CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-034168
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 2-hydroxyacyl-CoA lyase 1 
Protein Synonyms/Alias
  
Gene Name
 Hacl1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
21EEQVSGAKVIAQALKubiquitination[1]
112EACRLYTKFSARPSTubiquitination[1]
129LIPFIIEKAVRSSIYubiquitination[1]
190ASVLRDAKQPLLIIGubiquitination[1]
198QPLLIIGKGAAYSHAubiquitination[1]
211HAEDSIRKLVEQCSLubiquitination[1]
227FLPTPMGKGVVPDNHubiquitination[1]
314QLLEQFDKTPWQCPPacetylation[2]
327PPDSQWWKTLREKMKacetylation[3]
327PPDSQWWKTLREKMKsuccinylation[3]
334KTLREKMKSNEAISKacetylation[3]
334KTLREKMKSNEAISKsuccinylation[3]
341KSNEAISKELASQKSacetylation[2, 3]
341KSNEAISKELASQKSsuccinylation[3]
341KSNEAISKELASQKSubiquitination[1]
347SKELASQKSLPMNYYubiquitination[1]
527QALQDTSKPCLLNIMubiquitination[1]
542IEPQSTRKAQDFHWLacetylation[3]
542IEPQSTRKAQDFHWLsuccinylation[3]
542IEPQSTRKAQDFHWLubiquitination[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]
 [2] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 554 AA 
Protein Sequence
MPESNSAEGS DRSEEQVSGA KVIAQALKTQ DVEYMFGVVG IPVTEIALAA QELGIKYIGM 60
RNEQAACYAA SAVGYLTGRP LIVIGGSSER NQEAMGAFQE FPQVEACRLY TKFSARPSTI 120
ELIPFIIEKA VRSSIYGRPG ACYIDIPADF VTLQANVTSI KYKECCMPPP VSMAETSAVC 180
AAASVLRDAK QPLLIIGKGA AYSHAEDSIR KLVEQCSLPF LPTPMGKGVV PDNHPNCVGA 240
ARSRALQSAD VIVLFGARLN WILHFGLPPR YQADVKFIQI DICAEELGNN VRPSVILLGD 300
IDAVSKQLLE QFDKTPWQCP PDSQWWKTLR EKMKSNEAIS KELASQKSLP MNYYTVFYHV 360
QEQLPRDSFI VSEGANTMDI GRTMLQNCLP RHRLDAGSFG TMGVGLGFAI AAALVAKDRS 420
PGQRVICVEG DSAFGFSGME VETICRYNLP IILLVVNNNG IYQGFDADTW EKMLHFQEAA 480
TTVPPMCLLP NSHYEQVMTA FGGKGYFVRT PEELQHSLRQ ALQDTSKPCL LNIMIEPQST 540
RKAQDFHWLT RSNM 554 
Gene Ontology
 GO:0005777; C:peroxisome; TAS:MGI.
 GO:0016829; F:lyase activity; IDA:MGI.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
 GO:0006629; P:lipid metabolic process; IDA:MGI. 
Interpro
 IPR012000; Thiamin_PyroP_enz_cen_dom.
 IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
 IPR011766; TPP_enzyme-bd_C. 
Pfam
 PF02775; TPP_enzyme_C
 PF00205; TPP_enzyme_M
 PF02776; TPP_enzyme_N 
SMART
  
PROSITE
  
PRINTS