GMIP_HUMAN - dbPTM
GMIP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GMIP_HUMAN
UniProt AC Q9P107
Protein Name GEM-interacting protein
Gene Name GMIP
Organism Homo sapiens (Human).
Sequence Length 970
Subcellular Localization
Protein Description Stimulates, in vitro and in vivo, the GTPase activity of RhoA..
Protein Sequence MDAAEPGLPPGPEGRKRYSDIFRSLDNLEISLGNVTLEMLAGDPLLSEDPEPDKTPTATVTNEASCWSGPSPEGPVPLTGEELDLRLIRTKGGVDAALEYAKTWSRYAKELLAWTEKRASYELEFAKSTMKIAEAGKVSIQQQSHMPLQYIYTLFLEHDLSLGTLAMETVAQQKRDYYQPLAAKRTEIEKWRKEFKEQWMKEQKRMNEAVQALRRAQLQYVQRSEDLRARSQGSPEDSAPQASPGPSKQQERRRRSREEAQAKAQEAEALYQACVREANARQQDLEIAKQRIVSHVRKLVFQGDEVLRRVTLSLFGLRGAQAERGPRAFAALAECCAPFEPGQRYQEFVRALRPEAPPPPPPAFSFQEFLPSLNSSPLDIRKKLSGPLPPRLDENSAEPGPWEDPGTGWRWQGTPGPTPGSDVDSVGGGSESRSLDSPTSSPGAGTRQLVKASSTGTESSDDFEERDPDLGDGLENGLGSPFGKWTLSSAAQTHQLRRLRGPAKCRECEAFMVSGTECEECFLTCHKRCLETLLILCGHRRLPARTPLFGVDFLQLPRDFPEEVPFVVTKCTAEIEHRALDVQGIYRVSGSRVRVERLCQAFENGRALVELSGNSPHDVSSVLKRFLQELTEPVIPFHLYDAFISLAKTLHADPGDDPGTPSPSPEVIRSLKTLLVQLPDSNYNTLRHLVAHLFRVAARFMENKMSANNLGIVFGPTLLRPPDGPRAASAIPVTCLLDSGHQAQLVEFLIVHYEQIFGMDELPQATEPPPQDSSPAPGPLTTSSQPPPPHLDPDSQPPVLASDPGPDPQHHSTLEQHPTATPTEIPTPQSDQREDVAEDTKDGGGEVSSQGPEDSLLGTQSRGHFSRQPVKYPRGGVRPVTHQLSSLALVASKLCEETPITSVPRGSLRGRGPSPAAASPEGSPLRRTPLPKHFEITQETARLLSKLDSEAVPRATCCPDVQPEEAEDHL
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
18PhosphorylationGPEGRKRYSDIFRSL
CCCHHHHHHHHHHHH		17.4626074081
19PhosphorylationPEGRKRYSDIFRSLD
CCHHHHHHHHHHHHC		28.4122617229
71PhosphorylationASCWSGPSPEGPVPL
CCCCCCCCCCCCCCC		38.8215345747
91UbiquitinationDLRLIRTKGGVDAAL
EEEHHHHCCCHHHHH		43.76-
91UbiquitinationDLRLIRTKGGVDAAL
EEEHHHHCCCHHHHH		43.76-
100PhosphorylationGVDAALEYAKTWSRY
CHHHHHHHHHHHHHH		17.78-
103PhosphorylationAALEYAKTWSRYAKE
HHHHHHHHHHHHHHH		22.09-
117UbiquitinationELLAWTEKRASYELE
HHHHHHHHHHHHHHH		45.98-
117UbiquitinationELLAWTEKRASYELE
HHHHHHHHHHHHHHH		45.98-
129PhosphorylationELEFAKSTMKIAEAG
HHHHHHHHHHHHHHC		23.0628985074
177PhosphorylationVAQQKRDYYQPLAAK
HHHHCHHHHHHHHHH		14.1826552605
178PhosphorylationAQQKRDYYQPLAAKR
HHHCHHHHHHHHHHH		14.1426552605
184UbiquitinationYYQPLAAKRTEIEKW
HHHHHHHHHHHHHHH		55.00-
184UbiquitinationYYQPLAAKRTEIEKW
HHHHHHHHHHHHHHH		55.00-
196UbiquitinationEKWRKEFKEQWMKEQ
HHHHHHHHHHHHHHH		50.52-
196UbiquitinationEKWRKEFKEQWMKEQ
HHHHHHHHHHHHHHH		50.52-
224PhosphorylationQLQYVQRSEDLRARS
HHHHHHHHHHHHHHH		20.5521406692
231PhosphorylationSEDLRARSQGSPEDS
HHHHHHHHCCCCCCC		37.6023911959
234PhosphorylationLRARSQGSPEDSAPQ
HHHHHCCCCCCCCCC		19.9229255136
238PhosphorylationSQGSPEDSAPQASPG
HCCCCCCCCCCCCCC		39.9429255136
243PhosphorylationEDSAPQASPGPSKQQ
CCCCCCCCCCCHHHH		25.7419664994
247PhosphorylationPQASPGPSKQQERRR
CCCCCCCHHHHHHHH		49.3529255136
248UbiquitinationQASPGPSKQQERRRR
CCCCCCHHHHHHHHH		60.16-
248UbiquitinationQASPGPSKQQERRRR
CCCCCCHHHHHHHHH		60.16-
256PhosphorylationQQERRRRSREEAQAK
HHHHHHHHHHHHHHH		42.0828176443
263UbiquitinationSREEAQAKAQEAEAL
HHHHHHHHHHHHHHH		38.22-
271PhosphorylationAQEAEALYQACVREA
HHHHHHHHHHHHHHH		10.91-
289UbiquitinationQQDLEIAKQRIVSHV
HHHHHHHHHHHHHHH		45.85-
289UbiquitinationQQDLEIAKQRIVSHV
HHHHHHHHHHHHHHH		45.85-
289AcetylationQQDLEIAKQRIVSHV
HHHHHHHHHHHHHHH		45.8525953088
365PhosphorylationPPPPPAFSFQEFLPS
CCCCCCCCHHHHHHH		28.2928450419
372PhosphorylationSFQEFLPSLNSSPLD
CHHHHHHHCCCCCCC		42.1829496963
375PhosphorylationEFLPSLNSSPLDIRK
HHHHHCCCCCCCHHH		38.3328450419
376PhosphorylationFLPSLNSSPLDIRKK
HHHHCCCCCCCHHHH		28.5428464451
383UbiquitinationSPLDIRKKLSGPLPP
CCCCHHHHHCCCCCC		37.73-
385PhosphorylationLDIRKKLSGPLPPRL
CCHHHHHCCCCCCCC		47.4430108239
396PhosphorylationPPRLDENSAEPGPWE
CCCCCCCCCCCCCCC		31.7727251275
414PhosphorylationTGWRWQGTPGPTPGS
CCCCCCCCCCCCCCC		15.2421815630
418PhosphorylationWQGTPGPTPGSDVDS
CCCCCCCCCCCCCCC		46.3128450419
421PhosphorylationTPGPTPGSDVDSVGG
CCCCCCCCCCCCCCC		35.3528450419
425PhosphorylationTPGSDVDSVGGGSES
CCCCCCCCCCCCCCC		23.6228450419
430PhosphorylationVDSVGGGSESRSLDS
CCCCCCCCCCCCCCC		35.3630108239
432PhosphorylationSVGGGSESRSLDSPT
CCCCCCCCCCCCCCC		28.9430108239
434 (in isoform 2)Phosphorylation-45.8926434776
434PhosphorylationGGGSESRSLDSPTSS
CCCCCCCCCCCCCCC		45.8923911959
437 (in isoform 2)Phosphorylation-35.0626434776
437PhosphorylationSESRSLDSPTSSPGA
CCCCCCCCCCCCCCC		35.0625159151
439 (in isoform 2)Phosphorylation-45.8726434776
439PhosphorylationSRSLDSPTSSPGAGT
CCCCCCCCCCCCCCH		45.8730278072
440 (in isoform 2)Phosphorylation-37.6126434776
440PhosphorylationRSLDSPTSSPGAGTR
CCCCCCCCCCCCCHH		37.6130278072
441PhosphorylationSLDSPTSSPGAGTRQ
CCCCCCCCCCCCHHH		29.8125159151
441 (in isoform 2)Phosphorylation-29.8126434776
446PhosphorylationTSSPGAGTRQLVKAS
CCCCCCCHHHEEEHH		18.0828102081
453PhosphorylationTRQLVKASSTGTESS
HHHEEEHHHCCCCCC		23.7928450419
454 (in isoform 2)Phosphorylation-35.4028102081
454PhosphorylationRQLVKASSTGTESSD
HHEEEHHHCCCCCCC		35.4028450419
455PhosphorylationQLVKASSTGTESSDD
HEEEHHHCCCCCCCC		45.7028450419
457PhosphorylationVKASSTGTESSDDFE
EEHHHCCCCCCCCHH		32.5528464451
459PhosphorylationASSTGTESSDDFEER
HHHCCCCCCCCHHHH		38.6222617229
460PhosphorylationSSTGTESSDDFEERD
HHCCCCCCCCHHHHC		34.6622115753
480PhosphorylationGLENGLGSPFGKWTL
CHHCCCCCCCCCEEC		23.3021815630
486PhosphorylationGSPFGKWTLSSAAQT
CCCCCCEECCHHHHH		21.90-
488PhosphorylationPFGKWTLSSAAQTHQ
CCCCEECCHHHHHHH		15.57-
586PhosphorylationALDVQGIYRVSGSRV
CCCCCEEEEECCCCH		16.2830576142
591PhosphorylationGIYRVSGSRVRVERL
EEEEECCCCHHHHHH		21.7930576142
598UbiquitinationSRVRVERLCQAFENG
CCHHHHHHHHHHHHC		1.2821890473
624UbiquitinationHDVSSVLKRFLQELT
HHHHHHHHHHHHHHH		38.6621890473
631PhosphorylationKRFLQELTEPVIPFH
HHHHHHHHCCCCCHH		37.17-
645PhosphorylationHLYDAFISLAKTLHA
HHHHHHHHHHHHHCC		18.80-
646UbiquitinationLYDAFISLAKTLHAD
HHHHHHHHHHHHCCC		4.9121890473
660PhosphorylationDPGDDPGTPSPSPEV
CCCCCCCCCCCCHHH		26.4423401153
662PhosphorylationGDDPGTPSPSPEVIR
CCCCCCCCCCHHHHH		37.5428450419
664PhosphorylationDPGTPSPSPEVIRSL
CCCCCCCCHHHHHHH		37.7230108239
672UbiquitinationPEVIRSLKTLLVQLP
HHHHHHHHHHHHCCC		38.0721890473
855PhosphorylationSSQGPEDSLLGTQSR
CCCCCCCCCCCCCCC		24.6728555341
862MethylationSLLGTQSRGHFSRQP
CCCCCCCCCCCCCCC		32.56-
874MethylationRQPVKYPRGGVRPVT
CCCCCCCCCCCCCCH		51.94-
878MethylationKYPRGGVRPVTHQLS
CCCCCCCCCCHHHHH		24.20-
881PhosphorylationRGGVRPVTHQLSSLA
CCCCCCCHHHHHHHH		13.4426434776
885PhosphorylationRPVTHQLSSLALVAS
CCCHHHHHHHHHHHH		19.4123401153
886PhosphorylationPVTHQLSSLALVASK
CCHHHHHHHHHHHHH		26.6723401153
892PhosphorylationSSLALVASKLCEETP
HHHHHHHHHHCCCCC		20.7724117733
898PhosphorylationASKLCEETPITSVPR
HHHHCCCCCCCCCCC		9.5630108239
901PhosphorylationLCEETPITSVPRGSL
HCCCCCCCCCCCCCC		25.5230108239
902PhosphorylationCEETPITSVPRGSLR
CCCCCCCCCCCCCCC		30.7430108239
905MethylationTPITSVPRGSLRGRG
CCCCCCCCCCCCCCC		45.22-
907PhosphorylationITSVPRGSLRGRGPS
CCCCCCCCCCCCCCC		19.0323401153
909MethylationSVPRGSLRGRGPSPA
CCCCCCCCCCCCCCC		34.16-
911MethylationPRGSLRGRGPSPAAA
CCCCCCCCCCCCCCC		47.63-
914PhosphorylationSLRGRGPSPAAASPE
CCCCCCCCCCCCCCC		29.9623401153
919PhosphorylationGPSPAAASPEGSPLR
CCCCCCCCCCCCCCC		20.8229255136
923PhosphorylationAAASPEGSPLRRTPL
CCCCCCCCCCCCCCC		21.0629255136
928PhosphorylationEGSPLRRTPLPKHFE
CCCCCCCCCCCCCHH		23.8125159151
946UbiquitinationETARLLSKLDSEAVP
HHHHHHHHCCCCCCC		57.17-
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 GMIP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GMIP_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 GMIP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GEM_HUMANGEMphysical
12093360
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 GMIP_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 SER-234; SER-437 ANDSER-914, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-434, ANDMASS SPECTROMETRY.
"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-231; SER-234; SER-434;SER-437; SER-441; SER-919 AND SER-923, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234; SER-243; SER-914;SER-919 AND SER-923, AND MASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-441, ANDMASS SPECTROMETRY.

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