Full text data of PTPN23
PTPN23
(KIAA1471)
[Confidence: low (only semi-automatic identification from reviews)]
Tyrosine-protein phosphatase non-receptor type 23; 3.1.3.48 (His domain-containing protein tyrosine phosphatase; HD-PTP; Protein tyrosine phosphatase TD14; PTP-TD14)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Tyrosine-protein phosphatase non-receptor type 23; 3.1.3.48 (His domain-containing protein tyrosine phosphatase; HD-PTP; Protein tyrosine phosphatase TD14; PTP-TD14)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H3S7
ID PTN23_HUMAN Reviewed; 1636 AA.
AC Q9H3S7; A8K0D7; Q7KZF8; Q8N6Z5; Q9BSR5; Q9P257; Q9UG03; Q9UMZ4;
read moreDT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 23;
DE EC=3.1.3.48;
DE AltName: Full=His domain-containing protein tyrosine phosphatase;
DE Short=HD-PTP;
DE AltName: Full=Protein tyrosine phosphatase TD14;
DE Short=PTP-TD14;
GN Name=PTPN23; Synonyms=KIAA1471;
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], VARIANT SER-1099, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Stomach cancer;
RX PubMed=11095967; DOI=10.1006/bbrc.2000.3870;
RA Toyooka S., Ouchida M., Jitsumori Y., Tsukuda K., Sakai A.,
RA Nakamura A., Shimizu N., Shimizu K.;
RT "HD-PTP: a novel protein tyrosine phosphatase gene on human chromosome
RT 3p21.3.";
RL Biochem. Biophys. Res. Commun. 278:671-678(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Qu X., Zhai Y., Wei H., Zhang C., Xing G., Lu C., Wang M., He F.;
RT "Cloning, chromosomal assignment and tissue expression of a novel
RT human protein tyrosine phosphatase (PTP-TD14) gene.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle, Ovary, and Skin;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1383, AND VARIANT THR-944.
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [7]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 647-1636, AND VARIANT
RP THR-944.
RC TISSUE=Brain;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1060-1636.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1351-1493.
RA Dayton M.A., Blanchard K.L.;
RT "Differential expression of PTPase RNAs resulting from K562
RT differentiation induced by PMA.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1123, AND MASS
RP SPECTROMETRY.
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).
RN [12]
RP FUNCTION, INTERACTION WITH CHMP4B, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LEU-202 AND ILE-206.
RX PubMed=18434552; DOI=10.1073/pnas.0707601105;
RA Doyotte A., Mironov A., McKenzie E., Woodman P.;
RT "The Bro1-related protein HD-PTP/PTPN23 is required for endosomal
RT cargo sorting and multivesicular body morphogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6308-6313(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1123, AND MASS
RP SPECTROMETRY.
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).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20393563; DOI=10.1038/nature08895;
RA Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K.,
RA Ideker T., Aza-Blanc P., Gleeson J.G.;
RT "Functional genomic screen for modulators of ciliogenesis and cilium
RT length.";
RL Nature 464:1048-1051(2010).
RN [15]
RP INTERACTION WITH GRAP2 AND GRB2, AND SUBCELLULAR LOCATION.
RX PubMed=21179510; DOI=10.1371/journal.pone.0014339;
RA Tanase C.A.;
RT "Histidine domain-protein tyrosine phosphatase interacts with Grb2 and
RT GrpL.";
RL PLoS ONE 5:E14339-E14339(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP FUNCTION, INTERACTION WITH UBAP1, SUBCELLULAR LOCTION, AND MUTAGENESIS
RP OF PHE-678.
RX PubMed=21757351; DOI=10.1016/j.cub.2011.06.028;
RA Stefani F., Zhang L., Taylor S., Donovan J., Rollinson S., Doyotte A.,
RA Brownhill K., Bennion J., Pickering-Brown S., Woodman P.;
RT "UBAP1 is a component of an endosome-specific ESCRT-I complex that is
RT essential for MVB sorting.";
RL Curr. Biol. 21:1245-1250(2011).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 2-361.
RX PubMed=21889351; DOI=10.1016/j.str.2011.07.016;
RA Sette P., Mu R., Dussupt V., Jiang J., Snyder G., Smith P., Xiao T.S.,
RA Bouamr F.;
RT "The Phe105 loop of Alix Bro1 domain plays a key role in HIV-1
RT release.";
RL Structure 19:1485-1495(2011).
CC -!- FUNCTION: Plays a role in sorting of endocytic ubiquitinated
CC cargos into multivesicular bodies (MVBs) via its interaction with
CC the ESCRT-I complex (endosomal sorting complex required for
CC transport I), and possibly also other ESCRT complexes. May act as
CC a negative regulator of Ras-mediated mitogenic activity. Plays a
CC role in ciliogenesis.
CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- SUBUNIT: Interacts with GRAP2 and GRB2. Interacts with UBAP1 and
CC CHMP4B.
CC -!- INTERACTION:
CC Q9H444:CHMP4B; NbExp=2; IntAct=EBI-724478, EBI-749627;
CC O75791:GRAP2; NbExp=8; IntAct=EBI-724478, EBI-740418;
CC O89100:Grap2 (xeno); NbExp=2; IntAct=EBI-724478, EBI-642151;
CC P62993:GRB2; NbExp=6; IntAct=EBI-724478, EBI-401755;
CC O75340:PDCD6; NbExp=3; IntAct=EBI-724478, EBI-352915;
CC Q05397:PTK2; NbExp=4; IntAct=EBI-724478, EBI-702142;
CC Q99962:SH3GL2; NbExp=2; IntAct=EBI-724478, EBI-77938;
CC Q99816:TSG101; NbExp=2; IntAct=EBI-724478, EBI-346882;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasmic vesicle.
CC Endosome. Cytoplasm, cytoskeleton, cilium basal body. Early
CC endosome.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Non-receptor class subfamily.
CC -!- SIMILARITY: Contains 1 BRO1 domain.
CC -!- SIMILARITY: Contains 2 TPR repeats.
CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95995.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AB025194; BAB19280.1; -; mRNA.
DR EMBL; AF290614; AAK28025.1; -; mRNA.
DR EMBL; AK289502; BAF82191.1; -; mRNA.
DR EMBL; CH471055; EAW64823.1; -; Genomic_DNA.
DR EMBL; BC004881; AAH04881.2; -; mRNA.
DR EMBL; BC027711; AAH27711.2; -; mRNA.
DR EMBL; BC089042; AAH89042.1; -; mRNA.
DR EMBL; AB040904; BAA95995.2; ALT_INIT; mRNA.
DR EMBL; AL110210; CAB53676.1; -; mRNA.
DR EMBL; BT009758; AAP88760.1; -; mRNA.
DR EMBL; AF169350; AAD50276.1; -; mRNA.
DR PIR; T14756; T14756.
DR RefSeq; NP_056281.1; NM_015466.2.
DR UniGene; Hs.25524; -.
DR PDB; 3RAU; X-ray; 1.95 A; A/B=2-361.
DR PDBsum; 3RAU; -.
DR ProteinModelPortal; Q9H3S7; -.
DR SMR; Q9H3S7; 4-697, 1142-1459.
DR DIP; DIP-29923N; -.
DR IntAct; Q9H3S7; 14.
DR MINT; MINT-1425077; -.
DR STRING; 9606.ENSP00000265562; -.
DR PhosphoSite; Q9H3S7; -.
DR DMDM; 68053318; -.
DR PaxDb; Q9H3S7; -.
DR PeptideAtlas; Q9H3S7; -.
DR PRIDE; Q9H3S7; -.
DR DNASU; 25930; -.
DR Ensembl; ENST00000265562; ENSP00000265562; ENSG00000076201.
DR GeneID; 25930; -.
DR KEGG; hsa:25930; -.
DR UCSC; uc003crf.1; human.
DR CTD; 25930; -.
DR GeneCards; GC03P047397; -.
DR HGNC; HGNC:14406; PTPN23.
DR HPA; HPA016845; -.
DR MIM; 606584; gene.
DR neXtProt; NX_Q9H3S7; -.
DR PharmGKB; PA33996; -.
DR eggNOG; COG5599; -.
DR HOVERGEN; HBG082231; -.
DR InParanoid; Q9H3S7; -.
DR KO; K01104; -.
DR OMA; IARCYTM; -.
DR OrthoDB; EOG72C4ZH; -.
DR PhylomeDB; Q9H3S7; -.
DR ChiTaRS; PTPN23; human.
DR EvolutionaryTrace; Q9H3S7; -.
DR GeneWiki; PTPN23; -.
DR GenomeRNAi; 25930; -.
DR NextBio; 47476; -.
DR PRO; PR:Q9H3S7; -.
DR ArrayExpress; Q9H3S7; -.
DR Bgee; Q9H3S7; -.
DR CleanEx; HS_PTPN23; -.
DR Genevestigator; Q9H3S7; -.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005932; C:microtubule basal body; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0060271; P:cilium morphogenesis; IMP:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB.
DR Gene3D; 1.25.40.280; -; 1.
DR InterPro; IPR025304; ALIX_V_dom.
DR InterPro; IPR004328; BRO1_dom.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR Pfam; PF13949; ALIX_LYPXL_bnd; 1.
DR Pfam; PF03097; BRO1; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM01041; BRO1; 1.
DR SMART; SM00194; PTPc; 1.
DR PROSITE; PS51180; BRO1; 1.
DR PROSITE; PS50005; TPR; FALSE_NEG.
DR PROSITE; PS50293; TPR_REGION; FALSE_NEG.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Endosome; Hydrolase; Nucleus; Phosphoprotein;
KW Polymorphism; Protein phosphatase; Protein transport;
KW Reference proteome; Repeat; TPR repeat; Transport.
FT CHAIN 1 1636 Tyrosine-protein phosphatase non-receptor
FT type 23.
FT /FTId=PRO_0000094777.
FT DOMAIN 8 394 BRO1.
FT REPEAT 250 283 TPR 1.
FT REPEAT 374 407 TPR 2.
FT REPEAT 953 954 1.
FT REPEAT 955 956 2.
FT REPEAT 957 958 3.
FT REPEAT 959 960 4.
FT REPEAT 961 962 5.
FT REPEAT 963 964 6.
FT DOMAIN 1192 1452 Tyrosine-protein phosphatase.
FT REGION 770 1130 His.
FT REGION 953 964 6 X 2 AA approximate tandem repeats of P-
FT Q.
FT COILED 550 623 Potential.
FT COMPBIAS 716 1108 Pro-rich.
FT COMPBIAS 1509 1573 Pro-rich.
FT ACT_SITE 1392 1392 Phosphocysteine intermediate (By
FT similarity).
FT MOD_RES 1123 1123 Phosphoserine.
FT VARIANT 944 944 A -> T (in dbSNP:rs6780013).
FT /FTId=VAR_022682.
FT VARIANT 1099 1099 P -> S (in a lung cancer cell line; may
FT be a common polymorphism;
FT dbSNP:rs149563514).
FT /FTId=VAR_022683.
FT MUTAGEN 202 202 L->D: Nearly abolishes interaction with
FT CHMP4B. Abolishes interaction with
FT CHMP4B; when associated with D-206.
FT MUTAGEN 206 206 I->D: Abolishes interaction with CHMP4B;
FT when associated with D-202.
FT MUTAGEN 678 678 F->D: Abolishes interaction with UBAP1.
FT CONFLICT 647 647 L -> G (in Ref. 8; CAB53676).
FT CONFLICT 1087 1087 S -> P (in Ref. 8; CAB53676).
FT STRAND 17 20
FT HELIX 23 32
FT TURN 38 41
FT HELIX 42 56
FT HELIX 62 81
FT STRAND 94 97
FT TURN 99 101
FT STRAND 104 108
FT HELIX 110 131
FT HELIX 137 160
FT HELIX 167 169
FT HELIX 171 195
FT HELIX 200 221
FT HELIX 224 230
FT HELIX 233 262
FT HELIX 266 286
FT TURN 287 289
FT HELIX 292 318
FT HELIX 327 329
FT HELIX 349 352
FT TURN 356 359
SQ SEQUENCE 1636 AA; 178974 MW; 536BDDF9D3DC95C0 CRC64;
MEAVPRMPMI WLDLKEAGDF HFQPAVKKFV LKNYGENPEA YNEELKKLEL LRQNAVRVPR
DFEGCSVLRK YLGQLHYLQS RVPMGSGQEA AVPVTWTEIF SGKSVAHEDI KYEQACILYN
LGALHSMLGA MDKRVSEEGM KVSCTHFQCA AGAFAYLREH FPQAYSVDMS RQILTLNVNL
MLGQAQECLL EKSMLDNRKS FLVARISAQV VDYYKEACRA LENPDTASLL GRIQKDWKKL
VQMKIYYFAA VAHLHMGKQA EEQQKFGERV AYFQSALDKL NEAIKLAKGQ PDTVQDALRF
TMDVIGGKYN SAKKDNDFIY HEAVPALDTL QPVKGAPLVK PLPVNPTDPA VTGPDIFAKL
VPMAAHEASS LYSEEKAKLL REMMAKIEDK NEVLDQFMDS MQLDPETVDN LDAYSHIPPQ
LMEKCAALSV RPDTVRNLVQ SMQVLSGVFT DVEASLKDIR DLLEEDELLE QKFQEAVGQA
GAISITSKAE LAEVRREWAK YMEVHEKASF TNSELHRAMN LHVGNLRLLS GPLDQVRAAL
PTPALSPEDK AVLQNLKRIL AKVQEMRDQR VSLEQQLREL IQKDDITASL VTTDHSEMKK
LFEEQLKKYD QLKVYLEQNL AAQDRVLCAL TEANVQYAAV RRVLSDLDQK WNSTLQTLVA
SYEAYEDLMK KSQEGRDFYA DLESKVAALL ERTQSTCQAR EAARQQLLDR ELKKKPPPRP
TAPKPLLPRR EESEAVEAGD PPEELRSLPP DMVAGPRLPD TFLGSATPLH FPPSPFPSST
GPGPHYLSGP LPPGTYSGPT QLIQPRAPGP HAMPVAPGPA LYPAPAYTPE LGLVPRSSPQ
HGVVSSPYVG VGPAPPVAGL PSAPPPQFSG PELAMAVRPA TTTVDSIQAP IPSHTAPRPN
PTPAPPPPCF PVPPPQPLPT PYTYPAGAKQ PIPAQHHFSS GIPAGFPAPR IGPQPQPHPQ
PHPSQAFGPQ PPQQPLPLQH PHLFPPQAPG LLPPQSPYPY APQPGVLGQP PPPLHTQLYP
GPAQDPLPAH SGALPFPSPG PPQPPHPPLA YGPAPSTRPM GPQAAPLTIR GPSSAGQSTP
SPHLVPSPAP SPGPGPVPPR PPAAEPPPCL RRGAAAADLL SSSPESQHGG TQSPGGGQPL
LQPTKVDAAE GRRPQALRLI ERDPYEHPER LRQLQQELEA FRGQLGDVGA LDTVWRELQD
AQEHDARGRS IAIARCYSLK NRHQDVMPYD SNRVVLRSGK DDYINASCVE GLSPYCPPLV
ATQAPLPGTA ADFWLMVHEQ KVSVIVMLVS EAEMEKQKVA RYFPTERGQP MVHGALSLAL
SSVRSTETHV ERVLSLQFRD QSLKRSLVHL HFPTWPELGL PDSPSNLLRF IQEVHAHYLH
QRPLHTPIIV HCSSGVGRTG AFALLYAAVQ EVEAGNGIPE LPQLVRRMRQ QRKHMLQEKL
HLRFCYEAVV RHVEQVLQRH GVPPPCKPLA SASISQKNHL PQDSQDLVLG GDVPISSIQA
TIAKLSIRPP GGLESPVASL PGPAEPPGLP PASLPESTPI PSSSPPPLSS PLPEAPQPKE
EPPVPEAPSS GPPSSSLELL ASLTPEAFSL DSSLRGKQRM SKHNFLQAHN GQGLRATRPS
DDPLSLLDPL WTLNKT
//
ID PTN23_HUMAN Reviewed; 1636 AA.
AC Q9H3S7; A8K0D7; Q7KZF8; Q8N6Z5; Q9BSR5; Q9P257; Q9UG03; Q9UMZ4;
read moreDT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 23;
DE EC=3.1.3.48;
DE AltName: Full=His domain-containing protein tyrosine phosphatase;
DE Short=HD-PTP;
DE AltName: Full=Protein tyrosine phosphatase TD14;
DE Short=PTP-TD14;
GN Name=PTPN23; Synonyms=KIAA1471;
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], VARIANT SER-1099, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Stomach cancer;
RX PubMed=11095967; DOI=10.1006/bbrc.2000.3870;
RA Toyooka S., Ouchida M., Jitsumori Y., Tsukuda K., Sakai A.,
RA Nakamura A., Shimizu N., Shimizu K.;
RT "HD-PTP: a novel protein tyrosine phosphatase gene on human chromosome
RT 3p21.3.";
RL Biochem. Biophys. Res. Commun. 278:671-678(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Qu X., Zhai Y., Wei H., Zhang C., Xing G., Lu C., Wang M., He F.;
RT "Cloning, chromosomal assignment and tissue expression of a novel
RT human protein tyrosine phosphatase (PTP-TD14) gene.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle, Ovary, and Skin;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1383, AND VARIANT THR-944.
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [7]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 647-1636, AND VARIANT
RP THR-944.
RC TISSUE=Brain;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1060-1636.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1351-1493.
RA Dayton M.A., Blanchard K.L.;
RT "Differential expression of PTPase RNAs resulting from K562
RT differentiation induced by PMA.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1123, AND MASS
RP SPECTROMETRY.
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).
RN [12]
RP FUNCTION, INTERACTION WITH CHMP4B, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LEU-202 AND ILE-206.
RX PubMed=18434552; DOI=10.1073/pnas.0707601105;
RA Doyotte A., Mironov A., McKenzie E., Woodman P.;
RT "The Bro1-related protein HD-PTP/PTPN23 is required for endosomal
RT cargo sorting and multivesicular body morphogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6308-6313(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1123, AND MASS
RP SPECTROMETRY.
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).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20393563; DOI=10.1038/nature08895;
RA Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K.,
RA Ideker T., Aza-Blanc P., Gleeson J.G.;
RT "Functional genomic screen for modulators of ciliogenesis and cilium
RT length.";
RL Nature 464:1048-1051(2010).
RN [15]
RP INTERACTION WITH GRAP2 AND GRB2, AND SUBCELLULAR LOCATION.
RX PubMed=21179510; DOI=10.1371/journal.pone.0014339;
RA Tanase C.A.;
RT "Histidine domain-protein tyrosine phosphatase interacts with Grb2 and
RT GrpL.";
RL PLoS ONE 5:E14339-E14339(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP FUNCTION, INTERACTION WITH UBAP1, SUBCELLULAR LOCTION, AND MUTAGENESIS
RP OF PHE-678.
RX PubMed=21757351; DOI=10.1016/j.cub.2011.06.028;
RA Stefani F., Zhang L., Taylor S., Donovan J., Rollinson S., Doyotte A.,
RA Brownhill K., Bennion J., Pickering-Brown S., Woodman P.;
RT "UBAP1 is a component of an endosome-specific ESCRT-I complex that is
RT essential for MVB sorting.";
RL Curr. Biol. 21:1245-1250(2011).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 2-361.
RX PubMed=21889351; DOI=10.1016/j.str.2011.07.016;
RA Sette P., Mu R., Dussupt V., Jiang J., Snyder G., Smith P., Xiao T.S.,
RA Bouamr F.;
RT "The Phe105 loop of Alix Bro1 domain plays a key role in HIV-1
RT release.";
RL Structure 19:1485-1495(2011).
CC -!- FUNCTION: Plays a role in sorting of endocytic ubiquitinated
CC cargos into multivesicular bodies (MVBs) via its interaction with
CC the ESCRT-I complex (endosomal sorting complex required for
CC transport I), and possibly also other ESCRT complexes. May act as
CC a negative regulator of Ras-mediated mitogenic activity. Plays a
CC role in ciliogenesis.
CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- SUBUNIT: Interacts with GRAP2 and GRB2. Interacts with UBAP1 and
CC CHMP4B.
CC -!- INTERACTION:
CC Q9H444:CHMP4B; NbExp=2; IntAct=EBI-724478, EBI-749627;
CC O75791:GRAP2; NbExp=8; IntAct=EBI-724478, EBI-740418;
CC O89100:Grap2 (xeno); NbExp=2; IntAct=EBI-724478, EBI-642151;
CC P62993:GRB2; NbExp=6; IntAct=EBI-724478, EBI-401755;
CC O75340:PDCD6; NbExp=3; IntAct=EBI-724478, EBI-352915;
CC Q05397:PTK2; NbExp=4; IntAct=EBI-724478, EBI-702142;
CC Q99962:SH3GL2; NbExp=2; IntAct=EBI-724478, EBI-77938;
CC Q99816:TSG101; NbExp=2; IntAct=EBI-724478, EBI-346882;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasmic vesicle.
CC Endosome. Cytoplasm, cytoskeleton, cilium basal body. Early
CC endosome.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Non-receptor class subfamily.
CC -!- SIMILARITY: Contains 1 BRO1 domain.
CC -!- SIMILARITY: Contains 2 TPR repeats.
CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95995.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AB025194; BAB19280.1; -; mRNA.
DR EMBL; AF290614; AAK28025.1; -; mRNA.
DR EMBL; AK289502; BAF82191.1; -; mRNA.
DR EMBL; CH471055; EAW64823.1; -; Genomic_DNA.
DR EMBL; BC004881; AAH04881.2; -; mRNA.
DR EMBL; BC027711; AAH27711.2; -; mRNA.
DR EMBL; BC089042; AAH89042.1; -; mRNA.
DR EMBL; AB040904; BAA95995.2; ALT_INIT; mRNA.
DR EMBL; AL110210; CAB53676.1; -; mRNA.
DR EMBL; BT009758; AAP88760.1; -; mRNA.
DR EMBL; AF169350; AAD50276.1; -; mRNA.
DR PIR; T14756; T14756.
DR RefSeq; NP_056281.1; NM_015466.2.
DR UniGene; Hs.25524; -.
DR PDB; 3RAU; X-ray; 1.95 A; A/B=2-361.
DR PDBsum; 3RAU; -.
DR ProteinModelPortal; Q9H3S7; -.
DR SMR; Q9H3S7; 4-697, 1142-1459.
DR DIP; DIP-29923N; -.
DR IntAct; Q9H3S7; 14.
DR MINT; MINT-1425077; -.
DR STRING; 9606.ENSP00000265562; -.
DR PhosphoSite; Q9H3S7; -.
DR DMDM; 68053318; -.
DR PaxDb; Q9H3S7; -.
DR PeptideAtlas; Q9H3S7; -.
DR PRIDE; Q9H3S7; -.
DR DNASU; 25930; -.
DR Ensembl; ENST00000265562; ENSP00000265562; ENSG00000076201.
DR GeneID; 25930; -.
DR KEGG; hsa:25930; -.
DR UCSC; uc003crf.1; human.
DR CTD; 25930; -.
DR GeneCards; GC03P047397; -.
DR HGNC; HGNC:14406; PTPN23.
DR HPA; HPA016845; -.
DR MIM; 606584; gene.
DR neXtProt; NX_Q9H3S7; -.
DR PharmGKB; PA33996; -.
DR eggNOG; COG5599; -.
DR HOVERGEN; HBG082231; -.
DR InParanoid; Q9H3S7; -.
DR KO; K01104; -.
DR OMA; IARCYTM; -.
DR OrthoDB; EOG72C4ZH; -.
DR PhylomeDB; Q9H3S7; -.
DR ChiTaRS; PTPN23; human.
DR EvolutionaryTrace; Q9H3S7; -.
DR GeneWiki; PTPN23; -.
DR GenomeRNAi; 25930; -.
DR NextBio; 47476; -.
DR PRO; PR:Q9H3S7; -.
DR ArrayExpress; Q9H3S7; -.
DR Bgee; Q9H3S7; -.
DR CleanEx; HS_PTPN23; -.
DR Genevestigator; Q9H3S7; -.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005932; C:microtubule basal body; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0060271; P:cilium morphogenesis; IMP:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB.
DR Gene3D; 1.25.40.280; -; 1.
DR InterPro; IPR025304; ALIX_V_dom.
DR InterPro; IPR004328; BRO1_dom.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR Pfam; PF13949; ALIX_LYPXL_bnd; 1.
DR Pfam; PF03097; BRO1; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM01041; BRO1; 1.
DR SMART; SM00194; PTPc; 1.
DR PROSITE; PS51180; BRO1; 1.
DR PROSITE; PS50005; TPR; FALSE_NEG.
DR PROSITE; PS50293; TPR_REGION; FALSE_NEG.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Endosome; Hydrolase; Nucleus; Phosphoprotein;
KW Polymorphism; Protein phosphatase; Protein transport;
KW Reference proteome; Repeat; TPR repeat; Transport.
FT CHAIN 1 1636 Tyrosine-protein phosphatase non-receptor
FT type 23.
FT /FTId=PRO_0000094777.
FT DOMAIN 8 394 BRO1.
FT REPEAT 250 283 TPR 1.
FT REPEAT 374 407 TPR 2.
FT REPEAT 953 954 1.
FT REPEAT 955 956 2.
FT REPEAT 957 958 3.
FT REPEAT 959 960 4.
FT REPEAT 961 962 5.
FT REPEAT 963 964 6.
FT DOMAIN 1192 1452 Tyrosine-protein phosphatase.
FT REGION 770 1130 His.
FT REGION 953 964 6 X 2 AA approximate tandem repeats of P-
FT Q.
FT COILED 550 623 Potential.
FT COMPBIAS 716 1108 Pro-rich.
FT COMPBIAS 1509 1573 Pro-rich.
FT ACT_SITE 1392 1392 Phosphocysteine intermediate (By
FT similarity).
FT MOD_RES 1123 1123 Phosphoserine.
FT VARIANT 944 944 A -> T (in dbSNP:rs6780013).
FT /FTId=VAR_022682.
FT VARIANT 1099 1099 P -> S (in a lung cancer cell line; may
FT be a common polymorphism;
FT dbSNP:rs149563514).
FT /FTId=VAR_022683.
FT MUTAGEN 202 202 L->D: Nearly abolishes interaction with
FT CHMP4B. Abolishes interaction with
FT CHMP4B; when associated with D-206.
FT MUTAGEN 206 206 I->D: Abolishes interaction with CHMP4B;
FT when associated with D-202.
FT MUTAGEN 678 678 F->D: Abolishes interaction with UBAP1.
FT CONFLICT 647 647 L -> G (in Ref. 8; CAB53676).
FT CONFLICT 1087 1087 S -> P (in Ref. 8; CAB53676).
FT STRAND 17 20
FT HELIX 23 32
FT TURN 38 41
FT HELIX 42 56
FT HELIX 62 81
FT STRAND 94 97
FT TURN 99 101
FT STRAND 104 108
FT HELIX 110 131
FT HELIX 137 160
FT HELIX 167 169
FT HELIX 171 195
FT HELIX 200 221
FT HELIX 224 230
FT HELIX 233 262
FT HELIX 266 286
FT TURN 287 289
FT HELIX 292 318
FT HELIX 327 329
FT HELIX 349 352
FT TURN 356 359
SQ SEQUENCE 1636 AA; 178974 MW; 536BDDF9D3DC95C0 CRC64;
MEAVPRMPMI WLDLKEAGDF HFQPAVKKFV LKNYGENPEA YNEELKKLEL LRQNAVRVPR
DFEGCSVLRK YLGQLHYLQS RVPMGSGQEA AVPVTWTEIF SGKSVAHEDI KYEQACILYN
LGALHSMLGA MDKRVSEEGM KVSCTHFQCA AGAFAYLREH FPQAYSVDMS RQILTLNVNL
MLGQAQECLL EKSMLDNRKS FLVARISAQV VDYYKEACRA LENPDTASLL GRIQKDWKKL
VQMKIYYFAA VAHLHMGKQA EEQQKFGERV AYFQSALDKL NEAIKLAKGQ PDTVQDALRF
TMDVIGGKYN SAKKDNDFIY HEAVPALDTL QPVKGAPLVK PLPVNPTDPA VTGPDIFAKL
VPMAAHEASS LYSEEKAKLL REMMAKIEDK NEVLDQFMDS MQLDPETVDN LDAYSHIPPQ
LMEKCAALSV RPDTVRNLVQ SMQVLSGVFT DVEASLKDIR DLLEEDELLE QKFQEAVGQA
GAISITSKAE LAEVRREWAK YMEVHEKASF TNSELHRAMN LHVGNLRLLS GPLDQVRAAL
PTPALSPEDK AVLQNLKRIL AKVQEMRDQR VSLEQQLREL IQKDDITASL VTTDHSEMKK
LFEEQLKKYD QLKVYLEQNL AAQDRVLCAL TEANVQYAAV RRVLSDLDQK WNSTLQTLVA
SYEAYEDLMK KSQEGRDFYA DLESKVAALL ERTQSTCQAR EAARQQLLDR ELKKKPPPRP
TAPKPLLPRR EESEAVEAGD PPEELRSLPP DMVAGPRLPD TFLGSATPLH FPPSPFPSST
GPGPHYLSGP LPPGTYSGPT QLIQPRAPGP HAMPVAPGPA LYPAPAYTPE LGLVPRSSPQ
HGVVSSPYVG VGPAPPVAGL PSAPPPQFSG PELAMAVRPA TTTVDSIQAP IPSHTAPRPN
PTPAPPPPCF PVPPPQPLPT PYTYPAGAKQ PIPAQHHFSS GIPAGFPAPR IGPQPQPHPQ
PHPSQAFGPQ PPQQPLPLQH PHLFPPQAPG LLPPQSPYPY APQPGVLGQP PPPLHTQLYP
GPAQDPLPAH SGALPFPSPG PPQPPHPPLA YGPAPSTRPM GPQAAPLTIR GPSSAGQSTP
SPHLVPSPAP SPGPGPVPPR PPAAEPPPCL RRGAAAADLL SSSPESQHGG TQSPGGGQPL
LQPTKVDAAE GRRPQALRLI ERDPYEHPER LRQLQQELEA FRGQLGDVGA LDTVWRELQD
AQEHDARGRS IAIARCYSLK NRHQDVMPYD SNRVVLRSGK DDYINASCVE GLSPYCPPLV
ATQAPLPGTA ADFWLMVHEQ KVSVIVMLVS EAEMEKQKVA RYFPTERGQP MVHGALSLAL
SSVRSTETHV ERVLSLQFRD QSLKRSLVHL HFPTWPELGL PDSPSNLLRF IQEVHAHYLH
QRPLHTPIIV HCSSGVGRTG AFALLYAAVQ EVEAGNGIPE LPQLVRRMRQ QRKHMLQEKL
HLRFCYEAVV RHVEQVLQRH GVPPPCKPLA SASISQKNHL PQDSQDLVLG GDVPISSIQA
TIAKLSIRPP GGLESPVASL PGPAEPPGLP PASLPESTPI PSSSPPPLSS PLPEAPQPKE
EPPVPEAPSS GPPSSSLELL ASLTPEAFSL DSSLRGKQRM SKHNFLQAHN GQGLRATRPS
DDPLSLLDPL WTLNKT
//
MIM
606584
*RECORD*
*FIELD* NO
606584
*FIELD* TI
*606584 PROTEIN-TYROSINE PHOSPHATASE, NONRECEPTOR-TYPE, 23; PTPN23
;;HIS-DOMAIN PROTEIN-TYROSINE PHOSPHATASE; HDPTP;;
read moreKIAA1471
*FIELD* TX
CLONING
Toyooka et al. (2000) isolated a cDNA encoding a novel protein tyrosine
phosphatase, PTPN23, from a gastric cancer cell line. The predicted
protein contains at least 1,636 amino acids and has several features
distinct from those in previously identified PTPs, the most striking of
which is the sequence VHCSSG instead of the invariant VHCSAG sequence at
the PTP active center. PTPN23 contains a zinc-hand domain, which the
authors called a 'His domain' (HD); several SH3-binding motifs; a
tyrosine phosphatase domain; a C-terminal PEST motif; and an N-terminal
domain similar to yeast BRO1, mouse rhophilin (601031), and human AIP1
(605555). It appears to be the homolog of rat PTP-TD14 which has been
found to inhibit activated H-ras-mediated cell transformation (Cao et
al., 1998). Northern blot analysis in rat revealed ubiquitous expression
of a 6-kb PTPN23 transcript. Expression experiments demonstrated that
PTPN23 is distributed within the cytoplasm.
In the RERF-LCMA small cell lung cancer cell line (see 182280), Toyooka
et al. (2000) identified a hemizygous missense mutation in the PTPN23
gene, a CCT-to-TCT change resulting in a pro1099-to-ser substitution.
The mutation causes an alteration in the structure of one of the
SH3-binding motifs within the His domain.
GENE FUNCTION
In a functional genomic screen using RNA interference, Kim et al. (2010)
identified PTPN23 as a gene involved in ciliogenesis control. Silencing
of PTPN23 greatly reduced the number of ciliated cells in functional
assays.
GENE STRUCTURE
Toyooka et al. (2000) determined that the PTPN23 gene contains at least
25 exons.
MAPPING
By radiation hybrid analysis and sequence analysis, Toyooka et al.
(2000) mapped the PTPN23 gene between markers WI-11814 and WI-18411 on
chromosome 3p21.3, within a putative tumor suppressor region.
*FIELD* RF
1. Cao, L.; Zhang, L.; Ruiz-Lazano, P.; Yang, Q.; Chien, K. R.; Graham,
R. M.; Zhou, M.: A novel putative protein-tyrosine phosphatase contains
a BRO1-like domain and suppresses Ha-ras-mediated transformation. J.
Biol. Chem. 273: 21077-21083, 1998.
2. Kim, J.; Lee, J. E.; Heynen-Genel, S.; Suyama, E.; Ono, K.; Lee,
K.; Ideker, T.; Aza-Blanc, P.; Gleeson, J. G.: Functional genomic
screen for modulators of ciliogenesis and cilium length. Nature 464:
1048-1051, 2010.
3. Toyooka, S.; Ouchida, M.; Jitsumori, Y.; Tsukuda, K.; Sakai, A.;
Nakamura, A.; Shimizu, N.; Shimizu, K.: HD-PTP: a novel protein tyrosine
phosphatase gene on human chromosome 3p21.3. Biochem. Biophys. Res.
Commun. 278: 671-678, 2000.
*FIELD* CN
Ada Hamosh - updated: 05/10/2010
*FIELD* CD
Carol A. Bocchini: 12/27/2001
*FIELD* ED
alopez: 05/10/2010
alopez: 4/13/2007
terry: 3/5/2002
carol: 1/3/2002
terry: 12/27/2001
carol: 12/27/2001
*RECORD*
*FIELD* NO
606584
*FIELD* TI
*606584 PROTEIN-TYROSINE PHOSPHATASE, NONRECEPTOR-TYPE, 23; PTPN23
;;HIS-DOMAIN PROTEIN-TYROSINE PHOSPHATASE; HDPTP;;
read moreKIAA1471
*FIELD* TX
CLONING
Toyooka et al. (2000) isolated a cDNA encoding a novel protein tyrosine
phosphatase, PTPN23, from a gastric cancer cell line. The predicted
protein contains at least 1,636 amino acids and has several features
distinct from those in previously identified PTPs, the most striking of
which is the sequence VHCSSG instead of the invariant VHCSAG sequence at
the PTP active center. PTPN23 contains a zinc-hand domain, which the
authors called a 'His domain' (HD); several SH3-binding motifs; a
tyrosine phosphatase domain; a C-terminal PEST motif; and an N-terminal
domain similar to yeast BRO1, mouse rhophilin (601031), and human AIP1
(605555). It appears to be the homolog of rat PTP-TD14 which has been
found to inhibit activated H-ras-mediated cell transformation (Cao et
al., 1998). Northern blot analysis in rat revealed ubiquitous expression
of a 6-kb PTPN23 transcript. Expression experiments demonstrated that
PTPN23 is distributed within the cytoplasm.
In the RERF-LCMA small cell lung cancer cell line (see 182280), Toyooka
et al. (2000) identified a hemizygous missense mutation in the PTPN23
gene, a CCT-to-TCT change resulting in a pro1099-to-ser substitution.
The mutation causes an alteration in the structure of one of the
SH3-binding motifs within the His domain.
GENE FUNCTION
In a functional genomic screen using RNA interference, Kim et al. (2010)
identified PTPN23 as a gene involved in ciliogenesis control. Silencing
of PTPN23 greatly reduced the number of ciliated cells in functional
assays.
GENE STRUCTURE
Toyooka et al. (2000) determined that the PTPN23 gene contains at least
25 exons.
MAPPING
By radiation hybrid analysis and sequence analysis, Toyooka et al.
(2000) mapped the PTPN23 gene between markers WI-11814 and WI-18411 on
chromosome 3p21.3, within a putative tumor suppressor region.
*FIELD* RF
1. Cao, L.; Zhang, L.; Ruiz-Lazano, P.; Yang, Q.; Chien, K. R.; Graham,
R. M.; Zhou, M.: A novel putative protein-tyrosine phosphatase contains
a BRO1-like domain and suppresses Ha-ras-mediated transformation. J.
Biol. Chem. 273: 21077-21083, 1998.
2. Kim, J.; Lee, J. E.; Heynen-Genel, S.; Suyama, E.; Ono, K.; Lee,
K.; Ideker, T.; Aza-Blanc, P.; Gleeson, J. G.: Functional genomic
screen for modulators of ciliogenesis and cilium length. Nature 464:
1048-1051, 2010.
3. Toyooka, S.; Ouchida, M.; Jitsumori, Y.; Tsukuda, K.; Sakai, A.;
Nakamura, A.; Shimizu, N.; Shimizu, K.: HD-PTP: a novel protein tyrosine
phosphatase gene on human chromosome 3p21.3. Biochem. Biophys. Res.
Commun. 278: 671-678, 2000.
*FIELD* CN
Ada Hamosh - updated: 05/10/2010
*FIELD* CD
Carol A. Bocchini: 12/27/2001
*FIELD* ED
alopez: 05/10/2010
alopez: 4/13/2007
terry: 3/5/2002
carol: 1/3/2002
terry: 12/27/2001
carol: 12/27/2001