RHG19_HUMAN - dbPTM
RHG19_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHG19_HUMAN
UniProt AC Q14CB8
Protein Name Rho GTPase-activating protein 19
Gene Name ARHGAP19
Organism Homo sapiens (Human).
Sequence Length 494
Subcellular Localization Nucleus .
Protein Description GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state..
Protein Sequence MATEAQSEGEVPARESGRSDAICSFVICNDSSLRGQPIIFNPDFFVEKLRHEKPEIFTELVVSNITRLIDLPGTELAQLMGEVDLKLPGGAGPASGFFRSLMSLKRKEKGVIFGSPLTEEGIAQIYQLIEYLHKNLRVEGLFRVPGNSVRQQILRDALNNGTDIDLESGEFHSNDVATLLKMFLGELPEPLLTHKHFNAHLKIADLMQFDDKGNKTNIPDKDRQIEALQLLFLILPPPNRNLLKLLLDLLYQTAKKQDKNKMSAYNLALMFAPHVLWPKNVTANDLQENITKLNSGMAFMIKHSQKLFKAPAYIRECARLHYLGSRTQASKDDLDLIASCHTKSFQLAKSQKRNRVDSCPHQEETQHHTEEALRELFQHVHDMPESAKKKQLIRQFNKQSLTQTPGREPSTSQVQKRARSRSFSGLIKRKVLGNQMMSEKKKKNPTPESVAIGELKGTSKENRNLLFSGSPAVTMTPTRLKWSEGKKEGKKGFL
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------MATEAQSEG
------CCCCCCCCC		17.7219413330
7Phosphorylation-MATEAQSEGEVPAR
-CCCCCCCCCCCCCC		55.4029255136
31PhosphorylationSFVICNDSSLRGQPI
EEEEECCHHHCCCCE		19.79-
48UbiquitinationNPDFFVEKLRHEKPE
CCHHHHHHHHCCCCH		45.58-
48 (in isoform 2)Ubiquitination-45.58-
95PhosphorylationPGGAGPASGFFRSLM
CCCCCCHHHHHHHHH		38.9928555341
96UbiquitinationGGAGPASGFFRSLMS
CCCCCHHHHHHHHHH		28.0229967540
103PhosphorylationGFFRSLMSLKRKEKG
HHHHHHHHCCHHCCC		35.7123186163
105UbiquitinationFRSLMSLKRKEKGVI
HHHHHHCCHHCCCEE		54.8629967540
105 (in isoform 2)Ubiquitination-54.86-
186UbiquitinationLLKMFLGELPEPLLT
HHHHHHCCCCCCHHC		64.4029967540
193UbiquitinationELPEPLLTHKHFNAH
CCCCCHHCCCHHCCH		36.2429967540
195 (in isoform 2)Ubiquitination-44.66-
195UbiquitinationPEPLLTHKHFNAHLK
CCCHHCCCHHCCHHH		44.6629967540
202UbiquitinationKHFNAHLKIADLMQF
CHHCCHHHHHHHCCC		26.4429967540
203UbiquitinationHFNAHLKIADLMQFD
HHCCHHHHHHHCCCC		4.5429967540
207SulfoxidationHLKIADLMQFDDKGN
HHHHHHHCCCCCCCC		3.7221406390
212UbiquitinationDLMQFDDKGNKTNIP
HHCCCCCCCCCCCCC		67.2529967540
251PhosphorylationKLLLDLLYQTAKKQD
HHHHHHHHHHHHHCC		15.8926270265
253PhosphorylationLLDLLYQTAKKQDKN
HHHHHHHHHHHCCCC		27.2126270265
302AcetylationSGMAFMIKHSQKLFK
HHHCHHHHHCHHHHH		25.977672323
309UbiquitinationKHSQKLFKAPAYIRE
HHCHHHHHCCHHHHH		64.99-
309 (in isoform 2)Ubiquitination-64.99-
314UbiquitinationLFKAPAYIRECARLH
HHHCCHHHHHHHHHH		3.0429967540
320UbiquitinationYIRECARLHYLGSRT
HHHHHHHHHHCCCCC		1.3329967540
322PhosphorylationRECARLHYLGSRTQA
HHHHHHHHCCCCCCC		19.83-
325PhosphorylationARLHYLGSRTQASKD
HHHHHCCCCCCCCHH		29.56-
327 (in isoform 7)Phosphorylation-30.1322210691
331 (in isoform 2)Ubiquitination-59.27-
331UbiquitinationGSRTQASKDDLDLIA
CCCCCCCHHHHHHHH		59.27-
334UbiquitinationTQASKDDLDLIASCH
CCCCHHHHHHHHHHC		9.1729967540
340UbiquitinationDLDLIASCHTKSFQL
HHHHHHHHCHHHHHH		3.3229967540
343UbiquitinationLIASCHTKSFQLAKS
HHHHHCHHHHHHHHH		26.1329967540
344PhosphorylationIASCHTKSFQLAKSQ
HHHHCHHHHHHHHHH		21.27-
349 (in isoform 2)Ubiquitination-63.11-
349UbiquitinationTKSFQLAKSQKRNRV
HHHHHHHHHHHHCCC		63.1129967540
350PhosphorylationKSFQLAKSQKRNRVD
HHHHHHHHHHHCCCC		35.01-
358PhosphorylationQKRNRVDSCPHQEET
HHHCCCCCCCCHHHH		27.0529978859
359UbiquitinationKRNRVDSCPHQEETQ
HHCCCCCCCCHHHHH		2.7829967540
365PhosphorylationSCPHQEETQHHTEEA
CCCCHHHHHHCHHHH		32.2429978859
369PhosphorylationQEETQHHTEEALREL
HHHHHHCHHHHHHHH		33.1429978859
369UbiquitinationQEETQHHTEEALREL
HHHHHHCHHHHHHHH		33.1429967540
379UbiquitinationALRELFQHVHDMPES
HHHHHHHHHHHCCHH		16.1429967540
386PhosphorylationHVHDMPESAKKKQLI
HHHHCCHHHHHHHHH		39.2527050516
387UbiquitinationVHDMPESAKKKQLIR
HHHCCHHHHHHHHHH		26.4829967540
388UbiquitinationHDMPESAKKKQLIRQ
HHCCHHHHHHHHHHH		70.5529967540
389UbiquitinationDMPESAKKKQLIRQF
HCCHHHHHHHHHHHH		45.5329967540
390 (in isoform 2)Ubiquitination-50.02-
398UbiquitinationQLIRQFNKQSLTQTP
HHHHHHHHHCCCCCC		42.4229967540
400PhosphorylationIRQFNKQSLTQTPGR
HHHHHHHCCCCCCCC		34.6928450419
401UbiquitinationRQFNKQSLTQTPGRE
HHHHHHCCCCCCCCC		3.6929967540
402PhosphorylationQFNKQSLTQTPGREP
HHHHHCCCCCCCCCC		35.3328450419
404PhosphorylationNKQSLTQTPGREPST
HHHCCCCCCCCCCCH		23.6028450419
407UbiquitinationSLTQTPGREPSTSQV
CCCCCCCCCCCHHHH		54.5829967540
411UbiquitinationTPGREPSTSQVQKRA
CCCCCCCHHHHHHHH		33.6230230243
412PhosphorylationPGREPSTSQVQKRAR
CCCCCCHHHHHHHHH		32.4628450419
416UbiquitinationPSTSQVQKRARSRSF
CCHHHHHHHHHHCCC		49.5229967540
420PhosphorylationQVQKRARSRSFSGLI
HHHHHHHHCCCHHHH		31.1525159151
421UbiquitinationVQKRARSRSFSGLIK
HHHHHHHCCCHHHHH		35.8529967540
422PhosphorylationQKRARSRSFSGLIKR
HHHHHHCCCHHHHHH		25.6330266825
424PhosphorylationRARSRSFSGLIKRKV
HHHHCCCHHHHHHHH		33.6623401153
427UbiquitinationSRSFSGLIKRKVLGN
HCCCHHHHHHHHHHH		4.6529967540
428UbiquitinationRSFSGLIKRKVLGNQ
CCCHHHHHHHHHHHH		51.73-
430UbiquitinationFSGLIKRKVLGNQMM
CHHHHHHHHHHHHHH		36.4929967540
431UbiquitinationSGLIKRKVLGNQMMS
HHHHHHHHHHHHHHC		10.8530230243
438PhosphorylationVLGNQMMSEKKKKNP
HHHHHHHCCHHCCCC		40.7023401153
440UbiquitinationGNQMMSEKKKKNPTP
HHHHHCCHHCCCCCC		63.6930230243
446PhosphorylationEKKKKNPTPESVAIG
CHHCCCCCCCHHHHH		49.4321815630
447UbiquitinationKKKKNPTPESVAIGE
HHCCCCCCCHHHHHC		32.8729967540
449PhosphorylationKKNPTPESVAIGELK
CCCCCCCHHHHHCCC		20.3229396449
456UbiquitinationSVAIGELKGTSKENR
HHHHHCCCCCCCCCC		56.7029967540
468PhosphorylationENRNLLFSGSPAVTM
CCCCCEECCCCCEEE		38.0322199227
470PhosphorylationRNLLFSGSPAVTMTP
CCCEECCCCCEEECC		14.4225159151
474PhosphorylationFSGSPAVTMTPTRLK
ECCCCCEEECCCEEC		19.8921712546
475SulfoxidationSGSPAVTMTPTRLKW
CCCCCEEECCCEECC		3.2121406390
476PhosphorylationGSPAVTMTPTRLKWS
CCCCEEECCCEECCC		16.4925159151
478PhosphorylationPAVTMTPTRLKWSEG
CCEEECCCEECCCCC		39.1921712546
506 (in isoform 2)Phosphorylation-24114839
510 (in isoform 2)Phosphorylation-26552605
511 (in isoform 2)Phosphorylation-24114839
512 (in isoform 2)Phosphorylation-24114839
517 (in isoform 2)Phosphorylation-24114839
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
404TPhosphorylationKinaseCDK1P06493
PSP
422SPhosphorylationKinaseAKT1P31749
PSP
422SPhosphorylationKinaseROCK1Q13464
PSP
476TPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHG19_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 RHG19_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FHIT_HUMANFHITphysical
28514442
DCA16_HUMANDCAF16physical
28514442
RNF41_HUMANRNF41physical
28514442
TDRKH_HUMANTDRKHphysical
28514442
LRP2_HUMANLRP2physical
28514442
ERBIN_HUMANERBB2IPphysical
28514442
CBY1_HUMANCBY1physical
27173435
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 RHG19_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
"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-470 AND THR-478, ANDMASS 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-422, AND MASSSPECTROMETRY.

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