Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9D5U5 (HDHD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pseudouridine-5'-monophosphatase

Short name=5'-PsiMPase
EC=3.1.3.n6
Alternative name(s):
Haloacid dehalogenase-like hydrolase domain-containing protein 1
Haloacid dehalogenase-like hydrolase domain-containing protein 1A
Gene names
Name:Hdhd1
Synonyms:Hdhd1a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length234 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

pseudouridine 5'-monophosphate + H2O = Pseudouridine + phosphate.

Cofactor

Magnesium By similarity.

Sequence similarities

Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family.

Ontologies

Keywords
   Biological processNucleotide metabolism
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnucleotide metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 234234Pseudouridine-5'-monophosphatase
PRO_0000320103

Sites

Active site191Nucleophile By similarity
Active site211Proton donor By similarity
Metal binding191Magnesium By similarity
Metal binding211Magnesium By similarity

Experimental info

Sequence conflict2 – 43AAA → GGG in BAB24906. Ref.1
Sequence conflict151P → H in BAB24906. Ref.1
Sequence conflict151P → H in AAH48447. Ref.2
Sequence conflict20 – 234LDGL → REGF in BAB24906. Ref.1
Sequence conflict2141L → Q in BAB24906. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9D5U5 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 246AFF9DCF2ED9FF

FASTA23426,161
        10         20         30         40         50         60 
MAAAVPVPQF RPVTPLIFDL DGLILNTEDL YTDVFEEICN RYGKKYNWDV KSLVMGKKAL 

        70         80         90        100        110        120 
ETAQTIVEFL NLPISKEELL KESQEKLQMV LHTAGFMPGA EELIHHLKKH RLPFALATSS 

       130        140        150        160        170        180 
ETVTFQTKTS RHTGFFGLFH HIVLGDDPEV KNGKPGMDIF LTCAKRFSPP PDPKDCLVFE 

       190        200        210        220        230 
DSPNGVEAAI HCGMQVVMVP HENLSADLTR KATLVLSSLH DFKPELFGLP AFTE 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Testis.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK007231 mRNA. Translation: BAB24906.1.
AK014922 mRNA. Translation: BAB29622.1.
BC048447 mRNA. Translation: AAH48447.1.
CCDSCCDS29244.1.
RefSeqNP_080384.2. NM_026108.3.
UniGeneMm.158150.

3D structure databases

ProteinModelPortalQ9D5U5.
SMRQ9D5U5. Positions 11-232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000057378.

PTM databases

PhosphoSiteQ9D5U5.

Proteomic databases

PaxDbQ9D5U5.
PRIDEQ9D5U5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000056460; ENSMUSP00000057378; ENSMUSG00000048875.
GeneID67365.
KEGGmmu:67365.
UCSCuc008ewy.2. mouse.

Organism-specific databases

CTD67365.
MGIMGI:1914615. Hdhd1a.

Phylogenomic databases

eggNOGCOG0637.
GeneTreeENSGT00390000014753.
HOGENOMHOG000248341.
HOVERGENHBG005917.
InParanoidQ9D9A0.
KOK17623.
OrthoDBEOG7TF79X.
PhylomeDBQ9D5U5.
TreeFamTF105946.

Gene expression databases

BgeeQ9D5U5.
GenevestigatorQ9D5U5.

Family and domain databases

Gene3D3.40.50.1000. 2 hits.
InterProIPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
[Graphical view]
PfamPF13419. HAD_2. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR01509. HAD-SF-IA-v3. 1 hit.
ProtoNetSearch...

Other

NextBio324356.
SOURCESearch...

Entry information

Entry nameHDHD1_MOUSE
AccessionPrimary (citable) accession number: Q9D5U5
Secondary accession number(s): Q5RL33, Q9D9A0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot