CA198_HUMAN - dbPTM
CA198_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CA198_HUMAN
UniProt AC Q9H425
Protein Name Uncharacterized protein C1orf198
Gene Name C1orf198
Organism Homo sapiens (Human).
Sequence Length 327
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MASMAAAIAASRSAVMSGNRPLDDRERKRFTYFSSLSPMARKIMQDKEKIREKYGPEWARLPPAQQDEIIDRCLVGPRAPAPRDPGDSEELTRFPGLRGPTGQKVVRFGDEDLTWQDEHSAPFSWETKSQMEFSISALSIQEPSNGTAASEPRPLSKASQGSQALKSSQGSRSSSLDALGPTRKEEEASFWKINAERSRGEGPEAEFQSLTPSQIKSMEKGEKVLPPCYRQEPAPKDREAKVERPSTLRQEQRPLPNVSTERERPQPVQAFSSALHEAAPSQLEGKLPSPDVRQDDGEDTLFSEPKFAQVSSSNVVLKTGFDFLDNW
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------MASMAAAIA
------CHHHHHHHH		14.1722814378
3Phosphorylation-----MASMAAAIAA
-----CHHHHHHHHH		13.9921406692
11PhosphorylationMAAAIAASRSAVMSG
HHHHHHHHHHHHHCC		20.1121406692
13PhosphorylationAAIAASRSAVMSGNR
HHHHHHHHHHHCCCC		23.7922210691
17PhosphorylationASRSAVMSGNRPLDD
HHHHHHHCCCCCCCH		26.7325159151
31PhosphorylationDRERKRFTYFSSLSP
HHHHHHHHHHHHCCH		27.9123186163
32PhosphorylationRERKRFTYFSSLSPM
HHHHHHHHHHHCCHH		9.9626356563
34PhosphorylationRKRFTYFSSLSPMAR
HHHHHHHHHCCHHHH		21.6926356563
35PhosphorylationKRFTYFSSLSPMARK
HHHHHHHHCCHHHHH		23.9826356563
37PhosphorylationFTYFSSLSPMARKIM
HHHHHHCCHHHHHHH		17.9922617229
53UbiquitinationDKEKIREKYGPEWAR
CHHHHHHHHCHHHHH		45.73-
78MethylationDRCLVGPRAPAPRDP
HHHCCCCCCCCCCCC		47.47-
88PhosphorylationAPRDPGDSEELTRFP
CCCCCCCHHHHHCCC		38.6028348404
104UbiquitinationLRGPTGQKVVRFGDE
CCCCCCCEEEEECCC		44.00-
120PhosphorylationLTWQDEHSAPFSWET
CCCCCCCCCCCCEEC		35.2727251275
129PhosphorylationPFSWETKSQMEFSIS
CCCEECHHHEEEEEE		42.0229255136
134PhosphorylationTKSQMEFSISALSIQ
CHHHEEEEEEEEEEE		11.4329255136
136PhosphorylationSQMEFSISALSIQEP
HHEEEEEEEEEEECC		23.2029255136
139PhosphorylationEFSISALSIQEPSNG
EEEEEEEEEECCCCC		23.1829255136
150PhosphorylationPSNGTAASEPRPLSK
CCCCCCCCCCCCCCH		45.7418077418
162PhosphorylationLSKASQGSQALKSSQ
CCHHHHHHHHHHHCC		12.4928857561
166UbiquitinationSQGSQALKSSQGSRS
HHHHHHHHHCCCCCC		51.59-
167PhosphorylationQGSQALKSSQGSRSS
HHHHHHHHCCCCCCC		28.8323090842
168PhosphorylationGSQALKSSQGSRSSS
HHHHHHHCCCCCCCC		36.6523090842
171PhosphorylationALKSSQGSRSSSLDA
HHHHCCCCCCCCCHH		22.7325056879
173PhosphorylationKSSQGSRSSSLDALG
HHCCCCCCCCCHHHC		26.4430278072
174PhosphorylationSSQGSRSSSLDALGP
HCCCCCCCCCHHHCC		33.5330266825
175PhosphorylationSQGSRSSSLDALGPT
CCCCCCCCCHHHCCC		31.3628731282
182PhosphorylationSLDALGPTRKEEEAS
CCHHHCCCCHHHHHC		53.2023090842
184UbiquitinationDALGPTRKEEEASFW
HHHCCCCHHHHHCCE		72.46-
189PhosphorylationTRKEEEASFWKINAE
CCHHHHHCCEEECCC		34.6123403867
192UbiquitinationEEEASFWKINAERSR
HHHHCCEEECCCHHC		24.87-
198PhosphorylationWKINAERSRGEGPEA
EEECCCHHCCCCCHH		35.8229396449
209PhosphorylationGPEAEFQSLTPSQIK
CCHHHHHCCCHHHHH		39.2630266825
211PhosphorylationEAEFQSLTPSQIKSM
HHHHHCCCHHHHHHH		26.5830266825
213PhosphorylationEFQSLTPSQIKSMEK
HHHCCCHHHHHHHHC		39.0230266825
246PhosphorylationEAKVERPSTLRQEQR
CCCCCCCCHHCHHCC		46.4228060719
247PhosphorylationAKVERPSTLRQEQRP
CCCCCCCHHCHHCCC		28.7428060719
259PhosphorylationQRPLPNVSTERERPQ
CCCCCCCCCCCCCCC		31.0628348404
260PhosphorylationRPLPNVSTERERPQP
CCCCCCCCCCCCCCC		34.4828348404
272PhosphorylationPQPVQAFSSALHEAA
CCCHHHHHHHHHHHC		20.0926699800
273PhosphorylationQPVQAFSSALHEAAP
CCHHHHHHHHHHHCH		28.5326699800
281PhosphorylationALHEAAPSQLEGKLP
HHHHHCHHHHCCCCC		42.5430266825
289PhosphorylationQLEGKLPSPDVRQDD
HHCCCCCCCCCCCCC		44.1419664994
293MethylationKLPSPDVRQDDGEDT
CCCCCCCCCCCCCCC		41.41-
300PhosphorylationRQDDGEDTLFSEPKF
CCCCCCCCCCCCCCE		25.9628102081
303PhosphorylationDGEDTLFSEPKFAQV
CCCCCCCCCCCEEEE		56.9828102081
306UbiquitinationDTLFSEPKFAQVSSS
CCCCCCCCEEEECCC		49.6421906983
311O-linked_GlycosylationEPKFAQVSSSNVVLK
CCCEEEECCCCEEEE		18.9030379171
311PhosphorylationEPKFAQVSSSNVVLK
CCCEEEECCCCEEEE		18.9028857561
312PhosphorylationPKFAQVSSSNVVLKT
CCEEEECCCCEEEEC		27.3728555341
313PhosphorylationKFAQVSSSNVVLKTG
CEEEECCCCEEEECC		26.5728857561
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
37SPhosphorylationKinaseCDK2P24941
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CA198_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 CA198_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CA198_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 CA198_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 2-12, AND ACETYLATION AT ALA-2.
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-37, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASSSPECTROMETRY.

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