FA83D_HUMAN - dbPTM
FA83D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FA83D_HUMAN
UniProt AC Q9H4H8
Protein Name Protein FAM83D {ECO:0000305}
Gene Name FAM83D {ECO:0000312|HGNC:HGNC:16122}
Organism Homo sapiens (Human).
Sequence Length 585
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole . Primarily cytoplasmic during interphase, but at prophase, associates with spindle microtubules, with a clear concentration toward the spindle poles. It persists on s
Protein Description Probable proto-oncogene that regulates cell proliferation, growth, migration and epithelial to mesenchymal transition. Through the degradation of FBXW7, may act indirectly on the expression and downstream signaling of MTOR, JUN and MYC. [PubMed: 24344117 May play also a role in cell proliferation through activation of the ERK1/ERK2 signaling cascade]
Protein Sequence MALLSEGLDEVPAACLSPCGPPNPTELFSESRRLALEELVAGGPEAFAAFLRRERLARFLNPDEVHAILRAAERPGEEGAAAAAAAEDSFGSSHDCSSGTYFPEQSDLEPPLLELGWPAFYQGAYRGATRVETHFQPRGAGEGGPYGCKDALRQQLRSAREVIAVVMDVFTDIDIFRDLQEICRKQGVAVYILLDQALLSQFLDMCMDLKVHPEQEKLMTVRTITGNIYYARSGTKIIGKVHEKFTLIDGIRVATGSYSFTWTDGKLNSSNLVILSGQVVEHFDLEFRILYAQSKPISPKLLSHFQSSNKFDHLTNRKPQSKELTLGNLLRMRLARLSSTPRKADLDPEMPAEGKAERKPHDCESSTVSEEDYFSSHRDELQSRKAIDAATQTEPGEEMPGLSVSEVGTQTSITTACAGTQTAVITRIASSQTTIWSRSTTTQTDMDENILFPRGTQSTEGSPVSKMSVSRSSSLKSSSSVSSQGSVASSTGSPASIRTTDFHNPGYPKYLGTPHLELYLSDSLRNLNKERQFHFAGIRSRLNHMLAMLSRRTLFTENHLGLHSGNFSRVNLLAVRDVALYPSYQ
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
5Phosphorylation---MALLSEGLDEVP
---CCCCCCCCCCCC		30.3924532841
17PhosphorylationEVPAACLSPCGPPNP
CCCHHHCCCCCCCCH		20.3025159151
25PhosphorylationPCGPPNPTELFSESR
CCCCCCHHHHCCHHH		52.5426270265
29PhosphorylationPNPTELFSESRRLAL
CCHHHHCCHHHHHHH		47.49-
31PhosphorylationPTELFSESRRLALEE
HHHHCCHHHHHHHHH		22.85-
47PhosphorylationVAGGPEAFAAFLRRE
HHCCHHHHHHHHHHH		4.8619007248
51UbiquitinationPEAFAAFLRRERLAR
HHHHHHHHHHHHHHH		4.2927667366
70UbiquitinationDEVHAILRAAERPGE
HHHHHHHHHHHCCCH		26.1627667366
74UbiquitinationAILRAAERPGEEGAA
HHHHHHHCCCHHHHH		39.5327667366
129UbiquitinationQGAYRGATRVETHFQ
CCCCCCCCEEEEECC		37.7622817900
134UbiquitinationGATRVETHFQPRGAG
CCCEEEEECCCCCCC		13.0722817900
144UbiquitinationPRGAGEGGPYGCKDA
CCCCCCCCCCCHHHH		14.1421890473
146PhosphorylationGAGEGGPYGCKDALR
CCCCCCCCCHHHHHH		38.1318083107
149UbiquitinationEGGPYGCKDALRQQL
CCCCCCHHHHHHHHH		41.4921963094
177UbiquitinationFTDIDIFRDLQEICR
HCCCHHHHHHHHHHH		44.0222817900
179UbiquitinationDIDIFRDLQEICRKQ
CCHHHHHHHHHHHHC		4.25-
189UbiquitinationICRKQGVAVYILLDQ
HHHHCCCHHHHHCCH		8.6721963094
193UbiquitinationQGVAVYILLDQALLS
CCCHHHHHCCHHHHH		2.0621963094
217UbiquitinationKVHPEQEKLMTVRTI
CCCHHHHHCEEEEEE		43.1627667366
229PhosphorylationRTITGNIYYARSGTK
EEECCCEEEECCCCE		8.6225839225
230PhosphorylationTITGNIYYARSGTKI
EECCCEEEECCCCEE		7.5529496907
235PhosphorylationIYYARSGTKIIGKVH
EEEECCCCEEEEEEC		21.95-
236UbiquitinationYYARSGTKIIGKVHE
EEECCCCEEEEEECC		35.5327667366
240AcetylationSGTKIIGKVHEKFTL
CCCEEEEEECCCEEE		29.9722369047
240UbiquitinationSGTKIIGKVHEKFTL
CCCEEEEEECCCEEE		29.9727667366
247UbiquitinationKVHEKFTLIDGIRVA
EECCCEEEECCEEEE		3.65-
270UbiquitinationTDGKLNSSNLVILSG
CCCCCCCCCEEEEEC		32.86-
279 (in isoform 2)Ubiquitination-6.6021890473
291PhosphorylationDLEFRILYAQSKPIS
CEEEEEEEECCCCCC		10.5419664995
294PhosphorylationFRILYAQSKPISPKL
EEEEEECCCCCCHHH		32.0229978859
294 (in isoform 2)Ubiquitination-32.0221890473
295UbiquitinationRILYAQSKPISPKLL
EEEEECCCCCCHHHH		34.0022817900
298PhosphorylationYAQSKPISPKLLSHF
EECCCCCCHHHHHHH		25.2229978859
300UbiquitinationQSKPISPKLLSHFQS
CCCCCCHHHHHHHHH		56.0921963094
303PhosphorylationPISPKLLSHFQSSNK
CCCHHHHHHHHHCCC		32.4629978859
307PhosphorylationKLLSHFQSSNKFDHL
HHHHHHHHCCCCCHH		34.6329978859
308PhosphorylationLLSHFQSSNKFDHLT
HHHHHHHCCCCCHHC		33.0029978859
310UbiquitinationSHFQSSNKFDHLTNR
HHHHHCCCCCHHCCC		54.8621963094
315PhosphorylationSNKFDHLTNRKPQSK
CCCCCHHCCCCCCCC		29.5628555341
318UbiquitinationFDHLTNRKPQSKELT
CCHHCCCCCCCCCCC		49.8629967540
321PhosphorylationLTNRKPQSKELTLGN
HCCCCCCCCCCCHHH		36.3019664995
322UbiquitinationTNRKPQSKELTLGNL
CCCCCCCCCCCHHHH		52.0429967540
325PhosphorylationKPQSKELTLGNLLRM
CCCCCCCCHHHHHHH		33.4427174698
325UbiquitinationKPQSKELTLGNLLRM
CCCCCCCCHHHHHHH		33.44-
325 (in isoform 1)Ubiquitination-33.4421890473
327 (in isoform 2)Ubiquitination-19.9421890473
328PhosphorylationSKELTLGNLLRMRLA
CCCCCHHHHHHHHHH		38.73-
338PhosphorylationRMRLARLSSTPRKAD
HHHHHHHCCCCCCCC		26.9825849741
339PhosphorylationMRLARLSSTPRKADL
HHHHHHCCCCCCCCC		47.2030576142
339 (in isoform 2)Ubiquitination-47.2021890473
340PhosphorylationRLARLSSTPRKADLD
HHHHHCCCCCCCCCC		24.6025849741
340UbiquitinationRLARLSSTPRKADLD
HHHHHCCCCCCCCCC		24.60-
340 (in isoform 1)Ubiquitination-24.6021890473
343AcetylationRLSSTPRKADLDPEM
HHCCCCCCCCCCCCC		47.6725953088
343UbiquitinationRLSSTPRKADLDPEM
HHCCCCCCCCCCCCC		47.6721906983
348UbiquitinationPRKADLDPEMPAEGK
CCCCCCCCCCCCCCC		47.27-
351PhosphorylationADLDPEMPAEGKAER
CCCCCCCCCCCCCCC		26.04-
352UbiquitinationDLDPEMPAEGKAERK
CCCCCCCCCCCCCCC		36.54-
355UbiquitinationPEMPAEGKAERKPHD
CCCCCCCCCCCCCCC		38.2821906983
359UbiquitinationAEGKAERKPHDCESS
CCCCCCCCCCCCCCC		37.9021963094
365PhosphorylationRKPHDCESSTVSEED
CCCCCCCCCCCCHHH		37.3323927012
366PhosphorylationKPHDCESSTVSEEDY
CCCCCCCCCCCHHHH		15.5523927012
367PhosphorylationPHDCESSTVSEEDYF
CCCCCCCCCCHHHHH		37.0123927012
368PhosphorylationHDCESSTVSEEDYFS
CCCCCCCCCHHHHHH		7.9724719451
369PhosphorylationDCESSTVSEEDYFSS
CCCCCCCCHHHHHHH		35.0423927012
370PhosphorylationCESSTVSEEDYFSSH
CCCCCCCHHHHHHHC		51.0220068231
373PhosphorylationSTVSEEDYFSSHRDE
CCCCHHHHHHHCHHH		14.5123663014
373UbiquitinationSTVSEEDYFSSHRDE
CCCCHHHHHHHCHHH		14.51-
373 (in isoform 1)Ubiquitination-14.5121890473
375PhosphorylationVSEEDYFSSHRDELQ
CCHHHHHHHCHHHHH		21.0023663014
376PhosphorylationSEEDYFSSHRDELQS
CHHHHHHHCHHHHHH		16.7923663014
383PhosphorylationSHRDELQSRKAIDAA
HCHHHHHHHHHHHHH		48.6630576142
385UbiquitinationRDELQSRKAIDAATQ
HHHHHHHHHHHHHHC		55.74-
385 (in isoform 1)Ubiquitination-55.7421890473
389UbiquitinationQSRKAIDAATQTEPG
HHHHHHHHHHCCCCC		13.29-
395PhosphorylationDAATQTEPGEEMPGL
HHHHCCCCCCCCCCC		59.9024719451
396PhosphorylationAATQTEPGEEMPGLS
HHHCCCCCCCCCCCE		36.9524719451
397PhosphorylationATQTEPGEEMPGLSV
HHCCCCCCCCCCCEE		62.9324719451
399PhosphorylationQTEPGEEMPGLSVSE
CCCCCCCCCCCEECC		2.5124719451
430PhosphorylationAVITRIASSQTTIWS
EEEEEEHHCCCEEEE		22.1723312004
431PhosphorylationVITRIASSQTTIWSR
EEEEEHHCCCEEEEC		23.6423312004
433PhosphorylationTRIASSQTTIWSRST
EEEHHCCCEEEECCC		23.3823186163
434PhosphorylationRIASSQTTIWSRSTT
EEHHCCCEEEECCCC		16.8922210691
440PhosphorylationTTIWSRSTTTQTDMD
CEEEECCCCCCCCCC		32.5222210691
450 (in isoform 2)Ubiquitination-3.8421890473
456PhosphorylationNILFPRGTQSTEGSP
CCCCCCCCCCCCCCC		22.1822199227
458PhosphorylationLFPRGTQSTEGSPVS
CCCCCCCCCCCCCCC		28.4130278072
459PhosphorylationFPRGTQSTEGSPVSK
CCCCCCCCCCCCCCC		34.2528176443
460PhosphorylationPRGTQSTEGSPVSKM
CCCCCCCCCCCCCCC		64.0224719451
460 (in isoform 2)Ubiquitination-64.0221890473
461PhosphorylationRGTQSTEGSPVSKMS
CCCCCCCCCCCCCCE		37.02-
462PhosphorylationGTQSTEGSPVSKMSV
CCCCCCCCCCCCCEE		18.8530278072
465PhosphorylationSTEGSPVSKMSVSRS
CCCCCCCCCCEECCC		26.4828176443
466UbiquitinationTEGSPVSKMSVSRSS
CCCCCCCCCEECCCC		35.1121906983
468PhosphorylationGSPVSKMSVSRSSSL
CCCCCCCEECCCCCC		22.2230576142
470PhosphorylationPVSKMSVSRSSSLKS
CCCCCEECCCCCCCC		21.0930576142
472PhosphorylationSKMSVSRSSSLKSSS
CCCEECCCCCCCCCC		19.4423312004
473PhosphorylationKMSVSRSSSLKSSSS
CCEECCCCCCCCCCC		38.2822199227
474PhosphorylationMSVSRSSSLKSSSSV
CEECCCCCCCCCCCC		40.8525849741
476MethylationVSRSSSLKSSSSVSS
ECCCCCCCCCCCCCC		50.68-
476UbiquitinationVSRSSSLKSSSSVSS
ECCCCCCCCCCCCCC		50.6821906983
477PhosphorylationSRSSSLKSSSSVSSQ
CCCCCCCCCCCCCCC		40.5228348404
478PhosphorylationRSSSLKSSSSVSSQG
CCCCCCCCCCCCCCC		25.6624719451
479PhosphorylationSSSLKSSSSVSSQGS
CCCCCCCCCCCCCCC		41.6828348404
480PhosphorylationSSLKSSSSVSSQGSV
CCCCCCCCCCCCCCC		28.1522617229
482PhosphorylationLKSSSSVSSQGSVAS
CCCCCCCCCCCCCCC		20.9223312004
483PhosphorylationKSSSSVSSQGSVASS
CCCCCCCCCCCCCCC		36.0822617229
486PhosphorylationSSVSSQGSVASSTGS
CCCCCCCCCCCCCCC		13.5822210691
488PhosphorylationVSSQGSVASSTGSPA
CCCCCCCCCCCCCCC		10.2424719451
489PhosphorylationSSQGSVASSTGSPAS
CCCCCCCCCCCCCCC		26.6928102081
490PhosphorylationSQGSVASSTGSPASI
CCCCCCCCCCCCCCE		27.3528102081
491PhosphorylationQGSVASSTGSPASIR
CCCCCCCCCCCCCEE		38.9028102081
492PhosphorylationGSVASSTGSPASIRT
CCCCCCCCCCCCEEE		33.3124719451
493PhosphorylationSVASSTGSPASIRTT
CCCCCCCCCCCEEEC		19.8530576142
493 (in isoform 2)Ubiquitination-19.8521890473
496PhosphorylationSSTGSPASIRTTDFH
CCCCCCCCEEECCCC		18.9127535140
496UbiquitinationSSTGSPASIRTTDFH
CCCCCCCCEEECCCC		18.91-
496 (in isoform 1)Ubiquitination-18.9121890473
500PhosphorylationSPASIRTTDFHNPGY
CCCCEEECCCCCCCC		27.1524719451
504PhosphorylationIRTTDFHNPGYPKYL
EEECCCCCCCCCCCC		31.52-
506MethylationTTDFHNPGYPKYLGT
ECCCCCCCCCCCCCC		57.61-
506UbiquitinationTTDFHNPGYPKYLGT
ECCCCCCCCCCCCCC		57.61-
506 (in isoform 1)Ubiquitination-57.6121890473
508PhosphorylationDFHNPGYPKYLGTPH
CCCCCCCCCCCCCCC		25.4024719451
509UbiquitinationFHNPGYPKYLGTPHL
CCCCCCCCCCCCCCC		44.6221963094
510PhosphorylationHNPGYPKYLGTPHLE
CCCCCCCCCCCCCCE		13.0825072903
513PhosphorylationGYPKYLGTPHLELYL
CCCCCCCCCCCEEEE		12.6322617229
519PhosphorylationGTPHLELYLSDSLRN
CCCCCEEEECHHHHH		8.5225072903
521PhosphorylationPHLELYLSDSLRNLN
CCCEEEECHHHHHCC		16.1725072903
523PhosphorylationLELYLSDSLRNLNKE
CEEEECHHHHHCCHH		26.3324719451
539MethylationQFHFAGIRSRLNHML
CHHHHHHHHHHHHHH		18.14-
539UbiquitinationQFHFAGIRSRLNHML
CHHHHHHHHHHHHHH		18.14-
539 (in isoform 1)Ubiquitination-18.1421890473
543PhosphorylationAGIRSRLNHMLAMLS
HHHHHHHHHHHHHHH		19.8824719451
553PhosphorylationLAMLSRRTLFTENHL
HHHHHHCCCCCCCCC		25.7222210691
556PhosphorylationLSRRTLFTENHLGLH
HHHCCCCCCCCCCCC		38.7022210691
564PhosphorylationENHLGLHSGNFSRVN
CCCCCCCCCCCCCCE		40.2422210691
568PhosphorylationGLHSGNFSRVNLLAV
CCCCCCCCCCEEEEE		39.0414702039
569MethylationLHSGNFSRVNLLAVR
CCCCCCCCCEEEEEE		19.73-
598Phosphorylation--------------------
--------------------		-
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 FA83D_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FA83D_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 FA83D_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANM1_HUMANPRMT1physical
23455924
FBXW7_HUMANFBXW7physical
24344117
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 FA83D_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-462, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, 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 THR-513, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-513, AND MASSSPECTROMETRY.

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