Skip Header

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

Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1

Gene

Hddc3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

ppGpp hydrolyzing enzyme involved in starvation response.By similarity

Catalytic activityi

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

Cofactori

Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi35 – 351ManganeseBy similarity
Metal bindingi61 – 611ManganeseBy similarity
Metal bindingi62 – 621ManganeseBy similarity
Active sitei65 – 651NucleophileBy similarity
Active sitei66 – 661NucleophileBy similarity
Metal bindingi122 – 1221ManganeseBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Hddc3
Synonyms:Mesh1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1915945. Hddc3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 179178Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1PRO_0000263111Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycineBy similarity
Modified residuei25 – 251N6-acetyllysineBy similarity
Modified residuei97 – 971N6-acetyllysineBy similarity
Modified residuei123 – 1231N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9D114.
PaxDbiQ9D114.
PRIDEiQ9D114.

PTM databases

PhosphoSiteiQ9D114.

Expressioni

Gene expression databases

BgeeiQ9D114.
CleanExiMM_HDDC3.
GenevisibleiQ9D114. MM.

Interactioni

Protein-protein interaction databases

IntActiQ9D114. 1 interaction.
MINTiMINT-4126505.
STRINGi10090.ENSMUSP00000032747.

Structurei

3D structure databases

ProteinModelPortaliQ9D114.
SMRiQ9D114. Positions 2-179.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 12796HDAdd
BLAST

Sequence similaritiesi

Belongs to the MESH1 family.Curated
Contains 1 HD domain.Curated

Phylogenomic databases

eggNOGiNOG113345.
GeneTreeiENSGT00390000011608.
HOVERGENiHBG081594.
InParanoidiQ9D114.
KOiK01139.
OMAiRCTPEGW.
OrthoDBiEOG7X3QTC.
PhylomeDBiQ9D114.
TreeFamiTF313524.

Family and domain databases

InterProiIPR003607. HD/PDEase_dom.
[Graphical view]
SMARTiSM00471. HDc. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D114-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSEAAQLLE AADFAAHKHR QQRRKDPEGT PYINHPIGVA RILTHEAGIT
60 70 80 90 100
DIVVLQAALL HDTVEDTDTT LDEVELHFGA QVRRLVEEVT DDKTLPKLER
110 120 130 140 150
KRQQVEQAPH SSPGAKLVKL ADKLYNLRDL NRCTPTGWSE HRVQEYFEWA
160 170
AQVVKGLQGT NQQLEEALKQ LFEERGLTL
Length:179
Mass (Da):20,262
Last modified:June 1, 2001 - v1
Checksum:iD52FF1DA540A6ED3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004078 mRNA. Translation: BAB23158.1.
BC038310 mRNA. Translation: AAH38310.1.
CCDSiCCDS21396.1.
RefSeqiNP_081088.1. NM_026812.2.
UniGeneiMm.21171.

Genome annotation databases

EnsembliENSMUST00000032747; ENSMUSP00000032747; ENSMUSG00000030532.
GeneIDi68695.
KEGGimmu:68695.
UCSCiuc009ian.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004078 mRNA. Translation: BAB23158.1.
BC038310 mRNA. Translation: AAH38310.1.
CCDSiCCDS21396.1.
RefSeqiNP_081088.1. NM_026812.2.
UniGeneiMm.21171.

3D structure databases

ProteinModelPortaliQ9D114.
SMRiQ9D114. Positions 2-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D114. 1 interaction.
MINTiMINT-4126505.
STRINGi10090.ENSMUSP00000032747.

PTM databases

PhosphoSiteiQ9D114.

Proteomic databases

MaxQBiQ9D114.
PaxDbiQ9D114.
PRIDEiQ9D114.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032747; ENSMUSP00000032747; ENSMUSG00000030532.
GeneIDi68695.
KEGGimmu:68695.
UCSCiuc009ian.1. mouse.

Organism-specific databases

CTDi374659.
MGIiMGI:1915945. Hddc3.

Phylogenomic databases

eggNOGiNOG113345.
GeneTreeiENSGT00390000011608.
HOVERGENiHBG081594.
InParanoidiQ9D114.
KOiK01139.
OMAiRCTPEGW.
OrthoDBiEOG7X3QTC.
PhylomeDBiQ9D114.
TreeFamiTF313524.

Miscellaneous databases

NextBioi327714.
PROiQ9D114.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D114.
CleanExiMM_HDDC3.
GenevisibleiQ9D114. MM.

Family and domain databases

InterProiIPR003607. HD/PDEase_dom.
[Graphical view]
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiMESH1_MOUSE
AccessioniPrimary (citable) accession number: Q9D114
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: June 1, 2001
Last modified: July 22, 2015
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.