F117B_HUMAN - dbPTM
F117B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F117B_HUMAN
UniProt AC Q6P1L5
Protein Name Protein FAM117B
Gene Name FAM117B
Organism Homo sapiens (Human).
Sequence Length 589
Subcellular Localization
Protein Description
Protein Sequence MSQRVRRNGSPTPAGSLGGGAVATAGGPGSRLQPMRATVPFQLKQQQQQQHGSPTRSGGGGGGNNNGGCCGGASGPAGGGGGGGPRTASRSTSPTRGGGNAAARTSPTVATQTGASATSTRGTSPTRSAAPGARGSPPRPPPPPPLLGTVSSPSSSPTHLWTGEVSAAPPPARVRHRRRSPEQSRSSPEKRSPSAPVCKAGDKTRQPSSSPSSIIRRTSSLDTLAAPYLAGHWPRDSHGQAAPCMRDKATQTESAWAEEYSEKKKGSHKRSASWGSTDQLKEIAKLRQQLQRSKHSSRHHRDKERQSPFHGNHAAINQCQAPVPKSALIPVIPITKSTGSRFRNSVEGLNQEIEIIIKETGEKEEQLIPQDIPDGHRAPPPLVQRSSSTRSIDTQTPGGADRGSNNSSRSQSVSPTSFLTISNEGSEESPCSADDLLVDPRDKENGNNSPLPKYATSPKPNNSYMFKREPPEGCERVKVFEECSPKQLHEIPAFYCPDKNKVNFIPKSGSAFCLVSILKPLLPTPDLTLKGSGHSLTVTTGMTTTLLQPIAVASLSTNTEQDRVSRGTSTVMPSASLLPPPEPIEEAEG
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
10PhosphorylationQRVRRNGSPTPAGSL
CCCHHCCCCCCCCCC
29.2029255136
12PhosphorylationVRRNGSPTPAGSLGG
CHHCCCCCCCCCCCC
27.7130266825
16PhosphorylationGSPTPAGSLGGGAVA
CCCCCCCCCCCCCEE
26.4123927012
24PhosphorylationLGGGAVATAGGPGSR
CCCCCEECCCCCCCC
21.1623927012
30PhosphorylationATAGGPGSRLQPMRA
ECCCCCCCCCCCEEE
32.7123927012
38PhosphorylationRLQPMRATVPFQLKQ
CCCCEEECCCCCHHH
20.53-
44MethylationATVPFQLKQQQQQQH
ECCCCCHHHHHHHHC
34.97-
53PhosphorylationQQQQQHGSPTRSGGG
HHHHHCCCCCCCCCC
22.4525849741
55PhosphorylationQQQHGSPTRSGGGGG
HHHCCCCCCCCCCCC
38.8830619164
87PhosphorylationGGGGGPRTASRSTSP
CCCCCCCCCCCCCCC
31.9220068231
89PhosphorylationGGGPRTASRSTSPTR
CCCCCCCCCCCCCCC
26.5920068231
91PhosphorylationGPRTASRSTSPTRGG
CCCCCCCCCCCCCCC
30.6430576142
92PhosphorylationPRTASRSTSPTRGGG
CCCCCCCCCCCCCCC
37.3020068231
93PhosphorylationRTASRSTSPTRGGGN
CCCCCCCCCCCCCCC
26.0630576142
95PhosphorylationASRSTSPTRGGGNAA
CCCCCCCCCCCCCCC
41.5330576142
105PhosphorylationGGNAAARTSPTVATQ
CCCCCCCCCCCEEEC
34.0423927012
106PhosphorylationGNAAARTSPTVATQT
CCCCCCCCCCEEECC
17.0223927012
108PhosphorylationAAARTSPTVATQTGA
CCCCCCCCEEECCCC
23.6530266825
111PhosphorylationRTSPTVATQTGASAT
CCCCCEEECCCCCCC
23.4830266825
113PhosphorylationSPTVATQTGASATST
CCCEEECCCCCCCCC
30.2923403867
116PhosphorylationVATQTGASATSTRGT
EEECCCCCCCCCCCC
33.1623403867
118PhosphorylationTQTGASATSTRGTSP
ECCCCCCCCCCCCCC
28.3023403867
119PhosphorylationQTGASATSTRGTSPT
CCCCCCCCCCCCCCC
18.8023403867
120PhosphorylationTGASATSTRGTSPTR
CCCCCCCCCCCCCCC
28.8523403867
123PhosphorylationSATSTRGTSPTRSAA
CCCCCCCCCCCCCCC
28.3923090842
124PhosphorylationATSTRGTSPTRSAAP
CCCCCCCCCCCCCCC
27.3924719451
126PhosphorylationSTRGTSPTRSAAPGA
CCCCCCCCCCCCCCC
36.7023090842
128PhosphorylationRGTSPTRSAAPGARG
CCCCCCCCCCCCCCC
31.1228464451
136PhosphorylationAAPGARGSPPRPPPP
CCCCCCCCCCCCCCC
26.6128355574
149PhosphorylationPPPPLLGTVSSPSSS
CCCCCCCEECCCCCC
19.7225022875
151PhosphorylationPPLLGTVSSPSSSPT
CCCCCEECCCCCCCC
36.0528355574
152PhosphorylationPLLGTVSSPSSSPTH
CCCCEECCCCCCCCE
25.1925022875
154PhosphorylationLGTVSSPSSSPTHLW
CCEECCCCCCCCEEE
45.4528355574
155PhosphorylationGTVSSPSSSPTHLWT
CEECCCCCCCCEEEC
43.6630576142
156PhosphorylationTVSSPSSSPTHLWTG
EECCCCCCCCEEECC
37.8525022875
158PhosphorylationSSPSSSPTHLWTGEV
CCCCCCCCEEECCEE
31.3928464451
162PhosphorylationSSPTHLWTGEVSAAP
CCCCEEECCEECCCC
29.8030576142
166PhosphorylationHLWTGEVSAAPPPAR
EEECCEECCCCCCHH
17.8920873877
180PhosphorylationRVRHRRRSPEQSRSS
HHCCCCCCHHHHCCC
30.8630576142
184PhosphorylationRRRSPEQSRSSPEKR
CCCCHHHHCCCCCCC
32.2530576142
186PhosphorylationRSPEQSRSSPEKRSP
CCHHHHCCCCCCCCC
56.3329496963
187PhosphorylationSPEQSRSSPEKRSPS
CHHHHCCCCCCCCCC
35.6529496963
192PhosphorylationRSSPEKRSPSAPVCK
CCCCCCCCCCCCCCC
33.9830266825
194PhosphorylationSPEKRSPSAPVCKAG
CCCCCCCCCCCCCCC
46.5923401153
204PhosphorylationVCKAGDKTRQPSSSP
CCCCCCCCCCCCCCH
39.0023312004
208PhosphorylationGDKTRQPSSSPSSII
CCCCCCCCCCHHHHH
34.8022167270
209PhosphorylationDKTRQPSSSPSSIIR
CCCCCCCCCHHHHHH
53.6122167270
210PhosphorylationKTRQPSSSPSSIIRR
CCCCCCCCHHHHHHH
32.8922167270
212PhosphorylationRQPSSSPSSIIRRTS
CCCCCCHHHHHHHHC
35.8022167270
213PhosphorylationQPSSSPSSIIRRTSS
CCCCCHHHHHHHHCC
25.9722167270
218PhosphorylationPSSIIRRTSSLDTLA
HHHHHHHHCCCHHHH
16.9022617229
219PhosphorylationSSIIRRTSSLDTLAA
HHHHHHHCCCHHHHH
27.3924260401
220PhosphorylationSIIRRTSSLDTLAAP
HHHHHHCCCHHHHHH
29.6525159151
223PhosphorylationRRTSSLDTLAAPYLA
HHHCCCHHHHHHHHC
24.4821712546
228PhosphorylationLDTLAAPYLAGHWPR
CHHHHHHHHCCCCCC
12.4023403867
252PhosphorylationMRDKATQTESAWAEE
CCCCHHHCHHHHHHH
27.79-
261PhosphorylationSAWAEEYSEKKKGSH
HHHHHHHHHHCCCCC
46.34-
267PhosphorylationYSEKKKGSHKRSASW
HHHHCCCCCCCCCCC
34.41-
271PhosphorylationKKGSHKRSASWGSTD
CCCCCCCCCCCCCHH
31.3030266825
273PhosphorylationGSHKRSASWGSTDQL
CCCCCCCCCCCHHHH
32.9619664994
273 (in isoform 2)Phosphorylation-32.9622468782
276PhosphorylationKRSASWGSTDQLKEI
CCCCCCCCHHHHHHH
23.6630266825
277PhosphorylationRSASWGSTDQLKEIA
CCCCCCCHHHHHHHH
24.6730266825
307PhosphorylationHRDKERQSPFHGNHA
HHHHHHCCCCCCCHH
35.4425159151
335O-linked_GlycosylationLIPVIPITKSTGSRF
EEEEEEECCCCCHHH
17.3723301498
345PhosphorylationTGSRFRNSVEGLNQE
CCHHHHHHHHCHHHE
19.7922617229
386PhosphorylationPPPLVQRSSSTRSID
CCCCCCCCCCCCCCC
16.1425159151
387PhosphorylationPPLVQRSSSTRSIDT
CCCCCCCCCCCCCCC
37.6125159151
388PhosphorylationPLVQRSSSTRSIDTQ
CCCCCCCCCCCCCCC
29.1430576142
389PhosphorylationLVQRSSSTRSIDTQT
CCCCCCCCCCCCCCC
30.3130576142
391PhosphorylationQRSSSTRSIDTQTPG
CCCCCCCCCCCCCCC
25.5525159151
394PhosphorylationSSTRSIDTQTPGGAD
CCCCCCCCCCCCCCC
32.4530576142
396PhosphorylationTRSIDTQTPGGADRG
CCCCCCCCCCCCCCC
26.4529255136
404PhosphorylationPGGADRGSNNSSRSQ
CCCCCCCCCCCCCCC
33.4623663014
407PhosphorylationADRGSNNSSRSQSVS
CCCCCCCCCCCCCCC
31.2323663014
408PhosphorylationDRGSNNSSRSQSVSP
CCCCCCCCCCCCCCC
37.7723663014
410PhosphorylationGSNNSSRSQSVSPTS
CCCCCCCCCCCCCCC
28.8429978859
412PhosphorylationNNSSRSQSVSPTSFL
CCCCCCCCCCCCCEE
26.3028464451
414PhosphorylationSSRSQSVSPTSFLTI
CCCCCCCCCCCEEEE
27.9228102081
416PhosphorylationRSQSVSPTSFLTISN
CCCCCCCCCEEEECC
25.3028387310
417PhosphorylationSQSVSPTSFLTISNE
CCCCCCCCEEEECCC
22.9528464451
420PhosphorylationVSPTSFLTISNEGSE
CCCCCEEEECCCCCC
21.9828464451
422PhosphorylationPTSFLTISNEGSEES
CCCEEEECCCCCCCC
24.4829978859
426PhosphorylationLTISNEGSEESPCSA
EEECCCCCCCCCCCH
31.8229978859
429PhosphorylationSNEGSEESPCSADDL
CCCCCCCCCCCHHHC
27.4429978859
432PhosphorylationGSEESPCSADDLLVD
CCCCCCCCHHHCCCC
37.8129978859
449PhosphorylationDKENGNNSPLPKYAT
CCCCCCCCCCCCCCC
31.6423401153
454PhosphorylationNNSPLPKYATSPKPN
CCCCCCCCCCCCCCC
17.1121712546
456PhosphorylationSPLPKYATSPKPNNS
CCCCCCCCCCCCCCC
42.3325159151
457PhosphorylationPLPKYATSPKPNNSY
CCCCCCCCCCCCCCC
23.8225159151
463PhosphorylationTSPKPNNSYMFKREP
CCCCCCCCCCCCCCC
25.3128102081
464PhosphorylationSPKPNNSYMFKREPP
CCCCCCCCCCCCCCC
14.5426074081
467UbiquitinationPNNSYMFKREPPEGC
CCCCCCCCCCCCCCC
39.04-
478UbiquitinationPEGCERVKVFEECSP
CCCCCEEEEEECCCH
47.64-
484PhosphorylationVKVFEECSPKQLHEI
EEEEECCCHHHHHCC
38.1125159151
486UbiquitinationVFEECSPKQLHEIPA
EEECCCHHHHHCCCE
49.55-
499UbiquitinationPAFYCPDKNKVNFIP
CEEECCCCCCEEEEC
43.75-
501UbiquitinationFYCPDKNKVNFIPKS
EECCCCCCEEEECCC
44.27-
508PhosphorylationKVNFIPKSGSAFCLV
CEEEECCCCCCCHHH
32.4026074081
510PhosphorylationNFIPKSGSAFCLVSI
EEECCCCCCCHHHHH
25.8426074081
516PhosphorylationGSAFCLVSILKPLLP
CCCCHHHHHHHCCCC
14.8424719451
524PhosphorylationILKPLLPTPDLTLKG
HHHCCCCCCCEEECC
29.4226853621
532PhosphorylationPDLTLKGSGHSLTVT
CCEEECCCCCCEEEE
31.5722210691
543PhosphorylationLTVTTGMTTTLLQPI
EEEECCCCHHCCEEE
20.2722210691
568PhosphorylationQDRVSRGTSTVMPSA
CHHHCCCCCCCCCCH
21.80-
569PhosphorylationDRVSRGTSTVMPSAS
HHHCCCCCCCCCCHH
23.10-
574PhosphorylationGTSTVMPSASLLPPP
CCCCCCCCHHHCCCC
16.64-

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 F117B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F117B_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 F117B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TNKS1_HUMANTNKSphysical
28514442
DYR1B_HUMANDYRK1Bphysical
28514442
IMP1L_HUMANIMMP1Lphysical
28514442
TNKS2_HUMANTNKS2physical
28514442
DYR1A_HUMANDYRK1Aphysical
28514442
T22D2_HUMANTSC22D2physical
28514442
FNTB_HUMANFNTBphysical
28514442
T22D3_HUMANTSC22D3physical
28514442
PNMA2_HUMANPNMA2physical
28514442
NRBP_HUMANNRBP1physical
28514442
G3PT_HUMANGAPDHSphysical
28514442
A16A1_HUMANALDH16A1physical
28514442
FNTA_HUMANFNTAphysical
28514442
DYL1_HUMANDYNLL1physical
28514442
DYL1_HUMANDYNLL1physical
27173435
DYL2_HUMANDYNLL2physical
27173435
DCAF7_HUMANDCAF7physical
27173435

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 F117B_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-391, AND MASSSPECTROMETRY.
"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-219 AND SER-220, ANDMASS SPECTROMETRY.
"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 THR-218; SER-219 ANDSER-220, AND MASS SPECTROMETRY.

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