Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Thioredoxin domain-containing protein 12

Gene

TXNDC12

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

Functioni

Possesses significant protein thiol-disulfide oxidase activity.1 Publication

Catalytic activityi

2 glutathione + protein-disulfide = glutathione disulfide + protein-dithiol.

Kineticsi

  1. KM=25 µM for Asn-Arg-Cys-Ser-Gln-Gly-Ser-Cys-Trp-Asn

    pH dependencei

    Optimum pH is 6.5.

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thioredoxin domain-containing protein 12 (EC:1.8.4.2)
    Alternative name(s):
    Endoplasmic reticulum resident protein 18
    Short name:
    ER protein 18
    Short name:
    ERp18
    Endoplasmic reticulum resident protein 19
    Short name:
    ER protein 19
    Short name:
    ERp19
    Thioredoxin-like protein p19
    hTLP19
    Gene namesi
    Name:TXNDC12
    Synonyms:TLP19
    ORF Names:UNQ713/PRO1376
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:24626. TXNDC12.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi66 – 661C → S: Loss of oxidase activity. 1 Publication
    Mutagenesisi69 – 691C → S: Loss of oxidase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA142670665.

    Chemistry

    DrugBankiDB00143. Glutathione.

    Polymorphism and mutation databases

    BioMutaiTXNDC12.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 26261 PublicationAdd
    BLAST
    Chaini27 – 172146Thioredoxin domain-containing protein 12PRO_0000034189Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi66 ↔ 69Redox-activePROSITE-ProRule annotation2 Publications

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiO95881.
    PaxDbiO95881.
    PeptideAtlasiO95881.
    PRIDEiO95881.

    PTM databases

    PhosphoSiteiO95881.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    BgeeiO95881.
    CleanExiHS_TXNDC12.
    ExpressionAtlasiO95881. baseline and differential.
    GenevisibleiO95881. HS.

    Organism-specific databases

    HPAiHPA015086.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KLHL2O951983EBI-2564581,EBI-746999
    SGTAO437653EBI-2564581,EBI-347996
    SGTBQ96EQ03EBI-2564581,EBI-744081
    UBQLN1Q9UMX03EBI-2564581,EBI-741480
    UBQLN1Q9UMX0-23EBI-2564581,EBI-10173939

    Protein-protein interaction databases

    BioGridi119252. 9 interactions.
    IntActiO95881. 6 interactions.
    MINTiMINT-5005906.
    STRINGi9606.ENSP00000360688.

    Structurei

    Secondary structure

    1
    172
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi33 – 386Combined sources
    Helixi43 – 5311Combined sources
    Beta strandi57 – 626Combined sources
    Helixi67 – 7711Combined sources
    Helixi80 – 867Combined sources
    Beta strandi89 – 957Combined sources
    Helixi96 – 983Combined sources
    Helixi103 – 1053Combined sources
    Beta strandi112 – 1187Combined sources
    Turni120 – 1223Combined sources
    Turni135 – 1395Combined sources
    Helixi144 – 15815Combined sources
    Helixi159 – 1613Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SENX-ray1.20A23-172[»]
    2K8VNMR-A24-172[»]
    ProteinModelPortaliO95881.
    SMRiO95881. Positions 24-172.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95881.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi169 – 1724Prevents secretion from ERSequence Analysis

    Sequence similaritiesi

    Contains 1 thioredoxin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center, Signal

    Phylogenomic databases

    eggNOGiNOG77442.
    GeneTreeiENSGT00530000063273.
    HOGENOMiHOG000231100.
    HOVERGENiHBG107174.
    InParanoidiO95881.
    KOiK05360.
    OMAiSYKYFYT.
    OrthoDBiEOG7DNNX2.
    PhylomeDBiO95881.
    TreeFamiTF321449.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 1 hit.
    PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O95881-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    METRPRLGAT CLLGFSFLLL VISSDGHNGL GKGFGDHIHW RTLEDGKKEA
    60 70 80 90 100
    AASGLPLMVI IHKSWCGACK ALKPKFAEST EISELSHNFV MVNLEDEEEP
    110 120 130 140 150
    KDEDFSPDGG YIPRILFLDP SGKVHPEIIN ENGNPSYKYF YVSAEQVVQG
    160 170
    MKEAQERLTG DAFRKKHLED EL
    Length:172
    Mass (Da):19,206
    Last modified:May 1, 1999 - v1
    Checksum:i3092E9515A7C4094
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti102 – 1021D → H in AAH08913 (PubMed:15489334).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF543416 mRNA. Translation: AAN34781.1.
    AF131758 mRNA. Translation: AAD20035.1.
    AY358982 mRNA. Translation: AAQ89341.1.
    AK075409 mRNA. Translation: BAG52132.1.
    AL445685 Genomic DNA. Translation: CAI17031.1.
    BC001493 mRNA. Translation: AAH01493.1.
    BC008953 mRNA. Translation: AAH08953.1.
    BC008913 mRNA. Translation: AAH08913.1.
    CCDSiCCDS561.1.
    RefSeqiNP_056997.1. NM_015913.3.
    UniGeneiHs.476033.

    Genome annotation databases

    EnsembliENST00000371626; ENSP00000360688; ENSG00000117862.
    GeneIDi51060.
    KEGGihsa:51060.
    UCSCiuc001cti.4. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF543416 mRNA. Translation: AAN34781.1.
    AF131758 mRNA. Translation: AAD20035.1.
    AY358982 mRNA. Translation: AAQ89341.1.
    AK075409 mRNA. Translation: BAG52132.1.
    AL445685 Genomic DNA. Translation: CAI17031.1.
    BC001493 mRNA. Translation: AAH01493.1.
    BC008953 mRNA. Translation: AAH08953.1.
    BC008913 mRNA. Translation: AAH08913.1.
    CCDSiCCDS561.1.
    RefSeqiNP_056997.1. NM_015913.3.
    UniGeneiHs.476033.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SENX-ray1.20A23-172[»]
    2K8VNMR-A24-172[»]
    ProteinModelPortaliO95881.
    SMRiO95881. Positions 24-172.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi119252. 9 interactions.
    IntActiO95881. 6 interactions.
    MINTiMINT-5005906.
    STRINGi9606.ENSP00000360688.

    Chemistry

    DrugBankiDB00143. Glutathione.

    PTM databases

    PhosphoSiteiO95881.

    Polymorphism and mutation databases

    BioMutaiTXNDC12.

    Proteomic databases

    MaxQBiO95881.
    PaxDbiO95881.
    PeptideAtlasiO95881.
    PRIDEiO95881.

    Protocols and materials databases

    DNASUi51060.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000371626; ENSP00000360688; ENSG00000117862.
    GeneIDi51060.
    KEGGihsa:51060.
    UCSCiuc001cti.4. human.

    Organism-specific databases

    CTDi51060.
    GeneCardsiGC01M052485.
    H-InvDBHIX0116253.
    HGNCiHGNC:24626. TXNDC12.
    HPAiHPA015086.
    MIMi609448. gene.
    neXtProtiNX_O95881.
    PharmGKBiPA142670665.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG77442.
    GeneTreeiENSGT00530000063273.
    HOGENOMiHOG000231100.
    HOVERGENiHBG107174.
    InParanoidiO95881.
    KOiK05360.
    OMAiSYKYFYT.
    OrthoDBiEOG7DNNX2.
    PhylomeDBiO95881.
    TreeFamiTF321449.

    Miscellaneous databases

    ChiTaRSiTXNDC12. human.
    EvolutionaryTraceiO95881.
    GeneWikiiTXNDC12.
    GenomeRNAii51060.
    NextBioi53641.
    PROiO95881.
    SOURCEiSearch...

    Gene expression databases

    BgeeiO95881.
    CleanExiHS_TXNDC12.
    ExpressionAtlasiO95881. baseline and differential.
    GenevisibleiO95881. HS.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 1 hit.
    PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Isolation and characterization of a novel human thioredoxin-like gene hTLP19 encoding a secretory protein."
      Liu F., Rong Y.P., Zeng L.C., Zhang X., Han Z.G.
      Gene 315:71-78(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. Mei G., Yu W., Gibbs R.A.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
      Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
      , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
      DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Colon, Kidney and Ovary.
    7. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-41.
    8. "Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member."
      Alanen H.I., Williamson R.A., Howard M.J., Lappi A.-K., Jaentti H.P., Rautio S.M., Kellokumpu S., Ruddock L.W.
      J. Biol. Chem. 278:28912-28920(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BOND, MUTAGENESIS OF CYS-66 AND CYS-69.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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.
    11. "Solution structure and dynamics of ERp18, a small endoplasmic reticulum resident oxidoreductase."
      Rowe M.L., Ruddock L.W., Kelly G., Schmidt J.M., Williamson R.A., Howard M.J.
      Biochemistry 48:4596-4606(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 24-172, DISULFIDE BOND.

    Entry informationi

    Entry nameiTXD12_HUMAN
    AccessioniPrimary (citable) accession number: O95881
    Secondary accession number(s): B3KQS0, Q5T1T4, Q96H50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 11, 2003
    Last sequence update: May 1, 1999
    Last modified: July 22, 2015
    This is version 136 of the entry and version 1 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 1
      Human chromosome 1: 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

    External Data

    Dasty 3

    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 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.