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Protein

Iodotyrosine dehalogenase 1

Gene

IYD

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

Functioni

Catalyzes the oxidative NADPH-dependent deiodination of monoiodotyrosine (L-MIT) or diiodotyrosine (L-DIT). Acts during the hydrolysis of thyroglobulin to liberate iodide, which can then reenter the hormone-producing pathways. Acts more efficiently on monoiodotyrosine than on diiodotyrosine.1 Publication

Catalytic activityi

L-tyrosine + 2 NADP+ + 2 I- = 3,5-diiodo-L-tyrosine + 2 NADPH.

Cofactori

FMNCurated

Kineticsi

  1. KM=2.67 µM for L-DIT1 Publication
  2. KM=1.35 µM for L-MIT1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei104 – 1041SubstrateBy similarity
Binding sitei161 – 1611SubstrateBy similarity
Binding sitei182 – 1821SubstrateBy similarity
Binding sitei279 – 2791FMNBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi100 – 1045FMNBy similarity
Nucleotide bindingi127 – 1293FMNBy similarity
Nucleotide bindingi236 – 2394FMNBy similarity

GO - Molecular functioni

  1. iodide peroxidase activity Source: Ensembl
  2. oxidoreductase activity Source: Reactome

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. small molecule metabolic process Source: Reactome
  3. thyroid hormone generation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN, NADP

Enzyme and pathway databases

BRENDAi1.22.1.1. 2681.
ReactomeiREACT_15292. Thyroxine biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Iodotyrosine dehalogenase 1 (EC:1.22.1.1)
Short name:
IYD-1
Gene namesi
Name:IYD
Synonyms:C6orf71, DEHAL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21071. IYD.

Subcellular locationi

  1. Cell membrane 1 Publication; Single-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 214191ExtracellularSequence AnalysisAdd
BLAST
Transmembranei215 – 23521HelicalSequence AnalysisAdd
BLAST
Topological domaini236 – 28954CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Thyroid dyshormonogenesis 4 (TDH4)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder due to thyroid dyshormonogenesis, causing severe hypothyroidism, goiter, excessive levels of iodotyrosine in serum and urine, and variable mental deficits derived from unrecognized and untreated hypothyroidism.

See also OMIM:274800
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti101 – 1011R → W in TDH4; strongly reduces activity; does not respond to the increase of flavin mononucleotide concentration. 1 Publication
VAR_045963
Natural varianti105 – 1062FI → L in TDH4; strongly reduces activity; does not respond to the increase of flavin mononucleotide concentration.
VAR_045964
Natural varianti116 – 1161I → T in TDH4; strongly reduces activity; marginally respond to the increase of flavin mononucleotide concentration; reduces protein stability. 1 Publication
VAR_045965

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi101 – 1011R → A: Strongly reduces activity. 1 Publication
Mutagenesisi101 – 1011R → H: Reduces activity. 1 Publication
Mutagenesisi105 – 1051F → A: Activity as the wild type. 1 Publication
Mutagenesisi105 – 1051F → Y: Activity as the wild type. 1 Publication
Mutagenesisi116 – 1161I → V: Activity as the wild type. 1 Publication

Keywords - Diseasei

Congenital hypothyroidism, Disease mutation

Organism-specific databases

MIMi274800. phenotype.
Orphaneti95716. Familial thyroid dyshormonogenesis.
PharmGKBiPA162392352.

Polymorphism and mutation databases

BioMutaiIYD.
DMDMi91207083.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 289266Iodotyrosine dehalogenase 1PRO_0000230278Add
BLAST

Proteomic databases

PaxDbiQ6PHW0.
PRIDEiQ6PHW0.

PTM databases

PhosphoSiteiQ6PHW0.

Expressioni

Tissue specificityi

Expressed at a high level in thyroid gland and at lower level in kidney and trachea.1 Publication

Gene expression databases

BgeeiQ6PHW0.
ExpressionAtlasiQ6PHW0. baseline and differential.
GenevestigatoriQ6PHW0.

Organism-specific databases

HPAiHPA059627.

Interactioni

Subunit structurei

Homodimer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
TRIM69Q86WT63EBI-10253668,EBI-749955

Protein-protein interaction databases

BioGridi133150. 3 interactions.
IntActiQ6PHW0. 1 interaction.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi73 – 753Combined sources
Beta strandi77 – 793Combined sources
Helixi83 – 9816Combined sources
Helixi113 – 12311Combined sources
Helixi129 – 1313Combined sources
Beta strandi135 – 1406Combined sources
Helixi143 – 15715Combined sources
Helixi167 – 1726Combined sources
Helixi174 – 1763Combined sources
Helixi184 – 1874Combined sources
Beta strandi188 – 19710Combined sources
Beta strandi207 – 2093Combined sources
Helixi213 – 23119Combined sources
Helixi244 – 2507Combined sources
Beta strandi255 – 26612Combined sources
Beta strandi273 – 2753Combined sources
Helixi282 – 2843Combined sources
Beta strandi286 – 2894Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4TTBX-ray2.45A/B32-289[»]
4TTCX-ray2.65A/B/C/D/E/F32-289[»]
ProteinModelPortaliQ6PHW0.
SMRiQ6PHW0. Positions 70-289.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the nitroreductase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0778.
GeneTreeiENSGT00390000004348.
HOGENOMiHOG000146731.
HOVERGENiHBG055004.
InParanoidiQ6PHW0.
KOiK17231.
OMAiRPAHEKL.
OrthoDBiEOG7HMS24.
PhylomeDBiQ6PHW0.
TreeFamiTF313415.

Family and domain databases

Gene3Di3.40.109.10. 1 hit.
InterProiIPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
[Graphical view]
PfamiPF00881. Nitroreductase. 1 hit.
[Graphical view]
SUPFAMiSSF55469. SSF55469. 1 hit.

Sequences (6)i

Sequence statusi: Complete.

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

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6PHW0-1) [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
MYFLTPILVA ILCILVVWIF KNADRSMEKK KGEPRTRAEA RPWVDEDLKD
60 70 80 90 100
SSDLHQAEED ADEWQESEEN VEHIPFSHNH YPEKEMVKRS QEFYELLNKR
110 120 130 140 150
RSVRFISNEQ VPMEVIDNVI RTAGTAPSGA HTEPWTFVVV KDPDVKHKIR
160 170 180 190 200
KIIEEEEEIN YMKRMGHRWV TDLKKLRTNW IKEYLDTAPI LILIFKQVHG
210 220 230 240 250
FAANGKKKVH YYNEISVSIA CGILLAALQN AGLVTVTTTP LNCGPRLRVL
260 270 280
LGRPAHEKLL MLLPVGYPSK EATVPDLKRK PLDQIMVTV
Length:289
Mass (Da):33,360
Last modified:April 4, 2006 - v2
Checksum:iB73560A682BF6045
GO
Isoform 3 (identifier: Q6PHW0-3) [UniParc]FASTAAdd to basket

Also known as: E

The sequence of this isoform differs from the canonical sequence as follows:
     230-248: NAGLVTVTTTPLNCGPRLR → VFGKIILKELALISFLNL
     249-289: Missing.

Show »
Length:247
Mass (Da):28,858
Checksum:i256CCEE175E985A1
GO
Isoform 4 (identifier: Q6PHW0-4) [UniParc]FASTAAdd to basket

Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     230-289: NAGLVTVTTT...KPLDQIMVTV → VNNGITMRHQ...TEGAPGPPRT

Show »
Length:293
Mass (Da):33,781
Checksum:i2DEF1D502CC9F28E
GO
Isoform 5 (identifier: Q6PHW0-5) [UniParc]FASTAAdd to basket

Also known as: C

The sequence of this isoform differs from the canonical sequence as follows:
     230-284: NAGLVTVTTT...PDLKRKPLDQ → VNNGITMRHQ...FHFAIEFAAP
     285-289: Missing.

Show »
Length:284
Mass (Da):32,642
Checksum:i2C8639AEB123CF4F
GO
Isoform 6 (identifier: Q6PHW0-6) [UniParc]FASTAAdd to basket

Also known as: D

The sequence of this isoform differs from the canonical sequence as follows:
     230-270: NAGLVTVTTT...MLLPVGYPSK → VNNGITMRHQ...SSQGRPGFYC
     271-289: Missing.

Show »
Length:270
Mass (Da):31,367
Checksum:i501B6AC58642354A
GO
Isoform 7 (identifier: Q6PHW0-7) [UniParc]FASTAAdd to basket

Also known as: F

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: Missing.
     56-61: QAEEDA → MKEADV
     230-248: NAGLVTVTTTPLNCGPRLR → VFGKIILKELALISFLNL
     249-289: Missing.

Show »
Length:192
Mass (Da):22,460
Checksum:i5EFAEB7D3AF9FFBC
GO

Sequence cautioni

The sequence BAC85255.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 4 (identifier: Q6PHW0-4)
Sequence conflicti265 – 2651C → R in AAP22073 (Ref. 1) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti101 – 1011R → W in TDH4; strongly reduces activity; does not respond to the increase of flavin mononucleotide concentration. 1 Publication
VAR_045963
Natural varianti105 – 1062FI → L in TDH4; strongly reduces activity; does not respond to the increase of flavin mononucleotide concentration.
VAR_045964
Natural varianti116 – 1161I → T in TDH4; strongly reduces activity; marginally respond to the increase of flavin mononucleotide concentration; reduces protein stability. 1 Publication
VAR_045965
Natural varianti260 – 2601L → P.1 Publication
Corresponds to variant rs17854906 [ dbSNP | Ensembl ].
VAR_025785
Natural varianti271 – 2711E → K.
Corresponds to variant rs36063028 [ dbSNP | Ensembl ].
VAR_045966

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5555Missing in isoform 7. 1 PublicationVSP_017802Add
BLAST
Alternative sequencei56 – 616QAEEDA → MKEADV in isoform 7. 1 PublicationVSP_017803
Alternative sequencei230 – 28960NAGLV…IMVTV → VNNGITMRHQTARHRHLIEG PGRSSEACSKLSSQGCPECR SGDCHYHSSQLWPSTEGAPG PPRT in isoform 4. 1 PublicationVSP_017805Add
BLAST
Alternative sequencei230 – 28455NAGLV…KPLDQ → VNNGITMRHQTARHRHLIEG PGRSSEACSKLSSQGRPGAS AAGSLFHFAIEFAAP in isoform 5. 1 PublicationVSP_017806Add
BLAST
Alternative sequencei230 – 27041NAGLV…GYPSK → VNNGITMRHQTARHRHLIEG PGRSSEACSKLSSQGRPGFY C in isoform 6. 1 PublicationVSP_017807Add
BLAST
Alternative sequencei230 – 24819NAGLV…GPRLR → VFGKIILKELALISFLNL in isoform 3 and isoform 7. 1 PublicationVSP_017809Add
BLAST
Alternative sequencei249 – 28941Missing in isoform 3 and isoform 7. 1 PublicationVSP_017810Add
BLAST
Alternative sequencei271 – 28919Missing in isoform 6. 1 PublicationVSP_017812Add
BLAST
Alternative sequencei285 – 2895Missing in isoform 5. 1 PublicationVSP_017813

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY259176 mRNA. Translation: AAP22072.1.
AY259177 mRNA. Translation: AAP22073.1.
AY424901 mRNA. Translation: AAR84259.1.
AY424902 mRNA. Translation: AAR84260.1.
AY957659 mRNA. Translation: AAY41465.1.
AY957660 mRNA. Translation: AAY41466.1.
AY957661 mRNA. Translation: AAY41467.1. Sequence problems.
AL031010 Genomic DNA. No translation available.
BC056253 mRNA. Translation: AAH56253.1.
AK129950 mRNA. Translation: BAC85255.1. Different initiation.
CCDSiCCDS5227.1. [Q6PHW0-1]
CCDS55066.1. [Q6PHW0-3]
CCDS55067.1. [Q6PHW0-4]
RefSeqiNP_001158166.1. NM_001164694.1. [Q6PHW0-4]
NP_001158167.1. NM_001164695.1. [Q6PHW0-3]
NP_981932.1. NM_203395.2. [Q6PHW0-1]
UniGeneiHs.310225.

Genome annotation databases

EnsembliENST00000229447; ENSP00000229447; ENSG00000009765. [Q6PHW0-4]
ENST00000344419; ENSP00000343763; ENSG00000009765. [Q6PHW0-1]
ENST00000367335; ENSP00000356304; ENSG00000009765. [Q6PHW0-3]
ENST00000392256; ENSP00000376085; ENSG00000009765. [Q6PHW0-3]
GeneIDi389434.
KEGGihsa:389434.
UCSCiuc003qnu.2. human. [Q6PHW0-1]
uc003qnv.2. human. [Q6PHW0-3]

Polymorphism and mutation databases

BioMutaiIYD.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY259176 mRNA. Translation: AAP22072.1.
AY259177 mRNA. Translation: AAP22073.1.
AY424901 mRNA. Translation: AAR84259.1.
AY424902 mRNA. Translation: AAR84260.1.
AY957659 mRNA. Translation: AAY41465.1.
AY957660 mRNA. Translation: AAY41466.1.
AY957661 mRNA. Translation: AAY41467.1. Sequence problems.
AL031010 Genomic DNA. No translation available.
BC056253 mRNA. Translation: AAH56253.1.
AK129950 mRNA. Translation: BAC85255.1. Different initiation.
CCDSiCCDS5227.1. [Q6PHW0-1]
CCDS55066.1. [Q6PHW0-3]
CCDS55067.1. [Q6PHW0-4]
RefSeqiNP_001158166.1. NM_001164694.1. [Q6PHW0-4]
NP_001158167.1. NM_001164695.1. [Q6PHW0-3]
NP_981932.1. NM_203395.2. [Q6PHW0-1]
UniGeneiHs.310225.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4TTBX-ray2.45A/B32-289[»]
4TTCX-ray2.65A/B/C/D/E/F32-289[»]
ProteinModelPortaliQ6PHW0.
SMRiQ6PHW0. Positions 70-289.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi133150. 3 interactions.
IntActiQ6PHW0. 1 interaction.

PTM databases

PhosphoSiteiQ6PHW0.

Polymorphism and mutation databases

BioMutaiIYD.
DMDMi91207083.

Proteomic databases

PaxDbiQ6PHW0.
PRIDEiQ6PHW0.

Protocols and materials databases

DNASUi389434.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000229447; ENSP00000229447; ENSG00000009765. [Q6PHW0-4]
ENST00000344419; ENSP00000343763; ENSG00000009765. [Q6PHW0-1]
ENST00000367335; ENSP00000356304; ENSG00000009765. [Q6PHW0-3]
ENST00000392256; ENSP00000376085; ENSG00000009765. [Q6PHW0-3]
GeneIDi389434.
KEGGihsa:389434.
UCSCiuc003qnu.2. human. [Q6PHW0-1]
uc003qnv.2. human. [Q6PHW0-3]

Organism-specific databases

CTDi389434.
GeneCardsiGC06P150731.
H-InvDBHIX0025059.
HGNCiHGNC:21071. IYD.
HPAiHPA059627.
MIMi274800. phenotype.
612025. gene.
neXtProtiNX_Q6PHW0.
Orphaneti95716. Familial thyroid dyshormonogenesis.
PharmGKBiPA162392352.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0778.
GeneTreeiENSGT00390000004348.
HOGENOMiHOG000146731.
HOVERGENiHBG055004.
InParanoidiQ6PHW0.
KOiK17231.
OMAiRPAHEKL.
OrthoDBiEOG7HMS24.
PhylomeDBiQ6PHW0.
TreeFamiTF313415.

Enzyme and pathway databases

BRENDAi1.22.1.1. 2681.
ReactomeiREACT_15292. Thyroxine biosynthesis.

Miscellaneous databases

ChiTaRSiIYD. human.
GeneWikiiIodotyrosine_deiodinase.
GenomeRNAii389434.
NextBioi102878.
PROiQ6PHW0.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PHW0.
ExpressionAtlasiQ6PHW0. baseline and differential.
GenevestigatoriQ6PHW0.

Family and domain databases

Gene3Di3.40.109.10. 1 hit.
InterProiIPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
[Graphical view]
PfamiPF00881. Nitroreductase. 1 hit.
[Graphical view]
SUPFAMiSSF55469. SSF55469. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a novel thyroidal gene encoding proteins with a conserved nitroreductase domain."
    Moreno J.C., Keijser R., Aarraas S., De Vijlder J.J.M., Ris-Stalpers C.
    J. Endocrinol. Invest. 25 Suppl. 7:S23-S23(2002)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 4 AND 5).
    Tissue: Thyroid.
  2. "Cloning and characterization of the human iodotyrosine dehalogenase isoform 1C."
    Gnidehou S., Ohayon R., Kaniewski J., Morand S., Noel-Hudson M.-S., Virion A., Dupuy C.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
    Tissue: Thyroid.
  3. "New transcript variants of the human iodotyrosine dehalogenase gene."
    Rodrigues-Serpa A.R., Laires R.S., Monteiro C.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 7).
    Tissue: Thyroid.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1), VARIANT PRO-260.
    Tissue: Kidney.
  6. "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] OF 11-289 (ISOFORM 1).
    Tissue: Kidney.
  7. "Iodotyrosine dehalogenase 1 (DEHAL1) is a transmembrane protein involved in the recycling of iodide close to the thyroglobulin iodination site."
    Gnidehou S., Caillou B., Talbot M., Ohayon R., Kaniewski J., Noel-Hudson M.-S., Morand S., Agnangji D., Sezan A., Courtin F., Virion A., Dupuy C.
    FASEB J. 18:1574-1576(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  8. "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.
  9. Cited for: VARIANTS TDH4 TRP-101; 105-PHE-ISO-106 DELINS LEU AND THR-116, CHARACTERIZATION OF VARIANTS TDH4 TRP-101; 105-PHE-ISO-106 DELINS LEU AND THR-116, MUTAGENESIS OF ARG-101; PHE-105 AND ILE-116.

Entry informationi

Entry nameiIYD1_HUMAN
AccessioniPrimary (citable) accession number: Q6PHW0
Secondary accession number(s): C9JFW2
, Q2VPW0, Q2VPW1, Q5F1L5, Q5F1L6, Q5THM4, Q6ZP69, Q7Z7D7, Q7Z7D8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 4, 2006
Last modified: April 29, 2015
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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.