S39A6_HUMAN - dbPTM
S39A6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S39A6_HUMAN
UniProt AC Q13433
Protein Name Zinc transporter ZIP6
Gene Name SLC39A6
Organism Homo sapiens (Human).
Sequence Length 755
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description May act as a zinc-influx transporter..
Protein Sequence MARKLSVILILTFALSVTNPLHELKAAAFPQTTEKISPNWESGINVDLAISTRQYHLQQLFYRYGENNSLSVEGFRKLLQNIGIDKIKRIHIHHDHDHHSDHEHHSDHERHSDHEHHSEHEHHSDHDHHSHHNHAASGKNKRKALCPDHDSDSSGKDPRNSQGKGAHRPEHASGRRNVKDSVSASEVTSTVYNTVSEGTHFLETIETPRPGKLFPKDVSSSTPPSVTSKSRVSRLAGRKTNESVSEPRKGFMYSRNTNENPQECFNASKLLTSHGMGIQVPLNATEFNYLCPAIINQIDARSCLIHTSEKKAEIPPKTYSLQIAWVGGFIAISIISFLSLLGVILVPLMNRVFFKFLLSFLVALAVGTLSGDAFLHLLPHSHASHHHSHSHEEPAMEMKRGPLFSHLSSQNIEESAYFDSTWKGLTALGGLYFMFLVEHVLTLIKQFKDKKKKNQKKPENDDDVEIKKQLSKYESQLSTNEEKVDTDDRTEGYLRADSQEPSHFDSQQPAVLEEEEVMIAHAHPQEVYNEYVPRGCKNKCHSHFHDTLGQSDDLIHHHHDYHHILHHHHHQNHHPHSHSQRYSREELKDAGVATLAWMVIMGDGLHNFSDGLAIGAAFTEGLSSGLSTSVAVFCHELPHELGDFAVLLKAGMTVKQAVLYNALSAMLAYLGMATGIFIGHYAENVSMWIFALTAGLFMYVALVDMVPEMLHNDASDHGCSRWGYFFLQNAGMLLGFGIMLLISIFEHKIVFRINF
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
32O-linked_GlycosylationKAAAFPQTTEKISPN
HHHHCCCCCCCCCCC		36.84OGP
33O-linked_GlycosylationAAAFPQTTEKISPNW
HHHCCCCCCCCCCCC		29.99OGP
35UbiquitinationAFPQTTEKISPNWES
HCCCCCCCCCCCCCC		46.5229967540
67N-linked_GlycosylationLFYRYGENNSLSVEG
HHHHHCCCCCCCHHH		38.7419349973
67N-linked_GlycosylationLFYRYGENNSLSVEG
HHHHHCCCCCCCHHH		38.7419349973
68N-linked_GlycosylationFYRYGENNSLSVEGF
HHHHCCCCCCCHHHH		39.7719349973
68N-linked_GlycosylationFYRYGENNSLSVEGF
HHHHCCCCCCCHHHH		39.7719349973
71PhosphorylationYGENNSLSVEGFRKL
HCCCCCCCHHHHHHH		20.2427251275
77 (in isoform 1)Ubiquitination-51.8221906983
77UbiquitinationLSVEGFRKLLQNIGI
CCHHHHHHHHHHCCC		51.8222817900
86UbiquitinationLQNIGIDKIKRIHIH
HHHCCCCCCEEEEEC		48.4829967540
88UbiquitinationNIGIDKIKRIHIHHD
HCCCCCCEEEEECCC		51.55-
143UbiquitinationASGKNKRKALCPDHD
CCCCCCCHHCCCCCC		47.5229967540
176UbiquitinationPEHASGRRNVKDSVS
CCCCCCCCCCCCCCC		56.6822817900
177UbiquitinationEHASGRRNVKDSVSA
CCCCCCCCCCCCCCH		43.7822817900
178UbiquitinationHASGRRNVKDSVSAS
CCCCCCCCCCCCCHH		7.4622817900
181UbiquitinationGRRNVKDSVSASEVT
CCCCCCCCCCHHHHH		16.5622817900
181 (in isoform 2)Ubiquitination-16.5621906983
182UbiquitinationRRNVKDSVSASEVTS
CCCCCCCCCHHHHHH		8.7522817900
182 (in isoform 2)Ubiquitination-8.7521906983
188PhosphorylationSVSASEVTSTVYNTV
CCCHHHHHHHHHHHH		18.0330576142
189PhosphorylationVSASEVTSTVYNTVS
CCHHHHHHHHHHHHH		22.5030576142
190O-linked_GlycosylationSASEVTSTVYNTVSE
CHHHHHHHHHHHHHC		20.04OGP
192 (in isoform 2)Ubiquitination-12.7621906983
192UbiquitinationSEVTSTVYNTVSEGT
HHHHHHHHHHHHCCC		12.7627667366
192PhosphorylationSEVTSTVYNTVSEGT
HHHHHHHHHHHHCCC		12.7629759185
193 (in isoform 2)Ubiquitination-29.6621906983
193UbiquitinationEVTSTVYNTVSEGTH
HHHHHHHHHHHCCCC		29.6621963094
194O-linked_GlycosylationVTSTVYNTVSEGTHF
HHHHHHHHHHCCCCE		14.02OGP
196PhosphorylationSTVYNTVSEGTHFLE
HHHHHHHHCCCCEEE		28.4129759185
196O-linked_GlycosylationSTVYNTVSEGTHFLE
HHHHHHHHCCCCEEE		28.4155828943
197 (in isoform 2)Ubiquitination-64.8721906983
197UbiquitinationTVYNTVSEGTHFLET
HHHHHHHCCCCEEEE		64.8721963094
198PhosphorylationVYNTVSEGTHFLETI
HHHHHHCCCCEEEEC		19.5832142685
203PhosphorylationSEGTHFLETIETPRP
HCCCCEEEECCCCCC		46.9632142685
204O-linked_GlycosylationEGTHFLETIETPRPG
CCCCEEEECCCCCCC		26.68OGP
207PhosphorylationHFLETIETPRPGKLF
CEEEECCCCCCCCCC		22.2830576142
208 (in isoform 2)Ubiquitination-27.9021906983
208UbiquitinationFLETIETPRPGKLFP
EEEECCCCCCCCCCC		27.9021963094
212UbiquitinationIETPRPGKLFPKDVS
CCCCCCCCCCCCCCC		50.0329967540
219O-linked_GlycosylationKLFPKDVSSSTPPSV
CCCCCCCCCCCCCCC		28.8055835647
220O-linked_GlycosylationLFPKDVSSSTPPSVT
CCCCCCCCCCCCCCC		37.77OGP
221PhosphorylationFPKDVSSSTPPSVTS
CCCCCCCCCCCCCCC		37.1125627689
221O-linked_GlycosylationFPKDVSSSTPPSVTS
CCCCCCCCCCCCCCC		37.1155835651
222PhosphorylationPKDVSSSTPPSVTSK
CCCCCCCCCCCCCCH		40.9625627689
222O-linked_GlycosylationPKDVSSSTPPSVTSK
CCCCCCCCCCCCCCH		40.9655835657
225O-linked_GlycosylationVSSSTPPSVTSKSRV
CCCCCCCCCCCHHHH		38.9555835663
227O-linked_GlycosylationSSTPPSVTSKSRVSR
CCCCCCCCCHHHHHH		34.4755835669
228O-linked_GlycosylationSTPPSVTSKSRVSRL
CCCCCCCCHHHHHHH		26.8655835675
229UbiquitinationTPPSVTSKSRVSRLA
CCCCCCCHHHHHHHH		32.6829967540
241N-linked_GlycosylationRLAGRKTNESVSEPR
HHHCCCCCCCCCCCC		42.4519349973
241N-linked_GlycosylationRLAGRKTNESVSEPR
HHHCCCCCCCCCCCC		42.4519349973
245PhosphorylationRKTNESVSEPRKGFM
CCCCCCCCCCCCCCC		51.6824719451
249UbiquitinationESVSEPRKGFMYSRN
CCCCCCCCCCCCCCC		68.1829967540
266N-linked_GlycosylationENPQECFNASKLLTS
CCHHHHCHHHHHHHH		55.77UniProtKB CARBOHYD
283N-linked_GlycosylationMGIQVPLNATEFNYL
CCEEECCCHHHHHHH		38.45UniProtKB CARBOHYD
307PhosphorylationARSCLIHTSEKKAEI
CCCCEEECCCCCCCC		31.4225690035
308PhosphorylationRSCLIHTSEKKAEIP
CCCEEECCCCCCCCC		33.0025690035
310UbiquitinationCLIHTSEKKAEIPPK
CEEECCCCCCCCCCC		57.9829967540
311UbiquitinationLIHTSEKKAEIPPKT
EEECCCCCCCCCCCE		47.39-
409PhosphorylationPLFSHLSSQNIEESA
CHHHHHCCCCCCHHH		33.34-
451UbiquitinationIKQFKDKKKKNQKKP
HHHHHHHHHHCCCCC		78.2022817900
452UbiquitinationKQFKDKKKKNQKKPE
HHHHHHHHHCCCCCC		63.8022817900
453UbiquitinationQFKDKKKKNQKKPEN
HHHHHHHHCCCCCCC		73.7722817900
456UbiquitinationDKKKKNQKKPENDDD
HHHHHCCCCCCCCCH		78.6221906983
456 (in isoform 1)Ubiquitination-78.6221906983
457UbiquitinationKKKKNQKKPENDDDV
HHHHCCCCCCCCCHH		48.0421906983
457 (in isoform 1)Ubiquitination-48.0421906983
467 (in isoform 1)Ubiquitination-22.4421906983
467UbiquitinationNDDDVEIKKQLSKYE
CCCHHHHHHHHHHHH		22.4421906983
468 (in isoform 1)Ubiquitination-63.2321906983
468UbiquitinationDDDVEIKKQLSKYES
CCHHHHHHHHHHHHH		63.2321906983
471PhosphorylationVEIKKQLSKYESQLS
HHHHHHHHHHHHHHC		30.6026055452
472 (in isoform 1)Ubiquitination-62.7221906983
472UbiquitinationEIKKQLSKYESQLST
HHHHHHHHHHHHHCC		62.7221906983
473PhosphorylationIKKQLSKYESQLSTN
HHHHHHHHHHHHCCC		19.8923927012
475PhosphorylationKQLSKYESQLSTNEE
HHHHHHHHHHCCCCC		33.0723927012
478PhosphorylationSKYESQLSTNEEKVD
HHHHHHHCCCCCCCC		22.8819664994
479PhosphorylationKYESQLSTNEEKVDT
HHHHHHCCCCCCCCC		56.0729255136
483 (in isoform 1)Ubiquitination-38.9521906983
483UbiquitinationQLSTNEEKVDTDDRT
HHCCCCCCCCCCCCC		38.9521963094
486PhosphorylationTNEEKVDTDDRTEGY
CCCCCCCCCCCCCCE		42.6729978859
490PhosphorylationKVDTDDRTEGYLRAD
CCCCCCCCCCEECCC		40.5323927012
493PhosphorylationTDDRTEGYLRADSQE
CCCCCCCEECCCCCC		6.1825884760
498PhosphorylationEGYLRADSQEPSHFD
CCEECCCCCCCCCCC		35.1428796482
502PhosphorylationRADSQEPSHFDSQQP
CCCCCCCCCCCCCCC		35.7128796482
506PhosphorylationQEPSHFDSQQPAVLE
CCCCCCCCCCCCEEC		29.7629523821
528PhosphorylationHAHPQEVYNEYVPRG
ECCHHHHHHHCCCCC		11.0928796482
531PhosphorylationPQEVYNEYVPRGCKN
HHHHHHHCCCCCCCC		16.4728796482
583PhosphorylationHSHSQRYSREELKDA
CCCCCCCCHHHHHHH		35.0924719451
684N-linked_GlycosylationFIGHYAENVSMWIFA
HHHHHHHHHHHHHHH		24.00UniProtKB CARBOHYD
719S-palmitoylationNDASDHGCSRWGYFF
CCCCCCCCCHHHHHH		1.9329575903
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 S39A6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S39A6_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 S39A6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of S39A6_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 S39A6_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-67; ASN-68 AND ASN-241,AND MASS SPECTROMETRY.
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-478, AND MASSSPECTROMETRY.

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