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Protein

Thioredoxin-like protein 1

Gene

TXNL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Active thioredoxin with a redox potential of about -250 mV.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin-like protein 1
Alternative name(s):
32 kDa thioredoxin-related protein
Gene namesi
Name:TXNL1
Synonyms:TRP32, TXL, TXNL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:12436. TXNL1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • mitochondrion Source: GO_Central
  • nucleus Source: UniProtKB-SubCell
  • proteasome complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134967488.

Polymorphism and mutation databases

BioMutaiTXNL1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 289288Thioredoxin-like protein 1PRO_0000120016Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 37Redox-active1 Publication
Modified residuei113 – 1131PhosphoserineBy similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

EPDiO43396.
PaxDbiO43396.
PRIDEiO43396.
TopDownProteomicsiO43396.

2D gel databases

OGPiO43396.
REPRODUCTION-2DPAGEIPI00305692.

PTM databases

iPTMnetiO43396.
PhosphoSiteiO43396.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiO43396.
CleanExiHS_TXNL1.
ExpressionAtlasiO43396. baseline and differential.
GenevisibleiO43396. HS.

Organism-specific databases

HPAiCAB016446.
HPA002828.
HPA002829.

Interactioni

Subunit structurei

Component of the 19S regulatory cap of the 26S proteasome. Interacts with PSMD14/RPN11. Interacts with, and reduces EEF1A1.1 Publication

Protein-protein interaction databases

BioGridi114755. 59 interactions.
IntActiO43396. 9 interactions.
MINTiMINT-5005836.
STRINGi9606.ENSP00000217515.

Structurei

Secondary structure

1
289
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Helixi10 – 123Combined sources
Helixi13 – 197Combined sources
Turni20 – 223Combined sources
Beta strandi25 – 306Combined sources
Helixi35 – 5016Combined sources
Beta strandi54 – 607Combined sources
Turni61 – 633Combined sources
Helixi65 – 706Combined sources
Beta strandi75 – 839Combined sources
Beta strandi86 – 949Combined sources
Helixi96 – 10712Combined sources
Helixi127 – 1293Combined sources
Turni132 – 1343Combined sources
Beta strandi136 – 1394Combined sources
Beta strandi142 – 1443Combined sources
Beta strandi150 – 1545Combined sources
Beta strandi166 – 18217Combined sources
Beta strandi186 – 1883Combined sources
Beta strandi193 – 1997Combined sources
Helixi208 – 2114Combined sources
Turni222 – 2243Combined sources
Turni235 – 2373Combined sources
Beta strandi241 – 2488Combined sources
Beta strandi263 – 2719Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GH2X-ray2.22A2-108[»]
1WWYNMR-A122-279[»]
ProteinModelPortaliO43396.
SMRiO43396. Positions 2-108, 123-279.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43396.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 109108ThioredoxinAdd
BLAST
Domaini115 – 285171PITHPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PITH domain.PROSITE-ProRule annotation
Contains 1 thioredoxin domain.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0908. Eukaryota.
ENOG410YQ2G. LUCA.
HOGENOMiHOG000189802.
HOVERGENiHBG055982.
InParanoidiO43396.
OMAiMSVRVIN.
OrthoDBiEOG7H4DX9.
PhylomeDBiO43396.
TreeFamiTF314399.

Family and domain databases

Gene3Di2.60.120.470. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR010400. PITH_dom.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF06201. PITH. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS51532. PITH. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O43396-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVGVKPVGSD PDFQPELSGA GSRLAVVKFT MRGCGPCLRI APAFSSMSNK
60 70 80 90 100
YPQAVFLEVD VHQCQGTAAT NNISATPTFL FFRNKVRIDQ YQGADAVGLE
110 120 130 140 150
EKIKQHLEND PGSNEDTDIP KGYMDLMPFI NKAGCECLNE SDEHGFDNCL
160 170 180 190 200
RKDTTFLESD CDEQLLITVA FNQPVKLYSM KFQGPDNGQG PKYVKIFINL
210 220 230 240 250
PRSMDFEEAE RSEPTQALEL TEDDIKEDGI VPLRYVKFQN VNSVTIFVQS
260 270 280
NQGEEETTRI SYFTFIGTPV QATNMNDFKR VVGKKGESH
Length:289
Mass (Da):32,251
Last modified:January 23, 2007 - v3
Checksum:iB2CC0BD8042225C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF003938 mRNA. Translation: AAC39599.1.
AF052659 mRNA. Translation: AAC39898.1.
AF143897
, AF143890, AF143891, AF143892, AF143893, AF143894, AF143895, AF143896 Genomic DNA. Translation: AAF66676.1.
AF051896 mRNA. Translation: AAC05830.1.
BC001156 mRNA. Translation: AAH01156.1.
CCDSiCCDS11961.1.
PIRiJC5938.
RefSeqiNP_004777.1. NM_004786.2.
UniGeneiHs.114412.

Genome annotation databases

EnsembliENST00000217515; ENSP00000217515; ENSG00000091164.
ENST00000590954; ENSP00000464918; ENSG00000091164.
GeneIDi9352.
KEGGihsa:9352.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF003938 mRNA. Translation: AAC39599.1.
AF052659 mRNA. Translation: AAC39898.1.
AF143897
, AF143890, AF143891, AF143892, AF143893, AF143894, AF143895, AF143896 Genomic DNA. Translation: AAF66676.1.
AF051896 mRNA. Translation: AAC05830.1.
BC001156 mRNA. Translation: AAH01156.1.
CCDSiCCDS11961.1.
PIRiJC5938.
RefSeqiNP_004777.1. NM_004786.2.
UniGeneiHs.114412.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GH2X-ray2.22A2-108[»]
1WWYNMR-A122-279[»]
ProteinModelPortaliO43396.
SMRiO43396. Positions 2-108, 123-279.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114755. 59 interactions.
IntActiO43396. 9 interactions.
MINTiMINT-5005836.
STRINGi9606.ENSP00000217515.

PTM databases

iPTMnetiO43396.
PhosphoSiteiO43396.

Polymorphism and mutation databases

BioMutaiTXNL1.

2D gel databases

OGPiO43396.
REPRODUCTION-2DPAGEIPI00305692.

Proteomic databases

EPDiO43396.
PaxDbiO43396.
PRIDEiO43396.
TopDownProteomicsiO43396.

Protocols and materials databases

DNASUi9352.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000217515; ENSP00000217515; ENSG00000091164.
ENST00000590954; ENSP00000464918; ENSG00000091164.
GeneIDi9352.
KEGGihsa:9352.

Organism-specific databases

CTDi9352.
GeneCardsiTXNL1.
HGNCiHGNC:12436. TXNL1.
HPAiCAB016446.
HPA002828.
HPA002829.
MIMi603049. gene.
neXtProtiNX_O43396.
PharmGKBiPA134967488.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0908. Eukaryota.
ENOG410YQ2G. LUCA.
HOGENOMiHOG000189802.
HOVERGENiHBG055982.
InParanoidiO43396.
OMAiMSVRVIN.
OrthoDBiEOG7H4DX9.
PhylomeDBiO43396.
TreeFamiTF314399.

Miscellaneous databases

ChiTaRSiTXNL1. human.
EvolutionaryTraceiO43396.
GeneWikiiTXNL1.
GenomeRNAii9352.
PROiO43396.
SOURCEiSearch...

Gene expression databases

BgeeiO43396.
CleanExiHS_TXNL1.
ExpressionAtlasiO43396. baseline and differential.
GenevisibleiO43396. HS.

Family and domain databases

Gene3Di2.60.120.470. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR010400. PITH_dom.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF06201. PITH. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS51532. PITH. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression of a cDNA encoding a human thioredoxin-like protein."
    Miranda-Vizuete A., Gustafsson J.-A., Spyrou G.
    Biochem. Biophys. Res. Commun. 243:284-288(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Purification, molecular cloning, and characterization of TRP32, a novel thioredoxin-related mammalian protein of 32 kDa."
    Lee K.-K., Murakawa M., Takahashi S., Tsubuki S., Kawashima S., Sakamaki K., Yonehara S.
    J. Biol. Chem. 273:19160-19166(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Genomic structure and chromosomal localization of human thioredoxin-like protein gene (txl)."
    Miranda-Vizuete A., Spyrou G.
    DNA Seq. 10:419-424(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The discovery of a new gene that has high homology to the human thioredoxin gene."
    Zhou Y., Pan M.H., Yuan J.G., Qiang B.Q.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-23.
    Tissue: Platelet.
  7. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 238-259, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  8. "Thioredoxin Txnl1/TRP32 is a redox-active cofactor of the 26 S proteasome."
    Andersen K.M., Madsen L., Prag S., Johnsen A.H., Semple C.A., Hendil K.B., Hartmann-Petersen R.
    J. Biol. Chem. 284:15246-15254(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PSMD14/RPN11 AND EEF1A1, SUBCELLULAR LOCATION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Crystal structure of the catalytic domain of a human thioredoxin-like protein."
    Jin J., Chen X., Zhou Y., Bartlam M., Guo Q., Liu Y., Sun Y., Gao Y., Ye S., Li G., Rao Z., Qiang B., Yuan J.
    Eur. J. Biochem. 269:2060-2068(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 1-108, DISULFIDE BOND.
  13. "Solution structure of the C-terminal DUF1000 domain of the human thioredoxin-like 1 protein."
    Goroncy A.K., Koshiba S., Tochio N., Tomizawa T., Inoue M., Tanaka A., Sugano S., Kigawa T., Yokoyama S.
    Proteins 78:2176-2180(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 122-279.

Entry informationi

Entry nameiTXNL1_HUMAN
AccessioniPrimary (citable) accession number: O43396
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.