S20A1_HUMAN - dbPTM
S20A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S20A1_HUMAN
UniProt AC Q8WUM9
Protein Name Sodium-dependent phosphate transporter 1
Gene Name SLC20A1
Organism Homo sapiens (Human).
Sequence Length 679
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description Sodium-phosphate symporter which plays a fundamental housekeeping role in phosphate transport, such as absorbing phosphate from interstitial fluid for normal cellular functions such as cellular metabolism, signal transduction, and nucleic acid and lipid synthesis. May play a role in extracellular matrix and cartilage calcification as well as in vascular calcification.; (Microbial infection) May function as a retroviral receptor as it confers human cells susceptibility to infection to Gibbon Ape Leukemia Virus (GaLV), Simian sarcoma-associated virus (SSAV) and Feline leukemia virus subgroup B (FeLV-B) as well as 10A1 murine leukemia virus (10A1 MLV)..
Protein Sequence MATLITSTTAATAASGPLVDYLWMLILGFIIAFVLAFSVGANDVANSFGTAVGSGVVTLKQACILASIFETVGSVLLGAKVSETIRKGLIDVEMYNSTQGLLMAGSVSAMFGSAVWQLVASFLKLPISGTHCIVGATIGFSLVAKGQEGVKWSELIKIVMSWFVSPLLSGIMSGILFFLVRAFILHKADPVPNGLRALPVFYACTVGINLFSIMYTGAPLLGFDKLPLWGTILISVGCAVFCALIVWFFVCPRMKRKIEREIKCSPSESPLMEKKNSLKEDHEETKLSVGDIENKHPVSEVGPATVPLQAVVEERTVSFKLGDLEEAPERERLPSVDLKEETSIDSTVNGAVQLPNGNLVQFSQAVSNQINSSGHYQYHTVHKDSGLYKELLHKLHLAKVGDCMGDSGDKPLRRNNSYTSYTMAICGMPLDSFRAKEGEQKGEEMEKLTWPNADSKKRIRMDSYTSYCNAVSDLHSASEIDMSVKAEMGLGDRKGSNGSLEEWYDQDKPEVSLLFQFLQILTACFGSFAHGGNDVSNAIGPLVALYLVYDTGDVSSKVATPIWLLLYGGVGICVGLWVWGRRVIQTMGKDLTPITPSSGFSIELASALTVVIASNIGLPISTTHCKVGSVVSVGWLRSKKAVDWRLFRNIFMAWFVTVPISGVISAAIMAIFRYVILRM
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
121PhosphorylationAVWQLVASFLKLPIS
HHHHHHHHHHCCCCC		24.5124719451
263UbiquitinationRKIEREIKCSPSESP
HHHHHHCCCCCCCCH		24.73-
265PhosphorylationIEREIKCSPSESPLM
HHHHCCCCCCCCHHH		26.8529255136
267PhosphorylationREIKCSPSESPLMEK
HHCCCCCCCCHHHHH		34.1229255136
269PhosphorylationIKCSPSESPLMEKKN
CCCCCCCCHHHHHHH		27.8929255136
275UbiquitinationESPLMEKKNSLKEDH
CCHHHHHHHCCCCCH		38.16-
277PhosphorylationPLMEKKNSLKEDHEE
HHHHHHHCCCCCHHH		50.0923898821
279UbiquitinationMEKKNSLKEDHEETK
HHHHHCCCCCHHHHC		62.0021906983
285PhosphorylationLKEDHEETKLSVGDI
CCCCHHHHCCCHHHH		34.0129255136
286UbiquitinationKEDHEETKLSVGDIE
CCCHHHHCCCHHHHC		41.8821906983
288PhosphorylationDHEETKLSVGDIENK
CHHHHCCCHHHHCCC		26.1329255136
295UbiquitinationSVGDIENKHPVSEVG
CHHHHCCCCCCCCCC		36.1721906983
299PhosphorylationIENKHPVSEVGPATV
HCCCCCCCCCCCCCC		30.8929514088
305PhosphorylationVSEVGPATVPLQAVV
CCCCCCCCCCHHHHE		26.2825850435
316PhosphorylationQAVVEERTVSFKLGD
HHHEEEEEEEEECCC		24.6329514088
318PhosphorylationVVEERTVSFKLGDLE
HEEEEEEEEECCCHH		18.9528464451
320UbiquitinationEERTVSFKLGDLEEA
EEEEEEEECCCHHHC		44.0121906983
335PhosphorylationPERERLPSVDLKEET
CCHHCCCCCCCCCCC		32.6227273156
376PhosphorylationQINSSGHYQYHTVHK
CCCCCCCCEEEEEEC		17.8125884760
378PhosphorylationNSSGHYQYHTVHKDS
CCCCCCEEEEEECCC		7.7225884760
385PhosphorylationYHTVHKDSGLYKELL
EEEEECCCCHHHHHH		35.1928796482
388PhosphorylationVHKDSGLYKELLHKL
EECCCCHHHHHHHHH		13.1228796482
389UbiquitinationHKDSGLYKELLHKLH
ECCCCHHHHHHHHHH		47.1021906983
394UbiquitinationLYKELLHKLHLAKVG
HHHHHHHHHHHHHHC		37.2621906983
399UbiquitinationLHKLHLAKVGDCMGD
HHHHHHHHHCCCCCC		53.78-
410UbiquitinationCMGDSGDKPLRRNNS
CCCCCCCCCCCCCCC		49.86-
417PhosphorylationKPLRRNNSYTSYTMA
CCCCCCCCCCCEEEE		33.0822167270
418PhosphorylationPLRRNNSYTSYTMAI
CCCCCCCCCCEEEEE		11.2222167270
419PhosphorylationLRRNNSYTSYTMAIC
CCCCCCCCCEEEEEC		18.3222167270
420PhosphorylationRRNNSYTSYTMAICG
CCCCCCCCEEEEECC		15.4622167270
421PhosphorylationRNNSYTSYTMAICGM
CCCCCCCEEEEECCC		7.8522167270
422PhosphorylationNNSYTSYTMAICGMP
CCCCCCEEEEECCCC		10.4122167270
432PhosphorylationICGMPLDSFRAKEGE
ECCCCHHHHCHHHCH		25.0626356563
436UbiquitinationPLDSFRAKEGEQKGE
CHHHHCHHHCHHCCH		63.0921906983
441UbiquitinationRAKEGEQKGEEMEKL
CHHHCHHCCHHHHHC		65.0821906983
447UbiquitinationQKGEEMEKLTWPNAD
HCCHHHHHCCCCCCC		50.3221906983
455PhosphorylationLTWPNADSKKRIRMD
CCCCCCCCCCEECCH		37.3528355574
456UbiquitinationTWPNADSKKRIRMDS
CCCCCCCCCEECCHH		46.7721906983
463PhosphorylationKKRIRMDSYTSYCNA
CCEECCHHHHHHHHH		22.4427273156
464PhosphorylationKRIRMDSYTSYCNAV
CEECCHHHHHHHHHH		8.7428450419
465PhosphorylationRIRMDSYTSYCNAVS
EECCHHHHHHHHHHH		19.7125884760
466PhosphorylationIRMDSYTSYCNAVSD
ECCHHHHHHHHHHHC		21.3225884760
467PhosphorylationRMDSYTSYCNAVSDL
CCHHHHHHHHHHHCC		5.0728450419
472PhosphorylationTSYCNAVSDLHSASE
HHHHHHHHCCCCHHC		31.8528450419
476PhosphorylationNAVSDLHSASEIDMS
HHHHCCCCHHCCCCH		40.5623401153
478PhosphorylationVSDLHSASEIDMSVK
HHCCCCHHCCCCHHE		37.7928450419
483PhosphorylationSASEIDMSVKAEMGL
CHHCCCCHHEECCCC		19.4028450419
485UbiquitinationSEIDMSVKAEMGLGD
HCCCCHHEECCCCCC		31.18-
629PhosphorylationTTHCKVGSVVSVGWL
CCCCCCCCEEEEEHH		23.49-
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 S20A1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S20A1_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 S20A1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPP6_HUMANMPP6physical
28514442
MPP2_HUMANMPP2physical
28514442
CEGT_HUMANUGCGphysical
28514442
FLVC1_HUMANFLVCR1physical
28514442
S20A2_HUMANSLC20A2physical
28514442
ADCY9_HUMANADCY9physical
28514442
MFAP3_HUMANMFAP3physical
28514442
LIN7A_HUMANLIN7Aphysical
28514442
LRP10_HUMANLRP10physical
28514442
BMR1A_HUMANBMPR1Aphysical
28514442
SL9A1_HUMANSLC9A1physical
28514442
NFIP1_HUMANNDFIP1physical
28514442
RN149_HUMANRNF149physical
28514442
ARL5B_HUMANARL5Bphysical
28514442
MTX3_HUMANMTX3physical
28514442
LIN7C_HUMANLIN7Cphysical
28514442
NOTC3_HUMANNOTCH3physical
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 S20A1_HUMAN

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Related Literatures of Post-Translational Modification
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-267 AND SER-269, ANDMASS SPECTROMETRY.
"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-265 AND SER-269, ANDMASS SPECTROMETRY.

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