CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008578
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphatidylserine decarboxylase proenzyme 2 
Protein Synonyms/Alias
 Phosphatidylserine decarboxylase 2 beta chain; Phosphatidylserine decarboxylase 2 alpha chain 
Gene Name
 PSD2 
Gene Synonyms/Alias
 YGR170W 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
753SKEHKTLKPSYVSSAubiquitination[1]
Reference
 [1] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047
Functional Description
 May be involved in the regulation of phospholipid biosynthesis and interorganelle trafficking of phosphatidylserine. 
Sequence Annotation
 DOMAIN 480 583 C2.
 MOD_RES 1043 1043 Pyruvic acid (Ser) (By similarity).  
Keyword
 Complete proteome; Decarboxylase; Golgi apparatus; Lipid biosynthesis; Lipid metabolism; Lyase; Phospholipid biosynthesis; Phospholipid metabolism; Pyruvate; Reference proteome; Vacuole; Zymogen. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1138 AA 
Protein Sequence
MRIIKGRKRG KNKKPTLILK IHVIQAENIE ALKTFNCNPV CFVTTNTFYS QKTNKLKNSN 60
THWNQTLRIK LPRNPTSEWL RIIVYDALPT GAPPTTPSRP RTTTANTSSS TLSNSGLSSH 120
SHSSRNLNVT SKGNQTSTSI NSVSSSATPA PSHSSSSLST TGPGSTHKNR INSYLYLGEA 180
KISLLDLFKR KDTTTSYKFS IEAQRYHLYD MKGGKDQDSL NCNFLVGDIL LGFKLECNVK 240
RTPTFQAFNA WRNELNTYLG RIDRNKARMR SSSSLPPPLE DMLSNSSAVS GNEIRREKPY 300
SDTDLAHDEE VNAEDEIDAE ESIEDMNSSG SICTERRYDI DNDTIFDSIS EVVSLNDEEL 360
DILNDFEEAD HPNVPDINVH DIDEDTRISL SSMITALDEY DIVEPEDVAK LPAVSENDIT 420
SVDDEESENQ QESDEEFDIY NEDEREDSDF QSKEYIGSRL LHLQRGKHNK SYANYLYRRA 480
KSNFFISKKE HAMGVVFMHI GAIKNLPALR NRLSKTNYEM DPFIVISFGR RVFKTSWRKH 540
TLNPEFNEYA AFEVFPHETN FAFSIKVVDK DSFSFNDDVA KCELAWFDML QQQQHENEWI 600
PYEIPLDLTV EPAHAPKQPV LYSSFKYVSY PFLKKSFWKE AVDTSVNLER LDIIQVMLYL 660
ERLGSFTMAD SFELFQHFNK SAWAGQSITR SQLVEGLQSW RKSTNFKRIW TCPRCMRSCK 720
PTRNARRSKL VLENDLITHF AICTFSKEHK TLKPSYVSSA FASKRWFSKV LIKLTYGKYA 780
LGSNNANILV QDRDTGIIIE EKISAHVKLG MRIIYNGKSP ESKKFRSLLK TLSIRQGKKF 840
DSTASAKQIE PFIKFHSLDL SQCRDKDFKT FNEFFYRKLK PGSRLPESNN KEILFSPADS 900
RCTVFPTIQE SKEIWVKGRK FSIKKLANNY NPETFNDNNC SIGIFRLAPQ DYHRFHSPCN 960
GTIGKPVYVD GEYYTVNPMA VRSELDVFGE NIRVIIPIDS PQFGKLLYIP IGAMMVGSIL 1020
LTCKENDVVE SGQELGYFKF GGSTIIIIIP HNNFMFDSDL VKNSSERIET LVKVGMSIGH 1080
TSNVNELKRI RIKVDDPKKI ERIKRTISVS DENAKSTGNV TWEYHTLREM MNKDFAGL 1138 
Gene Ontology
 GO:0005768; C:endosome; IDA:SGD.
 GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
 GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
 GO:0004609; F:phosphatidylserine decarboxylase activity; IGI:SGD.
 GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:SGD.
 GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR000008; C2_Ca-dep.
 IPR008973; C2_Ca/lipid-bd_dom_CaLB.
 IPR003817; PS_Dcarbxylase.
 IPR005221; PS_decarb. 
Pfam
 PF00168; C2
 PF02666; PS_Dcarbxylase 
SMART
 SM00239; C2 
PROSITE
 PS50004; C2 
PRINTS