CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018111
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
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
212FEKKIDEKKNDHTYRacetylation[1]
437DRDGVMPKMDIISGTubiquitination[2]
541VRVADAAKNTEICDEubiquitination[2]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] 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
  
Sequence Annotation
 ACT_SITE 447 447 By similarity.
 BINDING 219 219 Substrate (By similarity).
 BINDING 336 336 Substrate (By similarity).
 BINDING 355 355 Substrate (By similarity).
 BINDING 388 388 Pyridoxal phosphate (By similarity).
 BINDING 416 416 Pyridoxal phosphate (By similarity).
 BINDING 444 444 Pyridoxal phosphate (By similarity).
 BINDING 476 476 Pyridoxal phosphate (By similarity).
 BINDING 477 477 Pyridoxal phosphate (By similarity).
 BINDING 564 564 Substrate (By similarity).
 MOD_RES 447 447 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Acyltransferase; Complete proteome; Heme biosynthesis; Mitochondrion; Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 642 AA 
Protein Sequence
METVVRRCPF LSRVPQAFLQ KAGKSLLFYA QNCPKMMEVG AKPAPRTLST SAVHCQQVKE 60
TPPANEKEKT AKAAVQQAPD ESQMAQTPDG TQLPSGHPSP ATSQGSGSKC PFLAAQLSQT 120
GSSVFRKASL ELQEDVQEMH AVRKEAAQSP VPPSLVNVKT DGEDPSRLLK NFQDIMRKQR 180
PERVSHLLQD NLPKSVSTFQ YDHFFEKKID EKKNDHTYRV FKTVNRRAQI FPMADDYTDS 240
LITKKQVSVW CSNDYLGMSR HPRVCGAVME TVKQHGAGAG GTRNISGTSK FHVELEQALA 300
DLHGKDAALL FSSCFVANDS TLFTLAKMMP GCEIYSDSGN HASMIQGIRN SRVPKYIFRH 360
NDVNHLRELL QRSDPSVPKI VAFETVHSMD GAVCPLEELC DVAHEFGAIT FVDEVHAVGL 420
YGARGGGIGD RDGVMPKMDI ISGTLGKAFG CVGGYIASTS LLIDTVRSYA AGFIFTTSLP 480
PMLLAGALES VRILKSSEGR ALRRQHQRNV KLLRQMLMDA GLPVIHCPSH IIPVRVADAA 540
KNTEICDELM TRHNIYVQAI NYPTVPRGEE LLRIAPTPHH TPQMMNFFVE KLLVTWKRVG 600
LELKPHSSAE CNFCRRPLHF EVMSEREKAY FSGMSKMVSA QA 642 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0003870; F:5-aminolevulinate synthase activity; IEA:EC.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. 
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