CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008323
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Biotin--protein ligase 
Protein Synonyms/Alias
 Biotin apo-protein ligase; Biotin--[methylmalonyl-CoA-carboxytransferase] ligase; Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase; Holocarboxylase synthetase; HCS; Biotin--[methylcrotonoyl-CoA-carboxylase] ligase; Biotin--[acetyl-CoA-carboxylase] ligase 
Gene Name
 HLCS 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
274VQNLVFSKADQSEVKubiquitination[1]
567QDINLRVKWPNDIYYubiquitination[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
 Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl- CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase. 
Sequence Annotation
 MOD_RES 147 147 Phosphoserine.  
Keyword
 ATP-binding; Complete proteome; Cytoplasm; Disease mutation; Ligase; Mitochondrion; Multifunctional enzyme; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 726 AA 
Protein Sequence
MEDRLHMDNG LVPQKIVSVH LQDSTLKEVK DQVSNKQAQI LEPKPEPSLE IKPEQDGMEH 60
VGRDDPKALG EEPKQRRGSA SGSEPAGDSD RGGGPVEHYH LHLSSCHECL ELENSTIESV 120
KFASAENIPD LPYDYSSSLE SVADETSPER EGRRVNLTGK APNILLYVGS DSQEALGRFH 180
EVRSVLADCV DIDSYILYHL LEDSALRDPW TDNCLLLVIA TRESIPEDLY QKFMAYLSQG 240
GKVLGLSSSF TFGGFQVTSK GALHKTVQNL VFSKADQSEV KLSVLSSGCR YQEGPVRLSP 300
GRLQGHLENE DKDRMIVHVP FGTRGGEAVL CQVHLELPPS SNIVQTPEDF NLLKSSNFRR 360
YEVLREILTT LGLSCDMKQV PALTPLYLLS AAEEIRDPLM QWLGKHVDSE GEIKSGQLSL 420
RFVSSYVSEV EITPSCIPVV TNMEAFSSEH FNLEIYRQNL QTKQLGKVIL FAEVTPTTMR 480
LLDGLMFQTP QEMGLIVIAA RQTEGKGRGG NVWLSPVGCA LSTLLISIPL RSQLGQRIPF 540
VQHLMSVAVV EAVRSIPEYQ DINLRVKWPN DIYYSDLMKI GGVLVNSTLM GETFYILIGC 600
GFNVTNSNPT ICINDLITEY NKQHKAELKP LRADYLIARV VTVLEKLIKE FQDKGPNSVL 660
PLYYRYWVHS GQQVHLGSAE GPKVSIVGLD DSGFLQVHQE GGEVVTVHPD GNSFDMLRNL 720
ILPKRR 726 
Gene Ontology
 GO:0000785; C:chromatin; IDA:UniProtKB.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0005652; C:nuclear lamina; IDA:UniProtKB.
 GO:0016363; C:nuclear matrix; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0009374; F:biotin binding; IDA:UniProtKB.
 GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:EC.
 GO:0004078; F:biotin-[methylcrotonoyl-CoA-carboxylase] ligase activity; IEA:EC.
 GO:0004079; F:biotin-[methylmalonyl-CoA-carboxytransferase] ligase activity; IEA:EC.
 GO:0004080; F:biotin-[propionyl-CoA-carboxylase (ATP-hydrolyzing)] ligase activity; IDA:UniProtKB.
 GO:0008283; P:cell proliferation; IMP:UniProtKB.
 GO:0071110; P:histone biotinylation; IDA:UniProtKB.
 GO:0070781; P:response to biotin; IDA:UniProtKB. 
Interpro
 IPR004408; Biotin_CoA_COase_ligase.
 IPR003142; BPL_C.
 IPR004143; BPL_LipA_LipB. 
Pfam
 PF02237; BPL_C
 PF03099; BPL_LplA_LipB 
SMART
  
PROSITE
  
PRINTS