CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018974
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 GPI transamidase component PIG-T 
Protein Synonyms/Alias
 Phosphatidylinositol-glycan biosynthesis class T protein 
Gene Name
 PIGT 
Gene Synonyms/Alias
 CGI-06; PSEC0163; UNQ716/PRO1379 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
190TENLTPWKKLLPCSSubiquitination[1]
191ENLTPWKKLLPCSSKubiquitination[1]
198KLLPCSSKAGLSVLLubiquitination[1]
206AGLSVLLKADRLFHTubiquitination[1, 2]
339LNIQLKWKRPPENEAubiquitination[1]
365VSGYGLQKGELSTLLubiquitination[1, 3, 4, 5]
405HTLTITSKGKENKPSubiquitination[6]
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] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] 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
Functional Description
 Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates. 
Sequence Annotation
 CARBOHYD 164 164 N-linked (GlcNAc...).
 CARBOHYD 291 291 N-linked (GlcNAc...) (Potential).
 CARBOHYD 327 327 N-linked (GlcNAc...) (Potential).
 DISULFID 182 182 Interchain (with C-92 in PIGK/GPI8).  
Keyword
 Alternative splicing; Complete proteome; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; Glycoprotein; GPI-anchor biosynthesis; Membrane; Polymorphism; Reference proteome; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 578 AA 
Protein Sequence
MAAAMPLALL VLLLLGPGGW CLAEPPRDSL REELVITPLP SGDVAATFQF RTRWDSELQR 60
EGVSHYRLFP KALGQLISKY SLRELHLSFT QGFWRTRYWG PPFLQAPSGA ELWVWFQDTV 120
TDVDKSWKEL SNVLSGIFCA SLNFIDSTNT VTPTASFKPL GLANDTDHYF LRYAVLPREV 180
VCTENLTPWK KLLPCSSKAG LSVLLKADRL FHTSYHSQAV HIRPVCRNAR CTSISWELRQ 240
TLSVVFDAFI TGQGKKDWSL FRMFSRTLTE PCPLASESRV YVDITTYNQD NETLEVHPPP 300
TTTYQDVILG TRKTYAIYDL LDTAMINNSR NLNIQLKWKR PPENEAPPVP FLHAQRYVSG 360
YGLQKGELST LLYNTHPYRA FPVLLLDTVP WYLRLYVHTL TITSKGKENK PSYIHYQPAQ 420
DRLQPHLLEM LIQLPANSVT KVSIQFERAL LKWTEYTPDP NHGFYVSPSV LSALVPSMVA 480
AKPVDWEESP LFNSLFPVSD GSNYFVRLYT EPLLVNLPTP DFSMPYNVIC LTCTVVAVCY 540
GSFYNLLTRT FHIEEPRTGG LAKRLANLIR RARGVPPL 578 
Gene Ontology
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:Compara.
 GO:0042765; C:GPI-anchor transamidase complex; TAS:UniProtKB.
 GO:0003923; F:GPI-anchor transamidase activity; IEA:Compara.
 GO:0016255; P:attachment of GPI anchor to protein; TAS:UniProtKB.
 GO:0006501; P:C-terminal protein lipidation; TAS:Reactome.
 GO:0051402; P:neuron apoptotic process; IEA:Compara.
 GO:0030182; P:neuron differentiation; IEA:Compara. 
Interpro
 IPR007245; PIG-T. 
Pfam
 PF04113; Gpi16 
SMART
  
PROSITE
  
PRINTS