RHG12_HUMAN - dbPTM
RHG12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHG12_HUMAN
UniProt AC Q8IWW6
Protein Name Rho GTPase-activating protein 12
Gene Name ARHGAP12
Organism Homo sapiens (Human).
Sequence Length 846
Subcellular Localization
Protein Description GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state..
Protein Sequence MKMADRSGKIIPGQVYIEVEYDYEYEAKDRKIVIKQGERYILVKKTNDDWWQVKPDENSKAFYVPAQYVKEVTRKALMPPVKQVAGLPNNSTKIMQSLHLQRSTENVNKLPELSSFGKPSSSVQGTGLIRDANQNFGPSYNQGQTVNLSLDLTHNNGKFNNDSHSPKVSSQNRTRSFGHFPGPEFLDVEKTSFSQEQSCDSAGEGSERIHQDSESGDELSSSSTEQIRATTPPNQGRPDSPVYANLQELKISQSALPPLPGSPAIQINGEWETHKDSSGRCYYYNRGTQERTWKPPRWTRDASISKGDFQNPGDQELLSSEENYYSTSYSQSDSQCGSPPRGWSEELDERGHTLYTSDYTNEKWLKHVDDQGRQYYYSADGSRSEWELPKYNASSQQQREIIKSRSLDRRLQEPIVLTKWRHSTIVLDTNDKESPTASKPCFPENESSPSSPKHQDTASSPKDQEKYGLLNVTKIAENGKKVRKNWLSSWAVLQGSSLLFTKTQGSSTSWFGSNQSKPEFTVDLKGATIEMASKDKSSKKNVFELKTRQGTELLIQSDNDTVINDWFKVLSSTINNQAVETDEGIEEEIPDSPGIEKHDKEKEQKDPKKLRSFKVSSIDSSEQKKTKKNLKKFLTRRPTLQAVREKGYIKDQVFGSNLANLCQRENGTVPKFVKLCIEHVEEHGLDIDGIYRVSGNLAVIQKLRFAVNHDEKLDLNDSKWEDIHVITGALKMFFRELPEPLFTFNHFNDFVNAIKQEPRQRVAAVKDLIRQLPKPNQDTMQILFRHLRRVIENGEKNRMTYQSIAIVFGPTLLKPEKETGNIAVHTVYQNQIVELILLELSSIFGR
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
40PhosphorylationVIKQGERYILVKKTN
EEECCCEEEEEEECC
8.3623917254
46PhosphorylationRYILVKKTNDDWWQV
EEEEEEECCCCCEEC
37.8626074081
59PhosphorylationQVKPDENSKAFYVPA
ECCCCCCCCEEEEEH
24.2626074081
63PhosphorylationDENSKAFYVPAQYVK
CCCCCEEEEEHHHHH
15.4728152594
68PhosphorylationAFYVPAQYVKEVTRK
EEEEEHHHHHHHHHH
18.6528152594
91PhosphorylationVAGLPNNSTKIMQSL
HCCCCCCHHHHHHHH
37.4030576142
92PhosphorylationAGLPNNSTKIMQSLH
CCCCCCHHHHHHHHH
27.0630576142
97PhosphorylationNSTKIMQSLHLQRST
CHHHHHHHHHHHHCC
10.6129514088
103PhosphorylationQSLHLQRSTENVNKL
HHHHHHHCCCCHHHC
27.4130266825
104PhosphorylationSLHLQRSTENVNKLP
HHHHHHCCCCHHHCC
33.4930266825
114PhosphorylationVNKLPELSSFGKPSS
HHHCCHHHHCCCCCC
23.2028152594
115PhosphorylationNKLPELSSFGKPSSS
HHCCHHHHCCCCCCC
51.1228464451
120PhosphorylationLSSFGKPSSSVQGTG
HHHCCCCCCCCCCCC
38.4423927012
121PhosphorylationSSFGKPSSSVQGTGL
HHCCCCCCCCCCCCE
42.9523927012
122PhosphorylationSFGKPSSSVQGTGLI
HCCCCCCCCCCCCEE
23.8523927012
126PhosphorylationPSSSVQGTGLIRDAN
CCCCCCCCCEECCCC
16.2423927012
163PhosphorylationNGKFNNDSHSPKVSS
CCCCCCCCCCCCCCC
28.1729255136
165PhosphorylationKFNNDSHSPKVSSQN
CCCCCCCCCCCCCCC
30.3029255136
174PhosphorylationKVSSQNRTRSFGHFP
CCCCCCCCCCCCCCC
37.9125159151
176PhosphorylationSSQNRTRSFGHFPGP
CCCCCCCCCCCCCCH
34.6629255136
191PhosphorylationEFLDVEKTSFSQEQS
HHCCCCCCCCCCCCC
22.8425159151
192PhosphorylationFLDVEKTSFSQEQSC
HCCCCCCCCCCCCCC
33.6925159151
194PhosphorylationDVEKTSFSQEQSCDS
CCCCCCCCCCCCCCC
32.3525159151
198PhosphorylationTSFSQEQSCDSAGEG
CCCCCCCCCCCCCCC
21.0923927012
201PhosphorylationSQEQSCDSAGEGSER
CCCCCCCCCCCCCCC
42.3623927012
206PhosphorylationCDSAGEGSERIHQDS
CCCCCCCCCCCCCCC
21.2823927012
213PhosphorylationSERIHQDSESGDELS
CCCCCCCCCCCCCCC
27.3925159151
215PhosphorylationRIHQDSESGDELSSS
CCCCCCCCCCCCCCC
56.3429255136
220PhosphorylationSESGDELSSSSTEQI
CCCCCCCCCCCCCHH
26.5723927012
221PhosphorylationESGDELSSSSTEQIR
CCCCCCCCCCCCHHH
40.7225849741
222PhosphorylationSGDELSSSSTEQIRA
CCCCCCCCCCCHHHC
37.5923927012
223PhosphorylationGDELSSSSTEQIRAT
CCCCCCCCCCHHHCC
37.6023927012
224PhosphorylationDELSSSSTEQIRATT
CCCCCCCCCHHHCCC
33.5823403867
230PhosphorylationSTEQIRATTPPNQGR
CCCHHHCCCCCCCCC
29.9529255136
231PhosphorylationTEQIRATTPPNQGRP
CCHHHCCCCCCCCCC
35.4529255136
240PhosphorylationPNQGRPDSPVYANLQ
CCCCCCCCCCCCHHH
20.9629255136
243PhosphorylationGRPDSPVYANLQELK
CCCCCCCCCHHHHCE
7.9922167270
254PhosphorylationQELKISQSALPPLPG
HHCEECHHCCCCCCC
25.6128102081
262PhosphorylationALPPLPGSPAIQING
CCCCCCCCCCEEECC
14.8225159151
273PhosphorylationQINGEWETHKDSSGR
EECCEEEEEECCCCC
34.9925002506
303PhosphorylationPRWTRDASISKGDFQ
CCCCCCCCCCCCCCC
31.5127251275
303 (in isoform 3)Phosphorylation-31.5130266825
305 (in isoform 3)Phosphorylation-28.2630266825
306UbiquitinationTRDASISKGDFQNPG
CCCCCCCCCCCCCCC
61.9121906983
306 (in isoform 3)Ubiquitination-61.9121906983
327PhosphorylationSEENYYSTSYSQSDS
CCCCCCCCCCCCCCC
18.6330576142
330PhosphorylationNYYSTSYSQSDSQCG
CCCCCCCCCCCCCCC
23.9926657352
332PhosphorylationYSTSYSQSDSQCGSP
CCCCCCCCCCCCCCC
33.0330576142
334PhosphorylationTSYSQSDSQCGSPPR
CCCCCCCCCCCCCCC
32.3928348404
338PhosphorylationQSDSQCGSPPRGWSE
CCCCCCCCCCCCCCH
39.0828348404
353PhosphorylationELDERGHTLYTSDYT
HHHHCCCEEECCCCC
25.0428796482
355PhosphorylationDERGHTLYTSDYTNE
HHCCCEEECCCCCCC
12.8328796482
356PhosphorylationERGHTLYTSDYTNEK
HCCCEEECCCCCCCC
20.4528796482
357PhosphorylationRGHTLYTSDYTNEKW
CCCEEECCCCCCCCH
18.3128796482
359PhosphorylationHTLYTSDYTNEKWLK
CEEECCCCCCCCHHC
15.9528796482
360PhosphorylationTLYTSDYTNEKWLKH
EEECCCCCCCCHHCC
41.7228796482
366MethylationYTNEKWLKHVDDQGR
CCCCCHHCCCCCCCC
40.23-
375PhosphorylationVDDQGRQYYYSADGS
CCCCCCEEEECCCCC
11.7423917254
376PhosphorylationDDQGRQYYYSADGSR
CCCCCEEEECCCCCC
5.2122817900
377PhosphorylationDQGRQYYYSADGSRS
CCCCEEEECCCCCCC
7.7622817900
391PhosphorylationSEWELPKYNASSQQQ
CCCCCCCCCCCHHHH
17.6420068231
394PhosphorylationELPKYNASSQQQREI
CCCCCCCCHHHHHHH
25.6620068231
395PhosphorylationLPKYNASSQQQREII
CCCCCCCHHHHHHHH
29.6020068231
400 (in isoform 3)Phosphorylation-44.7329116813
401 (in isoform 3)Phosphorylation-5.3929116813
403 (in isoform 3)Phosphorylation-45.5425159151
404PhosphorylationQQREIIKSRSLDRRL
HHHHHHHHHHHHHHH
19.3820068231
404 (in isoform 3)Phosphorylation-19.3825849741
406PhosphorylationREIIKSRSLDRRLQE
HHHHHHHHHHHHHCC
41.5326699800
423PhosphorylationVLTKWRHSTIVLDTN
EEEECCCCEEEEECC
15.9729255136
423 (in isoform 2)Phosphorylation-15.9725850435
424PhosphorylationLTKWRHSTIVLDTND
EEECCCCEEEEECCC
14.6929255136
424 (in isoform 2)Phosphorylation-14.6925850435
429PhosphorylationHSTIVLDTNDKESPT
CCEEEEECCCCCCCC
40.9527050516
432"N6,N6-dimethyllysine"IVLDTNDKESPTASK
EEEECCCCCCCCCCC
63.26-
432MethylationIVLDTNDKESPTASK
EEEECCCCCCCCCCC
63.26-
434PhosphorylationLDTNDKESPTASKPC
EECCCCCCCCCCCCC
33.0425849741
436PhosphorylationTNDKESPTASKPCFP
CCCCCCCCCCCCCCC
53.4923663014
438PhosphorylationDKESPTASKPCFPEN
CCCCCCCCCCCCCCC
39.3423663014
447PhosphorylationPCFPENESSPSSPKH
CCCCCCCCCCCCCCC
60.1623663014
447 (in isoform 4)Phosphorylation-60.1629116813
448PhosphorylationCFPENESSPSSPKHQ
CCCCCCCCCCCCCCC
23.7123663014
448 (in isoform 4)Phosphorylation-23.7129116813
450PhosphorylationPENESSPSSPKHQDT
CCCCCCCCCCCCCCC
62.3123663014
450 (in isoform 4)Phosphorylation-62.3125159151
451PhosphorylationENESSPSSPKHQDTA
CCCCCCCCCCCCCCC
41.1523663014
451 (in isoform 4)Phosphorylation-41.1525849741
457PhosphorylationSSPKHQDTASSPKDQ
CCCCCCCCCCCHHHH
23.1328348404
459PhosphorylationPKHQDTASSPKDQEK
CCCCCCCCCHHHHHH
49.6328348404
460PhosphorylationKHQDTASSPKDQEKY
CCCCCCCCHHHHHHH
33.2428348404
467PhosphorylationSPKDQEKYGLLNVTK
CHHHHHHHCCEEHHH
16.5627642862
513PhosphorylationSSTSWFGSNQSKPEF
CCCCCCCCCCCCCEE
23.4028857561
521PhosphorylationNQSKPEFTVDLKGAT
CCCCCEEEEECCCCE
16.0821082442
528PhosphorylationTVDLKGATIEMASKD
EEECCCCEEEECCCC
26.5821406692
531SulfoxidationLKGATIEMASKDKSS
CCCCEEEECCCCCCC
4.5130846556
533PhosphorylationGATIEMASKDKSSKK
CCEEEECCCCCCCCC
39.8221406692
571PhosphorylationNDWFKVLSSTINNQA
HHHHHHHHHHHCCEE
28.5523927012
572PhosphorylationDWFKVLSSTINNQAV
HHHHHHHHHHCCEEE
29.1923927012
573PhosphorylationWFKVLSSTINNQAVE
HHHHHHHHHCCEEEE
25.0923927012
581PhosphorylationINNQAVETDEGIEEE
HCCEEEECCCCHHHH
32.5230266825
592PhosphorylationIEEEIPDSPGIEKHD
HHHHCCCCCCCCCCC
21.4830266825
600UbiquitinationPGIEKHDKEKEQKDP
CCCCCCCHHHHHCCH
71.10-
602UbiquitinationIEKHDKEKEQKDPKK
CCCCCHHHHHCCHHH
71.79-
612PhosphorylationKDPKKLRSFKVSSID
CCHHHHHCCEECCCC
39.6027422710
614MethylationPKKLRSFKVSSIDSS
HHHHHCCEECCCCCH
42.31-
616PhosphorylationKLRSFKVSSIDSSEQ
HHHCCEECCCCCHHH
23.3629255136
617PhosphorylationLRSFKVSSIDSSEQK
HHCCEECCCCCHHHH
33.1426657352
620PhosphorylationFKVSSIDSSEQKKTK
CEECCCCCHHHHHHH
33.8229255136
621PhosphorylationKVSSIDSSEQKKTKK
EECCCCCHHHHHHHH
40.0628857561
639PhosphorylationKFLTRRPTLQAVREK
HHHHHCHHHHHHHHH
29.6830266825
691PhosphorylationGLDIDGIYRVSGNLA
CCCCCCEEEEECCEE
15.53-
694PhosphorylationIDGIYRVSGNLAVIQ
CCCEEEEECCEEHHH
16.99-
796AcetylationRVIENGEKNRMTYQS
HHHHCCCCCCCEEEE
51.7822368431
796UbiquitinationRVIENGEKNRMTYQS
HHHHCCCCCCCEEEE
51.78-

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 RHG12_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHG12_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 RHG12_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MUC5B_HUMANMUC5Bphysical
28514442
BPIB1_HUMANBPIFB1physical
28514442
DMBT1_HUMANDMBT1physical
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 RHG12_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; SER-215; SER-240AND TYR-243, AND MASS SPECTROMETRY.
"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-201; THR-231 ANDSER-240, AND MASS SPECTROMETRY.
"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-201; SER-213; SER-215;THR-230; SER-240 AND SER-592, AND MASS SPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-231; SER-240 ANDTYR-243, AND MASS SPECTROMETRY.

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