| Tag | Content |
|---|
| CPLM ID | CPLM-003836 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | AMP deaminase 1 |
Protein Synonyms/Alias | AMP deaminase isoform M; Myoadenylate deaminase |
Gene Name | Ampd1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 11 | FKLTGQGKQIDDAMR | acetylation | [1] | | 164 | RFPKTPSKYLRNIDG | acetylation | [1] | | 265 | TYTHRRLKFLSSKFQ | acetylation | [1] | | 321 | HLLRFIKKSYHIDAD | acetylation | [1] | | 469 | IYDVFRSKNFLPHFG | acetylation | [1] | | 699 | ISHEEKAKFLGNNYL | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | AMP deaminase plays a critical role in energy metabolism. |
Sequence Annotation | REGION 374 379 Substrate binding (By similarity).
REGION 650 653 Substrate binding (By similarity).
ACT_SITE 594 594 Proton acceptor (By similarity).
METAL 303 303 Zinc; catalytic (By similarity).
METAL 305 305 Zinc; catalytic (By similarity).
METAL 572 572 Zinc; catalytic (By similarity).
METAL 649 649 Zinc; catalytic (By similarity).
BINDING 305 305 Substrate (By similarity).
BINDING 575 575 Substrate (By similarity). |
Keyword | Complete proteome; Direct protein sequencing; Hydrolase; Metal-binding; Nucleotide metabolism; Reference proteome; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 747 AA |
Protein Sequence | MPLFKLTGQG KQIDDAMRSF AEKVFASEVK DEGGRHEISP FDVDEICPIS LREMQAHIFH 60
MENLSMSMDG RRKRRFQGRK TVNLSIPQSE TSSTKLSHIE EFISSSPTYE SVPDFQRVQI 120
TGDYASGVTV EDFEVVCKGL YRALCIREKY MQKSFQRFPK TPSKYLRNID GEALVAIESF 180
YPVFTPPPKK GEDPFRREDL PANLGYHLKM KGGVIYIYPD EAAASRDEPK PYPYPNLDDF 240
LDDMNFLLAL IAQGPVKTYT HRRLKFLSSK FQVHQMLNEM DELKELKNNP HRDFYNCRKV 300
DTHIHAAACM NQKHLLRFIK KSYHIDADRV VYSTKEKNLT LKELFAQLNM HPYDLTVDSL 360
DVHAGRQTFQ RFDKFNDKYN PVGASELRDL YLKTDNYING EYFATIIKEV GADLVDAKYQ 420
HAEPRLSIYG RSPDEWSKLS SWFVGNRIYC PNMTWMIQVP RIYDVFRSKN FLPHFGKMLE 480
NIFLPVFEAT INPQTHPDLS VFLKHITGFD SVDDESKHSG HMFSSKSPKP EEWTMENNPS 540
YTYYAYYMYA NIMVLNCLRK ERGMNTFLFR PHCGEAGALT HLMTAFMIAD NISHGLNLKK 600
SPVLQYLFFL AQIPIAMSPL SNNSLFLEYA KNPFLDFLQK GLMISLSTDD PMQFHFTKEP 660
LMEEYAIAAQ VFKLSTCDMC EVARNSVLQC GISHEEKAKF LGNNYLEEGP VGNDIRRTNV 720
AQIRMAYRYE TWCYELNLIA EGLKSTE 747 |
Gene Ontology | GO:0003876; F:AMP deaminase activity; IEA:EC. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0032036; F:myosin heavy chain binding; IDA:RGD. GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway. GO:0010033; P:response to organic substance; IDA:RGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |