ARHGI_HUMAN - dbPTM
ARHGI_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARHGI_HUMAN
UniProt AC Q6ZSZ5
Protein Name Rho guanine nucleotide exchange factor 18
Gene Name ARHGEF18
Organism Homo sapiens (Human).
Sequence Length 1173
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton . Apical cell membrane .
Protein Description Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPases. Its activation induces formation of actin stress fibers. Also act as a GEF for RAC1, inducing production of reactive oxygen species (ROS). Does not act as a GEF for CDC42. The G protein beta-gamma (Gbetagamma) subunits of heterotrimeric G proteins act as activators, explaining the integrated effects of LPA and other G-protein coupled receptor agonists on actin stress fiber formation, cell shape change and ROS production. Required for EPB41L4B-mediated regulation of the circumferential actomyosin belt in epithelial cells. [PubMed: 22006950]
Protein Sequence MVTVGTNILPSRPAASANTAREDAALFSRRIPPRHKNGAAQPGAAPGPGAPGANMGNAHSKSGDRHSALPGRPELSFYGSFPRKWSENVFLDNELLTSKILSVLRPQSERGFRAGDLRYPTHFLSTNSVLASVTASLKEHPRGTLLSDGSPALSRNVGMTVSQKGGPQPTPSPAGPGTQLGPITGEMDEADSAFLKFKQTADDSLSLTSPNTESIFVEDPYTASLRSEIESDGHEFEAESWSLAVDAAYAKKQKREVVKRQDVLYELMQTEVHHVRTLKIMLKVYSRALQEELQFSSKAIGRLFPCADDLLETHSHFLARLKERRQESLEEGSDRNYVIQKIGDLLVQQFSGENGERMKEKYGVFCSGHNEAVSHYKLLLQQNKKFQNLIKKIGNFSIVRRLGVQECILLVTQRITKYPVLVERIIQNTEAGTEDYEDLTQALNLIKDIISQVDAKVSECEKGQRLREIAGKMDLKSSSKLKNGLTFRKEDMLQRQLHLEGMLCWKTTSGRLKDILAILLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAMFLISASLQGPEMYEIYTSSKEDRNAWMAHIQRAVESCPDEEEGPFSLPEEERKVVEARATRLRDFQERLSMKDQLIAQSLLEKQQIYLEMAEMGGLEDLPQPRGLFRGGDPSETLQGELILKSAMSEIEGIQSLICRQLGSANGQAEDGGSSTGPPRRAETFAGYDCTNSPTKNGSFKKKVSSTDPRPRDWRGPPNSPDLKLSDSDIPGSSEESPQVVEAPGTESDPRLPTVLESELVQRIQTLSQLLLNLQAVIAHQDSYVETQRAAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAALEKLQSQLRHEQQRWERERQWQHQELERAGARLQEREGEARQLRERLEQERAELERQRQAYQHDLERLREAQRAVERERERLELLRRLKKQNTAPGALPPDTLAEAQPPSHPPSFNGEGLEGPRVSMLPSGVGPEYAERPEVARRDSAPTENRLAKSDVPIQLLSATNQFQRQAAVQQQIPTKLAASTKGGKDKGGKSRGSQRWESSASFDLKQQLLLNKLMGKDESTSRNRRSLSPILPGRHSPAPPPDPGFPAPSPPPADSPSEGFSLKAGGTALLPGPPAPSPLPATPLSAKEDASKEDVIFF
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
3Phosphorylation-----MVTVGTNILP
-----CCEECCCCCC
25.6929255136
6Phosphorylation--MVTVGTNILPSRP
--CCEECCCCCCCCC
18.1029255136
11PhosphorylationVGTNILPSRPAASAN
ECCCCCCCCCCCCCC
47.6629255136
16PhosphorylationLPSRPAASANTARED
CCCCCCCCCCCHHHH
24.9424043423
19PhosphorylationRPAASANTAREDAAL
CCCCCCCCHHHHHHH
27.1524043423
28PhosphorylationREDAALFSRRIPPRH
HHHHHHHHCCCCCCC
22.8424043423
71PhosphorylationDRHSALPGRPELSFY
CCCCCCCCCCCCEEE
59.6428450419
75PhosphorylationALPGRPELSFYGSFP
CCCCCCCCEEEECCC
4.8026714015
83PhosphorylationSFYGSFPRKWSENVF
EEEECCCCCCCCCCC
51.5728450419
85PhosphorylationYGSFPRKWSENVFLD
EECCCCCCCCCCCCC
16.5028450419
87PhosphorylationSFPRKWSENVFLDNE
CCCCCCCCCCCCCCH
57.1928450419
89PhosphorylationPRKWSENVFLDNELL
CCCCCCCCCCCCHHH
4.4127251275
98PhosphorylationLDNELLTSKILSVLR
CCCHHHHHHHHHHHC
20.0530576142
102PhosphorylationLLTSKILSVLRPQSE
HHHHHHHHHHCCCCC
23.6824719451
124PhosphorylationLRYPTHFLSTNSVLA
CCCCCHHCCCCHHHH
4.8526552605
126PhosphorylationYPTHFLSTNSVLASV
CCCHHCCCCHHHHHH
33.3926552605
131PhosphorylationLSTNSVLASVTASLK
CCCCHHHHHHHHHHH
10.3728450419
135PhosphorylationSVLASVTASLKEHPR
HHHHHHHHHHHCCCC
15.6528450419
139PhosphorylationSVTASLKEHPRGTLL
HHHHHHHCCCCCCCC
65.5028450419
144PhosphorylationLKEHPRGTLLSDGSP
HHCCCCCCCCCCCCC
26.3030301811
146PhosphorylationEHPRGTLLSDGSPAL
CCCCCCCCCCCCCCH
4.3828450419
147PhosphorylationHPRGTLLSDGSPALS
CCCCCCCCCCCCCHH
42.9328450419
150PhosphorylationGTLLSDGSPALSRNV
CCCCCCCCCCHHCCC
16.4023401153
153PhosphorylationLSDGSPALSRNVGMT
CCCCCCCHHCCCCCE
5.8426657352
154PhosphorylationSDGSPALSRNVGMTV
CCCCCCHHCCCCCEE
24.7429978859
155PhosphorylationDGSPALSRNVGMTVS
CCCCCHHCCCCCEEC
42.5822115753
159PhosphorylationALSRNVGMTVSQKGG
CHHCCCCCEECCCCC
2.6627251275
162PhosphorylationRNVGMTVSQKGGPQP
CCCCCEECCCCCCCC
19.6024247654
204PhosphorylationFKQTADDSLSLTSPN
HHHCCCCCCCCCCCC
22.0221712546
208PhosphorylationADDSLSLTSPNTESI
CCCCCCCCCCCCCCE
38.4718669648
209PhosphorylationDDSLSLTSPNTESIF
CCCCCCCCCCCCCEE
22.8018669648
212PhosphorylationLSLTSPNTESIFVED
CCCCCCCCCCEEEEC
34.2018669648
263PhosphorylationEVVKRQDVLYELMQT
HHHHHHHHHHHHHHH
4.6724719451
265PhosphorylationVKRQDVLYELMQTEV
HHHHHHHHHHHHHCC
13.5824043423
270PhosphorylationVLYELMQTEVHHVRT
HHHHHHHHCCHHHHH
26.4724043423
328PhosphorylationLKERRQESLEEGSDR
HHHHHHHHHHCCCCH
32.5122985185
333PhosphorylationQESLEEGSDRNYVIQ
HHHHHCCCCHHHHHH
36.3626471730
359AcetylationGENGERMKEKYGVFC
CCCCCHHHHHHCEEC
58.2219824939
361AcetylationNGERMKEKYGVFCSG
CCCHHHHHHCEECCC
41.6119824947
376PhosphorylationHNEAVSHYKLLLQQN
CHHHHHHHHHHHHHH
8.88-
377AcetylationNEAVSHYKLLLQQNK
HHHHHHHHHHHHHHH
27.5119824955
412PhosphorylationQECILLVTQRITKYP
HHHHHHHHHHHHCCH
16.4624719451
416PhosphorylationLLVTQRITKYPVLVE
HHHHHHHHCCHHHHH
27.0724719451
418PhosphorylationVTQRITKYPVLVERI
HHHHHHCCHHHHHHH
7.0224719451
477PhosphorylationAGKMDLKSSSKLKNG
HCCCCCCCCHHHCCC
47.3322210691
478PhosphorylationGKMDLKSSSKLKNGL
CCCCCCCCHHHCCCC
29.8822210691
479PhosphorylationKMDLKSSSKLKNGLT
CCCCCCCHHHCCCCC
49.4522210691
533AcetylationLLQEKDQKYVFASVD
HHHHCCCCEEEEECC
54.227367749
534PhosphorylationLQEKDQKYVFASVDS
HHHCCCCEEEEECCC
8.6528348404
538PhosphorylationDQKYVFASVDSKPPV
CCCEEEEECCCCCCE
18.2628348404
541PhosphorylationYVFASVDSKPPVISL
EEEEECCCCCCEEEE
44.9327251275
542AcetylationVFASVDSKPPVISLQ
EEEECCCCCCEEEEE
49.217367759
547PhosphorylationDSKPPVISLQKLIVR
CCCCCEEEEEHHHHH
25.6124719451
550AcetylationPPVISLQKLIVREVA
CCEEEEEHHHHHHHC
45.537367769
583AcetylationYEIYTSSKEDRNAWM
EEEECCCHHHHHHHH
64.5030587007
635UbiquitinationFQERLSMKDQLIAQS
HHHHHCHHHHHHHHH
38.66-
642PhosphorylationKDQLIAQSLLEKQQI
HHHHHHHHHHHHHHH
26.3724719451
704PhosphorylationLICRQLGSANGQAED
HHHHHHCCCCCCCCC
27.4428122231
714PhosphorylationGQAEDGGSSTGPPRR
CCCCCCCCCCCCCCC
30.2028122231
715PhosphorylationQAEDGGSSTGPPRRA
CCCCCCCCCCCCCCC
40.4328122231
724PhosphorylationGPPRRAETFAGYDCT
CCCCCCEECCCCCCC
20.1427273156
728PhosphorylationRAETFAGYDCTNSPT
CCEECCCCCCCCCCC
12.3830266825
731PhosphorylationTFAGYDCTNSPTKNG
ECCCCCCCCCCCCCC
35.5130266825
733PhosphorylationAGYDCTNSPTKNGSF
CCCCCCCCCCCCCCC
18.7819664994
735PhosphorylationYDCTNSPTKNGSFKK
CCCCCCCCCCCCCCC
36.6423401153
739PhosphorylationNSPTKNGSFKKKVSS
CCCCCCCCCCCCCCC
43.2030108239
742UbiquitinationTKNGSFKKKVSSTDP
CCCCCCCCCCCCCCC
57.29-
745PhosphorylationGSFKKKVSSTDPRPR
CCCCCCCCCCCCCCC
36.0828348404
746PhosphorylationSFKKKVSSTDPRPRD
CCCCCCCCCCCCCCC
39.5625627689
747PhosphorylationFKKKVSSTDPRPRDW
CCCCCCCCCCCCCCC
42.3825159151
760PhosphorylationDWRGPPNSPDLKLSD
CCCCCCCCCCCCCCC
26.0923401153
766PhosphorylationNSPDLKLSDSDIPGS
CCCCCCCCCCCCCCC
33.2226657352
768PhosphorylationPDLKLSDSDIPGSSE
CCCCCCCCCCCCCCC
33.7826657352
773PhosphorylationSDSDIPGSSEESPQV
CCCCCCCCCCCCCCE
29.2627732954
774PhosphorylationDSDIPGSSEESPQVV
CCCCCCCCCCCCCEE
51.8329978859
777PhosphorylationIPGSSEESPQVVEAP
CCCCCCCCCCEEECC
19.3116964243
786PhosphorylationQVVEAPGTESDPRLP
CEEECCCCCCCCCCC
31.1229978859
788PhosphorylationVEAPGTESDPRLPTV
EECCCCCCCCCCCHH
53.4029978859
794PhosphorylationESDPRLPTVLESELV
CCCCCCCHHHHHHHH
42.17-
806PhosphorylationELVQRIQTLSQLLLN
HHHHHHHHHHHHHHH
26.4624043423
808PhosphorylationVQRIQTLSQLLLNLQ
HHHHHHHHHHHHHHH
23.3624043423
823PhosphorylationAVIAHQDSYVETQRA
HHHHCCCHHHHHHHH
25.2224043423
824PhosphorylationVIAHQDSYVETQRAA
HHHCCCHHHHHHHHH
15.5924043423
827PhosphorylationHQDSYVETQRAAIQE
CCCHHHHHHHHHHHH
17.2024043423
843PhosphorylationEKQFRLQSTRGNLLL
HHHHHHHHHHHHHHH
25.3526437602
844PhosphorylationKQFRLQSTRGNLLLE
HHHHHHHHHHHHHHH
29.6324719451
870AcetylationEERAALEKLQSQLRH
HHHHHHHHHHHHHHH
53.3123954790
912PhosphorylationGEARQLRERLEQERA
HHHHHHHHHHHHHHH
70.93-
921PhosphorylationLEQERAELERQRQAY
HHHHHHHHHHHHHHH
6.84-
960PhosphorylationRRLKKQNTAPGALPP
HHHHHCCCCCCCCCC
31.5626657352
1003PhosphorylationPSGVGPEYAERPEVA
CCCCCHHHHCCHHHH
19.5223917254
1014PhosphorylationPEVARRDSAPTENRL
HHHHCCCCCCCCCCC
34.0430177828
1049PhosphorylationAVQQQIPTKLAASTK
HHHCCCCCHHHHHCC
40.0828509920
1050AcetylationVQQQIPTKLAASTKG
HHCCCCCHHHHHCCC
30.6725953088
1064AcetylationGGKDKGGKSRGSQRW
CCCCCCCCCCCCHHH
45.7211791489
1065PhosphorylationGKDKGGKSRGSQRWE
CCCCCCCCCCCHHHH
45.1927251275
1068PhosphorylationKGGKSRGSQRWESSA
CCCCCCCCHHHHCCC
18.5727251275
1073PhosphorylationRGSQRWESSASFDLK
CCCHHHHCCCCCCHH
25.0123186163
1074PhosphorylationGSQRWESSASFDLKQ
CCHHHHCCCCCCHHH
19.2029802988
1076PhosphorylationQRWESSASFDLKQQL
HHHHCCCCCCHHHHH
22.6529507054
1080AcetylationSSASFDLKQQLLLNK
CCCCCCHHHHHHHHH
37.5311791499
1094PhosphorylationKLMGKDESTSRNRRS
HHCCCCCCCCCCCCC
41.64-
1095PhosphorylationLMGKDESTSRNRRSL
HCCCCCCCCCCCCCC
29.65-
1096PhosphorylationMGKDESTSRNRRSLS
CCCCCCCCCCCCCCC
36.52-
1101PhosphorylationSTSRNRRSLSPILPG
CCCCCCCCCCCCCCC
29.9322167270
1103PhosphorylationSRNRRSLSPILPGRH
CCCCCCCCCCCCCCC
15.9019664994
1111PhosphorylationPILPGRHSPAPPPDP
CCCCCCCCCCCCCCC
22.7726055452
1124PhosphorylationDPGFPAPSPPPADSP
CCCCCCCCCCCCCCC
52.7425159151
1130PhosphorylationPSPPPADSPSEGFSL
CCCCCCCCCCCCCCC
32.2225159151
1132PhosphorylationPPPADSPSEGFSLKA
CCCCCCCCCCCCCCC
55.0630175587
1136PhosphorylationDSPSEGFSLKAGGTA
CCCCCCCCCCCCCEE
39.5628102081
1142PhosphorylationFSLKAGGTALLPGPP
CCCCCCCEEECCCCC
17.1426074081
1152PhosphorylationLPGPPAPSPLPATPL
CCCCCCCCCCCCCCC
40.9725159151
1157PhosphorylationAPSPLPATPLSAKED
CCCCCCCCCCCCCCC
23.8725159151
1160PhosphorylationPLPATPLSAKEDASK
CCCCCCCCCCCCCCC
38.2028355574
1166PhosphorylationLSAKEDASKEDVIFF
CCCCCCCCCCCCCCC
49.2328450419
1289Phosphorylation---------------------------------------------------------------------------------------------------------------------------
---------------------------------------------------------------------------------------------------------------------------
-
1291Phosphorylation-----------------------------------------------------------------------------------------------------------------------------
-----------------------------------------------------------------------------------------------------------------------------
-

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 ARHGI_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARHGI_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 ARHGI_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GBB1_HUMANGNB1physical
14512443

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 ARHGI_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1103, 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-209; THR-212; SER-733;SER-1101; SER-1103; SER-1124 AND SER-1130, 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-1103, AND MASSSPECTROMETRY.

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