RHG15_HUMAN - dbPTM
RHG15_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHG15_HUMAN
UniProt AC Q53QZ3
Protein Name Rho GTPase-activating protein 15
Gene Name ARHGAP15
Organism Homo sapiens (Human).
Sequence Length 475
Subcellular Localization Cytoplasm . Membrane
Peripheral membrane protein .
Protein Description GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has activity toward RAC1. Overexpression results in an increase in actin stress fibers and cell contraction..
Protein Sequence MQKSTNSDTSVETLNSTRQGTGAVQMRIKNANSHHDRLSQSKSMILTDVGKVTEPISRHRRNHSQHILKDVIPPLEQLMVEKEGYLQKAKIADGGKKLRKNWSTSWIVLSSRRIEFYKESKQQALSNMKTGHKPESVDLCGAHIEWAKEKSSRKNVFQITTVSGNEFLLQSDIDFIILDWFHAIKNAIDRLPKDSSCPSRNLELFKIQRSSSTELLSHYDSDIKEQKPEHRKSLMFRLHHSASDTSDKNRVKSRLKKFITRRPSLKTLQEKGLIKDQIFGSHLHKVCERENSTVPWFVKQCIEAVEKRGLDVDGIYRVSGNLATIQKLRFIVNQEEKLNLDDSQWEDIHVVTGALKMFFRELPEPLFPYSFFEQFVEAIKKQDNNTRIEAVKSLVQKLPPPNRDTMKVLFGHLTKIVAKASKNLMSTQSLGIVFGPTLLRAENETGNMAIHMVYQNQIAELMLSEYSKIFGSEED
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
3Ubiquitination-----MQKSTNSDTS
-----CCCCCCCCCC		58.9324816145
4Phosphorylation----MQKSTNSDTSV
----CCCCCCCCCCH		18.8728450419
5Phosphorylation---MQKSTNSDTSVE
---CCCCCCCCCCHH		45.8628450419
7Phosphorylation-MQKSTNSDTSVETL
-CCCCCCCCCCHHHH		42.2128450419
9PhosphorylationQKSTNSDTSVETLNS
CCCCCCCCCHHHHHH		34.2026699800
10PhosphorylationKSTNSDTSVETLNST
CCCCCCCCHHHHHHC		23.9727732954
13PhosphorylationNSDTSVETLNSTRQG
CCCCCHHHHHHCCCC		29.1427732954
16PhosphorylationTSVETLNSTRQGTGA
CCHHHHHHCCCCCCE		28.2527732954
33PhosphorylationMRIKNANSHHDRLSQ
EEEECCCCCCHHHHH		21.5628122231
39PhosphorylationNSHHDRLSQSKSMIL
CCCCHHHHHCCCEEE		33.0523401153
41PhosphorylationHHDRLSQSKSMILTD
CCHHHHHCCCEEEEC		24.2620068231
42UbiquitinationHDRLSQSKSMILTDV
CHHHHHCCCEEEECC		36.0829967540
43PhosphorylationDRLSQSKSMILTDVG
HHHHHCCCEEEECCC		19.1223401153
44SulfoxidationRLSQSKSMILTDVGK
HHHHCCCEEEECCCC		3.1521406390
47PhosphorylationQSKSMILTDVGKVTE
HCCCEEEECCCCCCC		20.0828464451
51UbiquitinationMILTDVGKVTEPISR
EEEECCCCCCCCCHH		45.9229967540
64PhosphorylationSRHRRNHSQHILKDV
HHHCCCCCHHHHHHH		27.3123401153
69UbiquitinationNHSQHILKDVIPPLE
CCCHHHHHHHCCHHH		49.7129967540
82UbiquitinationLEQLMVEKEGYLQKA
HHHHHHHCCCHHEEE		45.0629967540
88UbiquitinationEKEGYLQKAKIADGG
HCCCHHEEEEECCCC		49.4029967540
88AcetylationEKEGYLQKAKIADGG
HCCCHHEEEEECCCC		49.4025953088
90UbiquitinationEGYLQKAKIADGGKK
CCHHEEEEECCCCCC		45.5233845483
103PhosphorylationKKLRKNWSTSWIVLS
CCCCCCCCCCEEEEE		23.2030108239
104PhosphorylationKLRKNWSTSWIVLSS
CCCCCCCCCEEEEEC		21.5027251275
105PhosphorylationLRKNWSTSWIVLSSR
CCCCCCCCEEEEECH		14.8628450419
111PhosphorylationTSWIVLSSRRIEFYK
CCEEEEECHHHHHHH		22.7824719451
118AcetylationSRRIEFYKESKQQAL
CHHHHHHHHHHHHHH		61.9119608861
118UbiquitinationSRRIEFYKESKQQAL
CHHHHHHHHHHHHHH		61.9119608861
121UbiquitinationIEFYKESKQQALSNM
HHHHHHHHHHHHHCC		47.7429967540
128UbiquitinationKQQALSNMKTGHKPE
HHHHHHCCCCCCCCC		3.5524816145
129UbiquitinationQQALSNMKTGHKPES
HHHHHCCCCCCCCCC		56.4529967540
130PhosphorylationQALSNMKTGHKPESV
HHHHCCCCCCCCCCC		33.4824260401
133UbiquitinationSNMKTGHKPESVDLC
HCCCCCCCCCCCCCC		52.4029967540
148UbiquitinationGAHIEWAKEKSSRKN
HHHHHHHHHHHCCCC		67.7429967540
163UbiquitinationVFQITTVSGNEFLLQ
EEEEEEEECCEEECC		33.5324816145
193UbiquitinationNAIDRLPKDSSCPSR
HHHHCCCCCCCCCCC		74.8829967540
195PhosphorylationIDRLPKDSSCPSRNL
HHCCCCCCCCCCCCC		39.7126074081
196O-linked_GlycosylationDRLPKDSSCPSRNLE
HCCCCCCCCCCCCCE		39.9329351928
196PhosphorylationDRLPKDSSCPSRNLE
HCCCCCCCCCCCCCE		39.9326074081
199PhosphorylationPKDSSCPSRNLELFK
CCCCCCCCCCCEEEE		37.8226074081
206UbiquitinationSRNLELFKIQRSSST
CCCCEEEEEECCCCH		51.0224816145
210PhosphorylationELFKIQRSSSTELLS
EEEEEECCCCHHHHH		16.5623401153
211PhosphorylationLFKIQRSSSTELLSH
EEEEECCCCHHHHHC		43.3922115753
212PhosphorylationFKIQRSSSTELLSHY
EEEECCCCHHHHHCC		27.4423401153
213PhosphorylationKIQRSSSTELLSHYD
EEECCCCHHHHHCCC		32.3823401153
217PhosphorylationSSSTELLSHYDSDIK
CCCHHHHHCCCCCHH		32.4023898821
219PhosphorylationSTELLSHYDSDIKEQ
CHHHHHCCCCCHHHH		17.4828787133
221PhosphorylationELLSHYDSDIKEQKP
HHHHCCCCCHHHHCH		33.7922115753
224UbiquitinationSHYDSDIKEQKPEHR
HCCCCCHHHHCHHHH		60.1129967540
232UbiquitinationEQKPEHRKSLMFRLH
HHCHHHHHHHHHHHH		50.26-
233PhosphorylationQKPEHRKSLMFRLHH
HCHHHHHHHHHHHHH		25.6426074081
241PhosphorylationLMFRLHHSASDTSDK
HHHHHHHCCCCCCCH		20.7929978859
243PhosphorylationFRLHHSASDTSDKNR
HHHHHCCCCCCCHHH		44.4220164059
245PhosphorylationLHHSASDTSDKNRVK
HHHCCCCCCCHHHHH		36.0129978859
246PhosphorylationHHSASDTSDKNRVKS
HHCCCCCCCHHHHHH		52.1329978859
248UbiquitinationSASDTSDKNRVKSRL
CCCCCCCHHHHHHHH		46.5529967540
260PhosphorylationSRLKKFITRRPSLKT
HHHHHHHHHCCCHHH		24.6123882029
264PhosphorylationKFITRRPSLKTLQEK
HHHHHCCCHHHHHHC		40.4626074081
266UbiquitinationITRRPSLKTLQEKGL
HHHCCCHHHHHHCCC		52.0729967540
267PhosphorylationTRRPSLKTLQEKGLI
HHCCCHHHHHHCCCC		38.6821949786
271AcetylationSLKTLQEKGLIKDQI
CHHHHHHCCCCCHHH		46.1625953088
271UbiquitinationSLKTLQEKGLIKDQI
CHHHHHHCCCCCHHH		46.1629967540
275UbiquitinationLQEKGLIKDQIFGSH
HHHCCCCCHHHHHHH		48.9329967540
285UbiquitinationIFGSHLHKVCERENS
HHHHHHHHHHHCCCC		55.7429967540
292PhosphorylationKVCERENSTVPWFVK
HHHHCCCCCCCHHHH		26.4828857561
299UbiquitinationSTVPWFVKQCIEAVE
CCCCHHHHHHHHHHH		29.9429967540
307UbiquitinationQCIEAVEKRGLDVDG
HHHHHHHHCCCCCCC		45.2129967540
319UbiquitinationVDGIYRVSGNLATIQ
CCCEEEECCCCHHHH		16.9924816145
319PhosphorylationVDGIYRVSGNLATIQ
CCCEEEECCCCHHHH		16.9922985185
324PhosphorylationRVSGNLATIQKLRFI
EECCCCHHHHHHEEE		27.40-
327UbiquitinationGNLATIQKLRFIVNQ
CCCHHHHHHEEECCC		37.4729967540
337UbiquitinationFIVNQEEKLNLDDSQ
EECCCHHHCCCCHHH		41.7529967540
343PhosphorylationEKLNLDDSQWEDIHV
HHCCCCHHHHHHHHH		36.5427067055
354UbiquitinationDIHVVTGALKMFFRE
HHHHHHHHHHHHHHH		8.4724816145
392UbiquitinationNTRIEAVKSLVQKLP
CHHHHHHHHHHHHCC		45.1529967540
393PhosphorylationTRIEAVKSLVQKLPP
HHHHHHHHHHHHCCC		27.4628857561
397UbiquitinationAVKSLVQKLPPPNRD
HHHHHHHHCCCCCHH		56.3224816145
405PhosphorylationLPPPNRDTMKVLFGH
CCCCCHHHHHHHHHH		18.6930576142
407UbiquitinationPPNRDTMKVLFGHLT
CCCHHHHHHHHHHHH		37.5729967540
415UbiquitinationVLFGHLTKIVAKASK
HHHHHHHHHHHHHHH		41.3629967540
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
4SPhosphorylationKinasePAK2Q13177
PSP
41SPhosphorylationKinasePAK2Q13177
PSP
43SPhosphorylationKinasePAK2Q13177
PSP
292SPhosphorylationKinasePAK2Q13177
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHG15_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 RHG15_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAC1_HUMANRAC1physical
12650940
KDM1A_HUMANKDM1Aphysical
23455924
DHYS_HUMANDHPSphysical
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 RHG15_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118, 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-43 AND SER-103, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory