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Protein

Pseudouridine-5'-phosphatase

Gene

HDHD1

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

Functioni

Dephosphorylates pseudouridine 5'-phosphate, a potential intermediate in rRNA degradation. Pseudouridine is then excreted intact in urine.1 Publication

Catalytic activityi

Pseudouridine 5'-phosphate + H2O = pseudouridine + phosphate.1 Publication

Cofactori

Mg2+1 Publication

Kineticsi

  1. KM=0.38 µM for 5'-PsiMP1 Publication
  2. KM=1.5 mM for 3'-AMP1 Publication
  3. KM=5.9 mM for Fructose-6-P1 Publication
  4. KM=9.4 mM for 5'-UMP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei14 – 141NucleophileBy similarity
    Metal bindingi14 – 141MagnesiumBy similarity
    Active sitei16 – 161Proton donorBy similarity
    Metal bindingi16 – 161MagnesiumBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pseudouridine-5'-phosphatase (EC:3.1.3.96)
    Alternative name(s):
    Haloacid dehalogenase-like hydrolase domain-containing protein 1
    Haloacid dehalogenase-like hydrolase domain-containing protein 1A
    Protein GS1
    Pseudouridine-5'-monophosphatase
    Short name:
    5'-PsiMPase
    Gene namesi
    Name:HDHD1
    Synonyms:DXF68S1E, FAM16AX, GS1, HDHD1A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome X

    Organism-specific databases

    HGNCiHGNC:16818. HDHD1.

    Subcellular locationi

    GO - Cellular componenti

    • extracellular exosome Source: UniProtKB
    Complete GO annotation...

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA165756731.

    Polymorphism and mutation databases

    BioMutaiHDHD1.
    DMDMi269849688.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 228228Pseudouridine-5'-phosphatasePRO_0000108068Add
    BLAST

    Proteomic databases

    MaxQBiQ08623.
    PaxDbiQ08623.
    PRIDEiQ08623.

    PTM databases

    DEPODiQ08623.
    PhosphoSiteiQ08623.

    Expressioni

    Inductioni

    Inhibited by low concentrations of calcium.

    Gene expression databases

    BgeeiQ08623.
    CleanExiHS_HDHD1A.
    ExpressionAtlasiQ08623. baseline and differential.
    GenevisibleiQ08623. HS.

    Interactioni

    Protein-protein interaction databases

    BioGridi113859. 2 interactions.
    MINTiMINT-5003687.
    STRINGi9606.ENSP00000396452.

    Structurei

    Secondary structure

    228
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1 – 33Combined sources
    Beta strandi9 – 146Combined sources
    Turni17 – 193Combined sources
    Helixi22 – 3615Combined sources
    Helixi43 – 497Combined sources
    Helixi54 – 6512Combined sources
    Helixi71 – 8515Combined sources
    Helixi86 – 883Combined sources
    Helixi95 – 10410Combined sources
    Beta strandi109 – 1124Combined sources
    Helixi117 – 1237Combined sources
    Turni124 – 1263Combined sources
    Helixi128 – 1314Combined sources
    Helixi153 – 1608Combined sources
    Beta strandi162 – 1643Combined sources
    Helixi168 – 1703Combined sources
    Beta strandi171 – 1777Combined sources
    Helixi178 – 1869Combined sources
    Beta strandi190 – 1934Combined sources
    Helixi201 – 2033Combined sources
    Beta strandi207 – 2104Combined sources
    Helixi214 – 2163Combined sources
    Helixi219 – 2224Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3L5KX-ray2.00A1-228[»]
    ProteinModelPortaliQ08623.
    SMRiQ08623. Positions 1-228.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ08623.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0637.
    GeneTreeiENSGT00390000014753.
    HOGENOMiHOG000248341.
    HOVERGENiHBG005917.
    KOiK17623.
    OMAiERIYTEV.
    OrthoDBiEOG7TF79X.
    PhylomeDBiQ08623.
    TreeFamiTF105946.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    InterProiIPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    [Graphical view]
    PfamiPF13419. HAD_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01509. HAD-SF-IA-v3. 1 hit.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q08623-1) [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
    MAAPPQPVTH LIFDMDGLLL DTERLYSVVF QEICNRYDKK YSWDVKSLVM
    60 70 80 90 100
    GKKALEAAQI IIDVLQLPMS KEELVEESQT KLKEVFPTAA LMPGAEKLII
    110 120 130 140 150
    HLRKHGIPFA LATSSGSASF DMKTSRHKEF FSLFSHIVLG DDPEVQHGKP
    160 170 180 190 200
    DPDIFLACAK RFSPPPAMEK CLVFEDAPNG VEAALAAGMQ VVMVPDGNLS
    210 220
    RDLTTKATLV LNSLQDFQPE LFGLPSYE
    Length:228
    Mass (Da):25,249
    Last modified:November 24, 2009 - v3
    Checksum:iEF9B8CC51C122924
    GO
    Isoform 2 (identifier: Q08623-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         51-93: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:185
    Mass (Da):20,529
    Checksum:i6AEAE431AC9D25BB
    GO
    Isoform 3 (identifier: Q08623-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         171-228: CLVFEDAPNG...PELFGLPSYE → SSIHRPRLLT...NQLLLCSDDT

    Note: No experimental confirmation available.Curated
    Show »
    Length:208
    Mass (Da):23,283
    Checksum:i9BE317B82AA8FF15
    GO
    Isoform 4 (identifier: Q08623-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         20-20: L → LGYTGSIVAAASGESSRGLQSRWT

    Note: No experimental confirmation available.
    Show »
    Length:251
    Mass (Da):27,573
    Checksum:i8671CFD416181D12
    GO

    Sequence cautioni

    The sequence AAA58622.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAH12494.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BAD97125.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BAG35973.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti116 – 1161G → R in AAH12494 (PubMed:15489334).Curated
    Sequence conflicti153 – 1531D → G in BAD97125 (PubMed:14702039).Curated
    Sequence conflicti191 – 1911V → A in AAA58622 (PubMed:1284467).Curated
    Isoform 3 (identifier: Q08623-3)
    Sequence conflicti198 – 1981C → S in BAH13339 (PubMed:14702039).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti88 – 881T → M.2 Publications
    Corresponds to variant rs1131197 [ dbSNP | Ensembl ].
    VAR_061094
    Natural varianti165 – 1651P → A.
    Corresponds to variant rs3747386 [ dbSNP | Ensembl ].
    VAR_060625

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei20 – 201L → LGYTGSIVAAASGESSRGLQ SRWT in isoform 4. 1 PublicationVSP_044804
    Alternative sequencei51 – 9343Missing in isoform 2. 1 PublicationVSP_040029Add
    BLAST
    Alternative sequencei171 – 22858CLVFE…LPSYE → SSIHRPRLLTAQKCQGCRDP FSALLLLCNQLLLCSDDT in isoform 3. 1 PublicationVSP_042020Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK300985 mRNA. Translation: BAG62605.1.
    AK313155 mRNA. Translation: BAG35973.1. Different initiation.
    AK223405 mRNA. Translation: BAD97125.1. Different initiation.
    AK300740 mRNA. Translation: BAH13339.1.
    AC073583 Genomic DNA. No translation available.
    CH471074 Genomic DNA. Translation: EAW98748.1.
    BC012494 mRNA. Translation: AAH12494.1. Different initiation.
    DR156836 mRNA. No translation available.
    M86934 mRNA. Translation: AAA58622.1. Different initiation.
    CCDSiCCDS48075.1. [Q08623-1]
    CCDS48076.1. [Q08623-4]
    CCDS55366.1. [Q08623-3]
    CCDS55367.1. [Q08623-2]
    RefSeqiNP_001129037.1. NM_001135565.1. [Q08623-4]
    NP_001171606.1. NM_001178135.1. [Q08623-3]
    NP_001171607.1. NM_001178136.1. [Q08623-2]
    NP_036212.3. NM_012080.4. [Q08623-1]
    UniGeneiHs.185910.

    Genome annotation databases

    EnsembliENST00000381077; ENSP00000370467; ENSG00000130021. [Q08623-1]
    ENST00000412827; ENSP00000406260; ENSG00000130021. [Q08623-2]
    ENST00000424830; ENSP00000396452; ENSG00000130021. [Q08623-4]
    ENST00000540122; ENSP00000441208; ENSG00000130021. [Q08623-3]
    GeneIDi8226.
    KEGGihsa:8226.
    UCSCiuc004crv.2. human. [Q08623-1]
    uc011mhn.1. human. [Q08623-2]
    uc011mho.1. human. [Q08623-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK300985 mRNA. Translation: BAG62605.1.
    AK313155 mRNA. Translation: BAG35973.1. Different initiation.
    AK223405 mRNA. Translation: BAD97125.1. Different initiation.
    AK300740 mRNA. Translation: BAH13339.1.
    AC073583 Genomic DNA. No translation available.
    CH471074 Genomic DNA. Translation: EAW98748.1.
    BC012494 mRNA. Translation: AAH12494.1. Different initiation.
    DR156836 mRNA. No translation available.
    M86934 mRNA. Translation: AAA58622.1. Different initiation.
    CCDSiCCDS48075.1. [Q08623-1]
    CCDS48076.1. [Q08623-4]
    CCDS55366.1. [Q08623-3]
    CCDS55367.1. [Q08623-2]
    RefSeqiNP_001129037.1. NM_001135565.1. [Q08623-4]
    NP_001171606.1. NM_001178135.1. [Q08623-3]
    NP_001171607.1. NM_001178136.1. [Q08623-2]
    NP_036212.3. NM_012080.4. [Q08623-1]
    UniGeneiHs.185910.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3L5KX-ray2.00A1-228[»]
    ProteinModelPortaliQ08623.
    SMRiQ08623. Positions 1-228.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi113859. 2 interactions.
    MINTiMINT-5003687.
    STRINGi9606.ENSP00000396452.

    PTM databases

    DEPODiQ08623.
    PhosphoSiteiQ08623.

    Polymorphism and mutation databases

    BioMutaiHDHD1.
    DMDMi269849688.

    Proteomic databases

    MaxQBiQ08623.
    PaxDbiQ08623.
    PRIDEiQ08623.

    Protocols and materials databases

    DNASUi8226.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000381077; ENSP00000370467; ENSG00000130021. [Q08623-1]
    ENST00000412827; ENSP00000406260; ENSG00000130021. [Q08623-2]
    ENST00000424830; ENSP00000396452; ENSG00000130021. [Q08623-4]
    ENST00000540122; ENSP00000441208; ENSG00000130021. [Q08623-3]
    GeneIDi8226.
    KEGGihsa:8226.
    UCSCiuc004crv.2. human. [Q08623-1]
    uc011mhn.1. human. [Q08623-2]
    uc011mho.1. human. [Q08623-3]

    Organism-specific databases

    CTDi8226.
    GeneCardsiGC0XM006966.
    HGNCiHGNC:16818. HDHD1.
    MIMi306480. gene.
    neXtProtiNX_Q08623.
    PharmGKBiPA165756731.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0637.
    GeneTreeiENSGT00390000014753.
    HOGENOMiHOG000248341.
    HOVERGENiHBG005917.
    KOiK17623.
    OMAiERIYTEV.
    OrthoDBiEOG7TF79X.
    PhylomeDBiQ08623.
    TreeFamiTF105946.

    Miscellaneous databases

    EvolutionaryTraceiQ08623.
    GeneWikiiHDHD1A.
    GenomeRNAii8226.
    NextBioi30966.
    PROiQ08623.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ08623.
    CleanExiHS_HDHD1A.
    ExpressionAtlasiQ08623. baseline and differential.
    GenevisibleiQ08623. HS.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    InterProiIPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    [Graphical view]
    PfamiPF13419. HAD_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01509. HAD-SF-IA-v3. 1 hit.
    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] (ISOFORMS 1; 2 AND 3), VARIANT MET-88.
      Tissue: Fetal brain, Neuroepithelioma and Small intestine.
    2. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Liver cancer.
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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] (ISOFORMS 1 AND 4).
      Tissue: Embryonic stem cell and Testis.
    6. "Isolation of a new gene from the distal short arm of the human X chromosome that escapes X-inactivation."
      Yen P.H., Ellison J., Salido E.C., Mohandas T., Shapiro L.
      Hum. Mol. Genet. 1:47-52(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-228 (ISOFORM 1), VARIANT MET-88.
    7. "HDHD1, which is often deleted in X-linked ichthyosis, encodes a pseudouridine-5'-phosphatase."
      Preumont A., Rzem R., Vertommen D., Van Schaftingen E.
      Biochem. J. 431:237-244(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Erythrocyte.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "The crystal structure of human haloacid dehalogenase-like hydrolase domain containing 1A (HDHD1A)."
      Structural genomics consortium (SGC)
      Submitted (MAR-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiHDHD1_HUMAN
    AccessioniPrimary (citable) accession number: Q08623
    Secondary accession number(s): B2R7X6
    , B4DV93, B7Z6Q3, E9PAV8, F5GWZ2, Q53F84, Q96EB8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: November 24, 2009
    Last modified: June 24, 2015
    This is version 126 of the entry and version 3 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 X
      Human chromosome X: 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.