S39A3_HUMAN - dbPTM
S39A3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S39A3_HUMAN
UniProt AC Q9BRY0
Protein Name Zinc transporter ZIP3
Gene Name SLC39A3
Organism Homo sapiens (Human).
Sequence Length 314
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Acts as a zinc-influx transporter..
Protein Sequence MVKLLVAKILCMVGVFFFMLLGSLLPVKIIETDFEKAHRSKKILSLCNTFGGGVFLATCFNALLPAVREKLQKVLSLGHISTDYPLAETILLLGFFMTVFLEQLILTFRKEKPSFIDLETFNAGSDVGSDSEYESPFMGGARGHALYVEPHGHGPSLSVQGLSRASPVRLLSLAFALSAHSVFEGLALGLQEEGEKVVSLFVGVAVHETLVAVALGISMARSAMPLRDAAKLAVTVSAMIPLGIGLGLGIESAQGVPGSVASVLLQGLAGGTFLFITFLEILAKELEEKSDRLLKVLFLVLGYTVLAGMVFLKW
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
36UbiquitinationIIETDFEKAHRSKKI
EHHCCHHHHHHCHHH
49.8733845483
98 (in isoform 2)Phosphorylation-11.71-
99 (in isoform 2)Phosphorylation-3.28-
112UbiquitinationILTFRKEKPSFIDLE
HHHHHHCCCCCEECE
49.34-
114PhosphorylationTFRKEKPSFIDLETF
HHHHCCCCCEECEEE
45.9927422710
120PhosphorylationPSFIDLETFNAGSDV
CCCEECEEECCCCCC
29.5025693802
125PhosphorylationLETFNAGSDVGSDSE
CEEECCCCCCCCCCC
27.0626503892
129PhosphorylationNAGSDVGSDSEYESP
CCCCCCCCCCCCCCC
37.5026055452
131PhosphorylationGSDVGSDSEYESPFM
CCCCCCCCCCCCCCC
43.7226503892
133PhosphorylationDVGSDSEYESPFMGG
CCCCCCCCCCCCCCC
26.1725693802
135PhosphorylationGSDSEYESPFMGGAR
CCCCCCCCCCCCCCC
23.6520873877
147PhosphorylationGARGHALYVEPHGHG
CCCCEEEEEECCCCC
11.9825884760
156PhosphorylationEPHGHGPSLSVQGLS
ECCCCCCCCCCCCCC
37.5626356563
158PhosphorylationHGHGPSLSVQGLSRA
CCCCCCCCCCCCCCC
19.4126356563
163PhosphorylationSLSVQGLSRASPVRL
CCCCCCCCCCCHHHH
32.4023401153
164MethylationLSVQGLSRASPVRLL
CCCCCCCCCCHHHHH
44.09115917117
166PhosphorylationVQGLSRASPVRLLSL
CCCCCCCCHHHHHHH
23.8724719451
222PhosphorylationLGISMARSAMPLRDA
HHHHHHHHCCCHHHH
21.2718691976

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 S39A3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S39A3_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 S39A3_HUMAN !!

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

Oops, there are no PPI records of S39A3_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 S39A3_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-125, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-129, 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-125 AND SER-129, 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-125 AND SER-129, ANDMASS SPECTROMETRY.

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