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Q9D967

- MGDP1_MOUSE

UniProt

Q9D967 - MGDP1_MOUSE

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Protein

Magnesium-dependent phosphatase 1

Gene
Mdp1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Magnesium-dependent phosphatase which may act as a tyrosine phosphatase.3 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Cofactori

Magnesium.1 Publication

Enzyme regulationi

Inhibited by vanadate and zinc, and slightly by calcium.1 Publication

Kineticsi

Dephosphorylates ribose-5-phosphate, 2-deoxy-ribose-5-phosphate, phosphotyrosine, arabinose-5-phosphate, fructose-6-phosphate, 5'-CMP, pNPP, 5'-AMP and glucose-6-phosphate with a decreasing relative rate of 1, 0.9, 0.8, 0.6, 0.5, 0.2, 0.2, 0.2 and 0.06. Dephosphorylates phosphotyrosine with a greater than 100 fold rate over phosphoserine or phosphothreonine.

  1. KM=9.5 mM for ribose-5-phosphate1 Publication
  2. KM=5.6 mM for 2-deoxy-ribose-5-phosphate
  3. KM=15 mM for phosphotyrosine
  4. KM=1.1 mM for arabinose-5-phosphate
  5. KM=21 mM for fructose-6-phosphate
  6. KM=12 mM for 5'-CMP
  7. KM=1.7 mM for pNPP
  8. KM=26 mM for 5'-AMP
  9. KM=31 mM for glucose-6-phosphate

pH dependencei

Optimum pH is 5.3.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei11 – 111Nucleophile Inferred
Metal bindingi11 – 111Magnesium
Binding sitei12 – 121Phosphate; via amide nitrogen
Active sitei13 – 131Proton donor Inferred
Metal bindingi13 – 131Magnesium
Binding sitei13 – 131Phosphate; via amide nitrogen
Binding sitei20 – 201Substrate Inferred
Binding sitei69 – 691Phosphate
Binding sitei70 – 701Phosphate
Binding sitei70 – 701Substrate Inferred
Binding sitei100 – 1001Phosphate
Metal bindingi123 – 1231Magnesium

GO - Molecular functioni

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

GO - Biological processi

  1. fructosamine metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Magnesium-dependent phosphatase 1 (EC:3.1.3.-, EC:3.1.3.48)
Short name:
MDP-1
Gene namesi
Name:Mdp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:1915131. Mdp1.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111D → N or E: Abolishes enzymatic activity. 1 Publication
Mutagenesisi13 – 131D → N: 92% loss of enzymatic activity. 1 Publication
Mutagenesisi69 – 691S → A: Abolishes enzymatic activity. 1 Publication
Mutagenesisi100 – 1001K → R: Abolishes enzymatic activity. 1 Publication
Mutagenesisi103 – 1031H → K or A: 50% decrease in enzymatic activity. 1 Publication
Mutagenesisi122 – 1221D → N: Abolishes enzymatic activity.
Mutagenesisi123 – 1231D → N: Abolishes enzymatic activity.
Mutagenesisi127 – 1271N → D: 50% decrease in enzymatic activity.
Mutagenesisi138 – 1381C → S, A or G: No effect on enzymatic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 164164Magnesium-dependent phosphatase 1PRO_0000068828Add
BLAST

Proteomic databases

MaxQBiQ9D967.
PaxDbiQ9D967.
PRIDEiQ9D967.

PTM databases

PhosphoSiteiQ9D967.

Expressioni

Gene expression databases

BgeeiQ9D967.
CleanExiMM_1810034K20RIK.
GenevestigatoriQ9D967.

Interactioni

Protein-protein interaction databases

IntActiQ9D967. 1 interaction.
MINTiMINT-4127783.

Structurei

Secondary structure

1
164
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 105
Turni13 – 153
Beta strandi16 – 194
Turni21 – 233
Beta strandi29 – 313
Beta strandi37 – 393
Helixi51 – 6010
Beta strandi65 – 695
Helixi74 – 8310
Helixi87 – 893
Beta strandi90 – 989
Helixi100 – 11112
Helixi115 – 1173
Beta strandi118 – 1236
Helixi125 – 1328
Turni133 – 1353
Beta strandi137 – 1404
Beta strandi142 – 1443
Helixi147 – 16014
Turni161 – 1633

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U7OX-ray1.90A1-164[»]
1U7PX-ray1.90A/B/C/D1-164[»]
ProteinModelPortaliQ9D967.
SMRiQ9D967. Positions 1-164.

Miscellaneous databases

EvolutionaryTraceiQ9D967.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG279690.
GeneTreeiENSGT00390000004110.
HOGENOMiHOG000216653.
HOVERGENiHBG081971.
InParanoidiQ9D967.
KOiK17619.
OMAiHVQNGMS.
OrthoDBiEOG7PK913.
PhylomeDBiQ9D967.
TreeFamiTF328413.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR010033. HAD_SF_ppase_IIIC.
IPR024734. MDP_1_eu.
IPR010036. MDP_1_eu_arc.
[Graphical view]
PANTHERiPTHR17901. PTHR17901. 1 hit.
PfamiPF12689. Acid_PPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01681. HAD-SF-IIIC. 1 hit.
TIGR01685. MDP-1. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9D967-1 [UniParc]FASTAAdd to Basket

« Hide

MTRLPKLAVF DLDYTLWPFW VDTHVDPPFH KSSDGTVRDR RGQNIQLYPE    50
VPEVLGRLQS LGVPVAAASR TSEIQGANQL LELFDLGKYF IQREIYPGSK 100
VTHFERLHHK TGVPFSQMVF FDDENRNIID VGRLGVTCIH IRDGMSLQTL 150
TQGLETFAKA QAGL 164
Length:164
Mass (Da):18,582
Last modified:June 1, 2001 - v1
Checksum:i209D39404DCB1930
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF230273 mRNA. Translation: AAK00763.1.
AK007319 mRNA. Translation: BAB24954.1.
AK160438 mRNA. Translation: BAE35788.1.
BC046613 mRNA. Translation: AAH46613.1.
CCDSiCCDS27123.1.
RefSeqiNP_075886.1. NM_023397.4.
UniGeneiMm.24601.

Genome annotation databases

EnsembliENSMUST00000002400; ENSMUSP00000002400; ENSMUSG00000002329.
GeneIDi67881.
KEGGimmu:67881.
UCSCiuc007uaa.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF230273 mRNA. Translation: AAK00763.1 .
AK007319 mRNA. Translation: BAB24954.1 .
AK160438 mRNA. Translation: BAE35788.1 .
BC046613 mRNA. Translation: AAH46613.1 .
CCDSi CCDS27123.1.
RefSeqi NP_075886.1. NM_023397.4.
UniGenei Mm.24601.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1U7O X-ray 1.90 A 1-164 [» ]
1U7P X-ray 1.90 A/B/C/D 1-164 [» ]
ProteinModelPortali Q9D967.
SMRi Q9D967. Positions 1-164.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9D967. 1 interaction.
MINTi MINT-4127783.

PTM databases

PhosphoSitei Q9D967.

Proteomic databases

MaxQBi Q9D967.
PaxDbi Q9D967.
PRIDEi Q9D967.

Protocols and materials databases

DNASUi 67881.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000002400 ; ENSMUSP00000002400 ; ENSMUSG00000002329 .
GeneIDi 67881.
KEGGi mmu:67881.
UCSCi uc007uaa.2. mouse.

Organism-specific databases

CTDi 145553.
MGIi MGI:1915131. Mdp1.

Phylogenomic databases

eggNOGi NOG279690.
GeneTreei ENSGT00390000004110.
HOGENOMi HOG000216653.
HOVERGENi HBG081971.
InParanoidi Q9D967.
KOi K17619.
OMAi HVQNGMS.
OrthoDBi EOG7PK913.
PhylomeDBi Q9D967.
TreeFami TF328413.

Miscellaneous databases

ChiTaRSi MDP1. mouse.
EvolutionaryTracei Q9D967.
NextBioi 325825.
PROi Q9D967.
SOURCEi Search...

Gene expression databases

Bgeei Q9D967.
CleanExi MM_1810034K20RIK.
Genevestigatori Q9D967.

Family and domain databases

Gene3Di 3.40.50.1000. 1 hit.
InterProi IPR023214. HAD-like_dom.
IPR010033. HAD_SF_ppase_IIIC.
IPR024734. MDP_1_eu.
IPR010036. MDP_1_eu_arc.
[Graphical view ]
PANTHERi PTHR17901. PTHR17901. 1 hit.
Pfami PF12689. Acid_PPase. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 1 hit.
TIGRFAMsi TIGR01681. HAD-SF-IIIC. 1 hit.
TIGR01685. MDP-1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "MDP-1: a novel eukaryotic magnesium-dependent phosphatase."
    Selengut J.D., Levine R.L.
    Biochemistry 39:8315-8324(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ENZYME REGULATION, MUTAGENESIS OF HIS-103 AND CYS-138.
  2. "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: Pancreas.
  3. "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: Eye.
  4. "MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases."
    Selengut J.D.
    Biochemistry 40:12704-12711(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-11; ASP-13; SER-69 AND LYS-100, FUNCTION.
  5. "X-ray crystal structure of the hypothetical phosphotyrosine phosphatase MDP-1 of the haloacid dehalogenase superfamily."
    Peisach E., Selengut J.D., Dunaway-Mariano D., Allen K.N.
    Biochemistry 43:12770-12779(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-164, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-164 WITH MAGNESIUM AND TUNGSTATE, FUNCTION.

Entry informationi

Entry nameiMGDP1_MOUSE
AccessioniPrimary (citable) accession number: Q9D967
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 94 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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