CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021341
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Thioredoxin-related transmembrane protein 1 
Protein Synonyms/Alias
 Thioredoxin domain-containing protein 1; Transmembrane Trx-related protein 
Gene Name
 TMX1 
Gene Synonyms/Alias
 TMX; TXNDC; TXNDC1; PSEC0085; UNQ235/PRO268 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
107LPTIYHCKDGEFRRYubiquitination[1, 2]
121YQGPRTKKDFINFISubiquitination[3, 4, 5]
130FINFISDKEWKSIEPubiquitination[1, 2]
223PYPYPSKKLLSESAQubiquitination[1, 2, 4]
233SESAQPLKKVEEEQEubiquitination[1, 2, 6, 7]
234ESAQPLKKVEEEQEAubiquitination[1]
279GPSLATDKS******ubiquitination[2]
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] 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]
 [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]
 [7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. 
Sequence Annotation
 DOMAIN 27 132 Thioredoxin.
 MOD_RES 247 247 Phosphoserine.
 MOD_RES 270 270 Phosphoserine.
 MOD_RES 280 280 Phosphoserine.
 DISULFID 56 59 Redox-active.  
Keyword
 3D-structure; Complete proteome; Disulfide bond; Electron transport; Endoplasmic reticulum; Membrane; Phosphoprotein; Redox-active center; Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 280 AA 
Protein Sequence
MAPSGSLAVP LAVLVLLLWG APWTHGRRSN VRVITDENWR ELLEGDWMIE FYAPWCPACQ 60
NLQPEWESFA EWGEDLEVNI AKVDVTEQPG LSGRFIITAL PTIYHCKDGE FRRYQGPRTK 120
KDFINFISDK EWKSIEPVSS WFGPGSVLMS SMSALFQLSM WIRTCHNYFI EDLGLPVWGS 180
YTVFALATLF SGLLLGLCMI FVADCLCPSK RRRPQPYPYP SKKLLSESAQ PLKKVEEEQE 240
ADEEDVSEEE AESKEGTNKD FPQNAIRQRS LGPSLATDKS 280 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0030612; F:arsenate reductase (thioredoxin) activity; NAS:UniProtKB.
 GO:0015036; F:disulfide oxidoreductase activity; IDA:UniProtKB.
 GO:0008283; P:cell proliferation; NAS:UniProtKB.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0006260; P:DNA replication; NAS:UniProtKB.
 GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
 GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:UniProtKB.
 GO:0045321; P:leukocyte activation; NAS:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
 GO:0045927; P:positive regulation of growth; NAS:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; NAS:UniProtKB.
 GO:0006950; P:response to stress; NAS:UniProtKB.
 GO:0007165; P:signal transduction; NAS:UniProtKB. 
Interpro
 IPR012336; Thioredoxin-like_fold.
 IPR017937; Thioredoxin_CS.
 IPR013766; Thioredoxin_domain. 
Pfam
 PF00085; Thioredoxin 
SMART
  
PROSITE
 PS00194; THIOREDOXIN_1
 PS51352; THIOREDOXIN_2 
PRINTS