Full text data of MTMR12
MTMR12
(KIAA1682, PIP3AP)
[Confidence: low (only semi-automatic identification from reviews)]
Myotubularin-related protein 12 (Phosphatidylinositol 3 phosphate 3-phosphatase adapter subunit; 3-PAP; 3-phosphatase adapter protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Myotubularin-related protein 12 (Phosphatidylinositol 3 phosphate 3-phosphatase adapter subunit; 3-PAP; 3-phosphatase adapter protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9C0I1
ID MTMRC_HUMAN Reviewed; 747 AA.
AC Q9C0I1; Q69YJ4; Q6PFW3; Q96QU2; Q9NX27;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-JAN-2008, sequence version 2.
DT 22-JAN-2014, entry version 71.
DE RecName: Full=Myotubularin-related protein 12;
DE AltName: Full=Phosphatidylinositol 3 phosphate 3-phosphatase adapter subunit;
DE Short=3-PAP;
DE Short=3-phosphatase adapter protein;
GN Name=MTMR12; Synonyms=KIAA1682, PIP3AP;
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 [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11504939; DOI=10.1073/pnas.171306098;
RA Nandurkar H.H., Caldwell K.K., Whisstock J.C., Layton M.J.,
RA Gaudet E.A., Norris F.A., Majerus P.W., Mitchell C.A.;
RT "Characterization of an adapter subunit to a phosphatidylinositol (3)P
RT 3-phosphatase: identification of a myotubularin-related protein
RT lacking catalytic activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9499-9504(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 354-747 (ISOFORM 1).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, INTERACTION WITH MTM1 AND MTMR2, SUBCELLULAR LOCATION, AND
RP REGION.
RX PubMed=12847286; DOI=10.1073/pnas.1033097100;
RA Nandurkar H.H., Layton M., Laporte J., Selan C., Corcoran L.,
RA Caldwell K.K., Mochizuki Y., Majerus P.W., Mitchell C.A.;
RT "Identification of myotubularin as the lipid phosphatase catalytic
RT subunit associated with the 3-phosphatase adapter protein, 3-PAP.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8660-8665(2003).
CC -!- FUNCTION: Catalytically inactive phosphatase that plays a role as
CC an adapter for the phosphatase myotubularin to regulate
CC myotubularin intracellular location.
CC -!- SUBUNIT: Interacts with myotubularin MTM1 and myotubularin-related
CC MTMR2.
CC -!- INTERACTION:
CC Q13496:MTM1; NbExp=4; IntAct=EBI-2829520, EBI-2864109;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localizes to punctate
CC vesicles when associated with MTM1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9C0I1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0I1-2; Sequence=VSP_030722;
CC Name=3;
CC IsoId=Q9C0I1-3; Sequence=VSP_030721;
CC -!- TISSUE SPECIFICITY: Ubiquitous with prominent expression in brain,
CC heart, kidney, placenta, and lung.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Non-receptor class myotubularin subfamily.
CC -!- SIMILARITY: Contains 1 myotubularin phosphatase domain.
CC -!- CAUTION: Lacks the phosphocysteine intermediate Cys active site in
CC position 391 that is replaced by a Glu residue, preventing the
CC hydrolase activity.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21773.1; Type=Erroneous initiation;
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; AY028703; AAK26171.1; -; mRNA.
DR EMBL; AB051469; BAB21773.1; ALT_INIT; mRNA.
DR EMBL; AK000483; BAA91195.1; -; mRNA.
DR EMBL; BC057393; AAH57393.1; -; mRNA.
DR EMBL; AL833231; CAH10604.1; -; mRNA.
DR RefSeq; NP_001035536.1; NM_001040446.1.
DR RefSeq; XP_005248372.1; XM_005248315.1.
DR RefSeq; XP_005248373.1; XM_005248316.1.
DR UniGene; Hs.481836; -.
DR ProteinModelPortal; Q9C0I1; -.
DR SMR; Q9C0I1; 143-541.
DR IntAct; Q9C0I1; 4.
DR MINT; MINT-8216953; -.
DR STRING; 9606.ENSP00000371577; -.
DR PhosphoSite; Q9C0I1; -.
DR DMDM; 166199459; -.
DR PaxDb; Q9C0I1; -.
DR PRIDE; Q9C0I1; -.
DR Ensembl; ENST00000264934; ENSP00000264934; ENSG00000150712.
DR Ensembl; ENST00000280285; ENSP00000280285; ENSG00000150712.
DR Ensembl; ENST00000382142; ENSP00000371577; ENSG00000150712.
DR GeneID; 54545; -.
DR KEGG; hsa:54545; -.
DR UCSC; uc003jhq.3; human.
DR CTD; 54545; -.
DR GeneCards; GC05M032227; -.
DR H-InvDB; HIX0004786; -.
DR HGNC; HGNC:18191; MTMR12.
DR HPA; HPA051333; -.
DR MIM; 606501; gene.
DR neXtProt; NX_Q9C0I1; -.
DR PharmGKB; PA128394670; -.
DR eggNOG; NOG322133; -.
DR HOGENOM; HOG000113684; -.
DR HOVERGEN; HBG108154; -.
DR InParanoid; Q9C0I1; -.
DR OMA; PTSGWKA; -.
DR OrthoDB; EOG7K0ZBZ; -.
DR GenomeRNAi; 54545; -.
DR NextBio; 56999; -.
DR PRO; PR:Q9C0I1; -.
DR ArrayExpress; Q9C0I1; -.
DR Bgee; Q9C0I1; -.
DR CleanEx; HS_MTMR12; -.
DR Genevestigator; Q9C0I1; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR022587; Myotubularin_assoc.
DR InterPro; IPR017906; Myotubularin_phosphatase_dom.
DR InterPro; IPR011993; PH_like_dom.
DR Pfam; PF12578; 3-PAP; 1.
DR Pfam; PF06602; Myotub-related; 2.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; FALSE_NEG.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Reference proteome.
FT CHAIN 1 747 Myotubularin-related protein 12.
FT /FTId=PRO_0000315825.
FT DOMAIN 205 643 Myotubularin phosphatase.
FT REGION 449 558 Interaction with MTM1.
FT VAR_SEQ 449 558 Missing (in isoform 3).
FT /FTId=VSP_030721.
FT VAR_SEQ 505 558 Missing (in isoform 2).
FT /FTId=VSP_030722.
FT CONFLICT 197 197 D -> V (in Ref. 3; BAA91195).
FT CONFLICT 591 591 L -> M (in Ref. 1; AAK26171).
SQ SEQUENCE 747 AA; 86148 MW; 1D11A678CC92F70B CRC64;
MLGKGVVGGG GGTKAPKPSF VSYVRPEEIH TNEKEVTEKE VTLHLLPGEQ LLCEASTVLK
YVQEDSCQHG VYGRLVCTDF KIAFLGDDES ALDNDETQFK NKVIGENDIT LHCVDQIYGV
FDEKKKTLFG QLKKYPEKLI IHCKDLRVFQ FCLRYTKEEE VKRIVSGIIH HTQAPKLLKR
LFLFSYATAA QNNTVTDPKN HTVMFDTLKD WCWELERTKG NMKYKAVSVN EGYKVCERLP
AYFVVPTPLP EENVQRFQGH GIPIWCWSCH NGSALLKMSA LPKEQDDGIL QIQKSFLDGI
YKTIHRPPYE IVKTEDLSSN FLSLQEIQTA YSKFKQLFLI DNSTEFWDTD IKWFSLLESS
SWLDIIRRCL KKAIEITECM EAQNMNVLLL EENASDLCCL ISSLVQLMMD PHCRTRIGFQ
SLIQKEWVMG GHCFLDRCNH LRQNDKEEVP VFLLFLDCVW QLVHQHPPAF EFTETYLTVL
SDSLYIPIFS TFFFNSPHQK DTNMGREGQD TQSKPLNLLT VWDWSVQFEP KAQTLLKNPL
YVEKPKLDKG QRKGMRFKHQ RQLSLPLTQS KSSPKRGFFR EETDHLIKNL LGKRISKLIN
SSDELQDNFR EFYDSWHSKS TDYHGLLLPH IEGPEIKVWA QRYLRWIPEA QILGGGQVAT
LSKLLEMMEE VQSLQEKIDE RHHSQQAPQA EAPCLLRNSA RLSSLFPFAL LQRHSSKPVL
PTSGWKALGD EDDLAKREDE FVDLGDV
//
ID MTMRC_HUMAN Reviewed; 747 AA.
AC Q9C0I1; Q69YJ4; Q6PFW3; Q96QU2; Q9NX27;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-JAN-2008, sequence version 2.
DT 22-JAN-2014, entry version 71.
DE RecName: Full=Myotubularin-related protein 12;
DE AltName: Full=Phosphatidylinositol 3 phosphate 3-phosphatase adapter subunit;
DE Short=3-PAP;
DE Short=3-phosphatase adapter protein;
GN Name=MTMR12; Synonyms=KIAA1682, PIP3AP;
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 [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11504939; DOI=10.1073/pnas.171306098;
RA Nandurkar H.H., Caldwell K.K., Whisstock J.C., Layton M.J.,
RA Gaudet E.A., Norris F.A., Majerus P.W., Mitchell C.A.;
RT "Characterization of an adapter subunit to a phosphatidylinositol (3)P
RT 3-phosphatase: identification of a myotubularin-related protein
RT lacking catalytic activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9499-9504(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 354-747 (ISOFORM 1).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, INTERACTION WITH MTM1 AND MTMR2, SUBCELLULAR LOCATION, AND
RP REGION.
RX PubMed=12847286; DOI=10.1073/pnas.1033097100;
RA Nandurkar H.H., Layton M., Laporte J., Selan C., Corcoran L.,
RA Caldwell K.K., Mochizuki Y., Majerus P.W., Mitchell C.A.;
RT "Identification of myotubularin as the lipid phosphatase catalytic
RT subunit associated with the 3-phosphatase adapter protein, 3-PAP.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8660-8665(2003).
CC -!- FUNCTION: Catalytically inactive phosphatase that plays a role as
CC an adapter for the phosphatase myotubularin to regulate
CC myotubularin intracellular location.
CC -!- SUBUNIT: Interacts with myotubularin MTM1 and myotubularin-related
CC MTMR2.
CC -!- INTERACTION:
CC Q13496:MTM1; NbExp=4; IntAct=EBI-2829520, EBI-2864109;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localizes to punctate
CC vesicles when associated with MTM1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9C0I1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0I1-2; Sequence=VSP_030722;
CC Name=3;
CC IsoId=Q9C0I1-3; Sequence=VSP_030721;
CC -!- TISSUE SPECIFICITY: Ubiquitous with prominent expression in brain,
CC heart, kidney, placenta, and lung.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Non-receptor class myotubularin subfamily.
CC -!- SIMILARITY: Contains 1 myotubularin phosphatase domain.
CC -!- CAUTION: Lacks the phosphocysteine intermediate Cys active site in
CC position 391 that is replaced by a Glu residue, preventing the
CC hydrolase activity.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21773.1; Type=Erroneous initiation;
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; AY028703; AAK26171.1; -; mRNA.
DR EMBL; AB051469; BAB21773.1; ALT_INIT; mRNA.
DR EMBL; AK000483; BAA91195.1; -; mRNA.
DR EMBL; BC057393; AAH57393.1; -; mRNA.
DR EMBL; AL833231; CAH10604.1; -; mRNA.
DR RefSeq; NP_001035536.1; NM_001040446.1.
DR RefSeq; XP_005248372.1; XM_005248315.1.
DR RefSeq; XP_005248373.1; XM_005248316.1.
DR UniGene; Hs.481836; -.
DR ProteinModelPortal; Q9C0I1; -.
DR SMR; Q9C0I1; 143-541.
DR IntAct; Q9C0I1; 4.
DR MINT; MINT-8216953; -.
DR STRING; 9606.ENSP00000371577; -.
DR PhosphoSite; Q9C0I1; -.
DR DMDM; 166199459; -.
DR PaxDb; Q9C0I1; -.
DR PRIDE; Q9C0I1; -.
DR Ensembl; ENST00000264934; ENSP00000264934; ENSG00000150712.
DR Ensembl; ENST00000280285; ENSP00000280285; ENSG00000150712.
DR Ensembl; ENST00000382142; ENSP00000371577; ENSG00000150712.
DR GeneID; 54545; -.
DR KEGG; hsa:54545; -.
DR UCSC; uc003jhq.3; human.
DR CTD; 54545; -.
DR GeneCards; GC05M032227; -.
DR H-InvDB; HIX0004786; -.
DR HGNC; HGNC:18191; MTMR12.
DR HPA; HPA051333; -.
DR MIM; 606501; gene.
DR neXtProt; NX_Q9C0I1; -.
DR PharmGKB; PA128394670; -.
DR eggNOG; NOG322133; -.
DR HOGENOM; HOG000113684; -.
DR HOVERGEN; HBG108154; -.
DR InParanoid; Q9C0I1; -.
DR OMA; PTSGWKA; -.
DR OrthoDB; EOG7K0ZBZ; -.
DR GenomeRNAi; 54545; -.
DR NextBio; 56999; -.
DR PRO; PR:Q9C0I1; -.
DR ArrayExpress; Q9C0I1; -.
DR Bgee; Q9C0I1; -.
DR CleanEx; HS_MTMR12; -.
DR Genevestigator; Q9C0I1; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR022587; Myotubularin_assoc.
DR InterPro; IPR017906; Myotubularin_phosphatase_dom.
DR InterPro; IPR011993; PH_like_dom.
DR Pfam; PF12578; 3-PAP; 1.
DR Pfam; PF06602; Myotub-related; 2.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; FALSE_NEG.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Reference proteome.
FT CHAIN 1 747 Myotubularin-related protein 12.
FT /FTId=PRO_0000315825.
FT DOMAIN 205 643 Myotubularin phosphatase.
FT REGION 449 558 Interaction with MTM1.
FT VAR_SEQ 449 558 Missing (in isoform 3).
FT /FTId=VSP_030721.
FT VAR_SEQ 505 558 Missing (in isoform 2).
FT /FTId=VSP_030722.
FT CONFLICT 197 197 D -> V (in Ref. 3; BAA91195).
FT CONFLICT 591 591 L -> M (in Ref. 1; AAK26171).
SQ SEQUENCE 747 AA; 86148 MW; 1D11A678CC92F70B CRC64;
MLGKGVVGGG GGTKAPKPSF VSYVRPEEIH TNEKEVTEKE VTLHLLPGEQ LLCEASTVLK
YVQEDSCQHG VYGRLVCTDF KIAFLGDDES ALDNDETQFK NKVIGENDIT LHCVDQIYGV
FDEKKKTLFG QLKKYPEKLI IHCKDLRVFQ FCLRYTKEEE VKRIVSGIIH HTQAPKLLKR
LFLFSYATAA QNNTVTDPKN HTVMFDTLKD WCWELERTKG NMKYKAVSVN EGYKVCERLP
AYFVVPTPLP EENVQRFQGH GIPIWCWSCH NGSALLKMSA LPKEQDDGIL QIQKSFLDGI
YKTIHRPPYE IVKTEDLSSN FLSLQEIQTA YSKFKQLFLI DNSTEFWDTD IKWFSLLESS
SWLDIIRRCL KKAIEITECM EAQNMNVLLL EENASDLCCL ISSLVQLMMD PHCRTRIGFQ
SLIQKEWVMG GHCFLDRCNH LRQNDKEEVP VFLLFLDCVW QLVHQHPPAF EFTETYLTVL
SDSLYIPIFS TFFFNSPHQK DTNMGREGQD TQSKPLNLLT VWDWSVQFEP KAQTLLKNPL
YVEKPKLDKG QRKGMRFKHQ RQLSLPLTQS KSSPKRGFFR EETDHLIKNL LGKRISKLIN
SSDELQDNFR EFYDSWHSKS TDYHGLLLPH IEGPEIKVWA QRYLRWIPEA QILGGGQVAT
LSKLLEMMEE VQSLQEKIDE RHHSQQAPQA EAPCLLRNSA RLSSLFPFAL LQRHSSKPVL
PTSGWKALGD EDDLAKREDE FVDLGDV
//
MIM
606501
*RECORD*
*FIELD* NO
606501
*FIELD* TI
*606501 MYOTUBULARIN-RELATED PROTEIN 12; MTMR12
;;PHOSPHATIDYLINOSITOL 3-PHOSPHATE 3-PHOSPHATASE ADAPTOR SUBUNIT; 3PAP;;
read moreKIAA1682
*FIELD* TX
DESCRIPTION
Phosphatidylinositide 3-kinase (see PIK3R1; 171833)-derived,
membrane-anchored phosphatidylinositides, such as phosphatidylinositol
3-phosphate (PtdIns(3)P), regulate diverse cellular processes. 3PAP
functions as an adaptor subunit in a complex with an active PtdIns(3)P
3-phosphatase.
CLONING
By screening for cDNAs with the potential to encode large proteins
expressed in brain, Nagase et al. (2000) identified a cDNA encoding
3PAP, which they called KIAA1682. KIAA1682 encodes a deduced 775-amino
acid protein. RT-PCR analysis detected moderate expression of KIAA1682
in all tissues tested.
By biochemical purification and microsequence analysis of the rat brain
cytosolic 3Pap protein, followed by PCR with degenerate primers,
screening of a K562 cDNA library, and RT-PCR, Nandurkar et al. (2001)
obtained a cDNA encoding human 3PAP. Sequence analysis predicted that
the 3PAP protein has homology to myotubularin but, like SBF1 (603560),
lacks the HCX5R catalytic motif. Northern blot analysis revealed
expression of 5.5- and 2.5-kb 3PAP transcripts that were prominent in
brain, heart, kidney, liver, placenta, and lung. Immunoblot analysis
showed expression of an 86-kD protein in various tissues and cell lines.
Immunoprecipitation analysis indicated that platelet 3PAP, but not
recombinant 3PAP, possesses lipid 3-phosphatase activity. Nandurkar et
al. (2001) concluded that 3PAP is an adaptor subunit in a complex with
an active PtdIns(3)P 3-phosphatase.
MAPPING
Using a human-rodent hybrid panel, Nagase et al. (2000) mapped the
KIAA1682 gene to both chromosomes 5 and 11. The International Radiation
Hybrid Mapping Consortium mapped the 3PAP gene to chromosome 5 (TMAP
RH26387).
*FIELD* RF
1. Nagase, T.; Kikuno, R.; Hattori, A.; Kondo, Y.; Okumura, K.; Ohara,
O.: Prediction of the coding sequences of unidentified human genes.
XIX. The complete sequences of 100 new cDNA clones from brain which
code for large proteins in vitro. DNA Res. 7: 347-355, 2000.
2. Nandurkar, H. H.; Caldwell, K. K.; Whisstock, J. C.; Layton, M.
J.; Gaudet, E. A.; Norris, F. A.; Majerus, P. W.; Mitchell, C. A.
: Characterization of an adapter subunit to a phosphatidylinositol
(3)P 3-phosphatase: identification of a myotubularin-related protein
lacking catalytic activity. Proc. Nat. Acad. Sci. 98: 9499-9504,
2001.
*FIELD* CD
Paul J. Converse: 11/26/2001
*FIELD* ED
alopez: 04/18/2005
mgross: 11/26/2001
*RECORD*
*FIELD* NO
606501
*FIELD* TI
*606501 MYOTUBULARIN-RELATED PROTEIN 12; MTMR12
;;PHOSPHATIDYLINOSITOL 3-PHOSPHATE 3-PHOSPHATASE ADAPTOR SUBUNIT; 3PAP;;
read moreKIAA1682
*FIELD* TX
DESCRIPTION
Phosphatidylinositide 3-kinase (see PIK3R1; 171833)-derived,
membrane-anchored phosphatidylinositides, such as phosphatidylinositol
3-phosphate (PtdIns(3)P), regulate diverse cellular processes. 3PAP
functions as an adaptor subunit in a complex with an active PtdIns(3)P
3-phosphatase.
CLONING
By screening for cDNAs with the potential to encode large proteins
expressed in brain, Nagase et al. (2000) identified a cDNA encoding
3PAP, which they called KIAA1682. KIAA1682 encodes a deduced 775-amino
acid protein. RT-PCR analysis detected moderate expression of KIAA1682
in all tissues tested.
By biochemical purification and microsequence analysis of the rat brain
cytosolic 3Pap protein, followed by PCR with degenerate primers,
screening of a K562 cDNA library, and RT-PCR, Nandurkar et al. (2001)
obtained a cDNA encoding human 3PAP. Sequence analysis predicted that
the 3PAP protein has homology to myotubularin but, like SBF1 (603560),
lacks the HCX5R catalytic motif. Northern blot analysis revealed
expression of 5.5- and 2.5-kb 3PAP transcripts that were prominent in
brain, heart, kidney, liver, placenta, and lung. Immunoblot analysis
showed expression of an 86-kD protein in various tissues and cell lines.
Immunoprecipitation analysis indicated that platelet 3PAP, but not
recombinant 3PAP, possesses lipid 3-phosphatase activity. Nandurkar et
al. (2001) concluded that 3PAP is an adaptor subunit in a complex with
an active PtdIns(3)P 3-phosphatase.
MAPPING
Using a human-rodent hybrid panel, Nagase et al. (2000) mapped the
KIAA1682 gene to both chromosomes 5 and 11. The International Radiation
Hybrid Mapping Consortium mapped the 3PAP gene to chromosome 5 (TMAP
RH26387).
*FIELD* RF
1. Nagase, T.; Kikuno, R.; Hattori, A.; Kondo, Y.; Okumura, K.; Ohara,
O.: Prediction of the coding sequences of unidentified human genes.
XIX. The complete sequences of 100 new cDNA clones from brain which
code for large proteins in vitro. DNA Res. 7: 347-355, 2000.
2. Nandurkar, H. H.; Caldwell, K. K.; Whisstock, J. C.; Layton, M.
J.; Gaudet, E. A.; Norris, F. A.; Majerus, P. W.; Mitchell, C. A.
: Characterization of an adapter subunit to a phosphatidylinositol
(3)P 3-phosphatase: identification of a myotubularin-related protein
lacking catalytic activity. Proc. Nat. Acad. Sci. 98: 9499-9504,
2001.
*FIELD* CD
Paul J. Converse: 11/26/2001
*FIELD* ED
alopez: 04/18/2005
mgross: 11/26/2001