Link
208PhosphoserineGHKGSFKDD
CCCCCCCCC
33.65PhosphoELM
Link
208PhosphoserineGHKGSFKDD
CCCCCCCCC
33.65Phosphositeplus
Link
208PhosphoserineGHKGSFKDD
CCCCCCCCC
33.65SysPTM
Link
208Phosphoserine.GHKGSFKDD
CCCCCCCCC
33.65UniProtKB
Link
216PhosphotyrosineDPQLYQEIQ
CCCCCCCCC
10.00Phosphositeplus
Link
227PhosphoserineGLNTSQESD
CCCCCCCCC
30.77HPRD
Link
227PhosphoserineGLNTSQESD
CCCCCCCCC
30.77PhosphoELM
Link
227PhosphoserineGLNTSQESD
CCCCCCCCC
30.77Phosphositeplus
Link
227PhosphoserineGLNTSQESD
CCCCCCCCC
30.77SysPTM
Link
227Phosphoserine.GLNTSQESD
CCCCCCCCC
30.77UniProtKB
Link
230PhosphoserineTSQESDDDI
CCCCCCCCC
38.41HPRD
Link
230PhosphoserineTSQESDDDI
CCCCCCCCC
38.41PhosphoELM
Link
230PhosphoserineTSQESDDDI
CCCCCCCCC
38.41Phosphositeplus
Link
230PhosphoserineTSQESDDDI
CCCCCCCCC
38.41SysPTM
Link
230Phosphoserine.TSQESDDDI
CCCCCCCCC
38.41UniProtKB
Link
240PhosphoserineDESSSPEGT
CCCCCCCCC
35.93HPRD
Link
240PhosphoserineDESSSPEGT
CCCCCCCCC
35.93PhosphoELM
Link
240PhosphoserineDESSSPEGT
CCCCCCCCC
35.93Phosphositeplus
Link
240PhosphoserineDESSSPEGT
CCCCCCCCC
35.93SysPTM
Link
240Phosphoserine.DESSSPEGT
CCCCCCCCC
35.93UniProtKB
Link
576PhosphoserineGGNRSSSVP
CCCCCCCCC
30.85HPRD
Link
576PhosphoserineGGNRSSSVP
CCCCCCCCC
30.85PhosphoELM
Link
577PhosphoserineGNRSSSVPH
CCCCCCCCC
31.92HPRD
Link
577PhosphoserineGNRSSSVPH
CCCCCCCCC
31.92PhosphoELM
Link
577PhosphoserineGNRSSSVPH
CCCCCCCCC
31.92Phosphositeplus
Link
577PhosphoserineGNRSSSVPH
CCCCCCCCC
31.92SysPTM
Link
577Phosphoserine.GNRSSSVPH
CCCCCCCCC
31.92UniProtKB
Link
578PhosphoserineNRSSSVPHP
CCCCCCCCE
40.70HPRD
Link
578PhosphoserineNRSSSVPHP
CCCCCCCCE
40.70PhosphoELM
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
1433S_HUMANphysical interactionMINT-3974919MINT15778465
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures