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Q9D114 (MESH1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. 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:
Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1

EC=3.1.7.2
Alternative name(s):
HD domain-containing protein 3
Metazoan SpoT homolog 1
Short name=MESH1
Penta-phosphate guanosine-3'-pyrophosphohydrolase
Short name=(ppGpp)ase
Gene names
Name:Hddc3
Synonyms:Mesh1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length179 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

ppGpp hydrolyzing enzyme involved in starvation response By similarity.

Catalytic activity

Guanosine 3',5'-bis(diphosphate) + H2O = guanosine 5'-diphosphate + diphosphate.

Cofactor

Manganese By similarity.

Sequence similarities

Belongs to the MESH1 family.

Contains 1 HD domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 179178Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1
PRO_0000263111

Regions

Domain32 – 12796HD

Sites

Active site651Nucleophile By similarity
Active site661Nucleophile By similarity
Metal binding351Manganese By similarity
Metal binding611Manganese By similarity
Metal binding621Manganese By similarity
Metal binding1221Manganese By similarity

Amino acid modifications

Modified residue21N-acetylglycine By similarity
Modified residue251N6-acetyllysine By similarity
Modified residue971N6-acetyllysine By similarity
Modified residue1231N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9D114 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: D52FF1DA540A6ED3

FASTA17920,262
        10         20         30         40         50         60 
MGSEAAQLLE AADFAAHKHR QQRRKDPEGT PYINHPIGVA RILTHEAGIT DIVVLQAALL 

        70         80         90        100        110        120 
HDTVEDTDTT LDEVELHFGA QVRRLVEEVT DDKTLPKLER KRQQVEQAPH SSPGAKLVKL 

       130        140        150        160        170 
ADKLYNLRDL NRCTPTGWSE HRVQEYFEWA AQVVKGLQGT NQQLEEALKQ LFEERGLTL 

« 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: Embryo.
[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].
Strain: Czech II.
Tissue: Lung.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK004078 mRNA. Translation: BAB23158.1.
BC038310 mRNA. Translation: AAH38310.1.
RefSeqNP_081088.1. NM_026812.2.
UniGeneMm.21171.

3D structure databases

ProteinModelPortalQ9D114.
SMRQ9D114. Positions 2-179.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9D114. 1 interaction.
MINTMINT-4126505.

PTM databases

PhosphoSiteQ9D114.

Proteomic databases

PaxDbQ9D114.
PRIDEQ9D114.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032747; ENSMUSP00000032747; ENSMUSG00000030532.
GeneID68695.
KEGGmmu:68695.
UCSCuc009ian.1. mouse.

Organism-specific databases

CTD374659.
MGIMGI:1915945. Hddc3.

Phylogenomic databases

eggNOGNOG113345.
GeneTreeENSGT00390000011608.
HOVERGENHBG081594.
InParanoidQ9D114.
KOK01139.
OMANRCTPEG.
OrthoDBEOG7X3QTC.
TreeFamTF313524.

Gene expression databases

BgeeQ9D114.
CleanExMM_HDDC3.
GenevestigatorQ9D114.

Family and domain databases

InterProIPR003607. HD/PDEase_dom.
[Graphical view]
SMARTSM00471. HDc. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio327714.
PROQ9D114.
SOURCESearch...

Entry information

Entry nameMESH1_MOUSE
AccessionPrimary (citable) accession number: Q9D114
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: June 1, 2001
Last modified: February 19, 2014
This is version 86 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