CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021179
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine racemase 
Protein Synonyms/Alias
 D-serine ammonia-lyase; D-serine dehydratase; L-serine ammonia-lyase; L-serine dehydratase 
Gene Name
 SRR 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
45TGRNLFFKCELFQKTubiquitination[1]
51FKCELFQKTGSFKIRubiquitination[1]
56FQKTGSFKIRGALNAubiquitination[1]
115QTAPDCKKLAIQAYGubiquitination[1]
205KALKPSVKVYAAEPSubiquitination[1]
221ADDCYQSKLKGKLMPubiquitination[1]
223DCYQSKLKGKLMPNLubiquitination[1]
225YQSKLKGKLMPNLYPubiquitination[1]
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
 Catalyzes the synthesis of D-serine from L-serine. D- serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine. 
Sequence Annotation
 REGION 238 239 Substrate binding (By similarity).
 ACT_SITE 56 56 Proton acceptor (By similarity).
 ACT_SITE 84 84 Proton acceptor (By similarity).
 METAL 210 210 Magnesium.
 METAL 214 214 Magnesium; via carbonyl oxygen.
 METAL 216 216 Magnesium.
 BINDING 51 51 ATP (By similarity).
 BINDING 121 121 ATP (By similarity).
 BINDING 135 135 Substrate (Probable).
 MOD_RES 56 56 N6-(pyridoxal phosphate)lysine.
 MOD_RES 113 113 S-nitrosocysteine (By similarity).  
Keyword
 3D-structure; Allosteric enzyme; ATP-binding; Complete proteome; Direct protein sequencing; Isomerase; Lyase; Magnesium; Metal-binding; Nucleotide-binding; Pyridoxal phosphate; Reference proteome; S-nitrosylation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 340 AA 
Protein Sequence
MCAQYCISFA DVEKAHINIR DSIHLTPVLT SSILNQLTGR NLFFKCELFQ KTGSFKIRGA 60
LNAVRSLVPD ALERKPKAVV THSSGNHGQA LTYAAKLEGI PAYIVVPQTA PDCKKLAIQA 120
YGASIVYCEP SDESRENVAK RVTEETEGIM VHPNQEPAVI AGQGTIALEV LNQVPLVDAL 180
VVPVGGGGML AGIAITVKAL KPSVKVYAAE PSNADDCYQS KLKGKLMPNL YPPETIADGV 240
KSSIGLNTWP IIRDLVDDIF TVTEDEIKCA TQLVWERMKL LIEPTAGVGV AAVLSQHFQT 300
VSPEVKNICI VLSGGNVDLT SSITWVKQAE RPASYQSVSV 340 
Gene Ontology
 GO:0045177; C:apical part of cell; IEA:Compara.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0043025; C:neuronal cell body; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0005509; F:calcium ion binding; ISS:UniProtKB.
 GO:0008721; F:D-serine ammonia-lyase activity; IEA:EC.
 GO:0016594; F:glycine binding; ISS:UniProtKB.
 GO:0003941; F:L-serine ammonia-lyase activity; IDA:UniProtKB.
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
 GO:0030378; F:serine racemase activity; IDA:UniProtKB.
 GO:0018114; F:threonine racemase activity; ISS:UniProtKB.
 GO:0007568; P:aging; IEA:Compara.
 GO:0007420; P:brain development; IEA:Compara.
 GO:0070179; P:D-serine biosynthetic process; IDA:UniProtKB.
 GO:0006563; P:L-serine metabolic process; IDA:UniProtKB.
 GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
 GO:0042866; P:pyruvate biosynthetic process; IDA:UniProtKB.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0032496; P:response to lipopolysaccharide; IEP:UniProtKB.
 GO:0043278; P:response to morphine; IEA:Compara. 
Interpro
 IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
 IPR001926; Trp_syn_b_sub_like_PLP_eny_SF. 
Pfam
 PF00291; PALP 
SMART
  
PROSITE
 PS00165; DEHYDRATASE_SER_THR 
PRINTS