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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

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

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
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

  1. Endoplasmic reticulum lumen 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
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.
GenevestigatoriO95881.

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. 13 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.

Polymorphism and mutation databases

BioMutaiTXNDC12.

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. 13 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.
GenevestigatoriO95881.

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: April 29, 2015
This is version 134 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.