CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013746
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Threonine synthase-like 2 
Protein Synonyms/Alias
 TSH2 
Gene Name
 Thnsl2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
354TQSLHLPKDLHSKLSacetylation[1]
448EILALEHKETRCTPMacetylation[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
 Acts as a catabolic phospho-lyase on both gamma- and beta-phosphorylated substrates. Degrades O-phospho-threonine (PThr) to alpha-ketobutyrate, ammonia and phosphate (By similarity). 
Sequence Annotation
 MOD_RES 113 113 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Complete proteome; Lyase; Pyridoxal phosphate; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 485 AA 
Protein Sequence
MWYTSTRGMA PRVNFEGALF SGYAPDGGLY MPEELPRLDK ETLRHWSTLS YRSLVKELCA 60
LFVGLELIPR HDLNGLIDQA FSRFRHRDVV HLCKLKNGLN ILELWHGVTY AFKDLSLSCT 120
AQFLQYFLEK KKKHVTIVVG TSGDTGSAAI ESVQGSKNVD IIVLLPKGHC SKIQELQMTT 180
VVKENVHVFG VEGNSDELDE PIKAVFADVA FVQRHNLMSL NSINWSRVLV QMAHHFFAYF 240
QCTPSLDMHL LPTVEVVVPT GAGGNLAAGC IAQKMGLPIS LVVAVNRNDI IHRTVQKGDF 300
SLCEVVRKTL ASAMDIQVPY NMERIFWLLA GSDSQTTRAL MEQFERTQSL HLPKDLHSKL 360
SEAVTSESVS DEAITQTMGR CWEENQYLLC PHSATAVSYH YQQTDSGQPS SIPRCCLAPA 420
SAVKFPEAVQ AAGLTPETPA EILALEHKET RCTPMRRGDD WTQMLRDTIE ALSLRWKGCV 480
ENTAE 485 
Gene Ontology
 GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
 GO:0030170; F:pyridoxal phosphate binding; IEA:Compara.
 GO:0070905; F:serine binding; IEA:Compara.
 GO:0046360; P:2-oxobutyrate biosynthetic process; IEA:Compara.
 GO:0016311; P:dephosphorylation; IEA:Compara.
 GO:0009071; P:serine family amino acid catabolic process; IEA:Compara. 
Interpro
 IPR004450; Thr_synthase_like.
 IPR001926; Trp_syn_b_sub_like_PLP_eny_SF.
 IPR027457; TSH2_metazoan. 
Pfam
 PF00291; PALP 
SMART
  
PROSITE
  
PRINTS