CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007393
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein MGA2 
Protein Synonyms/Alias
  
Gene Name
 MGA2 
Gene Synonyms/Alias
 YIR033W 
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
114EEDEHENKVFNEKNIubiquitination[1]
327WQNRLLGKFTTTPIMubiquitination[2]
493NLENDIGKPLFKHSFubiquitination[2]
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]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
  
Sequence Annotation
 DOMAIN 530 610 IPT/TIG.
 REPEAT 719 748 ANK 1.
 REPEAT 752 781 ANK 2.
 MOD_RES 255 255 Phosphoserine.  
Keyword
 ANK repeat; Complete proteome; Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1113 AA 
Protein Sequence
MQQNSEFLTE TPGSDPHISQ LHANSVMESQ LLDDFLLNGS PMYQDDSMAH INIDEGANFQ 60
NFIKTDEGDS PNLLSFEGIG NNTHVNQNVS TPLEEEMESN RALKEEEEDE HENKVFNEKN 120
IGNPAHDEIV FGRKETIQSV YINPLDYLKV NAAQLPLDVE VSGLPQVSRV ENQLKLKVKI 180
TSETPLNQSM LYLPSDSISR EKFYLKKNIE DFSEDFKKNL LYINAFVLCA VSNRTTNVCT 240
KCVKREQRRA ARRKSGIADN LLWCNNINRR LVVFNNKQVF PIMKTFDNVK EFELTTRLVC 300
YCRHHKANNG FVILFTITDW QNRLLGKFTT TPIMITDRKP ANMDTTKFNN TTTSSRRQLT 360
EEESTTEYYS TDNNQLSKDE NMPFQYTYQH NPYDNDSQMN NIPLKDKNVP FPYSISQQTD 420
LLQNNNLSLN LSLPNQHIPS PTSMSEEGSE SFNYHHRDND NPVRTISLTN IEQQSQLNQR 480
KRARNNLEND IGKPLFKHSF SNSISATNTM NPALHSMQDF SMKNNNNNLP SINRVIPSQG 540
PINGGIEVTL LGCNFKDGLS VKFGSNLALS TQCWSETTIV TYLPPAAYAG QVFVSITDTN 600
NENNNDDLPQ EIEINDNKKA IFTYVDDTDR QLIELALQIV GLKMNGKLED ARNIAKRIVG 660
NDSPDSGTNG NSCSKSTGPS PNQHSMNLNT SVLYSDEVLI QKVIKSLNIN SNISICDSLG 720
RTLLHLACLK NYSSLVYTLI KKGARVNDID SFGLTPLHFA CISGDPKIIK MLLNCKVNYS 780
LRSHNGLTAR EVFIANHIHS KEIDKKQDNR DNHKFVHNDT YISEVLSLFE EFQNGTKFTD 840
SVETDSNYSI SRKYSQSSFN SSLLDNESLN ENLFESQSMI NPTSMEIQHP TLQLFENSSY 900
SEYDQSDFEE DGDEDLFVTD EVEKPGVACR EEQSELLDIG SSANEPEEDN GSTSLWNRVL 960
HRINDDLPKY EDLFPLSWGK DDKLKTTNQD SIVEQSASNI ENSENSEEED YEEEEEFLKK 1020
QFNRFFQNKQ NFRNDKMLIF FWIPLTLLLL TWFIMYKFGN QDSSINHISE LISEYLRIAL 1080
AKFLLGNERM KTAFRSKLSN LQTTRMLNDL IVS 1113 
Gene Ontology
 GO:0030176; C:integral to endoplasmic reticulum membrane; ISM:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0070417; P:cellular response to cold; IMP:SGD.
 GO:0030466; P:chromatin silencing at silent mating-type cassette; IGI:SGD.
 GO:0048255; P:mRNA stabilization; IMP:SGD.
 GO:0061399; P:positive regulation of transcription from RNA polymerase II promoter in response to cobalt ion; IMP:SGD.
 GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; IMP:SGD.
 GO:0036083; P:positive regulation of unsaturated fatty acid biosynthetic process by positive regulation of transcription from RNA polymerase II promoter; IGI:SGD. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom.
 IPR013783; Ig-like_fold.
 IPR014756; Ig_E-set.
 IPR002909; IPT_TIG_rcpt. 
Pfam
 PF00023; Ank
 PF01833; TIG 
SMART
 SM00248; ANK
 SM00429; IPT 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT 
PRINTS