Full text data of HDHD1
HDHD1
(DXF68S1E, FAM16AX, GS1, HDHD1A)
[Confidence: low (only semi-automatic identification from reviews)]
Pseudouridine-5'-monophosphatase; 5'-PsiMPase; 3.1.3.n6 (Haloacid dehalogenase-like hydrolase domain-containing protein 1; Haloacid dehalogenase-like hydrolase domain-containing protein 1A; Protein GS1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Pseudouridine-5'-monophosphatase; 5'-PsiMPase; 3.1.3.n6 (Haloacid dehalogenase-like hydrolase domain-containing protein 1; Haloacid dehalogenase-like hydrolase domain-containing protein 1A; Protein GS1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q08623
ID HDHD1_HUMAN Reviewed; 228 AA.
AC Q08623; B2R7X6; B4DV93; B7Z6Q3; E9PAV8; F5GWZ2; Q53F84; Q96EB8;
read moreDT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=Pseudouridine-5'-monophosphatase;
DE Short=5'-PsiMPase;
DE EC=3.1.3.n6;
DE AltName: Full=Haloacid dehalogenase-like hydrolase domain-containing protein 1;
DE AltName: Full=Haloacid dehalogenase-like hydrolase domain-containing protein 1A;
DE AltName: Full=Protein GS1;
GN Name=HDHD1; Synonyms=DXF68S1E, FAM16AX, GS1, HDHD1A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
RP VARIANT MET-88.
RC TISSUE=Fetal brain, Neuroepithelioma, and Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver cancer;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Embryonic stem cell, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-228 (ISOFORM 1), AND VARIANT MET-88.
RX PubMed=1284467; DOI=10.1093/hmg/1.1.47;
RA Yen P.H., Ellison J., Salido E.C., Mohandas T., Shapiro L.;
RT "Isolation of a new gene from the distal short arm of the human X
RT chromosome that escapes X-inactivation.";
RL Hum. Mol. Genet. 1:47-52(1992).
RN [7]
RP FUNCTION, COFACTOR, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC TISSUE=Erythrocyte;
RX PubMed=20722631; DOI=10.1042/BJ20100174;
RA Preumont A., Rzem R., Vertommen D., Van Schaftingen E.;
RT "HDHD1, which is often deleted in X-linked ichthyosis, encodes a
RT pseudouridine-5'-phosphatase.";
RL Biochem. J. 431:237-244(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RG Structural genomics consortium (SGC);
RT "The crystal structure of human haloacid dehalogenase-like hydrolase
RT domain containing 1A (HDHD1A).";
RL Submitted (MAR-2010) to the PDB data bank.
CC -!- FUNCTION: Dephosphorylates pseudouridine 5'-phosphate, a potential
CC intermediate in rRNA degradation. Pseudouridine is then excreted
CC intact in urine.
CC -!- CATALYTIC ACTIVITY: pseudouridine 5'-monophosphate + H(2)O =
CC Pseudouridine + phosphate.
CC -!- COFACTOR: Magnesium.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.38 uM for 5'-PsiMP;
CC KM=1.5 mM for 3'-AMP;
CC KM=5.9 mM for Fructose-6-P;
CC KM=9.4 mM for 5'-UMP;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q08623-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08623-2; Sequence=VSP_040029;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q08623-3; Sequence=VSP_042020;
CC Note=Ref.1 (BAH13339) sequence is in conflict in position:
CC 198:C->S. No experimental confirmation available;
CC Name=4;
CC IsoId=Q08623-4; Sequence=VSP_044804;
CC Note=No experimental confirmation available;
CC -!- INDUCTION: Inhibited by low concentrations of calcium.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58622.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH12494.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAD97125.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAG35973.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK300985; BAG62605.1; -; mRNA.
DR EMBL; AK313155; BAG35973.1; ALT_INIT; mRNA.
DR EMBL; AK223405; BAD97125.1; ALT_INIT; mRNA.
DR EMBL; AK300740; BAH13339.1; -; mRNA.
DR EMBL; AC073583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW98748.1; -; Genomic_DNA.
DR EMBL; BC012494; AAH12494.1; ALT_INIT; mRNA.
DR EMBL; DR156836; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M86934; AAA58622.1; ALT_INIT; mRNA.
DR RefSeq; NP_001129037.1; NM_001135565.1.
DR RefSeq; NP_001171606.1; NM_001178135.1.
DR RefSeq; NP_001171607.1; NM_001178136.1.
DR RefSeq; NP_036212.3; NM_012080.4.
DR UniGene; Hs.185910; -.
DR PDB; 3L5K; X-ray; 2.00 A; A=1-228.
DR PDBsum; 3L5K; -.
DR ProteinModelPortal; Q08623; -.
DR SMR; Q08623; 1-228.
DR MINT; MINT-5003687; -.
DR PhosphoSite; Q08623; -.
DR DMDM; 269849688; -.
DR PaxDb; Q08623; -.
DR PRIDE; Q08623; -.
DR DNASU; 8226; -.
DR Ensembl; ENST00000381077; ENSP00000370467; ENSG00000130021.
DR Ensembl; ENST00000412827; ENSP00000406260; ENSG00000130021.
DR Ensembl; ENST00000424830; ENSP00000396452; ENSG00000130021.
DR Ensembl; ENST00000540122; ENSP00000441208; ENSG00000130021.
DR GeneID; 8226; -.
DR KEGG; hsa:8226; -.
DR UCSC; uc011mhm.1; human.
DR CTD; 8226; -.
DR GeneCards; GC0XM006966; -.
DR HGNC; HGNC:16818; HDHD1.
DR MIM; 306480; gene.
DR neXtProt; NX_Q08623; -.
DR PharmGKB; PA165756731; -.
DR eggNOG; COG0637; -.
DR HOGENOM; HOG000248341; -.
DR HOVERGEN; HBG005917; -.
DR InParanoid; Q08623; -.
DR KO; K17623; -.
DR OMA; ERIYTEV; -.
DR OrthoDB; EOG7TF79X; -.
DR PhylomeDB; Q08623; -.
DR EvolutionaryTrace; Q08623; -.
DR GeneWiki; HDHD1A; -.
DR GenomeRNAi; 8226; -.
DR NextBio; 30966; -.
DR PRO; PR:Q08623; -.
DR ArrayExpress; Q08623; -.
DR Bgee; Q08623; -.
DR CleanEx; HS_HDHD1A; -.
DR Genevestigator; Q08623; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:GOC.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Hydrolase;
KW Magnesium; Metal-binding; Nucleotide metabolism; Polymorphism;
KW Reference proteome.
FT CHAIN 1 228 Pseudouridine-5'-monophosphatase.
FT /FTId=PRO_0000108068.
FT ACT_SITE 14 14 Nucleophile (By similarity).
FT ACT_SITE 16 16 Proton donor (By similarity).
FT METAL 14 14 Magnesium (By similarity).
FT METAL 16 16 Magnesium (By similarity).
FT VAR_SEQ 20 20 L -> LGYTGSIVAAASGESSRGLQSRWT (in isoform
FT 4).
FT /FTId=VSP_044804.
FT VAR_SEQ 51 93 Missing (in isoform 2).
FT /FTId=VSP_040029.
FT VAR_SEQ 171 228 CLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVL
FT NSLQDFQPELFGLPSYE -> SSIHRPRLLTAQKCQGCRDP
FT FSALLLLCNQLLLCSDDT (in isoform 3).
FT /FTId=VSP_042020.
FT VARIANT 88 88 T -> M (in dbSNP:rs1131197).
FT /FTId=VAR_061094.
FT VARIANT 165 165 P -> A (in dbSNP:rs3747386).
FT /FTId=VAR_060625.
FT CONFLICT 116 116 G -> R (in Ref. 5; AAH12494).
FT CONFLICT 153 153 D -> G (in Ref. 1; BAD97125).
FT CONFLICT 191 191 V -> A (in Ref. 6; AAA58622).
FT STRAND 1 3
FT STRAND 9 14
FT TURN 17 19
FT HELIX 22 36
FT HELIX 43 49
FT HELIX 54 65
FT HELIX 71 85
FT HELIX 86 88
FT HELIX 95 104
FT STRAND 109 112
FT HELIX 117 123
FT TURN 124 126
FT HELIX 128 131
FT HELIX 153 160
FT STRAND 162 164
FT HELIX 168 170
FT STRAND 171 177
FT HELIX 178 186
FT STRAND 190 193
FT HELIX 201 203
FT STRAND 207 210
FT HELIX 214 216
FT HELIX 219 222
SQ SEQUENCE 228 AA; 25249 MW; EF9B8CC51C122924 CRC64;
MAAPPQPVTH LIFDMDGLLL DTERLYSVVF QEICNRYDKK YSWDVKSLVM GKKALEAAQI
IIDVLQLPMS KEELVEESQT KLKEVFPTAA LMPGAEKLII HLRKHGIPFA LATSSGSASF
DMKTSRHKEF FSLFSHIVLG DDPEVQHGKP DPDIFLACAK RFSPPPAMEK CLVFEDAPNG
VEAALAAGMQ VVMVPDGNLS RDLTTKATLV LNSLQDFQPE LFGLPSYE
//
ID HDHD1_HUMAN Reviewed; 228 AA.
AC Q08623; B2R7X6; B4DV93; B7Z6Q3; E9PAV8; F5GWZ2; Q53F84; Q96EB8;
read moreDT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=Pseudouridine-5'-monophosphatase;
DE Short=5'-PsiMPase;
DE EC=3.1.3.n6;
DE AltName: Full=Haloacid dehalogenase-like hydrolase domain-containing protein 1;
DE AltName: Full=Haloacid dehalogenase-like hydrolase domain-containing protein 1A;
DE AltName: Full=Protein GS1;
GN Name=HDHD1; Synonyms=DXF68S1E, FAM16AX, GS1, HDHD1A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
RP VARIANT MET-88.
RC TISSUE=Fetal brain, Neuroepithelioma, and Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver cancer;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Embryonic stem cell, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-228 (ISOFORM 1), AND VARIANT MET-88.
RX PubMed=1284467; DOI=10.1093/hmg/1.1.47;
RA Yen P.H., Ellison J., Salido E.C., Mohandas T., Shapiro L.;
RT "Isolation of a new gene from the distal short arm of the human X
RT chromosome that escapes X-inactivation.";
RL Hum. Mol. Genet. 1:47-52(1992).
RN [7]
RP FUNCTION, COFACTOR, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC TISSUE=Erythrocyte;
RX PubMed=20722631; DOI=10.1042/BJ20100174;
RA Preumont A., Rzem R., Vertommen D., Van Schaftingen E.;
RT "HDHD1, which is often deleted in X-linked ichthyosis, encodes a
RT pseudouridine-5'-phosphatase.";
RL Biochem. J. 431:237-244(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RG Structural genomics consortium (SGC);
RT "The crystal structure of human haloacid dehalogenase-like hydrolase
RT domain containing 1A (HDHD1A).";
RL Submitted (MAR-2010) to the PDB data bank.
CC -!- FUNCTION: Dephosphorylates pseudouridine 5'-phosphate, a potential
CC intermediate in rRNA degradation. Pseudouridine is then excreted
CC intact in urine.
CC -!- CATALYTIC ACTIVITY: pseudouridine 5'-monophosphate + H(2)O =
CC Pseudouridine + phosphate.
CC -!- COFACTOR: Magnesium.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.38 uM for 5'-PsiMP;
CC KM=1.5 mM for 3'-AMP;
CC KM=5.9 mM for Fructose-6-P;
CC KM=9.4 mM for 5'-UMP;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q08623-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08623-2; Sequence=VSP_040029;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q08623-3; Sequence=VSP_042020;
CC Note=Ref.1 (BAH13339) sequence is in conflict in position:
CC 198:C->S. No experimental confirmation available;
CC Name=4;
CC IsoId=Q08623-4; Sequence=VSP_044804;
CC Note=No experimental confirmation available;
CC -!- INDUCTION: Inhibited by low concentrations of calcium.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58622.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH12494.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAD97125.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAG35973.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK300985; BAG62605.1; -; mRNA.
DR EMBL; AK313155; BAG35973.1; ALT_INIT; mRNA.
DR EMBL; AK223405; BAD97125.1; ALT_INIT; mRNA.
DR EMBL; AK300740; BAH13339.1; -; mRNA.
DR EMBL; AC073583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW98748.1; -; Genomic_DNA.
DR EMBL; BC012494; AAH12494.1; ALT_INIT; mRNA.
DR EMBL; DR156836; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M86934; AAA58622.1; ALT_INIT; mRNA.
DR RefSeq; NP_001129037.1; NM_001135565.1.
DR RefSeq; NP_001171606.1; NM_001178135.1.
DR RefSeq; NP_001171607.1; NM_001178136.1.
DR RefSeq; NP_036212.3; NM_012080.4.
DR UniGene; Hs.185910; -.
DR PDB; 3L5K; X-ray; 2.00 A; A=1-228.
DR PDBsum; 3L5K; -.
DR ProteinModelPortal; Q08623; -.
DR SMR; Q08623; 1-228.
DR MINT; MINT-5003687; -.
DR PhosphoSite; Q08623; -.
DR DMDM; 269849688; -.
DR PaxDb; Q08623; -.
DR PRIDE; Q08623; -.
DR DNASU; 8226; -.
DR Ensembl; ENST00000381077; ENSP00000370467; ENSG00000130021.
DR Ensembl; ENST00000412827; ENSP00000406260; ENSG00000130021.
DR Ensembl; ENST00000424830; ENSP00000396452; ENSG00000130021.
DR Ensembl; ENST00000540122; ENSP00000441208; ENSG00000130021.
DR GeneID; 8226; -.
DR KEGG; hsa:8226; -.
DR UCSC; uc011mhm.1; human.
DR CTD; 8226; -.
DR GeneCards; GC0XM006966; -.
DR HGNC; HGNC:16818; HDHD1.
DR MIM; 306480; gene.
DR neXtProt; NX_Q08623; -.
DR PharmGKB; PA165756731; -.
DR eggNOG; COG0637; -.
DR HOGENOM; HOG000248341; -.
DR HOVERGEN; HBG005917; -.
DR InParanoid; Q08623; -.
DR KO; K17623; -.
DR OMA; ERIYTEV; -.
DR OrthoDB; EOG7TF79X; -.
DR PhylomeDB; Q08623; -.
DR EvolutionaryTrace; Q08623; -.
DR GeneWiki; HDHD1A; -.
DR GenomeRNAi; 8226; -.
DR NextBio; 30966; -.
DR PRO; PR:Q08623; -.
DR ArrayExpress; Q08623; -.
DR Bgee; Q08623; -.
DR CleanEx; HS_HDHD1A; -.
DR Genevestigator; Q08623; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:GOC.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Hydrolase;
KW Magnesium; Metal-binding; Nucleotide metabolism; Polymorphism;
KW Reference proteome.
FT CHAIN 1 228 Pseudouridine-5'-monophosphatase.
FT /FTId=PRO_0000108068.
FT ACT_SITE 14 14 Nucleophile (By similarity).
FT ACT_SITE 16 16 Proton donor (By similarity).
FT METAL 14 14 Magnesium (By similarity).
FT METAL 16 16 Magnesium (By similarity).
FT VAR_SEQ 20 20 L -> LGYTGSIVAAASGESSRGLQSRWT (in isoform
FT 4).
FT /FTId=VSP_044804.
FT VAR_SEQ 51 93 Missing (in isoform 2).
FT /FTId=VSP_040029.
FT VAR_SEQ 171 228 CLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVL
FT NSLQDFQPELFGLPSYE -> SSIHRPRLLTAQKCQGCRDP
FT FSALLLLCNQLLLCSDDT (in isoform 3).
FT /FTId=VSP_042020.
FT VARIANT 88 88 T -> M (in dbSNP:rs1131197).
FT /FTId=VAR_061094.
FT VARIANT 165 165 P -> A (in dbSNP:rs3747386).
FT /FTId=VAR_060625.
FT CONFLICT 116 116 G -> R (in Ref. 5; AAH12494).
FT CONFLICT 153 153 D -> G (in Ref. 1; BAD97125).
FT CONFLICT 191 191 V -> A (in Ref. 6; AAA58622).
FT STRAND 1 3
FT STRAND 9 14
FT TURN 17 19
FT HELIX 22 36
FT HELIX 43 49
FT HELIX 54 65
FT HELIX 71 85
FT HELIX 86 88
FT HELIX 95 104
FT STRAND 109 112
FT HELIX 117 123
FT TURN 124 126
FT HELIX 128 131
FT HELIX 153 160
FT STRAND 162 164
FT HELIX 168 170
FT STRAND 171 177
FT HELIX 178 186
FT STRAND 190 193
FT HELIX 201 203
FT STRAND 207 210
FT HELIX 214 216
FT HELIX 219 222
SQ SEQUENCE 228 AA; 25249 MW; EF9B8CC51C122924 CRC64;
MAAPPQPVTH LIFDMDGLLL DTERLYSVVF QEICNRYDKK YSWDVKSLVM GKKALEAAQI
IIDVLQLPMS KEELVEESQT KLKEVFPTAA LMPGAEKLII HLRKHGIPFA LATSSGSASF
DMKTSRHKEF FSLFSHIVLG DDPEVQHGKP DPDIFLACAK RFSPPPAMEK CLVFEDAPNG
VEAALAAGMQ VVMVPDGNLS RDLTTKATLV LNSLQDFQPE LFGLPSYE
//
MIM
306480
*RECORD*
*FIELD* NO
306480
*FIELD* TI
*306480 HALOACID DEHALOGENASE-LIKE HYDROLASE DOMAIN-CONTAINING 1A; HDHD1A
;;DXF68S1E;;
read moreGS1 GENE
*FIELD* TX
CLONING
Yen et al. (1992) identified a new gene, designated GS1, by its
association with a CpG island approximately 100 kb telomeric to the
steroid sulfatase locus (STS; 300747) on the distal short arm of the X
chromosome. They isolated and characterized both cDNA and genomic
clones. The cDNA clone detected a 2.3-kb transcript in human placenta
and fibroblasts and appeared to encode a protein of 214 amino acid
residues. The GS1 gene was expressed from mouse-human cell hybrids
containing either active or inactive human X chromosomes, indicating
that it escapes X inactivation.
MAPPING
Although Yen et al. (1992) detected homologous sequences on chromosomes
1, 20, and Y, the functional GS1 gene was located on the X chromosome.
GENE STRUCTURE
The GS1 gene contains 4 exons spanning over 105 kb, with its
transcriptional direction opposite to that of the STS gene.
MOLECULAR GENETICS
Yen et al. (1992) stated that there are no obvious clinical differences
between STS-deficient patients with point mutations in the STS gene and
patients with a deletion of both the STS and the GS1 genes.
*FIELD* RF
1. Yen, P. H.; Ellison, J.; Salido, E. C.; Mohandas, T.; Shapiro,
L.: Isolation of a new gene from the distal short arm of the human
X chromosome that escapes X-inactivation. Hum. Molec. Genet. 1:
47-52, 1992.
*FIELD* CD
Victor A. McKusick: 5/28/1992
*FIELD* ED
carol: 02/03/2014
carol: 10/31/2008
alopez: 8/31/1998
carol: 5/28/1992
*RECORD*
*FIELD* NO
306480
*FIELD* TI
*306480 HALOACID DEHALOGENASE-LIKE HYDROLASE DOMAIN-CONTAINING 1A; HDHD1A
;;DXF68S1E;;
read moreGS1 GENE
*FIELD* TX
CLONING
Yen et al. (1992) identified a new gene, designated GS1, by its
association with a CpG island approximately 100 kb telomeric to the
steroid sulfatase locus (STS; 300747) on the distal short arm of the X
chromosome. They isolated and characterized both cDNA and genomic
clones. The cDNA clone detected a 2.3-kb transcript in human placenta
and fibroblasts and appeared to encode a protein of 214 amino acid
residues. The GS1 gene was expressed from mouse-human cell hybrids
containing either active or inactive human X chromosomes, indicating
that it escapes X inactivation.
MAPPING
Although Yen et al. (1992) detected homologous sequences on chromosomes
1, 20, and Y, the functional GS1 gene was located on the X chromosome.
GENE STRUCTURE
The GS1 gene contains 4 exons spanning over 105 kb, with its
transcriptional direction opposite to that of the STS gene.
MOLECULAR GENETICS
Yen et al. (1992) stated that there are no obvious clinical differences
between STS-deficient patients with point mutations in the STS gene and
patients with a deletion of both the STS and the GS1 genes.
*FIELD* RF
1. Yen, P. H.; Ellison, J.; Salido, E. C.; Mohandas, T.; Shapiro,
L.: Isolation of a new gene from the distal short arm of the human
X chromosome that escapes X-inactivation. Hum. Molec. Genet. 1:
47-52, 1992.
*FIELD* CD
Victor A. McKusick: 5/28/1992
*FIELD* ED
carol: 02/03/2014
carol: 10/31/2008
alopez: 8/31/1998
carol: 5/28/1992