F102B_HUMAN - dbPTM
F102B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F102B_HUMAN
UniProt AC Q5T8I3
Protein Name Protein FAM102B
Gene Name FAM102B
Organism Homo sapiens (Human).
Sequence Length 360
Subcellular Localization
Protein Description
Protein Sequence MMKKKKFKFKVDFELEELSSVPFVNGVLFCKMRLLDGGSFTAESSREVVQANCVRWRKKFSFMCKMSASAATGILDPCIYRVSVRKELKGGKAYAKLGFADLNLAEFAGSGNTTRRCLLEGYDTKNTRQDNSILKVLISMQLMSGDPCFKTPPSTSMSIPIAGESESLQEDRKGGETLKVHLGIADLSAKSASVPDELGACGHSRTSSYASQQSKVSGYSTCHSRSSSFSELCHRRNTSVGSTSTGVESILEPCDEIEQKIAEPNLDTADKEDTASEKLSRCPVKQDSVESQLKRVDDTRVDADDIVEKILQSQDFSLDSSAEEEGLRLFVGPGGSTTFGSHHLPNRVGSGAYEQVVIKR
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
69PhosphorylationFMCKMSASAATGILD
HHHHHCHHHHHCCCC		15.8924114839
72PhosphorylationKMSASAATGILDPCI
HHCHHHHHCCCCCCE		25.1924114839
81DimethylationILDPCIYRVSVRKEL
CCCCCEEEEEEHHHH		8.36-
85DimethylationCIYRVSVRKELKGGK
CEEEEEEHHHHCCCC		21.16-
110PhosphorylationNLAEFAGSGNTTRRC
CHHHHCCCCCHHHCH		25.9917693683
122PhosphorylationRRCLLEGYDTKNTRQ
HCHHHCCCCCCCCCC		15.8622210691
124PhosphorylationCLLEGYDTKNTRQDN
HHHCCCCCCCCCCCC		20.0822210691
125UbiquitinationLLEGYDTKNTRQDNS
HHCCCCCCCCCCCCH		54.1229967540
127PhosphorylationEGYDTKNTRQDNSIL
CCCCCCCCCCCCHHH		31.1222210691
132PhosphorylationKNTRQDNSILKVLIS
CCCCCCCHHHHHHHH		37.2724719451
191PhosphorylationIADLSAKSASVPDEL
ECCCCCCCCCCCCCC		26.0328450419
193PhosphorylationDLSAKSASVPDELGA
CCCCCCCCCCCCCCC		41.0725159151
204PhosphorylationELGACGHSRTSSYAS
CCCCCCCCCCCCCCC		23.6525849741
208PhosphorylationCGHSRTSSYASQQSK
CCCCCCCCCCCCCCC		24.8928348404
209PhosphorylationGHSRTSSYASQQSKV
CCCCCCCCCCCCCCC		15.2727251275
219PhosphorylationQQSKVSGYSTCHSRS
CCCCCCCCCHHCCCC		8.0327642862
221PhosphorylationSKVSGYSTCHSRSSS
CCCCCCCHHCCCCCC		13.0224719451
224PhosphorylationSGYSTCHSRSSSFSE
CCCCHHCCCCCCHHH		35.6825849741
226PhosphorylationYSTCHSRSSSFSELC
CCHHCCCCCCHHHHH		33.0929116813
227PhosphorylationSTCHSRSSSFSELCH
CHHCCCCCCHHHHHH		34.0023898821
228PhosphorylationTCHSRSSSFSELCHR
HHCCCCCCHHHHHHH		33.7623401153
230PhosphorylationHSRSSSFSELCHRRN
CCCCCCHHHHHHHCC		31.4429978859
238PhosphorylationELCHRRNTSVGSTST
HHHHHCCCCCCCCCC		23.9927732954
239PhosphorylationLCHRRNTSVGSTSTG
HHHHCCCCCCCCCCC		28.2026657352
242PhosphorylationRRNTSVGSTSTGVES
HCCCCCCCCCCCHHH		19.6130576142
243PhosphorylationRNTSVGSTSTGVESI
CCCCCCCCCCCHHHH		25.1230576142
244PhosphorylationNTSVGSTSTGVESIL
CCCCCCCCCCHHHHH		25.5130576142
245PhosphorylationTSVGSTSTGVESILE
CCCCCCCCCHHHHHH		45.3925159151
249PhosphorylationSTSTGVESILEPCDE
CCCCCHHHHHHCCHH		30.0227732954
268PhosphorylationIAEPNLDTADKEDTA
HCCCCCCCCCCCCCH		39.6623401153
274PhosphorylationDTADKEDTASEKLSR
CCCCCCCCHHHHHHC		32.9225849741
276PhosphorylationADKEDTASEKLSRCP
CCCCCCHHHHHHCCC		37.0422617229
280PhosphorylationDTASEKLSRCPVKQD
CCHHHHHHCCCCCHH		42.7923186163
286PhosphorylationLSRCPVKQDSVESQL
HHCCCCCHHHHHHHH		48.7418669648
288PhosphorylationRCPVKQDSVESQLKR
CCCCCHHHHHHHHCC		25.8723401153
289PhosphorylationCPVKQDSVESQLKRV
CCCCHHHHHHHHCCC		12.6518669648
290PhosphorylationPVKQDSVESQLKRVD
CCCHHHHHHHHCCCC		36.4018669648
291PhosphorylationVKQDSVESQLKRVDD
CCHHHHHHHHCCCCC		38.3630266825
313PhosphorylationIVEKILQSQDFSLDS
HHHHHHHCCCCCCCC		28.4226074081
317PhosphorylationILQSQDFSLDSSAEE
HHHCCCCCCCCCCHH		39.2928102081
320PhosphorylationSQDFSLDSSAEEEGL
CCCCCCCCCCHHHCC		36.4230266825
321PhosphorylationQDFSLDSSAEEEGLR
CCCCCCCCCHHHCCE		39.0930266825
336PhosphorylationLFVGPGGSTTFGSHH
EEECCCCCCCCCCCC		30.1329449344
337PhosphorylationFVGPGGSTTFGSHHL
EECCCCCCCCCCCCC		29.4429449344
338PhosphorylationVGPGGSTTFGSHHLP
ECCCCCCCCCCCCCC		27.9129449344
341PhosphorylationGGSTTFGSHHLPNRV
CCCCCCCCCCCCCCC		11.9829449344
350PhosphorylationHLPNRVGSGAYEQVV
CCCCCCCCCCCEEEE		19.8621945579
353PhosphorylationNRVGSGAYEQVVIKR
CCCCCCCCEEEEEEC		15.4921945579
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 F102B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F102B_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 F102B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of F102B_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 F102B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-320 AND SER-321, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND MASSSPECTROMETRY.
"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-320 AND SER-321, ANDMASS SPECTROMETRY.

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