CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004102
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 5-aminolevulinate synthase, nonspecific, mitochondrial 
Protein Synonyms/Alias
 ALAS-H; 5-aminolevulinic acid synthase 1; Delta-ALA synthase 1; Delta-aminolevulinate synthase 1 
Gene Name
 ALAS1 
Gene Synonyms/Alias
 ALAS3; ALASH; OK/SW-cl.121 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
42KMMEVGAKPAPRALSubiquitination[1]
74KDKTAKAKVQQTPDGubiquitination[2]
142QEMNAVRKEVAETSAubiquitination[1]
157GPSVVSVKTDGGDPSubiquitination[1, 2, 3]
168GDPSGLLKNFQDIMQubiquitination[1, 2, 3]
176NFQDIMQKQRPERVSubiquitination[1, 2]
210FEKKIDEKKNDHTYRacetylation[4]
242YSDSLITKKQVSVWCubiquitination[2, 3]
243SDSLITKKQVSVWCSubiquitination[1]
271GAVMDTLKQHGAGAGubiquitination[1]
288RNISGTSKFHVDLERubiquitination[1]
353IRNSRVPKYIFRHNDubiquitination[1]
435DRDGVMPKMDIISGTubiquitination[1]
539VRVADAAKNTEVCDEubiquitination[1, 5]
602KQVGLELKPHSSAECubiquitination[1]
626EVMSEREKSYFSGLSubiquitination[1]
634SYFSGLSKLVSAQA*ubiquitination[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]
 [2] 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]
 [3] 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]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
Functional Description
  
Sequence Annotation
 ACT_SITE 445 445 By similarity.
 BINDING 217 217 Substrate (By similarity).
 BINDING 334 334 Substrate (By similarity).
 BINDING 353 353 Substrate (By similarity).
 BINDING 386 386 Pyridoxal phosphate (By similarity).
 BINDING 414 414 Pyridoxal phosphate (By similarity).
 BINDING 442 442 Pyridoxal phosphate (By similarity).
 BINDING 474 474 Pyridoxal phosphate (By similarity).
 BINDING 475 475 Pyridoxal phosphate (By similarity).
 BINDING 562 562 Substrate (By similarity).
 MOD_RES 445 445 N6-(pyridoxal phosphate)lysine  
Keyword
 Acyltransferase; Alternative splicing; Complete proteome; Heme biosynthesis; Mitochondrion; Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 640 AA 
Protein Sequence
MESVVRRCPF LSRVPQAFLQ KAGKSLLFYA QNCPKMMEVG AKPAPRALST AAVHYQQIKE 60
TPPASEKDKT AKAKVQQTPD GSQQSPDGTQ LPSGHPLPAT SQGTASKCPF LAAQMNQRGS 120
SVFCKASLEL QEDVQEMNAV RKEVAETSAG PSVVSVKTDG GDPSGLLKNF QDIMQKQRPE 180
RVSHLLQDNL PKSVSTFQYD RFFEKKIDEK KNDHTYRVFK TVNRRAHIFP MADDYSDSLI 240
TKKQVSVWCS NDYLGMSRHP RVCGAVMDTL KQHGAGAGGT RNISGTSKFH VDLERELADL 300
HGKDAALLFS SCFVANDSTL FTLAKMMPGC EIYSDSGNHA SMIQGIRNSR VPKYIFRHND 360
VSHLRELLQR SDPSVPKIVA FETVHSMDGA VCPLEELCDV AHEFGAITFV DEVHAVGLYG 420
ARGGGIGDRD GVMPKMDIIS GTLGKAFGCV GGYIASTSSL IDTVRSYAAG FIFTTSLPPM 480
LLAGALESVR ILKSAEGRVL RRQHQRNVKL MRQMLMDAGL PVVHCPSHII PVRVADAAKN 540
TEVCDELMSR HNIYVQAINY PTVPRGEELL RIAPTPHHTP QMMNYFLENL LVTWKQVGLE 600
LKPHSSAECN FCRRPLHFEV MSEREKSYFS GLSKLVSAQA 640 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003870; F:5-aminolevulinate synthase activity; IEA:EC.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0044255; P:cellular lipid metabolic process; TAS:Reactome.
 GO:0006783; P:heme biosynthetic process; TAS:Reactome.
 GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 
Interpro
 IPR010961; 4pyrrol_synth_NH2levulA_synth.
 IPR015118; 5aminolev_synth_preseq.
 IPR001917; Aminotrans_II_pyridoxalP_BS.
 IPR004839; Aminotransferase_I/II.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2. 
Pfam
 PF00155; Aminotran_1_2
 PF09029; Preseq_ALAS 
SMART
  
PROSITE
 PS00599; AA_TRANSFER_CLASS_2 
PRINTS