S39AA_HUMAN - dbPTM
S39AA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S39AA_HUMAN
UniProt AC Q9ULF5
Protein Name Zinc transporter ZIP10
Gene Name SLC39A10
Organism Homo sapiens (Human).
Sequence Length 831
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description May act as a zinc-influx transporter..
Protein Sequence MKVHMHTKFCLICLLTFIFHHCNHCHEEHDHGPEALHRQHRGMTELEPSKFSKQAAENEKKYYIEKLFERYGENGRLSFFGLEKLLTNLGLGERKVVEINHEDLGHDHVSHLDILAVQEGKHFHSHNHQHSHNHLNSENQTVTSVSTKRNHKCDPEKETVEVSVKSDDKHMHDHNHRLRHHHRLHHHLDHNNTHHFHNDSITPSERGEPSNEPSTETNKTQEQSDVKLPKGKRKKKGRKSNENSEVITPGFPPNHDQGEQYEHNRVHKPDRVHNPGHSHVHLPERNGHDPGRGHQDLDPDNEGELRHTRKREAPHVKNNAIISLRKDLNEDDHHHECLNVTQLLKYYGHGANSPISTDLFTYLCPALLYQIDSRLCIEHFDKLLVEDINKDKNLVPEDEANIGASAWICGIISITVISLLSLLGVILVPIINQGCFKFLLTFLVALAVGTMSGDALLHLLPHSQGGHDHSHQHAHGHGHSHGHESNKFLEEYDAVLKGLVALGGIYLLFIIEHCIRMFKHYKQQRGKQKWFMKQNTEESTIGRKLSDHKLNNTPDSDWLQLKPLAGTDDSVVSEDRLNETELTDLEGQQESPPKNYLCIEEEKIIDHSHSDGLHTIHEHDLHAAAHNHHGENKTVLRKHNHQWHHKHSHHSHGPCHSGSDLKETGIANIAWMVIMGDGIHNFSDGLAIGAAFSAGLTGGISTSIAVFCHELPHELGDFAVLLKAGMTVKQAIVYNLLSAMMAYIGMLIGTAVGQYANNITLWIFAVTAGMFLYVALVDMLPEMLHGDGDNEEHGFCPVGQFILQNLGLLFGFAIMLVIALYEDKIVFDIQF
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
44PhosphorylationHRQHRGMTELEPSKF
HHHHCCCCCCCCCHH		40.00-
49PhosphorylationGMTELEPSKFSKQAA
CCCCCCCCHHHHHHH		36.64-
49O-linked_GlycosylationGMTELEPSKFSKQAA
CCCCCCCCHHHHHHH		36.64OGP
50UbiquitinationMTELEPSKFSKQAAE
CCCCCCCHHHHHHHH		65.4621890473
52PhosphorylationELEPSKFSKQAAENE
CCCCCHHHHHHHHHH		27.82-
53UbiquitinationLEPSKFSKQAAENEK
CCCCHHHHHHHHHHH		47.27-
66UbiquitinationEKKYYIEKLFERYGE
HHHHHHHHHHHHHCC		49.2521890473
83UbiquitinationRLSFFGLEKLLTNLG
CEEEEHHHHHHHHCC		41.8821890473
112UbiquitinationGHDHVSHLDILAVQE
CCCCCCHHHEEEEEC		3.22-
139N-linked_GlycosylationHNHLNSENQTVTSVS
CCCCCCCCCEEEEEE		42.52UniProtKB CARBOHYD
141O-linked_GlycosylationHLNSENQTVTSVSTK
CCCCCCCEEEEEECC		37.01OGP
159O-linked_GlycosylationKCDPEKETVEVSVKS
CCCCCCCEEEEEEEC		32.79OGP
198N-linked_GlycosylationNNTHHFHNDSITPSE
CCCCCCCCCCCCHHH		43.72UniProtKB CARBOHYD
210O-linked_GlycosylationPSERGEPSNEPSTET
HHHCCCCCCCCCCCC		49.9155830831
214O-linked_GlycosylationGEPSNEPSTETNKTQ
CCCCCCCCCCCCCCH		32.47OGP
215O-linked_GlycosylationEPSNEPSTETNKTQE
CCCCCCCCCCCCCHH		58.50OGP
218N-linked_GlycosylationNEPSTETNKTQEQSD
CCCCCCCCCCHHHHC		38.86UniProtKB CARBOHYD
248O-linked_GlycosylationNENSEVITPGFPPNH
CCCCCCCCCCCCCCC		23.6455829247
323PhosphorylationVKNNAIISLRKDLNE
CCCCEEEEEECCCCC		18.9329691806
339N-linked_GlycosylationDHHHECLNVTQLLKY
CCHHHHCCHHHHHHH		46.58UniProtKB CARBOHYD
346PhosphorylationNVTQLLKYYGHGANS
CHHHHHHHHCCCCCC		18.0430576142
347PhosphorylationVTQLLKYYGHGANSP
HHHHHHHHCCCCCCC		10.8924043423
353PhosphorylationYYGHGANSPISTDLF
HHCCCCCCCCCHHHH		24.0730576142
356PhosphorylationHGANSPISTDLFTYL
CCCCCCCCHHHHHHH		21.1824043423
357PhosphorylationGANSPISTDLFTYLC
CCCCCCCHHHHHHHH		37.1224043423
361PhosphorylationPISTDLFTYLCPALL
CCCHHHHHHHHHHHH		23.9230576142
362PhosphorylationISTDLFTYLCPALLY
CCHHHHHHHHHHHHH		10.0424043423
369PhosphorylationYLCPALLYQIDSRLC
HHHHHHHHHHCCHHH		12.3124043423
373PhosphorylationALLYQIDSRLCIEHF
HHHHHHCCHHHHHHH		28.8724043423
390UbiquitinationLLVEDINKDKNLVPE
HHHHHHHCCCCCCCH		71.1121890473
435S-palmitoylationVPIINQGCFKFLLTF
HHHHCCHHHHHHHHH		2.1229575903
533UbiquitinationGKQKWFMKQNTEEST
CCCCCCHHCCCCCCC		30.8121890473
536PhosphorylationKWFMKQNTEESTIGR
CCCHHCCCCCCCHHH		38.3423401153
539PhosphorylationMKQNTEESTIGRKLS
HHCCCCCCCHHHHHC		21.0629255136
540PhosphorylationKQNTEESTIGRKLSD
HCCCCCCCHHHHHCC		30.6323401153
544UbiquitinationEESTIGRKLSDHKLN
CCCCHHHHHCCCCCC		47.32-
546PhosphorylationSTIGRKLSDHKLNNT
CCHHHHHCCCCCCCC		40.4825159151
549UbiquitinationGRKLSDHKLNNTPDS
HHHHCCCCCCCCCCC		58.88-
553PhosphorylationSDHKLNNTPDSDWLQ
CCCCCCCCCCCCCCC		27.6525159151
556PhosphorylationKLNNTPDSDWLQLKP
CCCCCCCCCCCCCCC		31.7122199227
562UbiquitinationDSDWLQLKPLAGTDD
CCCCCCCCCCCCCCC		25.6521890473
567PhosphorylationQLKPLAGTDDSVVSE
CCCCCCCCCCCCCCH		30.9030576142
570PhosphorylationPLAGTDDSVVSEDRL
CCCCCCCCCCCHHHC		27.5125159151
573PhosphorylationGTDDSVVSEDRLNET
CCCCCCCCHHHCCCC		31.4625159151
580PhosphorylationSEDRLNETELTDLEG
CHHHCCCCCCCCCCC		34.9129255136
583PhosphorylationRLNETELTDLEGQQE
HCCCCCCCCCCCCCC		32.1030266825
591PhosphorylationDLEGQQESPPKNYLC
CCCCCCCCCCCCEEE		42.0119664994
594UbiquitinationGQQESPPKNYLCIEE
CCCCCCCCCEEEEEC		62.70-
596PhosphorylationQESPPKNYLCIEEEK
CCCCCCCEEEEECEE		14.7430266825
608PhosphorylationEEKIIDHSHSDGLHT
CEEEECCCCCCCCEE		22.4229449344
610PhosphorylationKIIDHSHSDGLHTIH
EEECCCCCCCCEEHH		36.0729449344
615PhosphorylationSHSDGLHTIHEHDLH
CCCCCCEEHHHHHHH		29.1329449344
634PhosphorylationNHHGENKTVLRKHNH
CCCCCCCEECCCCCC		36.0324719451
638UbiquitinationENKTVLRKHNHQWHH
CCCEECCCCCCCCCC		44.60-
648PhosphorylationHQWHHKHSHHSHGPC
CCCCCCCCCCCCCCC		27.9129449344
651PhosphorylationHHKHSHHSHGPCHSG
CCCCCCCCCCCCCCC		25.3929449344
734PhosphorylationTVKQAIVYNLLSAMM
CHHHHHHHHHHHHHH		8.2523879269
743PhosphorylationLLSAMMAYIGMLIGT
HHHHHHHHHHHHHHH		4.7023879269
750PhosphorylationYIGMLIGTAVGQYAN
HHHHHHHHHHHHHHH		15.9223879269
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 S39AA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S39AA_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 S39AA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of S39AA_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 S39AA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, AND MASSSPECTROMETRY.
"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 THR-553, AND MASSSPECTROMETRY.

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