Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

Q08623

- HDHD1_HUMAN

UniProt

Q08623 - HDHD1_HUMAN

Protein

Pseudouridine-5'-monophosphatase

Gene

HDHD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 3 (24 Nov 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Magnesium.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

    1. metal ion binding Source: UniProtKB-KW
    2. phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. nucleotide metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pseudouridine-5'-monophosphatase (EC:3.1.3.n6)
    Short name:
    5'-PsiMPase
    Alternative name(s):
    Haloacid dehalogenase-like hydrolase domain-containing protein 1
    Haloacid dehalogenase-like hydrolase domain-containing protein 1A
    Protein GS1
    Gene namesi
    Name:HDHD1
    Synonyms:DXF68S1E, FAM16AX, GS1, HDHD1A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:16818. HDHD1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA165756731.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 228228Pseudouridine-5'-monophosphatasePRO_0000108068Add
    BLAST

    Proteomic databases

    MaxQBiQ08623.
    PaxDbiQ08623.
    PRIDEiQ08623.

    PTM databases

    PhosphoSiteiQ08623.

    Expressioni

    Inductioni

    Inhibited by low concentrations of calcium.

    Gene expression databases

    ArrayExpressiQ08623.
    BgeeiQ08623.
    CleanExiHS_HDHD1A.
    GenevestigatoriQ08623.

    Interactioni

    Protein-protein interaction databases

    BioGridi113859. 1 interaction.
    MINTiMINT-5003687.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000248341.
    HOVERGENiHBG005917.
    InParanoidiQ08623.
    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. Align

    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

    MAAPPQPVTH LIFDMDGLLL DTERLYSVVF QEICNRYDKK YSWDVKSLVM    50
    GKKALEAAQI IIDVLQLPMS KEELVEESQT KLKEVFPTAA LMPGAEKLII 100
    HLRKHGIPFA LATSSGSASF DMKTSRHKEF FSLFSHIVLG DDPEVQHGKP 150
    DPDIFLACAK RFSPPPAMEK CLVFEDAPNG VEAALAAGMQ VVMVPDGNLS 200
    RDLTTKATLV LNSLQDFQPE LFGLPSYE 228
    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.
    The sequence AAH12494.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAD97125.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAG35973.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi269849688.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS48075.1. [Q08623-1 ]
    CCDS48076.1. [Q08623-4 ]
    CCDS55366.1. [Q08623-3 ]
    CCDS55367.1. [Q08623-2 ]
    RefSeqi NP_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 ]
    UniGenei Hs.185910.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3L5K X-ray 2.00 A 1-228 [» ]
    ProteinModelPortali Q08623.
    SMRi Q08623. Positions 1-228.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113859. 1 interaction.
    MINTi MINT-5003687.

    PTM databases

    PhosphoSitei Q08623.

    Polymorphism databases

    DMDMi 269849688.

    Proteomic databases

    MaxQBi Q08623.
    PaxDbi Q08623.
    PRIDEi Q08623.

    Protocols and materials databases

    DNASUi 8226.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381077 ; ENSP00000370467 ; ENSG00000130021 . [Q08623-1 ]
    ENST00000412827 ; ENSP00000406260 ; ENSG00000130021 . [Q08623-2 ]
    ENST00000424830 ; ENSP00000396452 ; ENSG00000130021 . [Q08623-4 ]
    ENST00000540122 ; ENSP00000441208 ; ENSG00000130021 . [Q08623-3 ]
    GeneIDi 8226.
    KEGGi hsa:8226.
    UCSCi uc004crv.2. human. [Q08623-1 ]
    uc011mhn.1. human. [Q08623-2 ]
    uc011mho.1. human. [Q08623-3 ]

    Organism-specific databases

    CTDi 8226.
    GeneCardsi GC0XM006966.
    HGNCi HGNC:16818. HDHD1.
    MIMi 306480. gene.
    neXtProti NX_Q08623.
    PharmGKBi PA165756731.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0637.
    HOGENOMi HOG000248341.
    HOVERGENi HBG005917.
    InParanoidi Q08623.
    KOi K17623.
    OMAi ERIYTEV.
    OrthoDBi EOG7TF79X.
    PhylomeDBi Q08623.
    TreeFami TF105946.

    Miscellaneous databases

    EvolutionaryTracei Q08623.
    GeneWikii HDHD1A.
    GenomeRNAii 8226.
    NextBioi 30966.
    PROi Q08623.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q08623.
    Bgeei Q08623.
    CleanExi HS_HDHD1A.
    Genevestigatori Q08623.

    Family and domain databases

    Gene3Di 3.40.50.1000. 2 hits.
    InterProi IPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    [Graphical view ]
    Pfami PF13419. HAD_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR01509. HAD-SF-IA-v3. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 118 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