Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O95881

- TXD12_HUMAN

UniProt

O95881 - TXD12_HUMAN

Protein

Thioredoxin domain-containing protein 12

Gene

TXNDC12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. protein-disulfide reductase (glutathione) activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro

    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: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:24626. TXNDC12.

    Subcellular locationi

    Endoplasmic reticulum lumen 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    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.

    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-active2 PublicationsPROSITE-ProRule annotation

    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.
    GenevestigatoriO95881.

    Organism-specific databases

    HPAiHPA015086.

    Interactioni

    Protein-protein interaction databases

    BioGridi119252. 8 interactions.
    IntActiO95881. 2 interactions.
    MINTiMINT-5005906.
    STRINGi9606.ENSP00000360688.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    METRPRLGAT CLLGFSFLLL VISSDGHNGL GKGFGDHIHW RTLEDGKKEA    50
    AASGLPLMVI IHKSWCGACK ALKPKFAEST EISELSHNFV MVNLEDEEEP 100
    KDEDFSPDGG YIPRILFLDP SGKVHPEIIN ENGNPSYKYF YVSAEQVVQG 150
    MKEAQERLTG DAFRKKHLED EL 172
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS561.1.
    RefSeqi NP_056997.1. NM_015913.3.
    UniGenei Hs.476033.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SEN X-ray 1.20 A 23-172 [» ]
    2K8V NMR - A 24-172 [» ]
    ProteinModelPortali O95881.
    SMRi O95881. Positions 24-172.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119252. 8 interactions.
    IntActi O95881. 2 interactions.
    MINTi MINT-5005906.
    STRINGi 9606.ENSP00000360688.

    Chemistry

    DrugBanki DB00143. Glutathione.

    PTM databases

    PhosphoSitei O95881.

    Proteomic databases

    MaxQBi O95881.
    PaxDbi O95881.
    PeptideAtlasi O95881.
    PRIDEi O95881.

    Protocols and materials databases

    DNASUi 51060.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371626 ; ENSP00000360688 ; ENSG00000117862 .
    GeneIDi 51060.
    KEGGi hsa:51060.
    UCSCi uc001cti.4. human.

    Organism-specific databases

    CTDi 51060.
    GeneCardsi GC01M052485.
    H-InvDB HIX0116253.
    HGNCi HGNC:24626. TXNDC12.
    HPAi HPA015086.
    MIMi 609448. gene.
    neXtProti NX_O95881.
    PharmGKBi PA142670665.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG77442.
    HOGENOMi HOG000231100.
    HOVERGENi HBG107174.
    InParanoidi O95881.
    KOi K05360.
    OMAi SYKYFYT.
    OrthoDBi EOG7DNNX2.
    PhylomeDBi O95881.
    TreeFami TF321449.

    Miscellaneous databases

    ChiTaRSi TXNDC12. human.
    EvolutionaryTracei O95881.
    GeneWikii TXNDC12.
    GenomeRNAii 51060.
    NextBioi 53641.
    PROi O95881.
    SOURCEi Search...

    Gene expression databases

    Bgeei O95881.
    CleanExi HS_TXNDC12.
    Genevestigatori O95881.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 1 hit.
    PROSITEi PS00194. THIOREDOXIN_1. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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: October 1, 2014
    This is version 128 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