CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016063
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Threonine synthase-like 2 
Protein Synonyms/Alias
 TSH2; mTSH2 
Gene Name
 Thnsl2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
297IIHRTVQKGDFSLCEubiquitination[1]
354TQSLQLPKDLHNKLSubiquitination[1]
359LPKDLHNKLSEAVTSubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
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. Also degrades O-phospho-homoserine (PHS), but this is not its physiological substrate. 
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
 483 AA 
Protein Sequence
MWYTSTRGMA PRVNFEGALF SGYAPDGGLY MPEELPRLDE ETLRHWSTLS YRSLVKELCA 60
LFIGLELIPR HDLNDLIDRA FSRFRHRNVV HLCKLKNGLN ILELWHGVTY AFKDLSLSCT 120
AQFLQYFLEK KKKHVTIVVG TSGDTGSAAI ESVQGSKNVD IIVLLPKGHC SKIQELQMTT 180
VLKENVHVFE VEGNSDELDE PIKAVFADVA FVQRHNVMSL NSINWSRVLV QMAHHFFAYF 240
QCTPSLDTHP LPTVEVVVPT GAGGNLAAGC IAQKMGLPIC LVVAVNRNDI IHRTVQKGDF 300
SLCEVLRTTL ASAMDIQVPY NMERIFWLLS GSDSQTTRAL MEQFERTQSL QLPKDLHNKL 360
SEAVTSESVT DEAITQTMAR CWEENQYLLC PHSATAVNYH YQQTDSGQSS IRCCLASASA 420
VKFPEAVQAA GLTPETPAEI LALEHKETRC IPMRRGDDWT QMLRVTIEGL SQRWKDCVVN 480
PSE 483 
Gene Ontology
 GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
 GO:0030170; F:pyridoxal phosphate binding; IDA:MGI.
 GO:0070905; F:serine binding; IDA:BHF-UCL.
 GO:0046360; P:2-oxobutyrate biosynthetic process; IDA:BHF-UCL.
 GO:0016311; P:dephosphorylation; IDA:BHF-UCL.
 GO:0009071; P:serine family amino acid catabolic process; IDA:BHF-UCL. 
Interpro
 IPR004450; Thr_synthase_like.
 IPR001926; Trp_syn_b_sub_like_PLP_eny_SF.
 IPR027457; TSH2_metazoan. 
Pfam
 PF00291; PALP 
SMART
  
PROSITE
  
PRINTS