Full text data of MDP1
MDP1
[Confidence: low (only semi-automatic identification from reviews)]
Magnesium-dependent phosphatase 1; MDP-1; 3.1.3.-; 3.1.3.48
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Magnesium-dependent phosphatase 1; MDP-1; 3.1.3.-; 3.1.3.48
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q86V88
ID MGDP1_HUMAN Reviewed; 176 AA.
AC Q86V88; Q86Y84; Q8NAD9;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2003, sequence version 1.
DT 22-JAN-2014, entry version 91.
DE RecName: Full=Magnesium-dependent phosphatase 1;
DE Short=MDP-1;
DE EC=3.1.3.-;
DE EC=3.1.3.48;
GN Name=MDP1;
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] (ISOFORM 2).
RC TISSUE=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] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Liver;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- FUNCTION: Magnesium-dependent phosphatase which may act as a
CC tyrosine phosphatase (By similarity).
CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- ENZYME REGULATION: Inhibited by vanadate and zinc, and slightly by
CC calcium (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86V88-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86V88-2; Sequence=VSP_015986, VSP_015987;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q86V88-3; Sequence=VSP_015985, VSP_015988;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC -----------------------------------------------------------------------
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DR EMBL; AK092821; BAC03984.1; -; mRNA.
DR EMBL; BC046912; AAH46912.1; -; mRNA.
DR EMBL; BC051382; AAH51382.1; -; mRNA.
DR RefSeq; NP_001186750.1; NM_001199821.1.
DR RefSeq; NP_612485.2; NM_138476.3.
DR UniGene; Hs.220963; -.
DR PDB; 2WM8; X-ray; 1.75 A; A=1-165.
DR PDBsum; 2WM8; -.
DR ProteinModelPortal; Q86V88; -.
DR SMR; Q86V88; 1-161.
DR MINT; MINT-1464579; -.
DR STRING; 9606.ENSP00000288087; -.
DR PhosphoSite; Q86V88; -.
DR DMDM; 74727544; -.
DR PaxDb; Q86V88; -.
DR PRIDE; Q86V88; -.
DR DNASU; 145553; -.
DR Ensembl; ENST00000288087; ENSP00000288087; ENSG00000213920.
DR Ensembl; ENST00000396833; ENSP00000380045; ENSG00000213920.
DR GeneID; 145553; -.
DR KEGG; hsa:145553; -.
DR UCSC; uc001wnl.2; human.
DR CTD; 145553; -.
DR GeneCards; GC14M024683; -.
DR HGNC; HGNC:28781; MDP1.
DR HPA; HPA003064; -.
DR neXtProt; NX_Q86V88; -.
DR PharmGKB; PA165479165; -.
DR eggNOG; NOG279690; -.
DR HOGENOM; HOG000216653; -.
DR HOVERGEN; HBG081971; -.
DR InParanoid; Q86V88; -.
DR KO; K17619; -.
DR OMA; HVQNGMS; -.
DR OrthoDB; EOG7PK913; -.
DR EvolutionaryTrace; Q86V88; -.
DR GenomeRNAi; 145553; -.
DR NextBio; 85134; -.
DR PRO; PR:Q86V88; -.
DR ArrayExpress; Q86V88; -.
DR Bgee; Q86V88; -.
DR Genevestigator; Q86V88; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR010033; HAD_SF_ppase_IIIC.
DR InterPro; IPR024734; MDP_1_eu.
DR InterPro; IPR010036; MDP_1_eu_arc.
DR PANTHER; PTHR17901; PTHR17901; 1.
DR Pfam; PF12689; Acid_PPase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01681; HAD-SF-IIIC; 1.
DR TIGRFAMs; TIGR01685; MDP-1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Hydrolase;
KW Magnesium; Metal-binding; Protein phosphatase; Reference proteome.
FT CHAIN 1 176 Magnesium-dependent phosphatase 1.
FT /FTId=PRO_0000068827.
FT ACT_SITE 11 11 Nucleophile (By similarity).
FT ACT_SITE 13 13 Proton donor (By similarity).
FT METAL 11 11 Magnesium (By similarity).
FT METAL 13 13 Magnesium (By similarity).
FT METAL 123 123 Magnesium (By similarity).
FT BINDING 12 12 Phosphate; via amide nitrogen (By
FT similarity).
FT BINDING 13 13 Phosphate; via amide nitrogen (By
FT similarity).
FT BINDING 20 20 Substrate (By similarity).
FT BINDING 69 69 Phosphate (By similarity).
FT BINDING 70 70 Phosphate (By similarity).
FT BINDING 70 70 Substrate (By similarity).
FT BINDING 100 100 Phosphate (By similarity).
FT VAR_SEQ 89 122 YFVHREIYPGSKITHFERLQQKTGIPFSQMIFFD -> CYL
FT HSHPEWNESSNSKSRVRDICEGPNWAFEVQP (in
FT isoform 3).
FT /FTId=VSP_015985.
FT VAR_SEQ 107 127 LQQKTGIPFSQMIFFDDERRN -> YAEIREEQGEKVSERP
FT GKPRY (in isoform 2).
FT /FTId=VSP_015986.
FT VAR_SEQ 123 176 Missing (in isoform 3).
FT /FTId=VSP_015988.
FT VAR_SEQ 128 176 Missing (in isoform 2).
FT /FTId=VSP_015987.
FT STRAND 6 10
FT TURN 13 15
FT STRAND 16 19
FT TURN 21 23
FT HELIX 51 61
FT STRAND 65 69
FT HELIX 74 83
FT TURN 87 89
FT STRAND 90 98
FT HELIX 100 111
FT HELIX 115 117
FT STRAND 118 123
FT HELIX 125 132
FT TURN 133 135
FT STRAND 137 140
FT STRAND 142 144
FT HELIX 147 159
SQ SEQUENCE 176 AA; 20109 MW; B0A33BD02458B2EF CRC64;
MARLPKLAVF DLDYTLWPFW VDTHVDPPFH KSSDGTVRDR RGQDVRLYPE VPEVLKRLQS
LGVPGAAASR TSEIEGANQL LELFDLFRYF VHREIYPGSK ITHFERLQQK TGIPFSQMIF
FDDERRNIVD VSKLGVTCIH IQNGMNLQTL SQGLETFAKA QTGPLRSSLE ESPFEA
//
ID MGDP1_HUMAN Reviewed; 176 AA.
AC Q86V88; Q86Y84; Q8NAD9;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2003, sequence version 1.
DT 22-JAN-2014, entry version 91.
DE RecName: Full=Magnesium-dependent phosphatase 1;
DE Short=MDP-1;
DE EC=3.1.3.-;
DE EC=3.1.3.48;
GN Name=MDP1;
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] (ISOFORM 2).
RC TISSUE=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] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Liver;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- FUNCTION: Magnesium-dependent phosphatase which may act as a
CC tyrosine phosphatase (By similarity).
CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- ENZYME REGULATION: Inhibited by vanadate and zinc, and slightly by
CC calcium (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86V88-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86V88-2; Sequence=VSP_015986, VSP_015987;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q86V88-3; Sequence=VSP_015985, VSP_015988;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
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; AK092821; BAC03984.1; -; mRNA.
DR EMBL; BC046912; AAH46912.1; -; mRNA.
DR EMBL; BC051382; AAH51382.1; -; mRNA.
DR RefSeq; NP_001186750.1; NM_001199821.1.
DR RefSeq; NP_612485.2; NM_138476.3.
DR UniGene; Hs.220963; -.
DR PDB; 2WM8; X-ray; 1.75 A; A=1-165.
DR PDBsum; 2WM8; -.
DR ProteinModelPortal; Q86V88; -.
DR SMR; Q86V88; 1-161.
DR MINT; MINT-1464579; -.
DR STRING; 9606.ENSP00000288087; -.
DR PhosphoSite; Q86V88; -.
DR DMDM; 74727544; -.
DR PaxDb; Q86V88; -.
DR PRIDE; Q86V88; -.
DR DNASU; 145553; -.
DR Ensembl; ENST00000288087; ENSP00000288087; ENSG00000213920.
DR Ensembl; ENST00000396833; ENSP00000380045; ENSG00000213920.
DR GeneID; 145553; -.
DR KEGG; hsa:145553; -.
DR UCSC; uc001wnl.2; human.
DR CTD; 145553; -.
DR GeneCards; GC14M024683; -.
DR HGNC; HGNC:28781; MDP1.
DR HPA; HPA003064; -.
DR neXtProt; NX_Q86V88; -.
DR PharmGKB; PA165479165; -.
DR eggNOG; NOG279690; -.
DR HOGENOM; HOG000216653; -.
DR HOVERGEN; HBG081971; -.
DR InParanoid; Q86V88; -.
DR KO; K17619; -.
DR OMA; HVQNGMS; -.
DR OrthoDB; EOG7PK913; -.
DR EvolutionaryTrace; Q86V88; -.
DR GenomeRNAi; 145553; -.
DR NextBio; 85134; -.
DR PRO; PR:Q86V88; -.
DR ArrayExpress; Q86V88; -.
DR Bgee; Q86V88; -.
DR Genevestigator; Q86V88; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR010033; HAD_SF_ppase_IIIC.
DR InterPro; IPR024734; MDP_1_eu.
DR InterPro; IPR010036; MDP_1_eu_arc.
DR PANTHER; PTHR17901; PTHR17901; 1.
DR Pfam; PF12689; Acid_PPase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01681; HAD-SF-IIIC; 1.
DR TIGRFAMs; TIGR01685; MDP-1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Hydrolase;
KW Magnesium; Metal-binding; Protein phosphatase; Reference proteome.
FT CHAIN 1 176 Magnesium-dependent phosphatase 1.
FT /FTId=PRO_0000068827.
FT ACT_SITE 11 11 Nucleophile (By similarity).
FT ACT_SITE 13 13 Proton donor (By similarity).
FT METAL 11 11 Magnesium (By similarity).
FT METAL 13 13 Magnesium (By similarity).
FT METAL 123 123 Magnesium (By similarity).
FT BINDING 12 12 Phosphate; via amide nitrogen (By
FT similarity).
FT BINDING 13 13 Phosphate; via amide nitrogen (By
FT similarity).
FT BINDING 20 20 Substrate (By similarity).
FT BINDING 69 69 Phosphate (By similarity).
FT BINDING 70 70 Phosphate (By similarity).
FT BINDING 70 70 Substrate (By similarity).
FT BINDING 100 100 Phosphate (By similarity).
FT VAR_SEQ 89 122 YFVHREIYPGSKITHFERLQQKTGIPFSQMIFFD -> CYL
FT HSHPEWNESSNSKSRVRDICEGPNWAFEVQP (in
FT isoform 3).
FT /FTId=VSP_015985.
FT VAR_SEQ 107 127 LQQKTGIPFSQMIFFDDERRN -> YAEIREEQGEKVSERP
FT GKPRY (in isoform 2).
FT /FTId=VSP_015986.
FT VAR_SEQ 123 176 Missing (in isoform 3).
FT /FTId=VSP_015988.
FT VAR_SEQ 128 176 Missing (in isoform 2).
FT /FTId=VSP_015987.
FT STRAND 6 10
FT TURN 13 15
FT STRAND 16 19
FT TURN 21 23
FT HELIX 51 61
FT STRAND 65 69
FT HELIX 74 83
FT TURN 87 89
FT STRAND 90 98
FT HELIX 100 111
FT HELIX 115 117
FT STRAND 118 123
FT HELIX 125 132
FT TURN 133 135
FT STRAND 137 140
FT STRAND 142 144
FT HELIX 147 159
SQ SEQUENCE 176 AA; 20109 MW; B0A33BD02458B2EF CRC64;
MARLPKLAVF DLDYTLWPFW VDTHVDPPFH KSSDGTVRDR RGQDVRLYPE VPEVLKRLQS
LGVPGAAASR TSEIEGANQL LELFDLFRYF VHREIYPGSK ITHFERLQQK TGIPFSQMIF
FDDERRNIVD VSKLGVTCIH IQNGMNLQTL SQGLETFAKA QTGPLRSSLE ESPFEA
//