ARHGC_MOUSE - dbPTM
ARHGC_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARHGC_MOUSE
UniProt AC Q8R4H2
Protein Name Rho guanine nucleotide exchange factor 12
Gene Name Arhgef12
Organism Mus musculus (Mouse).
Sequence Length 1543
Subcellular Localization Cytoplasm . Membrane . Translocated to the membrane upon stimulation.
Protein Description May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13 (By similarity)..
Protein Sequence MSGTQSTITDRFPLKKPIRHGSILNRESPTDKKQKVERSSSHDFDPTDSSSKKTKSSSEESRSEIYGLVQRCVIIQKDDNGFGLTVSGDNPVFVQSVKEDGAAMRAGVQTGDRIIKVNGTLVTHSNHLEVVKLIRSGSYVALTVQGRPPGSPQIPLADSEVEPSVTGHMSPIMTSPHSPGAAGNMERITSPVLVGEENNVVHNQKVEILRKMLQKEQERLQLLQEDYNRTATQRLLKEIQEAKKHIPQLQEQLSKATGSAQDGAVIAPSRPLGDALTLSEAEADPGDGLCRTDWSSGDASRPSSDSADSPKSSLRERSYLEEAPERSEGVQDAEPQSLVGSPSTRGAPHIIGAEDDDFGTEHEQINGQCSCFQSIELLKSRPAHLAVFLHHVVSQFDPATLLCYLYSDLYKQTNSKETRRVFLEFHQFFLDRSAHLKVPVPEEISVDLEKRRPELIPEDLHRLYIQTMQERVHPEVQRHLEDFRQKRSMGLTLAESELTKLDAERDKDRGTLEKERACAEQIVTKIEEVLMTAQAVEEERSSTMQYVILMYMKYLGVKVKEPRNLEHKRGRIGFLPKIKQSMKKDREGEEKGKRRGFPSILGPPRRPSRHDNSAIGRAMEIQKSRHPKHLSTPSSVSPEPQDPAKLRQSGVANEGTDTGYLPASSMSSATSGTALSQEGGRENDTGTKQVGEASAPGDCLDSTPRVPTTVFDFPPPLLDQVQEEECEVERVAEHGTPKPFRKFDSIAFGESQSEDEQFENDLETDPPNWQQLVSREVLLGLKPSEIKRQEVINELFYTERAHVRTLKVLDQVFYQRVSREGILSPSELRKIFSNLEDILQLHVGLNEQMKAVRKRNETSVIDHIGEDLLIWFSGPGEEKLKHAAATFCSNQPFALEMIKSRQKKDSRFHTFVQDAESNPLCRRLQLKDIIPTQMQRLTKYPLLLDNIAKYTEWPPEREKVKKAADHCRQILNYVNQAVREAENKQRLEDYQRRLDTSNLKLSEYPNVDELRNLDLTKRKMIHEGPLVWKVNRDKSIDLYTLLLEDILVLLQKQDDRLVLRCHSKILASTADSKHTFSPVIKLSTVLVRQVATDNKALFVISMSDNGAQIYELVAQTVSEKTVWQDLICRMAASVKEQSTKPIPLPQPPPCEGDNDEEEPAKLKVEHHDLSVAGLQSPDRVLGLESPLISSKPQSHSLNTPGKSAAEHLFVTATQFAKEQHANGALKEGDGGYPVTIPGPHLPVSEERWALDALRNLGLLKQLLVQQLGLTEKSTQEDWQSFSRYGPASEEVQADSGIRDLENVKACHAREGQMSFKTGTGDIATCDSPRTSTESCAAQDSVILASQDSQASNVLVMDHMILTPEMPPAEPEGGLDESGEHFFDAREAHSDDNPSEGDGAVKKEEKDVNLRISGNCLILDGYDAVQESSTDEEVASSFPLQPVTGIPAVDSSHQQQHSPQNVHPEGPVSPFTPEFLVQRHWRAMEDTCFEIQSPSCTDSQSQILEYIHKIEADLEHLKKVEESYALLCQRLAGSALPDKLSDKS
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------MSGTQSTIT
------CCCCCCCCC		62.95-
2Phosphorylation------MSGTQSTIT
------CCCCCCCCC		62.9525338131
9PhosphorylationSGTQSTITDRFPLKK
CCCCCCCCCCCCCCC		22.62-
22PhosphorylationKKPIRHGSILNRESP
CCCCCCCCCCCCCCC		20.1326824392
28PhosphorylationGSILNRESPTDKKQK
CCCCCCCCCCCHHHH		29.8426824392
39PhosphorylationKKQKVERSSSHDFDP
HHHHCCHHCCCCCCC		23.7627742792
40PhosphorylationKQKVERSSSHDFDPT
HHHCCHHCCCCCCCC		37.6027742792
41PhosphorylationQKVERSSSHDFDPTD
HHCCHHCCCCCCCCC		28.4627742792
47PhosphorylationSSHDFDPTDSSSKKT
CCCCCCCCCCCCCCC		50.8120469934
49PhosphorylationHDFDPTDSSSKKTKS
CCCCCCCCCCCCCCC		38.7023375375
170PhosphorylationPSVTGHMSPIMTSPH
CCCCCCCCCCCCCCC		12.95-
178PhosphorylationPIMTSPHSPGAAGNM
CCCCCCCCCCCCCCC		28.5421082442
189PhosphorylationAGNMERITSPVLVGE
CCCCCCCCCCEEECC		32.9525266776
190PhosphorylationGNMERITSPVLVGEE
CCCCCCCCCEEECCC		15.6125521595
269PhosphorylationDGAVIAPSRPLGDAL
CCCEECCCCCCCCCE		37.1929472430
277PhosphorylationRPLGDALTLSEAEAD
CCCCCCEEHHHHHCC		29.9329472430
279PhosphorylationLGDALTLSEAEADPG
CCCCEEHHHHHCCCC		29.5329472430
295PhosphorylationGLCRTDWSSGDASRP
CCCCCCCCCCCCCCC		27.5325619855
300PhosphorylationDWSSGDASRPSSDSA
CCCCCCCCCCCCCCC		49.8425619855
303PhosphorylationSGDASRPSSDSADSP
CCCCCCCCCCCCCCC		45.7425619855
304PhosphorylationGDASRPSSDSADSPK
CCCCCCCCCCCCCCC		37.9625619855
306PhosphorylationASRPSSDSADSPKSS
CCCCCCCCCCCCCHH		35.6025619855
309PhosphorylationPSSDSADSPKSSLRE
CCCCCCCCCCHHHHH		33.6625521595
312PhosphorylationDSADSPKSSLRERSY
CCCCCCCHHHHHHHH		37.6821183079
318PhosphorylationKSSLRERSYLEEAPE
CHHHHHHHHHHHCCC		29.3528973931
319PhosphorylationSSLRERSYLEEAPER
HHHHHHHHHHHCCCC		25.1021183079
327PhosphorylationLEEAPERSEGVQDAE
HHHCCCCCCCCCCCC		36.7225619855
337PhosphorylationVQDAEPQSLVGSPST
CCCCCCHHHCCCCCC		35.4225619855
341PhosphorylationEPQSLVGSPSTRGAP
CCHHHCCCCCCCCCC		14.2725521595
343PhosphorylationQSLVGSPSTRGAPHI
HHHCCCCCCCCCCEE		32.2225619855
344PhosphorylationSLVGSPSTRGAPHII
HHCCCCCCCCCCEEC		36.1825619855
407PhosphorylationTLLCYLYSDLYKQTN
HHHHHHHHHHHHHCC		20.6725338131
500AcetylationLAESELTKLDAERDK
HHHHHHHHHHHHHHC		57.928275881
514AcetylationKDRGTLEKERACAEQ
CCCCHHHHHHHHHHH		56.468275895
551PhosphorylationMQYVILMYMKYLGVK
HHHHHHHHHHHHCCC		6.2422817900
608PhosphorylationLGPPRRPSRHDNSAI
CCCCCCCCCCCCCHH		40.2026824392
613PhosphorylationRPSRHDNSAIGRAME
CCCCCCCCHHHHHHH		27.5929472430
631PhosphorylationSRHPKHLSTPSSVSP
HCCCCCCCCCCCCCC		37.6825619855
632PhosphorylationRHPKHLSTPSSVSPE
CCCCCCCCCCCCCCC		33.2825619855
634PhosphorylationPKHLSTPSSVSPEPQ
CCCCCCCCCCCCCCC		43.3825619855
635PhosphorylationKHLSTPSSVSPEPQD
CCCCCCCCCCCCCCC		28.0225619855
637PhosphorylationLSTPSSVSPEPQDPA
CCCCCCCCCCCCCHH		26.0327087446
660PhosphorylationNEGTDTGYLPASSMS
CCCCCCCCCCHHHCC		16.1729514104
703PhosphorylationPGDCLDSTPRVPTTV
CCCCCCCCCCCCCCC		18.1225521595
708PhosphorylationDSTPRVPTTVFDFPP
CCCCCCCCCCCCCCC		32.5023984901
709PhosphorylationSTPRVPTTVFDFPPP
CCCCCCCCCCCCCCC		17.0723984901
736PhosphorylationERVAEHGTPKPFRKF
HHHHHHCCCCCCCCC		30.0126824392
745PhosphorylationKPFRKFDSIAFGESQ
CCCCCCCCCCCCCCC		20.9623649490
751PhosphorylationDSIAFGESQSEDEQF
CCCCCCCCCCCCHHH		39.1125195567
753PhosphorylationIAFGESQSEDEQFEN
CCCCCCCCCCHHHCH		57.1823649490
807UbiquitinationRAHVRTLKVLDQVFY
CHHHHHHHHHHHHHH		39.89-
824PhosphorylationVSREGILSPSELRKI
HCCCCCCCHHHHHHH		25.1820415495
826PhosphorylationREGILSPSELRKIFS
CCCCCCHHHHHHHHH		45.9820415495
1068PhosphorylationCHSKILASTADSKHT
ECCHHHHHHCCCCCC		22.2323926118
1170PhosphorylationKVEHHDLSVAGLQSP
EEEECCCCCCCCCCC		18.9129899451
1176PhosphorylationLSVAGLQSPDRVLGL
CCCCCCCCCCCCCCC		33.5425521595
1185PhosphorylationDRVLGLESPLISSKP
CCCCCCCCCCCCCCC		30.0126824392
1189PhosphorylationGLESPLISSKPQSHS
CCCCCCCCCCCCCCC		39.7428066266
1190PhosphorylationLESPLISSKPQSHSL
CCCCCCCCCCCCCCC		41.1628066266
1194PhosphorylationLISSKPQSHSLNTPG
CCCCCCCCCCCCCCC		24.4626370283
1280PhosphorylationSTQEDWQSFSRYGPA
CCHHHHHHHHHHCCC		22.4217242355
1288PhosphorylationFSRYGPASEEVQADS
HHHHCCCCHHCCCCC		37.11-
1317PhosphorylationEGQMSFKTGTGDIAT
CCCCEEECCCCCEEE		37.6627087446
1324PhosphorylationTGTGDIATCDSPRTS
CCCCCEEECCCCCCC		19.7227742792
1327PhosphorylationGDIATCDSPRTSTES
CCEEECCCCCCCHHH		20.5925521595
1377PhosphorylationPEGGLDESGEHFFDA
CCCCCCCCCCCCCCH		49.50-
1389PhosphorylationFDAREAHSDDNPSEG
CCHHHHCCCCCCCCC		54.4225521595
1394PhosphorylationAHSDDNPSEGDGAVK
HCCCCCCCCCCCCCC		61.5425521595
1457PhosphorylationSSHQQQHSPQNVHPE
CCCCCCCCCCCCCCC		24.68-
1492PhosphorylationDTCFEIQSPSCTDSQ
CCEEEEECCCCCCCH		25.1729899451
1540PhosphorylationSALPDKLSDKS----
CCCCHHHCCCC----		49.0526824392
1543PhosphorylationPDKLSDKS-------
CHHHCCCC-------		50.9023984901
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 ARHGC_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARHGC_MOUSE !!
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 ARHGC_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ARHGC_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARHGC_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-637, AND MASSSPECTROMETRY.

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