FA8A1_HUMAN - dbPTM
FA8A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FA8A1_HUMAN
UniProt AC Q9UBU6
Protein Name Protein FAM8A1
Gene Name FAM8A1
Organism Homo sapiens (Human).
Sequence Length 413
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MAEGPEEARGHPPGQDDGGGDHEPVPSLRGPPTTAVPCPRDDPQAEPQAPGRPTAPGLAAAAAADKLEPPRELRKRGEAASGSGAELQEQAGCEAPEAAAPRERPARLSAREYSRQVHEWLWQSYCGYLTWHSGLAAFPAYCSPQPSPQSFPSGGAAVPQAAAPPPPQLGYYNPFYFLSPGAAGPDPRTAAGISTPAPVAGLGPRAPHVQASVRATPVTRVGSAAPSRSPSETGRQAGREYVIPSLAHRFMAEMVDFFILFFIKATIVLSIMHLSGIKDISKFAMHYIIEEIDEDTSMEDLQKMMVVALIYRLLVCFYEIICIWGAGGATPGKFLLGLRVVTCDTSVLIAPSRVLVIPSSNVSITTSTIRALIKNFSIASFFPAFITLLFFQHNRTAYDIVAGTIVVKRNGVR
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
9MethylationAEGPEEARGHPPGQD
CCCCHHHCCCCCCCC		47.43-
27PhosphorylationGDHEPVPSLRGPPTT
CCCCCCCCCCCCCCC		30.8224719451
81PhosphorylationRKRGEAASGSGAELQ
HHHHHHCCCCCHHHH		40.3129255136
83PhosphorylationRGEAASGSGAELQEQ
HHHHCCCCCHHHHHH		32.1325849741
113PhosphorylationARLSAREYSRQVHEW
CCHHHHHHHHHHHHH		12.0030576142
189PhosphorylationAAGPDPRTAAGISTP
CCCCCCCCCCCCCCC		26.6727251275
194PhosphorylationPRTAAGISTPAPVAG
CCCCCCCCCCCCCCC		27.6729978859
195PhosphorylationRTAAGISTPAPVAGL
CCCCCCCCCCCCCCC		22.8828555341
212PhosphorylationRAPHVQASVRATPVT
CCCCEEEEEECCCCE		8.6129214152
216PhosphorylationVQASVRATPVTRVGS
EEEEEECCCCEECCC		14.0224719451
219PhosphorylationSVRATPVTRVGSAAP
EEECCCCEECCCCCC		22.35-
223PhosphorylationTPVTRVGSAAPSRSP
CCCEECCCCCCCCCC		20.5721712546
227PhosphorylationRVGSAAPSRSPSETG
ECCCCCCCCCCCHHH		40.4428555341
229PhosphorylationGSAAPSRSPSETGRQ
CCCCCCCCCCHHHHH		36.8021712546
231PhosphorylationAAPSRSPSETGRQAG
CCCCCCCCHHHHHCC		49.3827794612
233PhosphorylationPSRSPSETGRQAGRE
CCCCCCHHHHHCCHH		41.8427794612
241PhosphorylationGRQAGREYVIPSLAH
HHHCCHHCCHHHHHH		11.43-
245PhosphorylationGREYVIPSLAHRFMA
CHHCCHHHHHHHHHH		27.36-
266PhosphorylationILFFIKATIVLSIMH
HHHHHHHHHHHHHHH		13.4528258704
270PhosphorylationIKATIVLSIMHLSGI
HHHHHHHHHHHHCCC		13.63-
275PhosphorylationVLSIMHLSGIKDISK
HHHHHHHCCCCHHHH		24.6428258704
342PhosphorylationLLGLRVVTCDTSVLI
CCEEEEEEECCCEEE		11.21-
345PhosphorylationLRVVTCDTSVLIAPS
EEEEEECCCEEECCC		23.92-
346PhosphorylationRVVTCDTSVLIAPSR
EEEEECCCEEECCCE		11.15-
363PhosphorylationVIPSSNVSITTSTIR
EECCCCCCCCHHHHH		20.61-
366PhosphorylationSSNVSITTSTIRALI
CCCCCCCHHHHHHHH		23.39-
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 FA8A1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FA8A1_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
345Phosphorylation353 (8)R ⇒ Qrs79642714
  • Idiopathic intracranial hypertension
29608535
346Phosphorylation353 (7)R ⇒ Qrs79642714
  • Idiopathic intracranial hypertension
29608535
363Phosphorylation353 (10)R ⇒ Qrs79642714
  • Idiopathic intracranial hypertension
29608535
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SE1L1_HUMANSEL1Lphysical
22119785
SYVN1_HUMANSYVN1physical
22119785
OS9_HUMANOS9physical
22119785
CAPR2_HUMANCAPRIN2physical
22119785
ERLEC_HUMANERLEC1physical
22119785
UBB_HUMANUBBphysical
28514442
SYVN1_HUMANSYVN1physical
28514442
PLS1_HUMANPLSCR1physical
28514442
FGFR1_HUMANFGFR1physical
28514442
ZDH17_HUMANZDHHC17physical
28514442
CD320_HUMANCD320physical
28514442
SDCB1_HUMANSDCBPphysical
28514442
OSBL8_HUMANOSBPL8physical
28514442
GSLG1_HUMANGLG1physical
28514442
OMA1_HUMANOMA1physical
28514442
ZDHC9_HUMANZDHHC9physical
28514442
NFIP2_HUMANNDFIP2physical
28514442
NFIP1_HUMANNDFIP1physical
28514442
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 FA8A1_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-229, AND MASSSPECTROMETRY.
"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-229, AND MASSSPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233, AND MASSSPECTROMETRY.

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