RHG26_HUMAN - dbPTM
RHG26_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHG26_HUMAN
UniProt AC Q9UNA1
Protein Name Rho GTPase-activating protein 26
Gene Name ARHGAP26
Organism Homo sapiens (Human).
Sequence Length 814
Subcellular Localization Cell junction, focal adhesion. Cytoplasm, cytoskeleton. Colocalizes with actin stress fibers and cortical actin structures..
Protein Description GTPase-activating protein for RHOA and CDC42..
Protein Sequence MGLPALEFSDCCLDSPHFRETLKSHEAELDKTNKFIKELIKDGKSLISALKNLSSAKRKFADSLNEFKFQCIGDAETDDEMCIARSLQEFATVLRNLEDERIRMIENASEVLITPLEKFRKEQIGAAKEAKKKYDKETEKYCGILEKHLNLSSKKKESQLQEADSQVDLVRQHFYEVSLEYVFKVQEVQERKMFEFVEPLLAFLQGLFTFYHHGYELAKDFGDFKTQLTISIQNTRNRFEGTRSEVESLMKKMKENPLEHKTISPYTMEGYLYVQEKRHFGTSWVKHYCTYQRDSKQITMVPFDQKSGGKGGEDESVILKSCTRRKTDSIEKRFCFDVEAVDRPGVITMQALSEEDRRLWMEAMDGREPVYNSNKDSQSEGTAQLDSIGFSIIRKCIHAVETRGINEQGLYRIVGVNSRVQKLLSVLMDPKTASETETDICAEWEIKTITSALKTYLRMLPGPLMMYQFQRSFIKAAKLENQESRVSEIHSLVHRLPEKNRQMLQLLMNHLANVANNHKQNLMTVANLGVVFGPTLLRPQEETVAAIMDIKFQNIVIEILIENHEKIFNTVPDMPLTNAQLHLSRKKSSDSKPPSCSERPLTLFHTVQSTEKQEQRNSIINSSLESVSSNPNSILNSSSSLQPNMNSSDPDLAVVKPTRPNSLPPNPSPTSPLSPSWPMFSAPSSPMPTSSTSSDSSPVRSVAGFVWFSVAAVVLSLARSSLHAVFSLLVNFVPCHPNLHLLFDRPEEAVHEDSSTPFRKAKALYACKAEHDSELSFTAGTVFDNVHPSQEPGWLEGTLNGKTGLIPENYVEFL
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
9PhosphorylationGLPALEFSDCCLDSP
CCCCCCCHHHCCCCH		21.9924719451
15PhosphorylationFSDCCLDSPHFRETL
CHHHCCCCHHHHHHH		13.8124719451
21PhosphorylationDSPHFRETLKSHEAE
CCHHHHHHHHHCHHH		34.9224719451
48PhosphorylationKDGKSLISALKNLSS
HHCHHHHHHHHCHHH		32.6127486199
51UbiquitinationKSLISALKNLSSAKR
HHHHHHHHCHHHHHH		56.40-
59UbiquitinationNLSSAKRKFADSLNE
CHHHHHHHHHHHHHH		44.17-
77PhosphorylationQCIGDAETDDEMCIA
EECCCCCCCHHHHHH		50.9329449344
118UbiquitinationVLITPLEKFRKEQIG
EEECCHHHHHHHHHC		59.1421906983
118 (in isoform 1)Ubiquitination-59.1421890473
118 (in isoform 2)Ubiquitination-59.1421890473
128AcetylationKEQIGAAKEAKKKYD
HHHHCCHHHHHHHHC		58.6470813
152PhosphorylationLEKHLNLSSKKKESQ
HHHHCCCCCHHHHHH		38.7524719451
226PhosphorylationKDFGDFKTQLTISIQ
HHHCCCEEEEEEEEE		28.8928634120
229PhosphorylationGDFKTQLTISIQNTR
CCCEEEEEEEEECCC		11.6728634120
231PhosphorylationFKTQLTISIQNTRNR
CEEEEEEEEECCCCC		16.9428634120
235PhosphorylationLTISIQNTRNRFEGT
EEEEEECCCCCCCCC		16.9728634120
242PhosphorylationTRNRFEGTRSEVESL
CCCCCCCCHHHHHHH		24.6727251275
244PhosphorylationNRFEGTRSEVESLMK
CCCCCCHHHHHHHHH		45.9227251275
254UbiquitinationESLMKKMKENPLEHK
HHHHHHHHHCCCCCC		64.32-
262PhosphorylationENPLEHKTISPYTME
HCCCCCCCCCCCEEE		28.7026552605
264PhosphorylationPLEHKTISPYTMEGY
CCCCCCCCCCEEEEE		19.6526552605
266PhosphorylationEHKTISPYTMEGYLY
CCCCCCCCEEEEEEE		16.3626552605
267PhosphorylationHKTISPYTMEGYLYV
CCCCCCCEEEEEEEE		16.4826552605
271PhosphorylationSPYTMEGYLYVQEKR
CCCEEEEEEEEEECC		4.9926552605
273PhosphorylationYTMEGYLYVQEKRHF
CEEEEEEEEEECCCC		7.5126552605
295PhosphorylationYCTYQRDSKQITMVP
HHCEECCCCEEEEEE		28.7529978859
299PhosphorylationQRDSKQITMVPFDQK
ECCCCEEEEEECCCC		15.0429978859
310 (in isoform 2)Ubiquitination-68.2321890473
310 (in isoform 1)Ubiquitination-68.2321890473
310UbiquitinationFDQKSGGKGGEDESV
CCCCCCCCCCCCHHH		68.2321906983
320UbiquitinationEDESVILKSCTRRKT
CCHHHHHHHHCCCCC		32.15-
327PhosphorylationKSCTRRKTDSIEKRF
HHHCCCCCCCCCCCC		32.92-
371PhosphorylationMDGREPVYNSNKDSQ
HCCCCCCCCCCCCCC		24.4821945579
373PhosphorylationGREPVYNSNKDSQSE
CCCCCCCCCCCCCCC		27.8021945579
402PhosphorylationKCIHAVETRGINEQG
HHHHHHHHCCCCCCC		27.8322817900
425PhosphorylationSRVQKLLSVLMDPKT
HHHHHHHHHHHCCCC		24.5224719451
454 (in isoform 2)Ubiquitination-34.5421890473
454 (in isoform 1)Ubiquitination-34.5421890473
454UbiquitinationKTITSALKTYLRMLP
HHHHHHHHHHHHHCC		34.5421890473
456PhosphorylationITSALKTYLRMLPGP
HHHHHHHHHHHCCCC		7.25-
467PhosphorylationLPGPLMMYQFQRSFI
CCCCCHHHHHHHHHH		7.69-
472PhosphorylationMMYQFQRSFIKAAKL
HHHHHHHHHHHHHHH		22.1224719451
475UbiquitinationQFQRSFIKAAKLENQ
HHHHHHHHHHHHCCC		40.04-
524PhosphorylationNHKQNLMTVANLGVV
HHHHHHCHHHHCEEE		21.4523663014
535PhosphorylationLGVVFGPTLLRPQEE
CEEEECCCCCCCCHH		38.5123663014
570PhosphorylationNHEKIFNTVPDMPLT
CHHHHHHCCCCCCCC		23.7523312004
577PhosphorylationTVPDMPLTNAQLHLS
CCCCCCCCHHHHHHH		23.7227251275
584PhosphorylationTNAQLHLSRKKSSDS
CHHHHHHHCCCCCCC		31.1624117733
588PhosphorylationLHLSRKKSSDSKPPS
HHHHCCCCCCCCCCC		42.2726657352
589PhosphorylationHLSRKKSSDSKPPSC
HHHCCCCCCCCCCCC		55.5829116813
591PhosphorylationSRKKSSDSKPPSCSE
HCCCCCCCCCCCCCC		49.3526657352
595PhosphorylationSSDSKPPSCSERPLT
CCCCCCCCCCCCCCE		38.5127080861
597PhosphorylationDSKPPSCSERPLTLF
CCCCCCCCCCCCEEE		40.7624117733
602PhosphorylationSCSERPLTLFHTVQS
CCCCCCCEEEEECCC		30.0227080861
609PhosphorylationTLFHTVQSTEKQEQR
EEEEECCCCCHHHHH		33.9123312004
610PhosphorylationLFHTVQSTEKQEQRN
EEEECCCCCHHHHHH		30.0623312004
684PhosphorylationWPMFSAPSSPMPTSS
CCCCCCCCCCCCCCC		46.95-
684 (in isoform 2)Phosphorylation-46.95-
685 (in isoform 2)Phosphorylation-24.94-
685PhosphorylationPMFSAPSSPMPTSST
CCCCCCCCCCCCCCC		24.94-
803PhosphorylationEGTLNGKTGLIPENY
EEEECCCCCCCCHHH		38.3228796482
810PhosphorylationTGLIPENYVEFL---
CCCCCHHHEECC---		10.3328796482
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 RHG26_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHG26_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 RHG26_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHOA_HUMANRHOAphysical
11432776
CDC42_HUMANCDC42physical
11432776
FAK1_HUMANPTK2physical
8649427
ACADS_HUMANACADSphysical
26344197
RHG42_HUMANARHGAP42physical
28514442
OPHN1_HUMANOPHN1physical
28514442
RHG10_HUMANARHGAP10physical
28514442
MICA1_HUMANMICAL1physical
28514442
JPH1_HUMANJPH1physical
28514442
RFIP5_HUMANRAB11FIP5physical
28514442
RHG10_HUMANARHGAP10physical
27173435
CTR9_HUMANCTR9physical
27173435
TULP1_HUMANTULP1physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
607785Leukemia, juvenile myelomonocytic (JMML)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RHG26_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 THR-402, AND MASSSPECTROMETRY.

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