MT2_HUMAN - dbPTM
MT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MT2_HUMAN
UniProt AC P02795
Protein Name Metallothionein-2
Gene Name MT2A
Organism Homo sapiens (Human).
Sequence Length 61
Subcellular Localization
Protein Description Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids..
Protein Sequence MDPNCSCAAGDSCTCAGSCKCKECKCTSCKKSCCSCCPVGCAKCAQGCICKGASDKCSCCA
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
1Sulfoxidation-------MDPNCSCA
-------CCCCCCCC
20.4228465586
1Acetylation-------MDPNCSCA
-------CCCCCCCC
20.4219413330
6Phosphorylation--MDPNCSCAAGDSC
--CCCCCCCCCCCCC
17.2723927012
12PhosphorylationCSCAAGDSCTCAGSC
CCCCCCCCCCCCCCC
15.4823927012
14PhosphorylationCAAGDSCTCAGSCKC
CCCCCCCCCCCCCCC
14.8923927012
18PhosphorylationDSCTCAGSCKCKECK
CCCCCCCCCCCCCCC
7.5930576142
20AcetylationCTCAGSCKCKECKCT
CCCCCCCCCCCCCCC
50.4625953088
20UbiquitinationCTCAGSCKCKECKCT
CCCCCCCCCCCCCCC
50.4623503661
22UbiquitinationCAGSCKCKECKCTSC
CCCCCCCCCCCCCCC
52.2023503661
22AcetylationCAGSCKCKECKCTSC
CCCCCCCCCCCCCCC
52.2018528997
25UbiquitinationSCKCKECKCTSCKKS
CCCCCCCCCCCCCCC
41.4627667366
30UbiquitinationECKCTSCKKSCCSCC
CCCCCCCCCCCCCCC
47.7023503661
31UbiquitinationCKCTSCKKSCCSCCP
CCCCCCCCCCCCCCC
53.7223503661
32PhosphorylationKCTSCKKSCCSCCPV
CCCCCCCCCCCCCCC
13.0722777824
35PhosphorylationSCKKSCCSCCPVGCA
CCCCCCCCCCCCCCC
24.0728258704
43UbiquitinationCCPVGCAKCAQGCIC
CCCCCCCHHHCCCEE
33.8929901268
43AcetylationCCPVGCAKCAQGCIC
CCCCCCCHHHCCCEE
33.8925953088
43NeddylationCCPVGCAKCAQGCIC
CCCCCCCHHHCCCEE
33.8932015554
51AcetylationCAQGCICKGASDKCS
HHCCCEECCCCCCCC
37.2816916647
51UbiquitinationCAQGCICKGASDKCS
HHCCCEECCCCCCCC
37.2823000965
54PhosphorylationGCICKGASDKCSCCA
CCEECCCCCCCCCCC
46.3923312004
56AcetylationICKGASDKCSCCA--
EECCCCCCCCCCC--
26.0826210075
56UbiquitinationICKGASDKCSCCA--
EECCCCCCCCCCC--
26.0823000965
58PhosphorylationKGASDKCSCCA----
CCCCCCCCCCC----
20.2628985074

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 MT2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MT2_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 MT2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KPCD1_HUMANPRKD1physical
14550308
ZN363_HUMANRCHY1physical
21988832
JHD2C_HUMANJMJD1Cphysical
23455924
ARF6_HUMANARF6physical
15923660

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
DB00958Carboplatin
DB00515Cisplatin
DB00526Oxaliplatin
Regulatory Network of MT2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
"Primary structure of human hepatic metallothionein.";
Kissling M.M., Kaegi J.H.R.;
FEBS Lett. 82:247-250(1977).
Cited for: PRELIMINARY PROTEIN SEQUENCE.
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51, AND MASS SPECTROMETRY.

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