RHG22_HUMAN - dbPTM
RHG22_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHG22_HUMAN
UniProt AC Q7Z5H3
Protein Name Rho GTPase-activating protein 22
Gene Name ARHGAP22
Organism Homo sapiens (Human).
Sequence Length 698
Subcellular Localization Cytoplasm. Nucleus. Mainly cytoplasmic. Some fraction is nuclear (By similarity)..
Protein Description Rho GTPase-activating protein involved in the signal transduction pathway that regulates endothelial cell capillary tube formation during angiogenesis. Acts as a GTPase activator for the RAC1 by converting it to an inactive GDP-bound state. Inhibits RAC1-dependent lamellipodia formation. May also play a role in transcription regulation via its interaction with VEZF1, by regulating activity of the endothelin-1 (EDN1) promoter (By similarity)..
Protein Sequence MLSPKIRQARRARSKSLVMGEQSRSPGRMPCPHRLGPVLKAGWLKKQRSIMKNWQQRWFVLRGDQLFYYKDKDEIKPQGFISLQGTQVTELPPGPEDPGKHLFEISPGGAGEREKVPANPEALLLMASSQRDMEDWVQAIRRVIWAPLGGGIFGQRLEETVHHERKYGPRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVVPFARYEDFLSCAQLLTKDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILRPQVEDPVTIMEGTSLVQHLMTVLIRKHSQLFTAPVPEGPTSPRGGLQCAVGWGSEEVTRDSQGEPGGPGLPAHRTSSLDGAAVAVLSRTAPTGPGSRCSPGKKVQTLPSWKSSFRQPRSLSGSPKGGGSSLEVPIISSGGNWLMNGLSSLRGHRRASSGDRLKDSGSVQRLSTYDNVPAPGLVPGIPSVASMAWSGASSSESSVGGSLSSCTACRASDSSARSSLHTDWALEPSPLPSSSEDPKSLDLDHSMDEAGAGASNSEPSEPDSPTREHARRSEALQGLVTELRAELCRQRTEYERSVKRIEEGSADLRKRMSRLEEELDQEKKKYIMLEIKLRNSERAREDAERRNQLLQREMEEFFSTLGSLTVGAKGARAPK
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
7 (in isoform 5)Phosphorylation-30.1719664995
14PhosphorylationRQARRARSKSLVMGE
HHHHHHHHCCCCCCC		26.1328857561
16PhosphorylationARRARSKSLVMGEQS
HHHHHHCCCCCCCCC		27.6922617229
16 (in isoform 2)Phosphorylation-27.6927251275
23PhosphorylationSLVMGEQSRSPGRMP
CCCCCCCCCCCCCCC		30.3523312004
25PhosphorylationVMGEQSRSPGRMPCP
CCCCCCCCCCCCCCC		36.6324961811
44 (in isoform 4)Phosphorylation-4.9328270605
46 (in isoform 4)Phosphorylation-49.0928270605
47 (in isoform 4)Phosphorylation-42.6528270605
92 (in isoform 4)Phosphorylation-26.1028152594
97 (in isoform 4)Phosphorylation-61.4628152594
128PhosphorylationEALLLMASSQRDMED
HHHHHHHCCCCCHHH		17.0326471730
129PhosphorylationALLLMASSQRDMEDW
HHHHHHCCCCCHHHH		21.5026471730
209PhosphorylationLVRDLQDSFDCGEKP
HHHHHHHHCCCCCCC		15.2624719451
221PhosphorylationEKPLFDSTTDVHTVA
CCCCCCCCCCHHHHH		28.94-
225 (in isoform 2)Phosphorylation-19.8927251275
229PhosphorylationTDVHTVASLLKLYLR
CCHHHHHHHHHHHHH		29.8724719451
260UbiquitinationSCAQLLTKDEGEGTL
HHHHHHHCCCCCCHH		54.47-
304PhosphorylationYSNVNKMSVQNLATV
HHCCCCCCHHHHHHH		23.35-
310PhosphorylationMSVQNLATVFGPNIL
CCHHHHHHHHCCCCC		21.38-
346PhosphorylationTVLIRKHSQLFTAPV
HHHHHHHHCCEECCC		31.4524247654
350PhosphorylationRKHSQLFTAPVPEGP
HHHHCCEECCCCCCC		38.3523312004
358PhosphorylationAPVPEGPTSPRGGLQ
CCCCCCCCCCCCCEE		63.3222199227
359PhosphorylationPVPEGPTSPRGGLQC
CCCCCCCCCCCCEEE		18.7422617229
372PhosphorylationQCAVGWGSEEVTRDS
EEEEECCCCEECCCC		24.8728857561
375 (in isoform 2)Phosphorylation-4.7027251275
376PhosphorylationGWGSEEVTRDSQGEP
ECCCCEECCCCCCCC		31.8527251275
388 (in isoform 2)Phosphorylation-3.6927251275
393PhosphorylationPGLPAHRTSSLDGAA
CCCCCCCCCCCCCCE		16.8929255136
394PhosphorylationGLPAHRTSSLDGAAV
CCCCCCCCCCCCCEE		28.9429255136
395PhosphorylationLPAHRTSSLDGAAVA
CCCCCCCCCCCCEEE		29.8423401153
411 (in isoform 2)Phosphorylation-24.4227251275
417PhosphorylationTGPGSRCSPGKKVQT
CCCCCCCCCCCCEEC		35.2624961811
424PhosphorylationSPGKKVQTLPSWKSS
CCCCCEECCCCHHHH		43.5629514088
427PhosphorylationKKVQTLPSWKSSFRQ
CCEECCCCHHHHCCC		50.6929083192
430PhosphorylationQTLPSWKSSFRQPRS
ECCCCHHHHCCCCCC		28.5727251275
431PhosphorylationTLPSWKSSFRQPRSL
CCCCHHHHCCCCCCC		22.2629083192
437PhosphorylationSSFRQPRSLSGSPKG
HHCCCCCCCCCCCCC		33.3024706070
439PhosphorylationFRQPRSLSGSPKGGG
CCCCCCCCCCCCCCC		38.17-
441PhosphorylationQPRSLSGSPKGGGSS
CCCCCCCCCCCCCCC		21.7724706070
447PhosphorylationGSPKGGGSSLEVPII
CCCCCCCCCCEEEEE		34.7224719451
447 (in isoform 2)Phosphorylation-34.7227251275
466PhosphorylationNWLMNGLSSLRGHRR
CCHHHCHHHHCCCCC		28.8230301811
467PhosphorylationWLMNGLSSLRGHRRA
CHHHCHHHHCCCCCC		27.4225954137
476PhosphorylationRGHRRASSGDRLKDS
CCCCCCCCCCCCCCC		43.6721969604
541PhosphorylationASDSSARSSLHTDWA
CCCCCCCHHCCCCCC		36.6523401153
542PhosphorylationSDSSARSSLHTDWAL
CCCCCCHHCCCCCCC		20.7222199227
545PhosphorylationSARSSLHTDWALEPS
CCCHHCCCCCCCCCC		38.2322199227
552PhosphorylationTDWALEPSPLPSSSE
CCCCCCCCCCCCCCC		29.6927251275
556PhosphorylationLEPSPLPSSSEDPKS
CCCCCCCCCCCCCCC		54.9322199227
557PhosphorylationEPSPLPSSSEDPKSL
CCCCCCCCCCCCCCC		35.4922199227
558PhosphorylationPSPLPSSSEDPKSLD
CCCCCCCCCCCCCCC		50.8122199227
561 (in isoform 2)Phosphorylation-24.8827251275
563PhosphorylationSSSEDPKSLDLDHSM
CCCCCCCCCCCCCCC		32.2929759185
569PhosphorylationKSLDLDHSMDEAGAG
CCCCCCCCCCCCCCC		27.8227732954
578PhosphorylationDEAGAGASNSEPSEP
CCCCCCCCCCCCCCC		39.7129978859
580PhosphorylationAGAGASNSEPSEPDS
CCCCCCCCCCCCCCC		48.6822199227
583PhosphorylationGASNSEPSEPDSPTR
CCCCCCCCCCCCCCH		58.6822199227
587PhosphorylationSEPSEPDSPTREHAR
CCCCCCCCCCHHHHH		38.6023401153
589PhosphorylationPSEPDSPTREHARRS
CCCCCCCCHHHHHHH		53.2822199227
603 (in isoform 2)Phosphorylation-5.1027251275
636PhosphorylationADLRKRMSRLEEELD
HHHHHHHHHHHHHHH		37.4324961811
648AcetylationELDQEKKKYIMLEIK
HHHHHHHHHEEEEEE		51.597494173
648MethylationELDQEKKKYIMLEIK
HHHHHHHHHEEEEEE		51.5923644510
649PhosphorylationLDQEKKKYIMLEIKL
HHHHHHHHEEEEEEC		10.63-
655AcetylationKYIMLEIKLRNSERA
HHEEEEEECCCCHHH		31.837494183
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
16SPhosphorylationKinaseAKT1P31749
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHG22_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 RHG22_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AGAP3_HUMANAGAP3physical
28514442
PI42C_HUMANPIP4K2Cphysical
28514442
ATF1_HUMANATF1physical
28514442
PI42B_HUMANPIP4K2Bphysical
28514442
JUN_HUMANJUNphysical
28514442
KDM6A_HUMANKDM6Aphysical
28514442
SIR6_HUMANSIRT6physical
28514442
CAF17_HUMANIBA57physical
28514442
DOC11_HUMANDOCK11physical
28514442
PLCD3_HUMANPLCD3physical
28514442
ATF2_HUMANATF2physical
28514442
SRBD1_HUMANSRBD1physical
28514442
DAXX_HUMANDAXXphysical
28514442
KC1A_HUMANCSNK1A1physical
28514442
RAE1L_HUMANRAE1physical
28514442
PI42A_HUMANPIP4K2Aphysical
28514442
CANB1_HUMANPPP3R1physical
28514442
KC1E_HUMANCSNK1Ephysical
28514442
JUND_HUMANJUNDphysical
28514442
PI51A_HUMANPIP5K1Aphysical
28514442
PP2BC_HUMANPPP3CCphysical
28514442
CREB1_HUMANCREB1physical
28514442
SSBP2_HUMANSSBP2physical
28514442
ANK3_HUMANANK3physical
28514442
TFCP2_HUMANTFCP2physical
28514442
PDD2L_HUMANPDCD2Lphysical
28514442
ERI3_HUMANERI3physical
28514442
ARMC8_HUMANARMC8physical
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 RHG22_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-395, AND MASSSPECTROMETRY.

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