GTPB1_HUMAN - dbPTM
GTPB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GTPB1_HUMAN
UniProt AC O00178
Protein Name GTP-binding protein 1
Gene Name GTPBP1
Organism Homo sapiens (Human).
Sequence Length 669
Subcellular Localization Cytoplasm.
Protein Description Promotes degradation of target mRNA species. Plays a role in the regulation of circadian mRNA stability. Binds GTP and has GTPase activity (By similarity)..
Protein Sequence MATERSRSAMDSPVPASMFAPEPSSPGAARAAAAAARLHGGFDSDCSEDGEALNGEPELDLTSKLVLVSPTSEQYDSLLRQMWERMDEGCGETIYVIGQGSDGTEYGLSEADMEASYATVKSMAEQIEADVILLRERQEAGGRVRDYLVRKRVGDNDFLEVRVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEIESGRTSSVGNDILGFDSEGNVVNKPDSHGGSLEWTKICEKSTKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANILQETLKLLQRLLKSPGCRKIPVLVQSKDDVIVTASNFSSERMCPIFQISNVTGENLDLLKMFLNLLSPRTSYREEEPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPDPLGNFLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMVMVSPRLNPQASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMDKDCLRTGDKATVHFRFIKTPEYLHIDQRLVFREGRTKAVGTITKLLQTTNNSPMNSKPQQIKMQSTKKGPLTKRDEGGPSGGPAVGAPPPGDEASSVGAGQPAASSNLQPQPKPSSGGRRRGGQRHKVKSQGACVTPASGC
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
3Phosphorylation-----MATERSRSAM
-----CCCHHHHHCC		30.5426074081
6Phosphorylation--MATERSRSAMDSP
--CCCHHHHHCCCCC		25.1021712546
8PhosphorylationMATERSRSAMDSPVP
CCCHHHHHCCCCCCC		29.2329255136
12PhosphorylationRSRSAMDSPVPASMF
HHHHCCCCCCCHHHC		18.0829255136
17PhosphorylationMDSPVPASMFAPEPS
CCCCCCHHHCCCCCC		14.3623401153
24PhosphorylationSMFAPEPSSPGAARA
HHCCCCCCCHHHHHH		47.7229255136
25PhosphorylationMFAPEPSSPGAARAA
HCCCCCCCHHHHHHH		37.7629255136
44PhosphorylationRLHGGFDSDCSEDGE
HHCCCCCCCCCCCCC		37.9526846344
47PhosphorylationGGFDSDCSEDGEALN
CCCCCCCCCCCCHHC		43.6526846344
62PhosphorylationGEPELDLTSKLVLVS
CCCCCCCCCEEEEEC		24.3930266825
63PhosphorylationEPELDLTSKLVLVSP
CCCCCCCCEEEEECC		31.1530266825
69PhosphorylationTSKLVLVSPTSEQYD
CCEEEEECCCHHHHH		20.4929255136
71PhosphorylationKLVLVSPTSEQYDSL
EEEEECCCHHHHHHH		37.0729255136
72PhosphorylationLVLVSPTSEQYDSLL
EEEECCCHHHHHHHH		26.5329255136
77PhosphorylationPTSEQYDSLLRQMWE
CCHHHHHHHHHHHHH		25.1124719451
101PhosphorylationIYVIGQGSDGTEYGL
EEEEEECCCCCCCCC		25.6123403867
104PhosphorylationIGQGSDGTEYGLSEA
EEECCCCCCCCCCHH		30.9023403867
109PhosphorylationDGTEYGLSEADMEAS
CCCCCCCCHHHHHHH		26.7823403867
116PhosphorylationSEADMEASYATVKSM
CHHHHHHHHHHHHHH		11.2923403867
119O-linked_GlycosylationDMEASYATVKSMAEQ
HHHHHHHHHHHHHHH		21.89OGP
122O-linked_GlycosylationASYATVKSMAEQIEA
HHHHHHHHHHHHHCH		20.91OGP
174PhosphorylationGNVDAGKSTLLGVLT
ECCCCCCCEEEEEEC		24.30-
175PhosphorylationNVDAGKSTLLGVLTH
CCCCCCCEEEEEECC		29.50-
181PhosphorylationSTLLGVLTHGELDNG
CEEEEEECCCCCCCC		25.98-
205PhosphorylationRHKHEIESGRTSSVG
HCHHHHCCCCCCCCC		38.9621406692
208PhosphorylationHEIESGRTSSVGNDI
HHHCCCCCCCCCCCC		28.9527251275
209PhosphorylationEIESGRTSSVGNDIL
HHCCCCCCCCCCCCC		22.9727251275
210PhosphorylationIESGRTSSVGNDILG
HCCCCCCCCCCCCCC		33.1727251275
227UbiquitinationSEGNVVNKPDSHGGS
CCCCEECCCCCCCCC		38.2929967540
239UbiquitinationGGSLEWTKICEKSTK
CCCCEEHEEECCCCC		46.5729967540
258AcetylationIDLAGHEKYLKTTVF
EECCCCHHHHHHHHH		50.6519824831
259PhosphorylationDLAGHEKYLKTTVFG
ECCCCHHHHHHHHHC		15.50-
263PhosphorylationHEKYLKTTVFGMTGH
CHHHHHHHHHCCCCC		16.55-
330AcetylationKLLQRLLKSPGCRKI
HHHHHHHCCCCCCCC		60.2325953088
343PhosphorylationKIPVLVQSKDDVIVT
CCCEEEECCCCEEEE		30.4923663014
363UbiquitinationSERMCPIFQISNVTG
CCCCCCEEEEECCCC		2.9724816145
371UbiquitinationQISNVTGENLDLLKM
EEECCCCCCHHHHHH		45.3024816145
384PhosphorylationKMFLNLLSPRTSYRE
HHHHHHHCCCCCCCC		18.5918669648
433UbiquitinationTLLLGPDPLGNFLSI
EEEECCCCCHHHHHH		45.3524816145
456MethylationRMPVKEVRGGQTASF
CCCCEEECCCCCHHH		44.61-
460PhosphorylationKEVRGGQTASFALKK
EEECCCCCHHHHHHH		27.78-
462PhosphorylationVRGGQTASFALKKIK
ECCCCCHHHHHHHHH		17.9127251275
466AcetylationQTASFALKKIKRSSI
CCHHHHHHHHHHHHC		49.3625953088
472PhosphorylationLKKIKRSSIRKGMVM
HHHHHHHHCCCCEEE		30.3724719451
475UbiquitinationIKRSSIRKGMVMVSP
HHHHHCCCCEEEECC		50.0824816145
481PhosphorylationRKGMVMVSPRLNPQA
CCCEEEECCCCCCCC		6.0421712546
483UbiquitinationGMVMVSPRLNPQASW
CEEEECCCCCCCCCE		39.3224816145
517PhosphorylationQAMVHCGSIRQTATI
HHHEECCCHHHHEEE		21.7128857561
523PhosphorylationGSIRQTATILSMDKD
CCHHHHEEEEEECHH		26.32-
556MethylationEYLHIDQRLVFREGR
CEECCCCEEEECCCC		29.13-
565UbiquitinationVFREGRTKAVGTITK
EECCCCCCHHHHHHH		39.4529967540
569PhosphorylationGRTKAVGTITKLLQT
CCCCHHHHHHHHHHH		20.90-
576PhosphorylationTITKLLQTTNNSPMN
HHHHHHHHCCCCCCC		31.3130266825
577PhosphorylationITKLLQTTNNSPMNS
HHHHHHHCCCCCCCC		21.3130266825
580PhosphorylationLLQTTNNSPMNSKPQ
HHHHCCCCCCCCCCC		27.8222167270
584PhosphorylationTNNSPMNSKPQQIKM
CCCCCCCCCCCCCCC		39.1930266825
585UbiquitinationNNSPMNSKPQQIKMQ
CCCCCCCCCCCCCCC		41.6732015554
590UbiquitinationNSKPQQIKMQSTKKG
CCCCCCCCCCCCCCC		26.9229967540
600PhosphorylationSTKKGPLTKRDEGGP
CCCCCCCCCCCCCCC		27.4520860994
623PhosphorylationPPPGDEASSVGAGQP
CCCCCCCCCCCCCCC		24.4130177828
624PhosphorylationPPGDEASSVGAGQPA
CCCCCCCCCCCCCCC		31.4530177828
633PhosphorylationGAGQPAASSNLQPQP
CCCCCCCCCCCCCCC		23.1230177828
634PhosphorylationAGQPAASSNLQPQPK
CCCCCCCCCCCCCCC		36.5130177828
643PhosphorylationLQPQPKPSSGGRRRG
CCCCCCCCCCCCCCC		47.9830177828
644PhosphorylationQPQPKPSSGGRRRGG
CCCCCCCCCCCCCCC		54.5230177828
658PhosphorylationGQRHKVKSQGACVTP
CCCCCCCCCCCEECC		36.5128450419
664PhosphorylationKSQGACVTPASGC--
CCCCCEECCCCCC--		17.0225850435
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 GTPB1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GTPB1_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 GTPB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
IF2G_HUMANEIF2S3physical
26344197
PRC1_HUMANPRC1physical
26344197
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 GTPB1_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-44 AND SER-47, AND MASSSPECTROMETRY.
"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-12; SER-24; SER-25;SER-44; SER-47; SER-580 AND SER-584, 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-25; SER-44; SER-47 ANDSER-580, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-47, AND MASSSPECTROMETRY.

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