S20A2_HUMAN - dbPTM
S20A2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S20A2_HUMAN
UniProt AC Q08357
Protein Name Sodium-dependent phosphate transporter 2
Gene Name SLC20A2
Organism Homo sapiens (Human).
Sequence Length 652
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Sodium-phosphate symporter which seems to play a fundamental housekeeping role in phosphate transport by absorbing phosphate from interstitial fluid for normal cellular functions such as cellular metabolism, signal transduction, and nucleic acid and lipid synthesis. In vitro, sodium-dependent phosphate uptake is not siginificantly affected by acidic and alkaline conditions, however sodium-independent phosphate uptake occurs at acidic conditions. May play a role in extracellular matrix, cartilage and vascular calcification. Functions as a retroviral receptor and confers human cells susceptibility to infection to amphotropic murine leukemia virus (A-MuLV), 10A1 murine leukemia virus (10A1 MLV) and some feline leukemia virus subgroup B (FeLV-B) variants..
Protein Sequence MAMDEYLWMVILGFIIAFILAFSVGANDVANSFGTAVGSGVVTLRQACILASIFETTGSVLLGAKVGETIRKGIIDVNLYNETVETLMAGEVSAMVGSAVWQLIASFLRLPISGTHCIVGSTIGFSLVAIGTKGVQWMELVKIVASWFISPLLSGFMSGLLFVLIRIFILKKEDPVPNGLRALPVFYAATIAINVFSIMYTGAPVLGLVLPMWAIALISFGVALLFAFFVWLFVCPWMRRKITGKLQKEGALSRVSDESLSKVQEAESPVFKELPGAKANDDSTIPLTGAAGETLGTSEGTSAGSHPRAAYGRALSMTHGSVKSPISNGTFGFDGHTRSDGHVYHTVHKDSGLYKDLLHKIHIDRGPEEKPAQESNYRLLRRNNSYTCYTAAICGLPVHATFRAADSSAPEDSEKLVGDTVSYSKKRLRYDSYSSYCNAVAEAEIEAEEGGVEMKLASELADPDQPREDPAEEEKEEKDAPEVHLLFHFLQVLTACFGSFAHGGNDVSNAIGPLVALWLIYKQGGVTQEAATPVWLLFYGGVGICTGLWVWGRRVIQTMGKDLTPITPSSGFTIELASAFTVVIASNIGLPVSTTHCKVGSVVAVGWIRSRKAVDWRLFRNIFVAWFVTVPVAGLFSAAVMALLMYGILPYV
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
69PhosphorylationLGAKVGETIRKGIID
HCCCCCHHHHCCCCE
21.8323312004
81N-linked_GlycosylationIIDVNLYNETVETLM
CCEEECCCHHHHHHH
41.4511356966
106PhosphorylationAVWQLIASFLRLPIS
HHHHHHHHHHCCCCC
20.1624719451
243PhosphorylationPWMRRKITGKLQKEG
HHHHHHHHHCHHHCC
31.1630622161
253PhosphorylationLQKEGALSRVSDESL
HHHCCCHHHCCHHHH
30.0623927012
256PhosphorylationEGALSRVSDESLSKV
CCCHHHCCHHHHHHH
34.2529255136
259PhosphorylationLSRVSDESLSKVQEA
HHHCCHHHHHHHHHC
42.8229255136
261PhosphorylationRVSDESLSKVQEAES
HCCHHHHHHHHHCCC
39.8129255136
262UbiquitinationVSDESLSKVQEAESP
CCHHHHHHHHHCCCC
53.9121906983
268PhosphorylationSKVQEAESPVFKELP
HHHHHCCCCHHHCCC
33.1529255136
272UbiquitinationEAESPVFKELPGAKA
HCCCCHHHCCCCCCC
59.5821890473
278UbiquitinationFKELPGAKANDDSTI
HHCCCCCCCCCCCCC
54.3521890473
283PhosphorylationGAKANDDSTIPLTGA
CCCCCCCCCCCCCCC
30.9728555341
284PhosphorylationAKANDDSTIPLTGAA
CCCCCCCCCCCCCCC
33.3428555341
305PhosphorylationSEGTSAGSHPRAAYG
CCCCCCCCCCHHHHC
29.9928555341
316PhosphorylationAAYGRALSMTHGSVK
HHHCCHHHCCCCCCC
22.2029255136
318PhosphorylationYGRALSMTHGSVKSP
HCCHHHCCCCCCCCC
21.5123927012
321PhosphorylationALSMTHGSVKSPISN
HHHCCCCCCCCCCCC
20.8323927012
324PhosphorylationMTHGSVKSPISNGTF
CCCCCCCCCCCCCCC
25.8825159151
327PhosphorylationGSVKSPISNGTFGFD
CCCCCCCCCCCCCCC
32.3728450419
330PhosphorylationKSPISNGTFGFDGHT
CCCCCCCCCCCCCEE
25.4928450419
337PhosphorylationTFGFDGHTRSDGHVY
CCCCCCEECCCCCEE
37.0829978859
344PhosphorylationTRSDGHVYHTVHKDS
ECCCCCEEEEEECCC
6.0128796482
346PhosphorylationSDGHVYHTVHKDSGL
CCCCEEEEEECCCCH
13.4528796482
349UbiquitinationHVYHTVHKDSGLYKD
CEEEEEECCCCHHHH
49.61-
351PhosphorylationYHTVHKDSGLYKDLL
EEEEECCCCHHHHHH
35.1927642862
354PhosphorylationVHKDSGLYKDLLHKI
EECCCCHHHHHHHHH
13.1428796482
355UbiquitinationHKDSGLYKDLLHKIH
ECCCCHHHHHHHHHC
47.12-
360UbiquitinationLYKDLLHKIHIDRGP
HHHHHHHHHCCCCCC
35.6321890473
370UbiquitinationIDRGPEEKPAQESNY
CCCCCCCCCCHHHHC
43.9521906983
375PhosphorylationEEKPAQESNYRLLRR
CCCCCHHHHCHHHHH
27.3825394399
377PhosphorylationKPAQESNYRLLRRNN
CCCHHHHCHHHHHCC
16.3621082442
385PhosphorylationRLLRRNNSYTCYTAA
HHHHHCCCCEEEEEE
25.9323927012
386PhosphorylationLLRRNNSYTCYTAAI
HHHHCCCCEEEEEEC
11.7123927012
387PhosphorylationLRRNNSYTCYTAAIC
HHHCCCCEEEEEECC
10.0023927012
389PhosphorylationRNNSYTCYTAAICGL
HCCCCEEEEEECCCC
7.5123927012
390PhosphorylationNNSYTCYTAAICGLP
CCCCEEEEEECCCCC
16.2623927012
401PhosphorylationCGLPVHATFRAADSS
CCCCEEEEEECCCCC
9.97-
413PhosphorylationDSSAPEDSEKLVGDT
CCCCCCCHHHHCCCC
34.6623312004
415UbiquitinationSAPEDSEKLVGDTVS
CCCCCHHHHCCCCCC
53.0421906983
420PhosphorylationSEKLVGDTVSYSKKR
HHHHCCCCCCCCCCC
12.8621945579
422PhosphorylationKLVGDTVSYSKKRLR
HHCCCCCCCCCCCCC
26.2723401153
423PhosphorylationLVGDTVSYSKKRLRY
HCCCCCCCCCCCCCC
21.8521945579
424PhosphorylationVGDTVSYSKKRLRYD
CCCCCCCCCCCCCCC
24.9721945579
425UbiquitinationGDTVSYSKKRLRYDS
CCCCCCCCCCCCCCH
33.412190698
425MethylationGDTVSYSKKRLRYDS
CCCCCCCCCCCCCCH
33.41-
426MethylationDTVSYSKKRLRYDSY
CCCCCCCCCCCCCHH
51.21-
430PhosphorylationYSKKRLRYDSYSSYC
CCCCCCCCCHHHHHH
17.5228450419
432PhosphorylationKKRLRYDSYSSYCNA
CCCCCCCHHHHHHHH
20.2722617229
433PhosphorylationKRLRYDSYSSYCNAV
CCCCCCHHHHHHHHH
9.9528450419
434PhosphorylationRLRYDSYSSYCNAVA
CCCCCHHHHHHHHHH
20.8427422710
435PhosphorylationLRYDSYSSYCNAVAE
CCCCHHHHHHHHHHH
26.0228450419
436PhosphorylationRYDSYSSYCNAVAEA
CCCHHHHHHHHHHHH
5.4728450419
458PhosphorylationGVEMKLASELADPDQ
CEEEEEHHHHCCCCC
43.5130266825
637PhosphorylationVPVAGLFSAAVMALL
HHHHHHHHHHHHHHH
21.9924719451
646PhosphorylationAVMALLMYGILPYV-
HHHHHHHHCCCCCC-
10.8624719451
651PhosphorylationLMYGILPYV------
HHHCCCCCC------
18.49-

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 S20A2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S20A2_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 S20A2_HUMAN !!

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

Oops, there are no PPI records of S20A2_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
213600Basal ganglia calcification, idiopathic, 1 (IBGC1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of S20A2_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Transmembrane topology of PiT-2, a phosphate transporter-retrovirusreceptor.";
Salauen C., Rodrigues P., Heard J.M.;
J. Virol. 75:5584-5592(2001).
Cited for: TOPOLOGY, GLYCOSYLATION AT ASN-81, AND MUTAGENESIS OF ASN-81.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-377, AND MASSSPECTROMETRY.

TOP