ZNT1_HUMAN - dbPTM
ZNT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZNT1_HUMAN
UniProt AC Q9Y6M5
Protein Name Zinc transporter 1
Gene Name SLC30A1
Organism Homo sapiens (Human).
Sequence Length 507
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description May be involved in zinc transport out of the cell..
Protein Sequence MGCWGRNRGRLLCMLALTFMFMVLEVVVSRVTSSLAMLSDSFHMLSDVLALVVALVAERFARRTHATQKNTFGWIRAEVMGALVNAIFLTGLCFAILLEAIERFIEPHEMQQPLVVLGVGVAGLLVNVLGLCLFHHHSGFSQDSGHGHSHGGHGHGHGLPKGPRVKSTRPGSSDINVAPGEQGPDQEETNTLVANTSNSNGLKLDPADPENPRSGDTVEVQVNGNLVREPDHMELEEDRAGQLNMRGVFLHVLGDALGSVIVVVNALVFYFSWKGCSEGDFCVNPCFPDPCKAFVEIINSTHASVYEAGPCWVLYLDPTLCVVMVCILLYTTYPLLKESALILLQTVPKQIDIRNLIKELRNVEGVEEVHELHVWQLAGSRIIATAHIKCEDPTSYMEVAKTIKDVFHNHGIHATTIQPEFASVGSKSSVVPCELACRTQCALKQCCGTLPQAPSGKDAEKTPAVSISCLELSNNLEKKPRRTKAENIPAVVIEIKNMPNKQPESSL
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
18PhosphorylationLLCMLALTFMFMVLE
HHHHHHHHHHHHHHH		13.8824043423
29PhosphorylationMVLEVVVSRVTSSLA
HHHHHHHHHHHHHHH		14.9324043423
132S-palmitoylationLVNVLGLCLFHHHSG
HHHHHHHHHHCCCCC		3.4629575903
166UbiquitinationLPKGPRVKSTRPGSS
CCCCCCCCCCCCCCC		47.6029967540
167PhosphorylationPKGPRVKSTRPGSSD
CCCCCCCCCCCCCCC		27.1330266825
168PhosphorylationKGPRVKSTRPGSSDI
CCCCCCCCCCCCCCC		34.8530266825
172PhosphorylationVKSTRPGSSDINVAP
CCCCCCCCCCCCCCC		27.7630266825
173PhosphorylationKSTRPGSSDINVAPG
CCCCCCCCCCCCCCC		48.7230266825
189PhosphorylationQGPDQEETNTLVANT
CCCCHHHHCCEEEEC		32.5230266825
191PhosphorylationPDQEETNTLVANTSN
CCHHHHCCEEEECCC		29.9930266825
196PhosphorylationTNTLVANTSNSNGLK
HCCEEEECCCCCCCC		21.3926657352
197PhosphorylationNTLVANTSNSNGLKL
CCEEEECCCCCCCCC		37.7623927012
199PhosphorylationLVANTSNSNGLKLDP
EEEECCCCCCCCCCC		31.8523927012
203UbiquitinationTSNSNGLKLDPADPE
CCCCCCCCCCCCCCC		52.8523503661
299N-linked_GlycosylationKAFVEIINSTHASVY
HHHHHHHHCCCCCCC		46.66UniProtKB CARBOHYD
3492-HydroxyisobutyrylationILLQTVPKQIDIRNL
HHHHCCCCCCCHHHH		56.39-
358MalonylationIDIRNLIKELRNVEG
CCHHHHHHHHCCCCC		54.5926320211
358UbiquitinationIDIRNLIKELRNVEG
CCHHHHHHHHCCCCC		54.5933845483
389UbiquitinationIIATAHIKCEDPTSY
EEEEEEEECCCCCCH		23.0021963094
401UbiquitinationTSYMEVAKTIKDVFH
CCHHHHHHHHHHHHH		56.8333845483
404UbiquitinationMEVAKTIKDVFHNHG
HHHHHHHHHHHHHCC		53.7423503661
415PhosphorylationHNHGIHATTIQPEFA
HHCCCEEEEECHHHH		15.4020873877
416PhosphorylationNHGIHATTIQPEFAS
HCCCEEEEECHHHHC		20.5620873877
423PhosphorylationTIQPEFASVGSKSSV
EECHHHHCCCCCCCC		32.1220873877
426PhosphorylationPEFASVGSKSSVVPC
HHHHCCCCCCCCCCH		27.4920873877
427UbiquitinationEFASVGSKSSVVPCE
HHHCCCCCCCCCCHH		40.6021963094
428PhosphorylationFASVGSKSSVVPCEL
HHCCCCCCCCCCHHH		30.0225159151
429PhosphorylationASVGSKSSVVPCELA
HCCCCCCCCCCHHHH		30.7630576142
444UbiquitinationCRTQCALKQCCGTLP
HCHHHHHHHHHCCCC		23.8221963094
444AcetylationCRTQCALKQCCGTLP
HCHHHHHHHHHCCCC		23.8226051181
449PhosphorylationALKQCCGTLPQAPSG
HHHHHHCCCCCCCCC		22.7330576142
457UbiquitinationLPQAPSGKDAEKTPA
CCCCCCCCCCCCCCC		59.0921963094
461UbiquitinationPSGKDAEKTPAVSIS
CCCCCCCCCCCEEEH		62.6221963094
462PhosphorylationSGKDAEKTPAVSISC
CCCCCCCCCCEEEHH		14.1630266825
466PhosphorylationAEKTPAVSISCLELS
CCCCCCEEEHHHHHH		15.7630266825
468PhosphorylationKTPAVSISCLELSNN
CCCCEEEHHHHHHCC		12.7330266825
473PhosphorylationSISCLELSNNLEKKP
EEHHHHHHCCCCCCC		17.8130266825
478UbiquitinationELSNNLEKKPRRTKA
HHHCCCCCCCCCCHH		71.8421963094
479UbiquitinationLSNNLEKKPRRTKAE
HHCCCCCCCCCCHHH		34.0922817900
484UbiquitinationEKKPRRTKAENIPAV
CCCCCCCHHHCCCEE		52.4733845483
496UbiquitinationPAVVIEIKNMPNKQP
CEEEEEEECCCCCCC		34.1133845483
501UbiquitinationEIKNMPNKQPESSL-
EEECCCCCCCCCCC-		62.4521963094
505PhosphorylationMPNKQPESSL-----
CCCCCCCCCC-----		43.5630266825
506PhosphorylationPNKQPESSL------
CCCCCCCCC------		36.1130266825
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 ZNT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZNT1_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 ZNT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZNT1_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 ZNT1_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-506, AND MASSSPECTROMETRY.

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