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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
1 | Sulfoxidation | -------MDPNCSCA -------CCCCCCCC | 20.42 | 28465586 | |
1 | Acetylation | -------MDPNCSCA -------CCCCCCCC | 20.42 | 19413330 | |
6 | Phosphorylation | --MDPNCSCAAGDSC --CCCCCCCCCCCCC | 17.27 | 23927012 | |
12 | Phosphorylation | CSCAAGDSCTCAGSC CCCCCCCCCCCCCCC | 15.48 | 23927012 | |
14 | Phosphorylation | CAAGDSCTCAGSCKC CCCCCCCCCCCCCCC | 14.89 | 23927012 | |
18 | Phosphorylation | DSCTCAGSCKCKECK CCCCCCCCCCCCCCC | 7.59 | 30576142 | |
20 | Acetylation | CTCAGSCKCKECKCT CCCCCCCCCCCCCCC | 50.46 | 25953088 | |
20 | Ubiquitination | CTCAGSCKCKECKCT CCCCCCCCCCCCCCC | 50.46 | 23503661 | |
22 | Ubiquitination | CAGSCKCKECKCTSC CCCCCCCCCCCCCCC | 52.20 | 23503661 | |
22 | Acetylation | CAGSCKCKECKCTSC CCCCCCCCCCCCCCC | 52.20 | 18528997 | |
25 | Ubiquitination | SCKCKECKCTSCKKS CCCCCCCCCCCCCCC | 41.46 | 27667366 | |
30 | Ubiquitination | ECKCTSCKKSCCSCC CCCCCCCCCCCCCCC | 47.70 | 23503661 | |
31 | Ubiquitination | CKCTSCKKSCCSCCP CCCCCCCCCCCCCCC | 53.72 | 23503661 | |
32 | Phosphorylation | KCTSCKKSCCSCCPV CCCCCCCCCCCCCCC | 13.07 | 22777824 | |
35 | Phosphorylation | SCKKSCCSCCPVGCA CCCCCCCCCCCCCCC | 24.07 | 28258704 | |
43 | Ubiquitination | CCPVGCAKCAQGCIC CCCCCCCHHHCCCEE | 33.89 | 29901268 | |
43 | Acetylation | CCPVGCAKCAQGCIC CCCCCCCHHHCCCEE | 33.89 | 25953088 | |
43 | Neddylation | CCPVGCAKCAQGCIC CCCCCCCHHHCCCEE | 33.89 | 32015554 | |
51 | Acetylation | CAQGCICKGASDKCS HHCCCEECCCCCCCC | 37.28 | 16916647 | |
51 | Ubiquitination | CAQGCICKGASDKCS HHCCCEECCCCCCCC | 37.28 | 23000965 | |
54 | Phosphorylation | GCICKGASDKCSCCA CCEECCCCCCCCCCC | 46.39 | 23312004 | |
56 | Acetylation | ICKGASDKCSCCA-- EECCCCCCCCCCC-- | 26.08 | 26210075 | |
56 | Ubiquitination | ICKGASDKCSCCA-- EECCCCCCCCCCC-- | 26.08 | 23000965 | |
58 | Phosphorylation | KGASDKCSCCA---- CCCCCCCCCCC---- | 20.26 | 28985074 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MT2_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
KPCD1_HUMAN | PRKD1 | physical | 14550308 | |
ZN363_HUMAN | RCHY1 | physical | 21988832 | |
JHD2C_HUMAN | JMJD1C | physical | 23455924 | |
ARF6_HUMAN | ARF6 | physical | 15923660 |
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Acetylation | |
Reference | PubMed |
"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. |