CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000699
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Thioredoxin-like protein 1 
Protein Synonyms/Alias
 32 kDa thioredoxin-related protein 
Gene Name
 TXNL1 
Gene Synonyms/Alias
 TRP32; TXL; TXNL 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MVGVKPVGSDPDubiquitination[1, 2, 3]
28GSRLAVVKFTMRGCGubiquitination[1, 2, 3, 4, 5, 6]
102DAVGLEEKIKQHLENubiquitination[1, 2, 3]
104VGLEEKIKQHLENDPubiquitination[1, 2, 3]
121NEDTDIPKGYMDLMPubiquitination[1]
181PVKLYSMKFQGPDNGubiquitination[1, 2, 3, 4, 5, 6]
192PDNGQGPKYVKIFINubiquitination[2]
226ELTEDDIKEDGIVPLubiquitination[1, 3]
279ATNMNDFKRVVGKKGubiquitination[1, 2, 3, 4, 6]
Reference
 [1] 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]
 [2] 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]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] 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]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [6] 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] 
Functional Description
 Active thioredoxin with a redox potential of about -250 mV. 
Sequence Annotation
 DOMAIN 2 109 Thioredoxin.
 DOMAIN 115 285 PITH.
 MOD_RES 113 113 Phosphoserine.
 DISULFID 34 37 Redox-active.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Electron transport; Nucleus; Phosphoprotein; Proteasome; Redox-active center; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 289 AA 
Protein Sequence
MVGVKPVGSD PDFQPELSGA GSRLAVVKFT MRGCGPCLRI APAFSSMSNK YPQAVFLEVD 60
VHQCQGTAAT NNISATPTFL FFRNKVRIDQ YQGADAVGLE EKIKQHLEND PGSNEDTDIP 120
KGYMDLMPFI NKAGCECLNE SDEHGFDNCL RKDTTFLESD CDEQLLITVA FNQPVKLYSM 180
KFQGPDNGQG PKYVKIFINL PRSMDFEEAE RSEPTQALEL TEDDIKEDGI VPLRYVKFQN 240
VNSVTIFVQS NQGEEETTRI SYFTFIGTPV QATNMNDFKR VVGKKGESH 289 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
 GO:0015036; F:disulfide oxidoreductase activity; IDA:UniProtKB.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
 GO:0006662; P:glycerol ether metabolic process; IEA:InterPro. 
Interpro
 IPR008979; Galactose-bd-like.
 IPR010400; PITH_dom.
 IPR005746; Thioredoxin.
 IPR012336; Thioredoxin-like_fold.
 IPR017937; Thioredoxin_CS.
 IPR013766; Thioredoxin_domain. 
Pfam
 PF06201; PITH
 PF00085; Thioredoxin 
SMART
  
PROSITE
 PS51532; PITH
 PS00194; THIOREDOXIN_1
 PS51352; THIOREDOXIN_2 
PRINTS