F91A1_HUMAN - dbPTM
F91A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F91A1_HUMAN
UniProt AC Q658Y4
Protein Name Protein FAM91A1
Gene Name FAM91A1
Organism Homo sapiens (Human).
Sequence Length 838
Subcellular Localization Golgi apparatus, trans-Golgi network . Recruitment to the TGN requires the presence of GOLGA1, GOLGA4 and TBC1D23.
Protein Description
Protein Sequence MNIDVEFHIRHNYPWNKLPANVRQSLGNSQREYEKQVVLYSIRNQLRYRNNLVKHVKKDERRYYEELLKYSRDHLMLYPYHLSDIMVKGLRITPFSYYTGIMEDIMNSEKSYDSLPNFTAADCLRLLGIGRNQYIDLMNQCRSSKKFFRRKTARDLLPIKPVEIAIEAWWVVQAGYITEDDIKICTLPEKCAVDKIIDSGPQLSGSLDYNVVHSLYNKGFIYLDVPISDDSCIAVPPLEGFVMNRVQGDYFETLLYKIFVSIDEHTNVAELANVLEIDLSLVKNAVSMYCRLGFAHKKGQVINLDQLHSSWKNVPSVNRLKSTLDPQKMLLSWDGGESRSPVQEASSATDTDTNSQEDPADTASVSSLSLSTGHTKRIAFLFDSTLTAFLMMGNLSPNLKSHAVTMFEVGKLSDESLDSFLIELEKVQSTGEGEAQRYFDHALTLRNTILFLRHNKDLVAQTAQPDQPNYGFPLDLLRCESLLGLDPATCSRVLNKNYTLLVSMAPLTNEIRPVSSCTPQHIGPAIPEVSSVWFKLYIYHVTGQGPPSLLLSKGTRLRKLPDIFQSYDRLLITSWGHDPGVVPTSNVLTMLNDALTHSAVLIQGHGLHGIGETVHVPFPFDETELQGEFTRVNMGVHKALQILRNRVDLQHLCGYVTMLNASSQLADRKLSDASDERGEPDLASGSDVNGSTESFEMVIEEATIDSATKQTSGATTEADWVPLELCFGIPLFSSELNRKVCRKIAAHGLCRKESLQNLLHSSRKLSLQVLNFVHSFQEGASILDIHTEPSFSSLLSQSSCADMGVPLPAKNLIFKDGVLSEWSGRSPSSLLIANLHLQ
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
17UbiquitinationRHNYPWNKLPANVRQ
ECCCCHHHCCHHHHH		52.56-
41PhosphorylationEKQVVLYSIRNQLRY
HHHHHHHHHHHHHHH		15.7724719451
63PhosphorylationVKKDERRYYEELLKY
HHHHHHHHHHHHHHH		22.8128122231
64PhosphorylationKKDERRYYEELLKYS
HHHHHHHHHHHHHHC		10.9121130716
70PhosphorylationYYEELLKYSRDHLML
HHHHHHHHCHHHHHC		14.6528122231
71PhosphorylationYEELLKYSRDHLMLY
HHHHHHHCHHHHHCC		29.6428122231
78PhosphorylationSRDHLMLYPYHLSDI
CHHHHHCCCCCHHHH		6.4328122231
80PhosphorylationDHLMLYPYHLSDIMV
HHHHCCCCCHHHHHC		11.2228122231
83PhosphorylationMLYPYHLSDIMVKGL
HCCCCCHHHHHCCCC		16.2728122231
190UbiquitinationKICTLPEKCAVDKII
EEECCCHHHCCCCHH		26.08-
195AcetylationPEKCAVDKIIDSGPQ
CHHHCCCCHHHCCCC		34.6626051181
222PhosphorylationLYNKGFIYLDVPISD
HHCCCEEEEECEECC		8.4527050516
228PhosphorylationIYLDVPISDDSCIAV
EEEECEECCCCEEEC		29.3327050516
280PhosphorylationNVLEIDLSLVKNAVS
HHHHCHHHHHHHHHH		27.6324719451
309PhosphorylationINLDQLHSSWKNVPS
EEHHHHCHHHCCCCC		46.6230619164
310PhosphorylationNLDQLHSSWKNVPSV
EHHHHCHHHCCCCCH		31.1830619164
312UbiquitinationDQLHSSWKNVPSVNR
HHHCHHHCCCCCHHH		50.44-
316PhosphorylationSSWKNVPSVNRLKST
HHHCCCCCHHHHHHC		27.9527251275
321UbiquitinationVPSVNRLKSTLDPQK
CCCHHHHHHCCCHHH		37.85-
322PhosphorylationPSVNRLKSTLDPQKM
CCHHHHHHCCCHHHE		38.5028857561
323PhosphorylationSVNRLKSTLDPQKML
CHHHHHHCCCHHHEE		33.3324719451
328UbiquitinationKSTLDPQKMLLSWDG
HHCCCHHHEEEECCC		36.5821906983
332PhosphorylationDPQKMLLSWDGGESR
CHHHEEEECCCCCCC		21.1130266825
338PhosphorylationLSWDGGESRSPVQEA
EECCCCCCCCCCCCH		41.1429978859
340PhosphorylationWDGGESRSPVQEASS
CCCCCCCCCCCCHHC		38.4130278072
346PhosphorylationRSPVQEASSATDTDT
CCCCCCHHCCCCCCC		21.5430278072
347PhosphorylationSPVQEASSATDTDTN
CCCCCHHCCCCCCCC		42.0830278072
349PhosphorylationVQEASSATDTDTNSQ
CCCHHCCCCCCCCCC		41.1830278072
351PhosphorylationEASSATDTDTNSQED
CHHCCCCCCCCCCCC		40.1330278072
353PhosphorylationSSATDTDTNSQEDPA
HCCCCCCCCCCCCCC		38.5730278072
355PhosphorylationATDTDTNSQEDPADT
CCCCCCCCCCCCCCC		36.7230278072
362PhosphorylationSQEDPADTASVSSLS
CCCCCCCCCCCEEEE		23.9630278072
364PhosphorylationEDPADTASVSSLSLS
CCCCCCCCCEEEEEC		25.3230278072
366PhosphorylationPADTASVSSLSLSTG
CCCCCCCEEEEECCC		24.0630278072
367PhosphorylationADTASVSSLSLSTGH
CCCCCCEEEEECCCC		21.5930278072
369PhosphorylationTASVSSLSLSTGHTK
CCCCEEEEECCCCCH		23.4030278072
371PhosphorylationSVSSLSLSTGHTKRI
CCEEEEECCCCCHHE		29.0330278072
372PhosphorylationVSSLSLSTGHTKRIA
CEEEEECCCCCHHEE		37.9728450419
375PhosphorylationLSLSTGHTKRIAFLF
EEECCCCCHHEEEEH		24.3028450419
376UbiquitinationSLSTGHTKRIAFLFD
EECCCCCHHEEEEHH		35.8121890473
384PhosphorylationRIAFLFDSTLTAFLM
HEEEEHHHHHHHHHH		20.2726503514
385PhosphorylationIAFLFDSTLTAFLMM
EEEEHHHHHHHHHHH		29.9426503514
426UbiquitinationSFLIELEKVQSTGEG
HHEEEEEECCCCCCC		59.1921890473
508PhosphorylationLVSMAPLTNEIRPVS
EEEECCCCCCCCCCC		29.7329759185
537PhosphorylationSSVWFKLYIYHVTGQ
HCCEEEEEEEEHHCC		10.4627251275
539PhosphorylationVWFKLYIYHVTGQGP
CEEEEEEEEHHCCCC		4.0827251275
542PhosphorylationKLYIYHVTGQGPPSL
EEEEEEHHCCCCCCE		15.5227251275
548PhosphorylationVTGQGPPSLLLSKGT
HHCCCCCCEECCCCC		34.4824719451
552PhosphorylationGPPSLLLSKGTRLRK
CCCCEECCCCCCHHH		29.0724719451
555PhosphorylationSLLLSKGTRLRKLPD
CEECCCCCCHHHCCH		30.2127251275
559UbiquitinationSKGTRLRKLPDIFQS
CCCCCHHHCCHHHHH		69.80-
638UbiquitinationRVNMGVHKALQILRN
EECHHHHHHHHHHHC		48.6721890473
638UbiquitinationRVNMGVHKALQILRN
EECHHHHHHHHHHHC		48.6721890473
671PhosphorylationQLADRKLSDASDERG
HHHHCCCCCCCCCCC		33.8829255136
674PhosphorylationDRKLSDASDERGEPD
HCCCCCCCCCCCCCC		45.0223927012
684PhosphorylationRGEPDLASGSDVNGS
CCCCCCCCCCCCCCC		46.2430266825
686PhosphorylationEPDLASGSDVNGSTE
CCCCCCCCCCCCCCC		35.5730266825
691PhosphorylationSGSDVNGSTESFEMV
CCCCCCCCCCCEEHH		24.6530266825
692PhosphorylationGSDVNGSTESFEMVI
CCCCCCCCCCEEHHE		36.7330266825
694PhosphorylationDVNGSTESFEMVIEE
CCCCCCCCEEHHEEH		26.9630266825
703PhosphorylationEMVIEEATIDSATKQ
EHHEEHHHCCCCCCC		28.7030266825
706PhosphorylationIEEATIDSATKQTSG
EEHHHCCCCCCCCCC		33.7130266825
708PhosphorylationEATIDSATKQTSGAT
HHHCCCCCCCCCCCC		27.8630266825
743UbiquitinationLNRKVCRKIAAHGLC
HHHHHHHHHHHCCCC		31.41-
754PhosphorylationHGLCRKESLQNLLHS
CCCCCHHHHHHHHHH		37.9928450419
761PhosphorylationSLQNLLHSSRKLSLQ
HHHHHHHHHHHHHHH		31.6327251275
762PhosphorylationLQNLLHSSRKLSLQV
HHHHHHHHHHHHHHH		23.7620873877
815UbiquitinationPAKNLIFKDGVLSEW
CHHHEEECCCCCCCC		46.722190698
820PhosphorylationIFKDGVLSEWSGRSP
EECCCCCCCCCCCCH		34.3122115753
823PhosphorylationDGVLSEWSGRSPSSL
CCCCCCCCCCCHHHE		21.9222115753
826PhosphorylationLSEWSGRSPSSLLIA
CCCCCCCCHHHEEEE		32.4330266825
828PhosphorylationEWSGRSPSSLLIANL
CCCCCCHHHEEEEEC		34.5630266825
829PhosphorylationWSGRSPSSLLIANLH
CCCCCHHHEEEEECC		30.4930266825
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 F91A1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F91A1_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 F91A1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of F91A1_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 F91A1_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-829, 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-340 AND SER-671, ANDMASS SPECTROMETRY.
"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-340, 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-826, 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-671, AND MASSSPECTROMETRY.

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