SO4A1_HUMAN - dbPTM
SO4A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SO4A1_HUMAN
UniProt AC Q96BD0
Protein Name Solute carrier organic anion transporter family member 4A1
Gene Name SLCO4A1
Organism Homo sapiens (Human).
Sequence Length 722
Subcellular Localization Cell membrane
Multi-pass membrane protein.
Protein Description Mediates the Na(+)-independent transport of organic anions such as the thyroid hormones T3 (triiodo-L-thyronine), T4 (thyroxine) and rT3, and of estrone-3-sulfate and taurocholate..
Protein Sequence MPLHQLGDKPLTFPSPNSAMENGLDHTPPSRRASPGTPLSPGSLRSAAHSPLDTSKQPLCQLWAEKHGARGTHEVRYVSAGQSVACGWWAFAPPCLQVLNTPKGILFFLCAAAFLQGMTVNGFINTVITSLERRYDLHSYQSGLIASSYDIAACLCLTFVSYFGGSGHKPRWLGWGVLLMGTGSLVFALPHFTAGRYEVELDAGVRTCPANPGAVCADSTSGLSRYQLVFMLGQFLHGVGATPLYTLGVTYLDENVKSSCSPVYIAIFYTAAILGPAAGYLIGGALLNIYTEMGRRTELTTESPLWVGAWWVGFLGSGAAAFFTAVPILGYPRQLPGSQRYAVMRAAEMHQLKDSSRGEASNPDFGKTIRDLPLSIWLLLKNPTFILLCLAGATEATLITGMSTFSPKFLESQFSLSASEAATLFGYLVVPAGGGGTFLGGFFVNKLRLRGSAVIKFCLFCTVVSLLGILVFSLHCPSVPMAGVTASYGGSLLPEGHLNLTAPCNAACSCQPEHYSPVCGSDGLMYFSLCHAGCPAATETNVDGQKVYRDCSCIPQNLSSGFGHATAGKCTSTCQRKPLLLVFIFVVIFFTFLSSIPALTATLRCVRDPQRSFALGIQWIVVRILGGIPGPIAFGWVIDKACLLWQDQCGQQGSCLVYQNSAMSRYILIMGLLYKVLGVLFFAIACFLYKPLSESSDGLETCLPSQSSAPDSATDSQLQSSV
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
9UbiquitinationPLHQLGDKPLTFPSP
CHHHCCCCCCCCCCC
39.8829967540
12PhosphorylationQLGDKPLTFPSPNSA
HCCCCCCCCCCCCHH
41.8623186163
15PhosphorylationDKPLTFPSPNSAMEN
CCCCCCCCCCHHHHC
32.3025159151
18PhosphorylationLTFPSPNSAMENGLD
CCCCCCCHHHHCCCC
32.1725159151
27PhosphorylationMENGLDHTPPSRRAS
HHCCCCCCCCCCCCC
36.2425159151
30PhosphorylationGLDHTPPSRRASPGT
CCCCCCCCCCCCCCC
35.2925159151
34PhosphorylationTPPSRRASPGTPLSP
CCCCCCCCCCCCCCC
23.2730266825
37PhosphorylationSRRASPGTPLSPGSL
CCCCCCCCCCCCCCH
25.1723927012
40PhosphorylationASPGTPLSPGSLRSA
CCCCCCCCCCCHHHH
28.5523927012
43PhosphorylationGTPLSPGSLRSAAHS
CCCCCCCCHHHHCCC
24.8025159151
46PhosphorylationLSPGSLRSAAHSPLD
CCCCCHHHHCCCCCC
34.7925159151
50PhosphorylationSLRSAAHSPLDTSKQ
CHHHHCCCCCCCCCC
23.5628355574
54PhosphorylationAAHSPLDTSKQPLCQ
HCCCCCCCCCCCHHH
45.5729396449
55PhosphorylationAHSPLDTSKQPLCQL
CCCCCCCCCCCHHHH
29.0330576142
56UbiquitinationHSPLDTSKQPLCQLW
CCCCCCCCCCHHHHH
59.0121963094
66UbiquitinationLCQLWAEKHGARGTH
HHHHHHHHHCCCCEE
39.3221963094
197PhosphorylationPHFTAGRYEVELDAG
CCCCCCCEEEEEECC
24.33-
300PhosphorylationMGRRTELTTESPLWV
CCCCCCCCCCCCCEE
23.4522210691
353 (in isoform 3)Ubiquitination-49.3321906983
353 (in isoform 1)Ubiquitination-49.3321906983
353 (in isoform 4)Ubiquitination-49.3321906983
353UbiquitinationAAEMHQLKDSSRGEA
HHHHHHCCCCCCCCC
49.3321906983
355PhosphorylationEMHQLKDSSRGEASN
HHHHCCCCCCCCCCC
21.9825159151
356PhosphorylationMHQLKDSSRGEASNP
HHHCCCCCCCCCCCC
55.2125627689
361PhosphorylationDSSRGEASNPDFGKT
CCCCCCCCCCCCCCH
44.5926657352
367 (in isoform 1)Ubiquitination-40.5521906983
367 (in isoform 3)Ubiquitination-40.5521906983
367 (in isoform 4)Ubiquitination-40.5521906983
367UbiquitinationASNPDFGKTIRDLPL
CCCCCCCCHHHHCCH
40.5521963094
394PhosphorylationLLCLAGATEATLITG
HHHHCCCCHHHHHHC
25.82-
406PhosphorylationITGMSTFSPKFLESQ
HHCCCCCCHHHHHHC
27.5424719451
499N-linked_GlycosylationLLPEGHLNLTAPCNA
CCCCCCCCCCCCCCC
29.66UniProtKB CARBOHYD
557N-linked_GlycosylationDCSCIPQNLSSGFGH
CCCCCCCCCCCCCCC
36.21UniProtKB CARBOHYD
569UbiquitinationFGHATAGKCTSTCQR
CCCCCCCCCCCHHCC
31.6921963094
666PhosphorylationQNSAMSRYILIMGLL
CCCHHHHHHHHHHHH
7.8625072903
674PhosphorylationILIMGLLYKVLGVLF
HHHHHHHHHHHHHHH
12.2325072903

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 SO4A1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SO4A1_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 SO4A1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SO4A1_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 SO4A1_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-34; THR-37; SER-40;SER-43; SER-46 AND SER-50, AND MASS 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-50, 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-40, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND MASSSPECTROMETRY.

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