CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019946
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphoserine phosphatase 
Protein Synonyms/Alias
 PSP; PSPase; O-phosphoserine phosphohydrolase 
Gene Name
 Psph 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
122IVEHVAAKLNIPTTNacetylation[1]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441
Functional Description
 Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates (By similarity). 
Sequence Annotation
 REGION 109 110 Substrate binding (By similarity).
 ACT_SITE 20 20 Nucleophile (By similarity).
 ACT_SITE 22 22 Proton donor (By similarity).
 METAL 20 20 Magnesium (By similarity).
 METAL 22 22 Magnesium; via carbonyl oxygen (By
 METAL 179 179 Magnesium (By similarity).
 BINDING 29 29 Substrate (By similarity).
 BINDING 65 65 Substrate (By similarity).
 BINDING 158 158 Substrate (By similarity).
 MOD_RES 1 1 N-acetylmethionine (By similarity).  
Keyword
 Acetylation; Amino-acid biosynthesis; Complete proteome; Hydrolase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome; Serine biosynthesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 225 AA 
Protein Sequence
MVSHSELRKL FCSADAVCFD VDSTVIREEG IDELAKFCGV EAAVSEMTRR AMGGALPFKD 60
ALTQRLALIQ PSRDQVQRLL AEHPPHLTPG IRELVSRLQE RNVQVFLISG GFRSIVEHVA 120
AKLNIPTTNV FANRLKFYFN GEYAGFDEMQ PTAESGGKGK VIRFLKEKFH FKKIIMIGDG 180
ATDMEACPPA DAFIGFGGNV IRQQVKDNAK WYITDFVELL GELEE 225 
Gene Ontology
 GO:0005737; C:cytoplasm; IBA:RefGenome.
 GO:0043005; C:neuron projection; IEA:Compara.
 GO:0005509; F:calcium ion binding; ISS:UniProtKB.
 GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
 GO:0004647; F:phosphoserine phosphatase activity; ISS:UniProtKB.
 GO:0006564; P:L-serine biosynthetic process; IBA:RefGenome.
 GO:0009612; P:response to mechanical stimulus; IEA:Compara.
 GO:0031667; P:response to nutrient levels; IEA:Compara.
 GO:0033574; P:response to testosterone stimulus; IEA:Compara. 
Interpro
 IPR023214; HAD-like_dom.
 IPR006383; HAD-SF_hydro_IB_PSP-like.
 IPR023190; Pser_Pase_dom_2.
 IPR004469; SerB. 
Pfam
  
SMART
  
PROSITE
  
PRINTS