GPTC2_HUMAN - dbPTM
GPTC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPTC2_HUMAN
UniProt AC Q9NW75
Protein Name G patch domain-containing protein 2
Gene Name GPATCH2
Organism Homo sapiens (Human).
Sequence Length 528
Subcellular Localization Nucleus speckle . Nucleus, nucleolus .
Protein Description Enhances the ATPase activity of DHX15 in vitro..
Protein Sequence MFGAAGRQPIGAPAAGNSWHFSRTMEELVHDLVSALEESSEQARGGFAETGDHSRSISCPLKRQARKRRGRKRRSYNVHHPWETGHCLSEGSDSSLEEPSKDYRENHNNNKKDHSDSDDQMLVAKRRPSSNLNNNVRGKRPLWHESDFAVDNVGNRTLRRRRKVKRMAVDLPQDISNKRTMTQPPEGCRDQDMDSDRAYQYQEFTKNKVKKRKLKIIRQGPKIQDEGVVLESEETNQTNKDKMECEEQKVSDELMSESDSSSLSSTDAGLFTNDEGRQGDDEQSDWFYEKESGGACGITGVVPWWEKEDPTELDKNVPDPVFESILTGSFPLMSHPSRRGFQARLSRLHGMSSKNIKKSGGTPTSMVPIPGPVGNKRMVHFSPDSHHHDHWFSPGARTEHDQHQLLRDNRAERGHKKNCSVRTASRQTSMHLGSLCTGDIKRRRKAAPLPGPTTAGFVGENAQPILENNIGNRMLQNMGWTPGSGLGRDGKGISEPIQAMQRPKGLGLGFPLPKSTSATTTPNAGKSA
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
24PhosphorylationNSWHFSRTMEELVHD
CCCHHHCHHHHHHHH		27.9527732954
34PhosphorylationELVHDLVSALEESSE
HHHHHHHHHHHHCHH		34.1427732954
39PhosphorylationLVSALEESSEQARGG
HHHHHHHCHHHHCCC		29.7822617229
40PhosphorylationVSALEESSEQARGGF
HHHHHHCHHHHCCCC		36.6922617229
50PhosphorylationARGGFAETGDHSRSI
HCCCCCCCCCCCCCC		44.4729255136
54PhosphorylationFAETGDHSRSISCPL
CCCCCCCCCCCCCCH		32.2529255136
56PhosphorylationETGDHSRSISCPLKR
CCCCCCCCCCCCHHH		23.1325159151
58PhosphorylationGDHSRSISCPLKRQA
CCCCCCCCCCHHHHH		15.7827251275
75PhosphorylationRRGRKRRSYNVHHPW
HCCCCCCCCCCCCCC		25.7027732954
76PhosphorylationRGRKRRSYNVHHPWE
CCCCCCCCCCCCCCC		21.2827732954
84PhosphorylationNVHHPWETGHCLSEG
CCCCCCCCCCCCCCC		28.4923927012
89PhosphorylationWETGHCLSEGSDSSL
CCCCCCCCCCCCCCC		45.3523927012
92PhosphorylationGHCLSEGSDSSLEEP
CCCCCCCCCCCCCCC		30.2123927012
94PhosphorylationCLSEGSDSSLEEPSK
CCCCCCCCCCCCCCH		38.2223927012
95PhosphorylationLSEGSDSSLEEPSKD
CCCCCCCCCCCCCHH		44.8023927012
100PhosphorylationDSSLEEPSKDYRENH
CCCCCCCCHHHHHHC		41.2527732954
103PhosphorylationLEEPSKDYRENHNNN
CCCCCHHHHHHCCCC		24.4624144214
115PhosphorylationNNNKKDHSDSDDQML
CCCCCCCCCCHHHHH		49.2829255136
117PhosphorylationNKKDHSDSDDQMLVA
CCCCCCCCHHHHHHH		46.2129255136
129PhosphorylationLVAKRRPSSNLNNNV
HHHHCCCCCCCCCCC		30.0123927012
130PhosphorylationVAKRRPSSNLNNNVR
HHHCCCCCCCCCCCC		48.2820873877
139MethylationLNNNVRGKRPLWHES
CCCCCCCCCCCCCCC		40.03-
146PhosphorylationKRPLWHESDFAVDNV
CCCCCCCCCCCCCCC		25.7422617229
157PhosphorylationVDNVGNRTLRRRRKV
CCCCCCHHHHHHHHH		28.7230576142
176PhosphorylationVDLPQDISNKRTMTQ
CCCCCCCCCCCCCCC		44.5928555341
178AcetylationLPQDISNKRTMTQPP
CCCCCCCCCCCCCCC		42.3219810361
195PhosphorylationCRDQDMDSDRAYQYQ
CCCCCCCCHHHHHHH		23.5123401153
199PhosphorylationDMDSDRAYQYQEFTK
CCCCHHHHHHHHHHH		14.5130108239
201PhosphorylationDSDRAYQYQEFTKNK
CCHHHHHHHHHHHHH		9.4228111955
205PhosphorylationAYQYQEFTKNKVKKR
HHHHHHHHHHHHHHH		32.7127642862
206UbiquitinationYQYQEFTKNKVKKRK
HHHHHHHHHHHHHHH		61.1527667366
232PhosphorylationDEGVVLESEETNQTN
CCCEEECCCCCCCCC		36.25-
235PhosphorylationVVLESEETNQTNKDK
EEECCCCCCCCCHHH		28.68-
238PhosphorylationESEETNQTNKDKMEC
CCCCCCCCCHHHHHH		46.43-
284PhosphorylationRQGDDEQSDWFYEKE
CCCCCCCCCCEEECC		34.4625159151
288PhosphorylationDEQSDWFYEKESGGA
CCCCCCEEECCCCCC		23.1026552605
307UbiquitinationGVVPWWEKEDPTELD
EECCCCCCCCCCCCC		54.4129967540
327PhosphorylationPVFESILTGSFPLMS
HHHHHHHCCCCCCCC		29.1627080861
329PhosphorylationFESILTGSFPLMSHP
HHHHHCCCCCCCCCC		20.6027080861
334PhosphorylationTGSFPLMSHPSRRGF
CCCCCCCCCCCHHHH		39.6727080861
337PhosphorylationFPLMSHPSRRGFQAR
CCCCCCCCHHHHHHH		29.2327080861
352PhosphorylationLSRLHGMSSKNIKKS
HHHHHCCCCCCCCCC		42.6323403867
358AcetylationMSSKNIKKSGGTPTS
CCCCCCCCCCCCCCC		51.0019829153
359PhosphorylationSSKNIKKSGGTPTSM
CCCCCCCCCCCCCCE		37.1422199227
359 (in isoform 2)Phosphorylation-37.1425159151
362PhosphorylationNIKKSGGTPTSMVPI
CCCCCCCCCCCEEEC		27.2421815630
362 (in isoform 2)Phosphorylation-27.2425159151
364PhosphorylationKKSGGTPTSMVPIPG
CCCCCCCCCEEECCC		29.3229978859
365PhosphorylationKSGGTPTSMVPIPGP
CCCCCCCCEEECCCC		20.9828348404
428PhosphorylationVRTASRQTSMHLGSL
CHHCCCCCCHHHHHH		27.2327251275
429PhosphorylationRTASRQTSMHLGSLC
HHCCCCCCHHHHHHC		8.8928555341
515PhosphorylationLGFPLPKSTSATTTP
CCCCCCCCCCCCCCC		26.1723401153
516PhosphorylationGFPLPKSTSATTTPN
CCCCCCCCCCCCCCC		28.6223401153
517PhosphorylationFPLPKSTSATTTPNA
CCCCCCCCCCCCCCC		30.6123401153
519PhosphorylationLPKSTSATTTPNAGK
CCCCCCCCCCCCCCC		30.8523401153
520PhosphorylationPKSTSATTTPNAGKS
CCCCCCCCCCCCCCC		39.7223401153
521PhosphorylationKSTSATTTPNAGKSA
CCCCCCCCCCCCCCC		15.3623401153
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 GPTC2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GPTC2_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 GPTC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GPTC2_HUMAN !!
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 GPTC2_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-115; SER-117 ANDSER-195, 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-115; SER-117 ANDSER-195, 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-115 AND SER-117, ANDMASS 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 THR-50, AND MASSSPECTROMETRY.

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