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Protein

Thioredoxin domain-containing protein 11

Gene

TXNDC11

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

Functioni

May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H2O2 generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H2O2 generation.

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: GO_Central

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. protein folding Source: GO_Central
  3. response to endoplasmic reticulum stress Source: GO_Central
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin domain-containing protein 11
Alternative name(s):
EF-hand-binding protein 1
Gene namesi
Name:TXNDC11
Synonyms:EFP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:28030. TXNDC11.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei65 – 8521HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: GO_Central
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134915251.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 985985Thioredoxin domain-containing protein 11PRO_0000120173Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi469 ↔ 472Redox-activePROSITE-ProRule annotation
Disulfide bondi719 ↔ 722Redox-activePROSITE-ProRule annotation
Modified residuei828 – 8281Phosphoserine1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ6PKC3.
PaxDbiQ6PKC3.
PRIDEiQ6PKC3.

PTM databases

PhosphoSiteiQ6PKC3.

Expressioni

Tissue specificityi

Widely expressed at low level. Expressed at higher level in thyroid and prostate.1 Publication

Gene expression databases

BgeeiQ6PKC3.
CleanExiHS_TXNDC11.
ExpressionAtlasiQ6PKC3. baseline and differential.
GenevestigatoriQ6PKC3.

Organism-specific databases

HPAiHPA041174.
HPA041390.

Interactioni

Subunit structurei

Interacts with the cytoplasmic part of DUOX1 and DUOX2. Interacts with TPO and CYBA.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9WMX22EBI-749812,EBI-6863748From a different organism.

Protein-protein interaction databases

BioGridi119253. 35 interactions.
IntActiQ6PKC3. 43 interactions.
MINTiMINT-2872884.
STRINGi9606.ENSP00000283033.

Structurei

3D structure databases

ProteinModelPortaliQ6PKC3.
SMRiQ6PKC3. Positions 127-245, 569-827.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini92 – 214123Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini649 – 799151Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili821 – 91999Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 2 thioredoxin domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Redox-active center, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00390000016020.
HOGENOMiHOG000132983.
HOVERGENiHBG082866.
InParanoidiQ6PKC3.
OMAiQNFSVLY.
OrthoDBiEOG7ZSHSG.
PhylomeDBiQ6PKC3.
TreeFamiTF323602.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 2 hits.
PROSITEiPS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6PKC3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSECGGRGGG SSSSEDAEDE GGGGGGPAGS DCLSSSPTLA TASSAGRLRR
60 70 80 90 100
GLRGAFLMAR QRPELLCGAV ALGCALLLAL KFTCSRAKDV IIPAKPPVSF
110 120 130 140 150
FSLRSPVLDL FQGQLDYAEY VRRDSEVVLL FFYAPWCGQS IAARAEIEQA
160 170 180 190 200
ASRLSDQVLF VAINCWWNQG KCRKQKHFFY FPVIYLYHRS FGPIEYKGPM
210 220 230 240 250
SAVYIEKFVR RVMKPLLYIP SQSELLDFLS NYEPGVLGYF EFSGSPQPPG
260 270 280 290 300
YLTFFTSALH SLKKALESTS SPRALVSFTG EWHLETKIYV LDYLGTVRFG
310 320 330 340 350
VITNKHLAKL VSLVHSGSVY LHRHFNTSLV FPREVLNYTA ENICKWALEN
360 370 380 390 400
QETLFRWLRP HGGKSLLLNN ELKKGPALFL FIPFNPLAES HPLIDEITEV
410 420 430 440 450
ALEYNNCHGD QVVERLLQHL RRVDAPVLES LALEVPAQLP DPPTITASPC
460 470 480 490 500
CNTVVLPQWH SFSRTHNVCE LCVNQTSGGM KPSSVSVPQC SFFEMAAALD
510 520 530 540 550
SFYLKEQTFY HVASDSIECS NFLTSYSPFS YYTACCRTIS RGVSGFIDSE
560 570 580 590 600
QGVFEAPTVA FSSLEKKCEV DAPSSVPHIE ENRYLFPEVD MTSTNFTGLS
610 620 630 640 650
CRTNKTLNIY LLDSNLFWLY AERLGAPSST QVKEFAAIVD VKEESHYILD
660 670 680 690 700
PKQALMKLTL ESFIQNFSVL YSPLKRHLIG SGSAQFPSQH LITEVTTDTF
710 720 730 740 750
WEVVLQKQDV LLLYYAPWCG FCPSLNHIFI QLARNLPMDT FTVARIDVSQ
760 770 780 790 800
NDLPWEFMVD RLPTVLFFPC NRKDLSVKYP EDVPITLPNL LRFILHHSDP
810 820 830 840 850
ASSPQNVANS PTKECLQSEA VLQRGHISHL EREIQKLRAE ISSLQRAQVQ
860 870 880 890 900
VESQLSSARR DEHRLRQQQR ALEEQHSLLH AHSEQLQALY EQKTRELQEL
910 920 930 940 950
ARKLQELADA SENLLTENTW LKILVATMER KLEGRDGAES LAAQREVHPK
960 970 980
QPEPSATPQL PGSSPPPANV SATLVSERNK ENRTD
Length:985
Mass (Da):110,529
Last modified:July 5, 2005 - v2
Checksum:i4A8C852F8E81B8BC
GO
Isoform 2 (identifier: Q6PKC3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     265-291: Missing.

Note: No experimental confirmation available.

Show »
Length:958
Mass (Da):107,512
Checksum:i7E051E7BFA61B4F8
GO
Isoform 3 (identifier: Q6PKC3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     265-278: ALESTSSPRALVSF → DGVSPCRPGWSAVA
     279-985: Missing.

Note: No experimental confirmation available.

Show »
Length:278
Mass (Da):30,375
Checksum:iC89C635153ADE9F9
GO

Sequence cautioni

The sequence AAD20043.1 differs from that shown. Reason: Frameshift at position 618. Curated
The sequence AAH13727.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB55129.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC11044.1 differs from that shown.Intron retention.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti783 – 7831V → L.1 Publication
Corresponds to variant rs3190321 [ dbSNP | Ensembl ].
VAR_022767

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei265 – 29127Missing in isoform 2. 1 PublicationVSP_014335Add
BLAST
Alternative sequencei265 – 27814ALEST…ALVSF → DGVSPCRPGWSAVA in isoform 3. 1 PublicationVSP_014336Add
BLAST
Alternative sequencei279 – 985707Missing in isoform 3. 1 PublicationVSP_014337Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027464 mRNA. Translation: BAB55129.1. Different initiation.
AK027646 mRNA. Translation: BAB55262.1.
AK074534 mRNA. Translation: BAC11044.1. Sequence problems.
BC002856 mRNA. Translation: AAH02856.1.
BC013727 mRNA. Translation: AAH13727.1. Different initiation.
BC018635 mRNA. Translation: AAH18635.1.
AF131780 mRNA. Translation: AAD20043.1. Frameshift.
CR457152 mRNA. Translation: CAG33433.1.
CCDSiCCDS32387.1. [Q6PKC3-2]
RefSeqiNP_056998.4. NM_015914.6. [Q6PKC3-2]
UniGeneiHs.313847.

Genome annotation databases

EnsembliENST00000283033; ENSP00000283033; ENSG00000153066. [Q6PKC3-2]
ENST00000356957; ENSP00000349439; ENSG00000153066. [Q6PKC3-1]
GeneIDi51061.
KEGGihsa:51061.
UCSCiuc002dbg.1. human. [Q6PKC3-2]
uc010buu.1. human. [Q6PKC3-1]

Polymorphism databases

DMDMi68566185.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027464 mRNA. Translation: BAB55129.1. Different initiation.
AK027646 mRNA. Translation: BAB55262.1.
AK074534 mRNA. Translation: BAC11044.1. Sequence problems.
BC002856 mRNA. Translation: AAH02856.1.
BC013727 mRNA. Translation: AAH13727.1. Different initiation.
BC018635 mRNA. Translation: AAH18635.1.
AF131780 mRNA. Translation: AAD20043.1. Frameshift.
CR457152 mRNA. Translation: CAG33433.1.
CCDSiCCDS32387.1. [Q6PKC3-2]
RefSeqiNP_056998.4. NM_015914.6. [Q6PKC3-2]
UniGeneiHs.313847.

3D structure databases

ProteinModelPortaliQ6PKC3.
SMRiQ6PKC3. Positions 127-245, 569-827.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119253. 35 interactions.
IntActiQ6PKC3. 43 interactions.
MINTiMINT-2872884.
STRINGi9606.ENSP00000283033.

PTM databases

PhosphoSiteiQ6PKC3.

Polymorphism databases

DMDMi68566185.

Proteomic databases

MaxQBiQ6PKC3.
PaxDbiQ6PKC3.
PRIDEiQ6PKC3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000283033; ENSP00000283033; ENSG00000153066. [Q6PKC3-2]
ENST00000356957; ENSP00000349439; ENSG00000153066. [Q6PKC3-1]
GeneIDi51061.
KEGGihsa:51061.
UCSCiuc002dbg.1. human. [Q6PKC3-2]
uc010buu.1. human. [Q6PKC3-1]

Organism-specific databases

CTDi51061.
GeneCardsiGC16M011772.
H-InvDBHIX0017349.
HGNCiHGNC:28030. TXNDC11.
HPAiHPA041174.
HPA041390.
neXtProtiNX_Q6PKC3.
PharmGKBiPA134915251.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00390000016020.
HOGENOMiHOG000132983.
HOVERGENiHBG082866.
InParanoidiQ6PKC3.
OMAiQNFSVLY.
OrthoDBiEOG7ZSHSG.
PhylomeDBiQ6PKC3.
TreeFamiTF323602.

Miscellaneous databases

GenomeRNAii51061.
NextBioi53645.
PROiQ6PKC3.

Gene expression databases

BgeeiQ6PKC3.
CleanExiHS_TXNDC11.
ExpressionAtlasiQ6PKC3. baseline and differential.
GenevestigatoriQ6PKC3.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 2 hits.
PROSITEiPS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Embryo and Teratocarcinoma.
  2. "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] (ISOFORMS 1 AND 3), VARIANT LEU-783.
    Tissue: Placenta.
  3. Mei G., Yu W., Gibbs R.A.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 523-985.
    Tissue: Brain.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 656-985.
  5. "Identification of a novel partner of duox: EFP1, a thioredoxin-related protein."
    Wang D., De Deken X., Milenkovic M., Song Y., Pirson I., Dumont J.E., Miot F.
    J. Biol. Chem. 280:3096-3103(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INTERACTION WITH DUOX1; DUOX2; TPO AND CYBA.
  6. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
    Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
    Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-828, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.

Entry informationi

Entry nameiTXD11_HUMAN
AccessioniPrimary (citable) accession number: Q6PKC3
Secondary accession number(s): O95887
, Q6PJA6, Q8N2Q4, Q96K45, Q96K53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: March 4, 2015
This is version 113 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  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.