ZNT9_HUMAN - dbPTM
ZNT9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZNT9_HUMAN
UniProt AC Q6PML9
Protein Name Zinc transporter 9
Gene Name SLC30A9
Organism Homo sapiens (Human).
Sequence Length 568
Subcellular Localization Membrane
Multi-pass membrane protein . Nucleus . Cytoplasm . Cytoplasmic vesicle . Endoplasmic reticulum . Mainly in the cytoplasm (PubMed:10409434). Partial co-localization with endoplasmic reticulum (PubMed:28334855).
Protein Description Acts as a zinc transporter involved in intracellular zinc homeostasis. [PubMed: 28334855 Functions as a secondary coactivator for nuclear receptors by cooperating with p160 coactivators subtypes. Plays a role in transcriptional activation of Wnt-responsive genes (By similarity]
Protein Sequence MLPGLAAAAAHRCSWSSLCRLRLRCRAAACNPSDRQEWQNLVTFGSFSNMVPCSHPYIGTLSQVKLYSTNVQKEGQGSQTLRVEKVPSFETAEGIGTELKAPLKQEPLQVRVKAVLKKREYGSKYTQNNFITGVRAINEFCLKSSDLEQLRKIRRRSPHEDTESFTVYLRSDVEAKSLEVWGSPEALAREKKLRKEAEIEYRERLFRNQKILREYRDFLGNTKPRSRTASVFFKGPGKVVMVAICINGLNCFFKFLAWIYTGSASMFSEAIHSLSDTCNQGLLALGISKSVQTPDPSHPYGFSNMRYISSLISGVGIFMMGAGLSWYHGVMGLLHPQPIESLLWAYCILAGSLVSEGATLLVAVNELRRNARAKGMSFYKYVMESRDPSTNVILLEDTAAVLGVIIAATCMGLTSITGNPLYDSLGSLGVGTLLGMVSAFLIYTNTEALLGRSIQPEQVQRLTELLENDPSVRAIHDVKATDLGLGKVRFKAEVDFDGRVVTRSYLEKQDFDQMLQEIQEVKTPEELETFMLKHGENIIDTLGAEVDRLEKELKKRNPEVRHVDLEIL
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
73UbiquitinationLYSTNVQKEGQGSQT
EEECCCCCCCCCCCE
60.57-
88PhosphorylationLRVEKVPSFETAEGI
EEEEECCCCCCCCCC
38.4126471730
183PhosphorylationKSLEVWGSPEALARE
HHEEECCCHHHHHHH
12.1226471730
222PhosphorylationYRDFLGNTKPRSRTA
HHHHHCCCCCCCCEE
40.40-
223UbiquitinationRDFLGNTKPRSRTAS
HHHHCCCCCCCCEEE
42.29-
230PhosphorylationKPRSRTASVFFKGPG
CCCCCEEEEEEECCC
20.88-
303PhosphorylationPSHPYGFSNMRYISS
CCCCCCCCCHHHHHH
25.9224719451
374MalonylationLRRNARAKGMSFYKY
HHHHHHHCCCCHHHH
49.9826320211
471PhosphorylationELLENDPSVRAIHDV
HHHHCCCCCHHHEEE
27.3929449344
479UbiquitinationVRAIHDVKATDLGLG
CHHHEEEECCCCCCC
52.18-
4792-HydroxyisobutyrylationVRAIHDVKATDLGLG
CHHHEEEECCCCCCC
52.18-
479MalonylationVRAIHDVKATDLGLG
CHHHEEEECCCCCCC
52.1826320211
487UbiquitinationATDLGLGKVRFKAEV
CCCCCCCEEEEEEEE
34.97-
487MalonylationATDLGLGKVRFKAEV
CCCCCCCEEEEEEEE
34.9726320211
541O-linked_GlycosylationHGENIIDTLGAEVDR
HCCCHHHHHHHHHHH
19.38OGP

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 ZNT9_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZNT9_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 ZNT9_HUMAN !!

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

Oops, there are no PPI records of ZNT9_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZNT9_HUMAN

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Related Literatures of Post-Translational Modification

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