Tag | Content |
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CPLM ID | CPLM-022996 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | A/G-specific adenine DNA glycosylase |
Protein Synonyms/Alias | MutY homolog; hMYH |
Gene Name | MUTYH |
Gene Synonyms/Alias | MYH |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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41 | EGRQKHAKNNSQAKP | ubiquitination | [1] | 47 | AKNNSQAKPSACDGL | ubiquitination | [1] | 94 | LSWYDQEKRDLPWRR | ubiquitination | [1] | 178 | RLQEGARKVVEELGG | ubiquitination | [1] | 404 | PSEQLQRKALLQELQ | ubiquitination | [1] | 495 | PGTCMGSKRSQVSSP | ubiquitination | [1] |
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Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | Involved in oxidative DNA damage repair. Initiates repair of A*oxoG to C*G by removing the inappropriately paired adenine base from the DNA backbone. Possesses both adenine and 2- OH-A DNA glycosylase activities. |
Sequence Annotation | DOMAIN 364 495 Nudix hydrolase. MOTIF 404 426 Nudix box. METAL 287 287 Iron-sulfur (4Fe-4S) (By similarity). METAL 294 294 Iron-sulfur (4Fe-4S) (By similarity). METAL 297 297 Iron-sulfur (4Fe-4S) (By similarity). METAL 303 303 Iron-sulfur (4Fe-4S) (By similarity). |
Keyword | 3D-structure; 4Fe-4S; Alternative splicing; Complete proteome; Disease mutation; DNA damage; DNA repair; Glycosidase; Hydrolase; Iron; Iron-sulfur; Metal-binding; Nucleus; Polymorphism; Reference proteome; Tumor suppressor. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 546 AA |
Protein Sequence | MTPLVSRLSR LWAIMRKPRA AVGSGHRKQA ASQEGRQKHA KNNSQAKPSA CDGLARQPEE 60 VVLQASVSSY HLFRDVAEVT AFRGSLLSWY DQEKRDLPWR RRAEDEMDLD RRAYAVWVSE 120 VMLQQTQVAT VINYYTGWMQ KWPTLQDLAS ASLEEVNQLW AGLGYYSRGR RLQEGARKVV 180 EELGGHMPRT AETLQQLLPG VGRYTAGAIA SIAFGQATGV VDGNVARVLC RVRAIGADPS 240 STLVSQQLWG LAQQLVDPAR PGDFNQAAME LGATVCTPQR PLCSQCPVES LCRARQRVEQ 300 EQLLASGSLS GSPDVEECAP NTGQCHLCLP PSEPWDQTLG VVNFPRKASR KPPREESSAT 360 CVLEQPGALG AQILLVQRPN SGLLAGLWEF PSVTWEPSEQ LQRKALLQEL QRWAGPLPAT 420 HLRHLGEVVH TFSHIKLTYQ VYGLALEGQT PVTTVPPGAR WLTQEEFHTA AVSTAMKKVF 480 RVYQGQQPGT CMGSKRSQVS SPCSRKKPRM GQQVLDNFFR SHISTDAHSL NSAAQ 535 |
Gene Ontology | GO:0005739; C:mitochondrion; IEA:Compara. GO:0005654; C:nucleoplasm; TAS:Reactome. GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. GO:0004519; F:endonuclease activity; IEA:InterPro. GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0032407; F:MutSalpha complex binding; IDA:HGNC. GO:0045007; P:depurination; TAS:Reactome. GO:0006298; P:mismatch repair; TAS:ProtInc. |
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