Full text data of TMEM55B
TMEM55B
(C14orf9)
[Confidence: high (present in two of the MS resources)]
Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase; Type 1 PtdIns-4,5-P2 4-Ptase; 3.1.3.78 (PtdIns-4,5-P2 4-Ptase I; Transmembrane protein 55B)
Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase; Type 1 PtdIns-4,5-P2 4-Ptase; 3.1.3.78 (PtdIns-4,5-P2 4-Ptase I; Transmembrane protein 55B)
hRBCD
IPI00030530
IPI00030530 Splice Isoform 1 Of Hypothetical protein C14orf9 no information available soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned Isoform 1 or 2 expected molecular weight found in band at molecular weight
IPI00030530 Splice Isoform 1 Of Hypothetical protein C14orf9 no information available soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned Isoform 1 or 2 expected molecular weight found in band at molecular weight
Comments
Isoform Q86T03-2 was detected.
Isoform Q86T03-2 was detected.
UniProt
Q86T03
ID TM55B_HUMAN Reviewed; 277 AA.
AC Q86T03; B2RA35; Q86U09; Q8WUC0; Q9BU67; Q9NSU8;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2003, sequence version 1.
DT 22-JAN-2014, entry version 97.
DE RecName: Full=Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase;
DE Short=Type 1 PtdIns-4,5-P2 4-Ptase;
DE EC=3.1.3.78;
DE AltName: Full=PtdIns-4,5-P2 4-Ptase I;
DE AltName: Full=Transmembrane protein 55B;
GN Name=TMEM55B; Synonyms=C14orf9;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Neuroblastoma, and T-cell;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Substantia nigra;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Lung;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16365287; DOI=10.1073/pnas.0509740102;
RA Ungewickell A., Hugge C., Kisseleva M., Chang S.-C., Zou J., Feng Y.,
RA Galyov E.E., Wilson M., Majerus P.W.;
RT "The identification and characterization of two phosphatidylinositol-
RT 4,5-bisphosphate 4-phosphatases.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18854-18859(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC -!- FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of
CC phosphatidylinositol 4,5-bisphosphate. Does not hydrolyze
CC phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol
CC 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-
CC bisphosphate, phosphatidylinositol 5-monophosphate,
CC phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-
CC monophosphate.
CC -!- CATALYTIC ACTIVITY: 1-phosphatidyl-myo-inositol 4,5-bisphosphate +
CC H(2)O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate.
CC -!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
CC bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 5-phosphate
CC + phosphate.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane; Multi-pass membrane
CC protein. Lysosome membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86T03-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86T03-2; Sequence=VSP_007815;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q86T03-3; Sequence=VSP_007816, VSP_007817;
CC Note=May be due to intron retention.;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB70896.1; Type=Erroneous initiation;
CC Sequence=CAD62347.1; 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; BX161490; CAD61939.1; -; mRNA.
DR EMBL; BX248025; CAD62347.1; ALT_INIT; mRNA.
DR EMBL; AK314021; BAG36732.1; -; mRNA.
DR EMBL; AL137727; CAB70896.1; ALT_INIT; mRNA.
DR EMBL; CH471078; EAW66461.1; -; Genomic_DNA.
DR EMBL; BC002867; AAH02867.2; -; mRNA.
DR EMBL; BC020947; AAH20947.1; -; mRNA.
DR PIR; T46382; T46382.
DR RefSeq; NP_001094284.1; NM_001100814.1.
DR RefSeq; NP_653169.2; NM_144568.2.
DR UniGene; Hs.7001; -.
DR ProteinModelPortal; Q86T03; -.
DR IntAct; Q86T03; 1.
DR STRING; 9606.ENSP00000381102; -.
DR PhosphoSite; Q86T03; -.
DR DMDM; 33112243; -.
DR PaxDb; Q86T03; -.
DR PRIDE; Q86T03; -.
DR DNASU; 90809; -.
DR Ensembl; ENST00000250489; ENSP00000250489; ENSG00000165782.
DR Ensembl; ENST00000398020; ENSP00000381102; ENSG00000165782.
DR GeneID; 90809; -.
DR KEGG; hsa:90809; -.
DR UCSC; uc001vxl.2; human.
DR CTD; 90809; -.
DR GeneCards; GC14M020926; -.
DR HGNC; HGNC:19299; TMEM55B.
DR HPA; HPA048528; -.
DR MIM; 609865; gene.
DR neXtProt; NX_Q86T03; -.
DR PharmGKB; PA134919069; -.
DR eggNOG; NOG316118; -.
DR HOGENOM; HOG000231722; -.
DR HOVERGEN; HBG080409; -.
DR KO; K13084; -.
DR OMA; WCFLLCL; -.
DR OrthoDB; EOG7DZ8KH; -.
DR PhylomeDB; Q86T03; -.
DR BioCyc; MetaCyc:HS15363-MONOMER; -.
DR GenomeRNAi; 90809; -.
DR NextBio; 76969; -.
DR PRO; PR:Q86T03; -.
DR ArrayExpress; Q86T03; -.
DR Bgee; Q86T03; -.
DR CleanEx; HS_TMEM55B; -.
DR Genevestigator; Q86T03; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR InterPro; IPR019178; Transmembrane_protein_55A/B.
DR PANTHER; PTHR21014; PTHR21014; 1.
DR Pfam; PF09788; Tmemb_55A; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Endosome; Hydrolase;
KW Lysosome; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 277 Type 1 phosphatidylinositol 4,5-
FT bisphosphate 4-phosphatase.
FT /FTId=PRO_0000072579.
FT TRANSMEM 212 232 Helical; (Potential).
FT TRANSMEM 242 262 Helical; (Potential).
FT MOTIF 133 139 CX5R motif.
FT COMPBIAS 17 37 Gly-rich.
FT COMPBIAS 34 80 Pro-rich.
FT ACT_SITE 133 133 By similarity.
FT MOD_RES 162 162 Phosphoserine (By similarity).
FT VAR_SEQ 47 47 A -> AGKHAPPQ (in isoform 2).
FT /FTId=VSP_007815.
FT VAR_SEQ 48 224 AFPPFPEGHPAVLPGEDPPPYSPLTSPDSGSAPMITCRVCQ
FT SLINVEGKMHQHVVKCGVCNEATPIKNAPPGKKYVRCPCNC
FT LLICKVTSQRIACPRPYCKRIINLGPVHPGPLSPEPQPMGV
FT RVICGHCKNTFLWTEFTDRTLARCPHCRKVSSIGRRYPRKR
FT CICCFLLGLLLAV -> GKHAPPQGKPGRVRGAPRGTLKAG
FT EGAGPRAEAGPSRQVRDCCTCDWARLPSLRNRDHSLGTEGG
FT SEQPDRSANYEKPSELGQRVEDQKDFPTTVEHQWGCK (in
FT isoform 3).
FT /FTId=VSP_007816.
FT VAR_SEQ 225 277 Missing (in isoform 3).
FT /FTId=VSP_007817.
FT CONFLICT 208 208 P -> T (in Ref. 5; AAH20947).
SQ SEQUENCE 277 AA; 29470 MW; A85FE1F736366CBC CRC64;
MAADGERSPL LSEPIDGGAG GNGLVGPGGS GAGPGGGLTP SAPPYGAAFP PFPEGHPAVL
PGEDPPPYSP LTSPDSGSAP MITCRVCQSL INVEGKMHQH VVKCGVCNEA TPIKNAPPGK
KYVRCPCNCL LICKVTSQRI ACPRPYCKRI INLGPVHPGP LSPEPQPMGV RVICGHCKNT
FLWTEFTDRT LARCPHCRKV SSIGRRYPRK RCICCFLLGL LLAVTATGLA FGTWKHARRY
GGIYAAWAFV ILLAVLCLGR ALYWACMKVS HPVQNFS
//
ID TM55B_HUMAN Reviewed; 277 AA.
AC Q86T03; B2RA35; Q86U09; Q8WUC0; Q9BU67; Q9NSU8;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2003, sequence version 1.
DT 22-JAN-2014, entry version 97.
DE RecName: Full=Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase;
DE Short=Type 1 PtdIns-4,5-P2 4-Ptase;
DE EC=3.1.3.78;
DE AltName: Full=PtdIns-4,5-P2 4-Ptase I;
DE AltName: Full=Transmembrane protein 55B;
GN Name=TMEM55B; Synonyms=C14orf9;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Neuroblastoma, and T-cell;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Substantia nigra;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Lung;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16365287; DOI=10.1073/pnas.0509740102;
RA Ungewickell A., Hugge C., Kisseleva M., Chang S.-C., Zou J., Feng Y.,
RA Galyov E.E., Wilson M., Majerus P.W.;
RT "The identification and characterization of two phosphatidylinositol-
RT 4,5-bisphosphate 4-phosphatases.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18854-18859(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC -!- FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of
CC phosphatidylinositol 4,5-bisphosphate. Does not hydrolyze
CC phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol
CC 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-
CC bisphosphate, phosphatidylinositol 5-monophosphate,
CC phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-
CC monophosphate.
CC -!- CATALYTIC ACTIVITY: 1-phosphatidyl-myo-inositol 4,5-bisphosphate +
CC H(2)O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate.
CC -!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
CC bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 5-phosphate
CC + phosphate.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane; Multi-pass membrane
CC protein. Lysosome membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86T03-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86T03-2; Sequence=VSP_007815;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q86T03-3; Sequence=VSP_007816, VSP_007817;
CC Note=May be due to intron retention.;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB70896.1; Type=Erroneous initiation;
CC Sequence=CAD62347.1; 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; BX161490; CAD61939.1; -; mRNA.
DR EMBL; BX248025; CAD62347.1; ALT_INIT; mRNA.
DR EMBL; AK314021; BAG36732.1; -; mRNA.
DR EMBL; AL137727; CAB70896.1; ALT_INIT; mRNA.
DR EMBL; CH471078; EAW66461.1; -; Genomic_DNA.
DR EMBL; BC002867; AAH02867.2; -; mRNA.
DR EMBL; BC020947; AAH20947.1; -; mRNA.
DR PIR; T46382; T46382.
DR RefSeq; NP_001094284.1; NM_001100814.1.
DR RefSeq; NP_653169.2; NM_144568.2.
DR UniGene; Hs.7001; -.
DR ProteinModelPortal; Q86T03; -.
DR IntAct; Q86T03; 1.
DR STRING; 9606.ENSP00000381102; -.
DR PhosphoSite; Q86T03; -.
DR DMDM; 33112243; -.
DR PaxDb; Q86T03; -.
DR PRIDE; Q86T03; -.
DR DNASU; 90809; -.
DR Ensembl; ENST00000250489; ENSP00000250489; ENSG00000165782.
DR Ensembl; ENST00000398020; ENSP00000381102; ENSG00000165782.
DR GeneID; 90809; -.
DR KEGG; hsa:90809; -.
DR UCSC; uc001vxl.2; human.
DR CTD; 90809; -.
DR GeneCards; GC14M020926; -.
DR HGNC; HGNC:19299; TMEM55B.
DR HPA; HPA048528; -.
DR MIM; 609865; gene.
DR neXtProt; NX_Q86T03; -.
DR PharmGKB; PA134919069; -.
DR eggNOG; NOG316118; -.
DR HOGENOM; HOG000231722; -.
DR HOVERGEN; HBG080409; -.
DR KO; K13084; -.
DR OMA; WCFLLCL; -.
DR OrthoDB; EOG7DZ8KH; -.
DR PhylomeDB; Q86T03; -.
DR BioCyc; MetaCyc:HS15363-MONOMER; -.
DR GenomeRNAi; 90809; -.
DR NextBio; 76969; -.
DR PRO; PR:Q86T03; -.
DR ArrayExpress; Q86T03; -.
DR Bgee; Q86T03; -.
DR CleanEx; HS_TMEM55B; -.
DR Genevestigator; Q86T03; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR InterPro; IPR019178; Transmembrane_protein_55A/B.
DR PANTHER; PTHR21014; PTHR21014; 1.
DR Pfam; PF09788; Tmemb_55A; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Endosome; Hydrolase;
KW Lysosome; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 277 Type 1 phosphatidylinositol 4,5-
FT bisphosphate 4-phosphatase.
FT /FTId=PRO_0000072579.
FT TRANSMEM 212 232 Helical; (Potential).
FT TRANSMEM 242 262 Helical; (Potential).
FT MOTIF 133 139 CX5R motif.
FT COMPBIAS 17 37 Gly-rich.
FT COMPBIAS 34 80 Pro-rich.
FT ACT_SITE 133 133 By similarity.
FT MOD_RES 162 162 Phosphoserine (By similarity).
FT VAR_SEQ 47 47 A -> AGKHAPPQ (in isoform 2).
FT /FTId=VSP_007815.
FT VAR_SEQ 48 224 AFPPFPEGHPAVLPGEDPPPYSPLTSPDSGSAPMITCRVCQ
FT SLINVEGKMHQHVVKCGVCNEATPIKNAPPGKKYVRCPCNC
FT LLICKVTSQRIACPRPYCKRIINLGPVHPGPLSPEPQPMGV
FT RVICGHCKNTFLWTEFTDRTLARCPHCRKVSSIGRRYPRKR
FT CICCFLLGLLLAV -> GKHAPPQGKPGRVRGAPRGTLKAG
FT EGAGPRAEAGPSRQVRDCCTCDWARLPSLRNRDHSLGTEGG
FT SEQPDRSANYEKPSELGQRVEDQKDFPTTVEHQWGCK (in
FT isoform 3).
FT /FTId=VSP_007816.
FT VAR_SEQ 225 277 Missing (in isoform 3).
FT /FTId=VSP_007817.
FT CONFLICT 208 208 P -> T (in Ref. 5; AAH20947).
SQ SEQUENCE 277 AA; 29470 MW; A85FE1F736366CBC CRC64;
MAADGERSPL LSEPIDGGAG GNGLVGPGGS GAGPGGGLTP SAPPYGAAFP PFPEGHPAVL
PGEDPPPYSP LTSPDSGSAP MITCRVCQSL INVEGKMHQH VVKCGVCNEA TPIKNAPPGK
KYVRCPCNCL LICKVTSQRI ACPRPYCKRI INLGPVHPGP LSPEPQPMGV RVICGHCKNT
FLWTEFTDRT LARCPHCRKV SSIGRRYPRK RCICCFLLGL LLAVTATGLA FGTWKHARRY
GGIYAAWAFV ILLAVLCLGR ALYWACMKVS HPVQNFS
//
MIM
609865
*RECORD*
*FIELD* NO
609865
*FIELD* TI
*609865 TRANSMEMBRANE PROTEIN 55B; TMEM55B
;;PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 4-PHOSPHATASE, TYPE I
read more*FIELD* TX
DESCRIPTION
TMEM55B catalyzes the degradation of phosphatidylinositol
4,5-bisphosphate (PtdIns-4,5-P2) by removing the 4-phosphate
(Ungewickell et al., 2005).
CLONING
By searching a database for genes encoding proteins similar to
Burkholderia pseudomallei virulence factor BopB, a putative phosphatase,
Ungewickell et al. (2005) identified TMEM55B. The deduced 257-amino acid
protein contains a central Cx(5)R phosphatase catalytic motif and 2
transmembrane domains near its C terminus, a characteristic of lysosomal
transmembrane proteins. RNA dot blot analysis detected expression in all
tissues examined. Fluorescence-tagged TMEM55B localized with membrane
markers of late endosomes or lysosomes. Endogenous HeLa cell TMEM55B
showed a similar distribution.
GENE FUNCTION
Ungewickell et al. (2005) assayed the phosphatase activity of TMEM55B
synthesized in insect cells and found that it specifically catalyzed
removal of the 4-phosphate from PtdIns-4,5-P2. It showed no activity
toward other phosphatidylinositol substrates or inositol phosphates
tested. Overexpression of TMEM55B in human embryonic kidney cells
reduced the total cellular level of PtdIns-4,5-P2.
MAPPING
By genomic sequence analysis, Ungewickell et al. (2005) mapped the
TMEM55B gene to chromosome 14q11.2.
*FIELD* RF
1. Ungewickell, A.; Hugge, C.; Kisseleva, M.; Chang, S.-C.; Zou, J.;
Feng, Y.; Galyov, E. E.; Wilson, M.; Majerus, P. W.: The identification
and characterization of two phosphatidylinositol-4,5-bisphosphate
4-phosphatases. Proc. Nat. Acad. Sci. 102: 18854-18859, 2005.
*FIELD* CD
Patricia A. Hartz: 1/30/2006
*FIELD* ED
mgross: 01/30/2006
*RECORD*
*FIELD* NO
609865
*FIELD* TI
*609865 TRANSMEMBRANE PROTEIN 55B; TMEM55B
;;PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 4-PHOSPHATASE, TYPE I
read more*FIELD* TX
DESCRIPTION
TMEM55B catalyzes the degradation of phosphatidylinositol
4,5-bisphosphate (PtdIns-4,5-P2) by removing the 4-phosphate
(Ungewickell et al., 2005).
CLONING
By searching a database for genes encoding proteins similar to
Burkholderia pseudomallei virulence factor BopB, a putative phosphatase,
Ungewickell et al. (2005) identified TMEM55B. The deduced 257-amino acid
protein contains a central Cx(5)R phosphatase catalytic motif and 2
transmembrane domains near its C terminus, a characteristic of lysosomal
transmembrane proteins. RNA dot blot analysis detected expression in all
tissues examined. Fluorescence-tagged TMEM55B localized with membrane
markers of late endosomes or lysosomes. Endogenous HeLa cell TMEM55B
showed a similar distribution.
GENE FUNCTION
Ungewickell et al. (2005) assayed the phosphatase activity of TMEM55B
synthesized in insect cells and found that it specifically catalyzed
removal of the 4-phosphate from PtdIns-4,5-P2. It showed no activity
toward other phosphatidylinositol substrates or inositol phosphates
tested. Overexpression of TMEM55B in human embryonic kidney cells
reduced the total cellular level of PtdIns-4,5-P2.
MAPPING
By genomic sequence analysis, Ungewickell et al. (2005) mapped the
TMEM55B gene to chromosome 14q11.2.
*FIELD* RF
1. Ungewickell, A.; Hugge, C.; Kisseleva, M.; Chang, S.-C.; Zou, J.;
Feng, Y.; Galyov, E. E.; Wilson, M.; Majerus, P. W.: The identification
and characterization of two phosphatidylinositol-4,5-bisphosphate
4-phosphatases. Proc. Nat. Acad. Sci. 102: 18854-18859, 2005.
*FIELD* CD
Patricia A. Hartz: 1/30/2006
*FIELD* ED
mgross: 01/30/2006