RHG31_MOUSE - dbPTM
RHG31_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHG31_MOUSE
UniProt AC A6X8Z5
Protein Name Rho GTPase-activating protein 31
Gene Name Arhgap31
Organism Mus musculus (Mouse).
Sequence Length 1425
Subcellular Localization Cell projection, lamellipodium. Cell junction, focal adhesion.
Protein Description Functions as a GTPase-activating protein (GAP) for RAC1 and CDC42. Required for cell spreading, polarized lamellipodia formation and cell migration..
Protein Sequence MKNKGAKQKLKRKGAASAFGCDLTEYLESSGQDVPYVLKSCAEFIETHGIVDGIYRLSGITSNIQRLRQEFGSDQCPDLTREVYLQDIHCVGSLCKLYFRELPNPLLTYELYEKFTEAVSHRPEEGQLARIQNVILELPPPHYRTLEYLIRHLAHIASFSSKTNMHARNLALVWAPNLLRSKKIEATICNGDAAFLAVRVQQVVIEFILNHADQIFNGGAPGALQQDESRTITKSLTLPALSLPMKLVSLEEAQARSLATNHPARKERRENSLPEIVPPPFHTVLELPDNKRKLSSKSKKWKSIFNLGRSGSDSKSKLSRNGSVFVRGQRLSVEKATIRPAKSMDSLCSVPVEGKENKGNFSRTVTTGGFFIPATKMHASSTGSSCDLSKEGEWGQEGMPAGAEGGCEVGGQIRPLPEQLKVFRPIGDPESEQSAPKLLGMFYTSSDSPGKSVFTSSLFQMEPSPRHQRKALNISEPFAVSVPLRVSAVISTNSTPCRTPPKELQSLSSLEEFSFQGSESGGWPEEEKPLGAESFPGSVTKKAATEDTKPEPEVPGRAECSQSPPLDPGTQVEKKTLHVSLGSQVSKEAEKRPKAEKVMEESQGASQPKPSTPQESLGAGTEPLILHEMDEEDLAQALIWPEIQQELKIIESEEEFSSLPPAAQKTSPIPESSPAPFPFPEAPGSLPSSSAPREVWTRDAANQSIQEAAILTDREKLEPVCSLLESESQQELSPDPASLAPLEMLLFEKVSSPARIEIGGPRNLSPPLTPAPPPPTPLEEEPEVLLSKEGPDREDAARDSRTDVYTEQPTPKESPGIPTPCQREEAIASPNEKQNARHAVPENKGPGLPSPTKEVDIIPQEEGGAPHSAQEPSDCDEDDTVTDPAQHGLEMVEPWEEPQWVTSPLHSPTLKEVQESQTQGSQGHRLERRLCHRPSLRQSHSLDSKTTGNSHWTLEAPFSSSCANLETERNYEPLQPPAARTKIAGLEEKALKAFREFSGLKGLEVLPSQKGPSGIQPKPVETNFMGLAEGKEQEPQLELSNRQMKHSDVPGPDSSKESSPRAQDSTLPGEHPLQLQLKNTECGPSKGKHRPSSLNLDSATPIADLFRLENGAPFSSPGIELSELGDTKVTWMSSSHCKAAPWNSQDTQDLDIVAHTLTGRRNSAPVSVSAVRTSFMVKMCQAKAVPVIPPKIQYTQIPQPLPSQSTGEGGAQPLERSQEEPGSTPEIPQKSTKDDSPSSLGSPEEEQPKQETGASASRRQASITSCMYEGSSCSPEPSASTLASTQDAVVQCRKRTSETEPSGDNLLSSKLERASGGPKAFHRSRPGRPQSLILFPIMDHLPSSPTVIDSKVLLSPIRSPTQTVSPGLLCGELAENTWITPEGVTLRNKMTIPKNGQRLETSTSCFYQPQRRSVILDGRSGRQIE
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
235PhosphorylationESRTITKSLTLPALS
HHCCCCCCCCHHHHC
20.2429472430
237PhosphorylationRTITKSLTLPALSLP
CCCCCCCCHHHHCCC
37.4727180971
242PhosphorylationSLTLPALSLPMKLVS
CCCHHHHCCCEEEEE
32.3129514104
272PhosphorylationRKERRENSLPEIVPP
HHHHHHCCCCCCCCC
40.3125521595
283PhosphorylationIVPPPFHTVLELPDN
CCCCCCCEEEECCCC
27.4522817900
303PhosphorylationSKSKKWKSIFNLGRS
CCCHHHHHHHCCCCC
31.1525521595
323PhosphorylationSKLSRNGSVFVRGQR
CHHCCCCCEEECCEE
18.8724453211
332PhosphorylationFVRGQRLSVEKATIR
EECCEECEEEEEEEC
30.3526824392
337PhosphorylationRLSVEKATIRPAKSM
ECEEEEEEECCCCCC
28.6925619855
343PhosphorylationATIRPAKSMDSLCSV
EEECCCCCCCCCCCC
29.9025521595
344OxidationTIRPAKSMDSLCSVP
EECCCCCCCCCCCCE
3.9017242355
346PhosphorylationRPAKSMDSLCSVPVE
CCCCCCCCCCCCEEC
23.7225521595
349PhosphorylationKSMDSLCSVPVEGKE
CCCCCCCCCEECCCC
34.4523984901
366PhosphorylationGNFSRTVTTGGFFIP
CCCCEEEEECCEEEE
21.0722942356
380PhosphorylationPATKMHASSTGSSCD
ECEEECCCCCCCCCC
17.4727742792
381PhosphorylationATKMHASSTGSSCDL
CEEECCCCCCCCCCC
37.2627742792
382PhosphorylationTKMHASSTGSSCDLS
EEECCCCCCCCCCCC
38.2927742792
384PhosphorylationMHASSTGSSCDLSKE
ECCCCCCCCCCCCCC
28.0726824392
385PhosphorylationHASSTGSSCDLSKEG
CCCCCCCCCCCCCCC
17.0020139300
389PhosphorylationTGSSCDLSKEGEWGQ
CCCCCCCCCCCCCCC
18.5327742792
446PhosphorylationLGMFYTSSDSPGKSV
HCEEECCCCCCCCEE
34.0226643407
448PhosphorylationMFYTSSDSPGKSVFT
EEECCCCCCCCEEEC
37.1826643407
464PhosphorylationSLFQMEPSPRHQRKA
HHHCCCCCHHHHHHC
22.6626824392
487PhosphorylationVSVPLRVSAVISTNS
EECCEEEEEEEECCC
15.4725521595
491PhosphorylationLRVSAVISTNSTPCR
EEEEEEEECCCCCCC
18.2226643407
492PhosphorylationRVSAVISTNSTPCRT
EEEEEEECCCCCCCC
23.2826643407
494PhosphorylationSAVISTNSTPCRTPP
EEEEECCCCCCCCCC
33.5425521595
495PhosphorylationAVISTNSTPCRTPPK
EEEECCCCCCCCCCH
28.6026643407
499PhosphorylationTNSTPCRTPPKELQS
CCCCCCCCCCHHHHC
51.1426643407
561PhosphorylationVPGRAECSQSPPLDP
CCCCCCCCCCCCCCC
25.7930635358
563PhosphorylationGRAECSQSPPLDPGT
CCCCCCCCCCCCCCC
16.5227149854
570PhosphorylationSPPLDPGTQVEKKTL
CCCCCCCCCEEEEEE
34.5329233185
580PhosphorylationEKKTLHVSLGSQVSK
EEEEEEEECCCHHCH
19.1030635358
583PhosphorylationTLHVSLGSQVSKEAE
EEEEECCCHHCHHHH
32.4730635358
586PhosphorylationVSLGSQVSKEAEKRP
EECCCHHCHHHHHCH
19.6919367708
652PhosphorylationQELKIIESEEEFSSL
HHHHHHHCHHHHHCC
39.6427180971
657PhosphorylationIESEEEFSSLPPAAQ
HHCHHHHHCCCCHHC
33.9630635358
658PhosphorylationESEEEFSSLPPAAQK
HCHHHHHCCCCHHCC
50.6624453211
666PhosphorylationLPPAAQKTSPIPESS
CCCHHCCCCCCCCCC
27.8824723360
667PhosphorylationPPAAQKTSPIPESSP
CCHHCCCCCCCCCCC
28.0626824392
672PhosphorylationKTSPIPESSPAPFPF
CCCCCCCCCCCCCCC
35.9525619855
673PhosphorylationTSPIPESSPAPFPFP
CCCCCCCCCCCCCCC
24.3425619855
685PhosphorylationPFPEAPGSLPSSSAP
CCCCCCCCCCCCCCC
35.7325619855
688PhosphorylationEAPGSLPSSSAPREV
CCCCCCCCCCCCCCH
42.0725619855
689PhosphorylationAPGSLPSSSAPREVW
CCCCCCCCCCCCCHH
28.6925619855
690PhosphorylationPGSLPSSSAPREVWT
CCCCCCCCCCCCHHC
46.7825619855
751PhosphorylationMLLFEKVSSPARIEI
HHHHCCCCCCCEEEE
41.4929550500
752PhosphorylationLLFEKVSSPARIEIG
HHHCCCCCCCEEEEC
26.1029550500
765PhosphorylationIGGPRNLSPPLTPAP
ECCCCCCCCCCCCCC
28.2024925903
769PhosphorylationRNLSPPLTPAPPPPT
CCCCCCCCCCCCCCC
24.1524925903
776PhosphorylationTPAPPPPTPLEEEPE
CCCCCCCCCCCCCCC
46.4025619855
800PhosphorylationREDAARDSRTDVYTE
HHHHHHHCCCCCCCC
31.3725338131
814PhosphorylationEQPTPKESPGIPTPC
CCCCCCCCCCCCCCC
34.2525338131
829PhosphorylationQREEAIASPNEKQNA
CCHHHCCCCCHHHHH
23.3428285833
850PhosphorylationNKGPGLPSPTKEVDI
CCCCCCCCCCCEEEE
50.6924925903
852PhosphorylationGPGLPSPTKEVDIIP
CCCCCCCCCEEEECC
44.1424925903
935PhosphorylationRRLCHRPSLRQSHSL
HHHHCCCCCCCCCCC
35.8226824392
939PhosphorylationHRPSLRQSHSLDSKT
CCCCCCCCCCCCCCC
14.4923737553
941PhosphorylationPSLRQSHSLDSKTTG
CCCCCCCCCCCCCCC
38.8330352176
944PhosphorylationRQSHSLDSKTTGNSH
CCCCCCCCCCCCCCC
36.8830635358
959PhosphorylationWTLEAPFSSSCANLE
EEEECCCCCCCCCCC
21.9323984901
960PhosphorylationTLEAPFSSSCANLET
EEECCCCCCCCCCCC
29.8019060867
961PhosphorylationLEAPFSSSCANLETE
EECCCCCCCCCCCCC
18.9522817900
1054PhosphorylationSDVPGPDSSKESSPR
CCCCCCCCCCCCCCC
46.5829550500
1055PhosphorylationDVPGPDSSKESSPRA
CCCCCCCCCCCCCCC
48.0729550500
1058PhosphorylationGPDSSKESSPRAQDS
CCCCCCCCCCCCCCC
49.7530635358
1059PhosphorylationPDSSKESSPRAQDST
CCCCCCCCCCCCCCC
21.3530635358
1092PhosphorylationSKGKHRPSSLNLDSA
CCCCCCCCCCCCCCC
47.6225521595
1093PhosphorylationKGKHRPSSLNLDSAT
CCCCCCCCCCCCCCC
24.7825521595
1098PhosphorylationPSSLNLDSATPIADL
CCCCCCCCCCCHHHH
36.8919060867
1100PhosphorylationSLNLDSATPIADLFR
CCCCCCCCCHHHHHH
21.1225367039
1115PhosphorylationLENGAPFSSPGIELS
CCCCCCCCCCCEEHH
34.2724719451
1116PhosphorylationENGAPFSSPGIELSE
CCCCCCCCCCEEHHH
27.7626824392
1144PhosphorylationCKAAPWNSQDTQDLD
CCCCCCCCCCCCCCC
26.0924719451
1147PhosphorylationAPWNSQDTQDLDIVA
CCCCCCCCCCCCEEE
19.1523567750
1163PhosphorylationTLTGRRNSAPVSVSA
HHCCCCCCCCCCHHH
31.9425521595
1167PhosphorylationRRNSAPVSVSAVRTS
CCCCCCCCHHHHHHH
14.8625619855
1169PhosphorylationNSAPVSVSAVRTSFM
CCCCCCHHHHHHHHH
17.3423684622
1206PhosphorylationQPLPSQSTGEGGAQP
CCCCCCCCCCCCCCC
31.4525338131
1223PhosphorylationRSQEEPGSTPEIPQK
CCCCCCCCCCCCCCC
52.0530635358
1224PhosphorylationSQEEPGSTPEIPQKS
CCCCCCCCCCCCCCC
30.7530635358
1231PhosphorylationTPEIPQKSTKDDSPS
CCCCCCCCCCCCCCH
35.1330635358
1232PhosphorylationPEIPQKSTKDDSPSS
CCCCCCCCCCCCCHH
45.5930635358
1236PhosphorylationQKSTKDDSPSSLGSP
CCCCCCCCCHHCCCC
36.4925521595
1238PhosphorylationSTKDDSPSSLGSPEE
CCCCCCCHHCCCCCH
41.9927742792
1239PhosphorylationTKDDSPSSLGSPEEE
CCCCCCHHCCCCCHH
39.8827742792
1242PhosphorylationDSPSSLGSPEEEQPK
CCCHHCCCCCHHCCC
34.1425521595
1252PhosphorylationEEQPKQETGASASRR
HHCCCCCCCCCHHHH
35.2427742792
1255PhosphorylationPKQETGASASRRQAS
CCCCCCCCHHHHHHE
28.2827742792
1257PhosphorylationQETGASASRRQASIT
CCCCCCHHHHHHEEE
26.0427742792
1296PhosphorylationVVQCRKRTSETEPSG
HHHHHHCCCCCCCCC
33.6729550500
1297PhosphorylationVQCRKRTSETEPSGD
HHHHHCCCCCCCCCC
46.7029550500
1299PhosphorylationCRKRTSETEPSGDNL
HHHCCCCCCCCCCCC
53.6229550500
1324PhosphorylationGPKAFHRSRPGRPQS
CCCCCCCCCCCCCCE
33.9726160508
1331PhosphorylationSRPGRPQSLILFPIM
CCCCCCCEEEEEEEH
21.7626824392
1344PhosphorylationIMDHLPSSPTVIDSK
EHHCCCCCCEEECCE
23.7329514104
1355PhosphorylationIDSKVLLSPIRSPTQ
ECCEEECCCCCCCCC
17.7027180971
1359PhosphorylationVLLSPIRSPTQTVSP
EECCCCCCCCCCCCC
32.7826643407
1361PhosphorylationLSPIRSPTQTVSPGL
CCCCCCCCCCCCCCC
37.8126643407
1363PhosphorylationPIRSPTQTVSPGLLC
CCCCCCCCCCCCCCC
25.9823649490
1365PhosphorylationRSPTQTVSPGLLCGE
CCCCCCCCCCCCCHH
19.3523649490
1407PhosphorylationETSTSCFYQPQRRSV
EECCCCCCCCCCCEE
24.5029514104
1413PhosphorylationFYQPQRRSVILDGRS
CCCCCCCEEEEECCC
18.7225521595

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
769TPhosphorylationKinaseMAPK3P27361
GPS
776TPhosphorylationKinaseGSK3AP49840
PSP
776TPhosphorylationKinaseGSK3BP49841
PSP
776TPhosphorylationKinaseMAPK3P27361
GPS
776TPhosphorylationKinaseGSK-FAMILY-GPS
776TPhosphorylationKinaseGSK3-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
776TPhosphorylation

16024771

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 RHG31_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ITSN1_MOUSEItsn1physical
11744688

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RHG31_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-1163, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1092 AND SER-1093, ANDMASS SPECTROMETRY.
"Glycogen synthase kinase-3 phosphorylates CdGAP at a consensus ERK 1regulatory site.";
Danek E.I., Tcherkezian J., Triki I., Meriane M., Lamarche-Vane N.;
J. Biol. Chem. 282:3624-3631(2007).
Cited for: PHOSPHORYLATION AT THR-776, AND INDUCTION BY SERUM.
"Extracellular signal-regulated kinase 1 interacts with andphosphorylates CdGAP at an important regulatory site.";
Tcherkezian J., Danek E.I., Jenna S., Triki I., Lamarche-Vane N.;
Mol. Cell. Biol. 25:6314-6329(2005).
Cited for: IDENTIFICATION, AND PHOSPHORYLATION AT THR-776.

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