Skip Header

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

Q6PKC3

- TXD11_HUMAN

UniProt

Q6PKC3 - TXD11_HUMAN

(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)

Protein

Thioredoxin domain-containing protein 11

Gene

TXNDC11

Organism
Homo sapiens (Human)
Status
Reviewed - 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: RefGenome

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. protein folding Source: RefGenome
  3. response to endoplasmic reticulum stress Source: RefGenome
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

GO - Cellular componenti

  1. endoplasmic reticulum Source: RefGenome
  2. 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. 33 interactions.
IntActiQ6PKC3. 43 interactions.
MINTiMINT-2872884.
STRINGi9606.ENSP00000283033.

Structurei

3D structure databases

ProteinModelPortaliQ6PKC3.
SMRiQ6PKC3. Positions 127-245, 569-812.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

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

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.
OMAiNFSVLYS.
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. Align

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

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:
EMBL
GenBank
DDBJ
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_015914.5. [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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS32387.1. [Q6PKC3-2 ]
RefSeqi NP_056998.4. NM_015914.5. [Q6PKC3-2 ]
UniGenei Hs.313847.

3D structure databases

ProteinModelPortali Q6PKC3.
SMRi Q6PKC3. Positions 127-245, 569-812.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119253. 33 interactions.
IntActi Q6PKC3. 43 interactions.
MINTi MINT-2872884.
STRINGi 9606.ENSP00000283033.

PTM databases

PhosphoSitei Q6PKC3.

Polymorphism databases

DMDMi 68566185.

Proteomic databases

MaxQBi Q6PKC3.
PaxDbi Q6PKC3.
PRIDEi Q6PKC3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000283033 ; ENSP00000283033 ; ENSG00000153066 . [Q6PKC3-2 ]
ENST00000356957 ; ENSP00000349439 ; ENSG00000153066 . [Q6PKC3-1 ]
GeneIDi 51061.
KEGGi hsa:51061.
UCSCi uc002dbg.1. human. [Q6PKC3-2 ]
uc010buu.1. human. [Q6PKC3-1 ]

Organism-specific databases

CTDi 51061.
GeneCardsi GC16M011772.
H-InvDB HIX0017349.
HGNCi HGNC:28030. TXNDC11.
HPAi HPA041174.
HPA041390.
neXtProti NX_Q6PKC3.
PharmGKBi PA134915251.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0526.
GeneTreei ENSGT00390000016020.
HOGENOMi HOG000132983.
HOVERGENi HBG082866.
InParanoidi Q6PKC3.
OMAi NFSVLYS.
OrthoDBi EOG7ZSHSG.
PhylomeDBi Q6PKC3.
TreeFami TF323602.

Miscellaneous databases

GenomeRNAii 51061.
NextBioi 53645.
PROi Q6PKC3.

Gene expression databases

Bgeei Q6PKC3.
CleanExi HS_TXNDC11.
ExpressionAtlasi Q6PKC3. baseline and differential.
Genevestigatori Q6PKC3.

Family and domain databases

Gene3Di 3.40.30.10. 2 hits.
InterProi IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view ]
Pfami PF00085. Thioredoxin. 2 hits.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 2 hits.
PROSITEi PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 109 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