CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023021
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 2-hydroxyacyl-CoA lyase 1 
Protein Synonyms/Alias
 2-hydroxyphytanoyl-CoA lyase; 2-HPCL; Phytanoyl-CoA 2-hydroxylase 2 
Gene Name
 HACL1 
Gene Synonyms/Alias
 HPCL; HPCL2; PHYH2; HSPC279 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
18EEQVSGAKVIAQALKubiquitination[1, 2]
136EACRLYTKFSARPSSubiquitination[2]
153AIPFVIEKAVRSSIYubiquitination[2, 3, 4]
214ASVIRNAKQPLLIIGubiquitination[2, 4]
241KKLVEQYKLPFLPTPubiquitination[2, 4]
251FLPTPMGKGVVPDNHubiquitination[2]
365KSNEAASKELASKKSubiquitination[1, 2]
540QTPEELQKSLRQSLAubiquitination[1, 2, 4, 5, 6, 7]
551QSLADTTKPSLINIMubiquitination[2]
566IEPQATRKAQDFHWLubiquitination[2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] 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]
 [3] Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry.
 Denis NJ, Vasilescu J, Lambert JP, Smith JC, Figeys D.
 Proteomics. 2007 Mar;7(6):868-74. [PMID: 17370265]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Catalyzes a carbon-carbon cleavage reaction; cleaves a 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. 
Sequence Annotation
 REGION 401 486 Thiamine pyrophosphate binding.
 MOTIF 576 578 Microbody targeting signal.
 METAL 455 455 Magnesium (By similarity).
 METAL 482 482 Magnesium (By similarity).
 BINDING 60 60 Thiamine pyrophosphate (By similarity).
 MOD_RES 4 4 Phosphoserine (By similarity).  
Keyword
 Complete proteome; Lyase; Magnesium; Metal-binding; Peroxisome; Phosphoprotein; Reference proteome; Thiamine pyrophosphate. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 578 AA 
Protein Sequence
MPDSNFAERS EEQVSGAKVI AQALKTQDVE YIFGIVGIPV TEIAIAAQQL GIKYIGMRNE 60
QAACYAASAI GYLTSRPGVC LVVSGPGLIH ALGGMANANM NCWPLLVIGG SSERNQETMG 120
AFQEFPQVEA CRLYTKFSAR PSSIEAIPFV IEKAVRSSIY GRPGACYVDI PADFVNLQVN 180
VNSIKYMERC MSPPISMAET SAVCTAASVI RNAKQPLLII GKGAAYAHAE ESIKKLVEQY 240
KLPFLPTPMG KGVVPDNHPY CVGAARSRAL QFADVIVLFG ARLNWILHFG LPPRYQPDVK 300
FIQVDICAEE LGNNVKPAVT LLGNIHAVTK QLLEELDKTP WQYPPESKWW KTLREKMKSN 360
EAASKELASK KSLPMNYYTV FYHVQEQLPR DCFVVSEGAN TMDIGRTVLQ NYLPRHRLDA 420
GTFGTMGVGL GFAIAAAVVA KDRSPGQWII CVEGDSAFGF SGMEVETICR YNLPIILLVV 480
NNNGIYQGFD TDTWKEMLKF QDATAVVPPM CLLPNSHYEQ VMTAFGGKGY FVQTPEELQK 540
SLRQSLADTT KPSLINIMIE PQATRKAQDF HWLTRSNM 578 
Gene Ontology
 GO:0005782; C:peroxisomal matrix; TAS:Reactome.
 GO:0016830; F:carbon-carbon lyase activity; IDA:UniProtKB.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0030976; F:thiamine pyrophosphate binding; IDA:UniProtKB.
 GO:0001561; P:fatty acid alpha-oxidation; IDA:HGNC.
 GO:0051259; P:protein oligomerization; IDA:UniProtKB. 
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
 PS00187; TPP_ENZYMES 
PRINTS