PTN23_HUMAN
ID PTN23_HUMAN Reviewed; 1636 AA.
AC Q9H3S7; A8K0D7; Q7KZF8; Q8N6Z5; Q9BSR5; Q9P257; Q9UG03; Q9UMZ4;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 177.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-1099, AND SUBCELLULAR 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., Nakamura A.,
RA 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 human
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT 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 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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 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 differentiation
RT induced by PMA.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1123, AND IDENTIFICATION BY
RP 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).
RN [12]
RP FUNCTION, INTERACTION WITH CHMP4B, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 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 cargo
RT 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
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., Ideker T.,
RA 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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 LOCATION, AND MUTAGENESIS OF
RP 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., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1122 AND THR-1131, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-950 AND ARG-1615, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [23]
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 release.";
RL Structure 19:1485-1495(2011).
RN [24] {ECO:0007744|PDB:5LM1, ECO:0007744|PDB:5LM2}
RP X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 362-713 IN COMPLEX WITH UBAP1,
RP AND MUTAGENESIS OF PHE-678.
RX PubMed=27839950; DOI=10.1016/j.str.2016.10.006;
RA Gahloth D., Levy C., Heaven G., Stefani F., Wunderley L., Mould P.,
RA Cliff M.J., Bella J., Fielding A.J., Woodman P., Tabernero L.;
RT "Structural basis for selective interaction between the ESCRT regulator HD-
RT PTP and UBAP1.";
RL Structure 24:2115-2126(2016).
RN [25]
RP VARIANT NEDBASS LEU-1332, AND INVOLVEMENT IN NEDBASS.
RX PubMed=25558065; DOI=10.1016/j.celrep.2014.12.015;
RA Alazami A.M., Patel N., Shamseldin H.E., Anazi S., Al-Dosari M.S.,
RA Alzahrani F., Hijazi H., Alshammari M., Aldahmesh M.A., Salih M.A.,
RA Faqeih E., Alhashem A., Bashiri F.A., Al-Owain M., Kentab A.Y., Sogaty S.,
RA Al Tala S., Temsah M.H., Tulbah M., Aljelaify R.F., Alshahwan S.A.,
RA Seidahmed M.Z., Alhadid A.A., Aldhalaan H., Alqallaf F., Kurdi W.,
RA Alfadhel M., Babay Z., Alsogheer M., Kaya N., Al-Hassnan Z.N.,
RA Abdel-Salam G.M., Al-Sannaa N., Al Mutairi F., El Khashab H.Y., Bohlega S.,
RA Jia X., Nguyen H.C., Hammami R., Adly N., Mohamed J.Y., Abdulwahab F.,
RA Ibrahim N., Naim E.A., Al-Younes B., Meyer B.F., Hashem M., Shaheen R.,
RA Xiong Y., Abouelhoda M., Aldeeri A.A., Monies D.M., Alkuraya F.S.;
RT "Accelerating novel candidate gene discovery in neurogenetic disorders via
RT whole-exome sequencing of prescreened multiplex consanguineous families.";
RL Cell Rep. 10:148-161(2015).
RN [26]
RP VARIANT NEDBASS VAL-302, AND INVOLVEMENT IN NEDBASS.
RX PubMed=27848944; DOI=10.1038/ejhg.2016.146;
RA Trujillano D., Bertoli-Avella A.M., Kumar Kandaswamy K., Weiss M.E.,
RA Koester J., Marais A., Paknia O., Schroeder R., Garcia-Aznar J.M.,
RA Werber M., Brandau O., Calvo Del Castillo M., Baldi C., Wessel K.,
RA Kishore S., Nahavandi N., Eyaid W., Al Rifai M.T., Al-Rumayyan A.,
RA Al-Twaijri W., Alothaim A., Alhashem A., Al-Sannaa N., Al-Balwi M.,
RA Alfadhel M., Rolfs A., Abou Jamra R.;
RT "Clinical exome sequencing: results from 2819 samples reflecting 1000
RT families.";
RL Eur. J. Hum. Genet. 25:176-182(2017).
RN [27]
RP VARIANTS NEDBASS LEU-532 AND 1196-ARG--THR-1636 DEL, AND INVOLVEMENT IN
RP NEDBASS.
RX PubMed=29090338; DOI=10.1007/s00439-017-1850-3;
RA Sowada N., Hashem M.O., Yilmaz R., Hamad M., Kakar N., Thiele H.,
RA Arold S.T., Bode H., Alkuraya F.S., Borck G.;
RT "Mutations of PTPN23 in developmental and epileptic encephalopathy.";
RL Hum. Genet. 136:1455-1461(2017).
RN [28]
RP VARIANT NEDBASS LYS-634, AND INVOLVEMENT IN NEDBASS.
RX PubMed=29899372; DOI=10.1038/s41431-018-0179-2;
RA Smigiel R., Landsberg G., Schilling M., Rydzanicz M., Pollak A.,
RA Walczak A., Stodolak A., Stawinski P., Mierzewska H., Sasiadek M.M.,
RA Gruss O.J., Ploski R.;
RT "Developmental epileptic encephalopathy with hypomyelination and brain
RT atrophy associated with PTPN23 variants affecting the assembly of
RT UsnRNPs.";
RL Eur. J. Hum. Genet. 26:1502-1511(2018).
RN [29]
RP VARIANTS NEDBASS GLN-232; TRP-431; ARG-583; LEU-829; 857-VAL--PRO-865 DEL;
RP TYR-894; ARG-916; 960-GLN--PRO-963 DEL; HIS-1017; LYS-1250 AND LYS-1296
RP DEL.
RX PubMed=31395947; DOI=10.1038/s41431-019-0487-1;
RG Regeneron Genetics Center;
RA Bend R., Cohen L., Carter M.T., Lyons M.J., Niyazov D., Mikati M.A.,
RA Rojas S.K., Person R.E., Si Y., Wentzensen I.M., Torti E., Lee J.A.,
RA Boycott K.M., Basel-Salmon L., Ferreira C.R., Gonzaga-Jauregui C.;
RT "Phenotype and mutation expansion of the PTPN23 associated disorder
RT characterized by neurodevelopmental delay and structural brain
RT abnormalities.";
RL Eur. J. Hum. Genet. 28:76-87(2020).
CC -!- FUNCTION: Plays a role in sorting of endocytic ubiquitinated cargos
CC into multivesicular bodies (MVBs) via its interaction with the ESCRT-I
CC complex (endosomal sorting complex required for transport I), and
CC possibly also other ESCRT complexes (PubMed:18434552, PubMed:21757351).
CC May act as a negative regulator of Ras-mediated mitogenic activity
CC (PubMed:18434552). Plays a role in ciliogenesis (PubMed:20393563).
CC {ECO:0000269|PubMed:18434552, ECO:0000269|PubMed:20393563,
CC ECO:0000269|PubMed:21757351}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBUNIT: Interacts with GRAP2 and GRB2 (PubMed:21179510). Interacts
CC with UBAP1 (PubMed:21757351, PubMed:27839950). Interacts with CHMP4B
CC (PubMed:18434552). {ECO:0000269|PubMed:18434552,
CC ECO:0000269|PubMed:21179510, ECO:0000269|PubMed:21757351,
CC ECO:0000269|PubMed:27839950}.
CC -!- INTERACTION:
CC Q9H3S7; Q96LK0: CEP19; NbExp=3; IntAct=EBI-724478, EBI-741885;
CC Q9H3S7; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-724478, EBI-747776;
CC Q9H3S7; Q9H444: CHMP4B; NbExp=4; IntAct=EBI-724478, EBI-749627;
CC Q9H3S7; O75791: GRAP2; NbExp=6; IntAct=EBI-724478, EBI-740418;
CC Q9H3S7; P62993: GRB2; NbExp=7; IntAct=EBI-724478, EBI-401755;
CC Q9H3S7; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-724478, EBI-945833;
CC Q9H3S7; O75340: PDCD6; NbExp=3; IntAct=EBI-724478, EBI-352915;
CC Q9H3S7; P25788: PSMA3; NbExp=3; IntAct=EBI-724478, EBI-348380;
CC Q9H3S7; Q05397: PTK2; NbExp=4; IntAct=EBI-724478, EBI-702142;
CC Q9H3S7; Q99962: SH3GL2; NbExp=2; IntAct=EBI-724478, EBI-77938;
CC Q9H3S7; P14373: TRIM27; NbExp=3; IntAct=EBI-724478, EBI-719493;
CC Q9H3S7; Q99816: TSG101; NbExp=2; IntAct=EBI-724478, EBI-346882;
CC Q9H3S7; O89100: Grap2; Xeno; NbExp=3; IntAct=EBI-724478, EBI-642151;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasmic vesicle.
CC Endosome. Cytoplasm, cytoskeleton, cilium basal body. Early endosome.
CC -!- DISEASE: Neurodevelopmental disorder and structural brain anomalies
CC with or without seizures and spasticity (NEDBASS) [MIM:618890]: An
CC autosomal recessive disorder characterized by global developmental
CC delay, brain abnormalities, mainly ventriculomegaly and/or brain
CC atrophy, intellectual disability, absent speech, peripheral spasticity,
CC and microcephaly. Additional variable features include early-onset
CC seizures, optic atrophy, and dysmorphic facial features. Early death
CC may occur. {ECO:0000269|PubMed:25558065, ECO:0000269|PubMed:27848944,
CC ECO:0000269|PubMed:29090338, ECO:0000269|PubMed:29899372,
CC ECO:0000269|PubMed:31395947}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95995.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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 CCDS; CCDS2754.1; -.
DR PIR; T14756; T14756.
DR RefSeq; NP_001291411.1; NM_001304482.1.
DR RefSeq; NP_056281.1; NM_015466.3.
DR PDB; 3RAU; X-ray; 1.95 A; A/B=2-361.
DR PDB; 5CRU; X-ray; 2.40 A; A/B/C/D=1-361.
DR PDB; 5CRV; X-ray; 2.00 A; A/B=1-361.
DR PDB; 5LM1; X-ray; 2.55 A; A=362-713.
DR PDB; 5LM2; X-ray; 2.54 A; A/B=362-713.
DR PDB; 5MJY; X-ray; 2.25 A; A/B/C/D=1-361.
DR PDB; 5MJZ; X-ray; 1.87 A; A/B=1-361.
DR PDB; 5MK0; X-ray; 1.76 A; A/C=1-361.
DR PDB; 5MK1; X-ray; 2.50 A; A/B/C/D=1-361.
DR PDB; 5MK2; X-ray; 1.70 A; A/B=1-361.
DR PDB; 5MK3; X-ray; 2.00 A; A/B/C/D=1-361.
DR PDBsum; 3RAU; -.
DR PDBsum; 5CRU; -.
DR PDBsum; 5CRV; -.
DR PDBsum; 5LM1; -.
DR PDBsum; 5LM2; -.
DR PDBsum; 5MJY; -.
DR PDBsum; 5MJZ; -.
DR PDBsum; 5MK0; -.
DR PDBsum; 5MK1; -.
DR PDBsum; 5MK2; -.
DR PDBsum; 5MK3; -.
DR AlphaFoldDB; Q9H3S7; -.
DR SMR; Q9H3S7; -.
DR BioGRID; 117430; 108.
DR DIP; DIP-29923N; -.
DR IntAct; Q9H3S7; 45.
DR MINT; Q9H3S7; -.
DR STRING; 9606.ENSP00000265562; -.
DR DEPOD; PTPN23; -.
DR GlyGen; Q9H3S7; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q9H3S7; -.
DR PhosphoSitePlus; Q9H3S7; -.
DR BioMuta; PTPN23; -.
DR DMDM; 68053318; -.
DR EPD; Q9H3S7; -.
DR jPOST; Q9H3S7; -.
DR MassIVE; Q9H3S7; -.
DR MaxQB; Q9H3S7; -.
DR PaxDb; Q9H3S7; -.
DR PeptideAtlas; Q9H3S7; -.
DR PRIDE; Q9H3S7; -.
DR ProteomicsDB; 80750; -.
DR Antibodypedia; 12918; 151 antibodies from 25 providers.
DR DNASU; 25930; -.
DR Ensembl; ENST00000265562.5; ENSP00000265562.4; ENSG00000076201.16.
DR GeneID; 25930; -.
DR KEGG; hsa:25930; -.
DR MANE-Select; ENST00000265562.5; ENSP00000265562.4; NM_015466.4; NP_056281.1.
DR UCSC; uc003crf.2; human.
DR CTD; 25930; -.
DR DisGeNET; 25930; -.
DR GeneCards; PTPN23; -.
DR HGNC; HGNC:14406; PTPN23.
DR HPA; ENSG00000076201; Low tissue specificity.
DR MalaCards; PTPN23; -.
DR MIM; 606584; gene.
DR MIM; 618890; phenotype.
DR neXtProt; NX_Q9H3S7; -.
DR OpenTargets; ENSG00000076201; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA33996; -.
DR VEuPathDB; HostDB:ENSG00000076201; -.
DR eggNOG; KOG0789; Eukaryota.
DR eggNOG; KOG2220; Eukaryota.
DR GeneTree; ENSGT00940000157687; -.
DR HOGENOM; CLU_001129_0_0_1; -.
DR InParanoid; Q9H3S7; -.
DR OMA; GPTQLMQ; -.
DR OrthoDB; 550620at2759; -.
DR PhylomeDB; Q9H3S7; -.
DR TreeFam; TF323502; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; Q9H3S7; -.
DR Reactome; R-HSA-9008059; Interleukin-37 signaling.
DR SignaLink; Q9H3S7; -.
DR BioGRID-ORCS; 25930; 661 hits in 1091 CRISPR screens.
DR ChiTaRS; PTPN23; human.
DR EvolutionaryTrace; Q9H3S7; -.
DR GeneWiki; PTPN23; -.
DR GenomeRNAi; 25930; -.
DR Pharos; Q9H3S7; Tbio.
DR PRO; PR:Q9H3S7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9H3S7; protein.
DR Bgee; ENSG00000076201; Expressed in sural nerve and 159 other tissues.
DR ExpressionAtlas; Q9H3S7; baseline and differential.
DR Genevisible; Q9H3S7; HS.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IMP:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0045022; P:early endosome to late endosome transport; IMP:FlyBase.
DR GO; GO:0032456; P:endocytic recycling; IMP:FlyBase.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:1903393; P:positive regulation of adherens junction organization; IMP:UniProtKB.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; IMP:UniProtKB.
DR GO; GO:1903387; P:positive regulation of homophilic cell adhesion; IMP:UniProtKB.
DR GO; GO:0061357; P:positive regulation of Wnt protein secretion; IMP:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
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 Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR025304; ALIX_V_dom.
DR InterPro; IPR045251; BRO1-like.
DR InterPro; IPR004328; BRO1_dom.
DR InterPro; IPR038499; BRO1_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR23030; PTHR23030; 1.
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 SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51180; BRO1; 1.
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; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Disease variant;
KW Endosome; Epilepsy; Hydrolase; Intellectual disability; Methylation;
KW Nucleus; Phosphoprotein; Protein phosphatase; Protein transport;
KW Reference proteome; Repeat; TPR repeat; Transport.
FT CHAIN 1..1636
FT /note="Tyrosine-protein phosphatase non-receptor type 23"
FT /id="PRO_0000094777"
FT DOMAIN 8..394
FT /note="BRO1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT REPEAT 250..283
FT /note="TPR 1"
FT REPEAT 374..407
FT /note="TPR 2"
FT REPEAT 953..954
FT /note="1"
FT REPEAT 955..956
FT /note="2"
FT REPEAT 957..958
FT /note="3"
FT REPEAT 959..960
FT /note="4"
FT REPEAT 961..962
FT /note="5"
FT REPEAT 963..964
FT /note="6"
FT DOMAIN 1192..1452
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 701..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..1130
FT /note="His"
FT REGION 888..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..964
FT /note="6 X 2 AA approximate tandem repeats of P-Q"
FT REGION 1513..1636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 550..623
FT /evidence="ECO:0000255"
FT COMPBIAS 704..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..926
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..1019
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1055
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1108
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1520..1570
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1392
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 950
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 1131
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1615
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VARIANT 232
FT /note="R -> Q (in NEDBASS; unknown pathological
FT significance; dbSNP:rs577689618)"
FT /evidence="ECO:0000269|PubMed:31395947"
FT /id="VAR_084289"
FT VARIANT 302
FT /note="M -> V (in NEDBASS; unknown pathological
FT significance; dbSNP:rs748601492)"
FT /evidence="ECO:0000269|PubMed:27848944"
FT /id="VAR_084290"
FT VARIANT 431
FT /note="R -> W (in NEDBASS; unknown pathological
FT significance; dbSNP:rs150712932)"
FT /evidence="ECO:0000269|PubMed:31395947"
FT /id="VAR_084291"
FT VARIANT 532
FT /note="P -> L (in NEDBASS; dbSNP:rs1401681748)"
FT /evidence="ECO:0000269|PubMed:29090338"
FT /id="VAR_084292"
FT VARIANT 583
FT /note="K -> R (in NEDBASS; when associated in cis with H-
FT 1017; unknown pathological significance;
FT dbSNP:rs147293860)"
FT /evidence="ECO:0000269|PubMed:31395947"
FT /id="VAR_084293"
FT VARIANT 634
FT /note="N -> K (in NEDBASS)"
FT /evidence="ECO:0000269|PubMed:29899372"
FT /id="VAR_084294"
FT VARIANT 829
FT /note="P -> L (in NEDBASS; unknown pathological
FT significance; dbSNP:rs138076291)"
FT /evidence="ECO:0000269|PubMed:31395947"
FT /id="VAR_084295"
FT VARIANT 857..865
FT /note="Missing (in NEDBASS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31395947"
FT /id="VAR_084296"
FT VARIANT 894
FT /note="H -> Y (in NEDBASS; unknown pathological
FT significance; dbSNP:rs967738491)"
FT /evidence="ECO:0000269|PubMed:31395947"
FT /id="VAR_084297"
FT VARIANT 916
FT /note="Q -> R (in NEDBASS; unknown pathological
FT significance; dbSNP:rs770692989)"
FT /evidence="ECO:0000269|PubMed:31395947"
FT /id="VAR_084298"
FT VARIANT 944
FT /note="A -> T (in dbSNP:rs6780013)"
FT /evidence="ECO:0000269|PubMed:10819331,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_022682"
FT VARIANT 960..963
FT /note="Missing (in NEDBASS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31395947"
FT /id="VAR_084299"
FT VARIANT 1017
FT /note="Q -> H (in NEDBASS; when associated in cis with R-
FT 583; unknown pathological significance; dbSNP:rs201017613)"
FT /evidence="ECO:0000269|PubMed:31395947"
FT /id="VAR_084300"
FT VARIANT 1099
FT /note="P -> S (in dbSNP:rs149563514)"
FT /evidence="ECO:0000269|PubMed:11095967"
FT /id="VAR_022683"
FT VARIANT 1196..1636
FT /note="Missing (in NEDBASS)"
FT /evidence="ECO:0000269|PubMed:29090338"
FT /id="VAR_084301"
FT VARIANT 1250
FT /note="E -> K (in NEDBASS; unknown pathological
FT significance; dbSNP:rs148689441)"
FT /evidence="ECO:0000269|PubMed:31395947"
FT /id="VAR_084302"
FT VARIANT 1296
FT /note="Missing (in NEDBASS; unknown pathological
FT significance; dbSNP:rs751809435)"
FT /evidence="ECO:0000269|PubMed:31395947"
FT /id="VAR_084303"
FT VARIANT 1332
FT /note="R -> L (in NEDBASS; unknown pathological
FT significance; dbSNP:rs730882229)"
FT /evidence="ECO:0000269|PubMed:25558065"
FT /id="VAR_084304"
FT MUTAGEN 202
FT /note="L->D: Nearly abolishes interaction with CHMP4B.
FT Abolishes interaction with CHMP4B; when associated with D-
FT 206."
FT /evidence="ECO:0000269|PubMed:18434552"
FT MUTAGEN 206
FT /note="I->D: Abolishes interaction with CHMP4B; when
FT associated with D-202."
FT /evidence="ECO:0000269|PubMed:18434552"
FT MUTAGEN 678
FT /note="F->S,D: Abolishes interaction with UBAP1."
FT /evidence="ECO:0000269|PubMed:21757351,
FT ECO:0000269|PubMed:27839950"
FT CONFLICT 647
FT /note="L -> G (in Ref. 8; CAB53676)"
FT /evidence="ECO:0000305"
FT CONFLICT 1087
FT /note="S -> P (in Ref. 8; CAB53676)"
FT /evidence="ECO:0000305"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:5MK2"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:5MK2"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:5MK2"
FT HELIX 42..56
FT /evidence="ECO:0007829|PDB:5MK2"
FT HELIX 62..81
FT /evidence="ECO:0007829|PDB:5MK2"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:5MK2"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:5MK2"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:5MK2"
FT HELIX 110..131
FT /evidence="ECO:0007829|PDB:5MK2"
FT HELIX 137..160
FT /evidence="ECO:0007829|PDB:5MK2"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:5MK2"
FT HELIX 171..195
FT /evidence="ECO:0007829|PDB:5MK2"
FT HELIX 200..221
FT /evidence="ECO:0007829|PDB:5MK2"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:5MK2"
FT HELIX 232..262
FT /evidence="ECO:0007829|PDB:5MK2"
FT HELIX 266..286
FT /evidence="ECO:0007829|PDB:5MK2"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:5MK2"
FT HELIX 292..318
FT /evidence="ECO:0007829|PDB:5MK2"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:5MK2"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:5MK2"
FT TURN 356..359
FT /evidence="ECO:0007829|PDB:5MK2"
FT HELIX 365..370
FT /evidence="ECO:0007829|PDB:5LM2"
FT HELIX 373..400
FT /evidence="ECO:0007829|PDB:5LM2"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:5LM2"
FT HELIX 419..429
FT /evidence="ECO:0007829|PDB:5LM2"
FT HELIX 434..475
FT /evidence="ECO:0007829|PDB:5LM2"
FT HELIX 490..529
FT /evidence="ECO:0007829|PDB:5LM2"
FT HELIX 533..539
FT /evidence="ECO:0007829|PDB:5LM2"
FT HELIX 547..583
FT /evidence="ECO:0007829|PDB:5LM2"
FT TURN 588..591
FT /evidence="ECO:0007829|PDB:5LM1"
FT HELIX 601..605
FT /evidence="ECO:0007829|PDB:5LM2"
FT HELIX 606..609
FT /evidence="ECO:0007829|PDB:5LM2"
FT HELIX 610..621
FT /evidence="ECO:0007829|PDB:5LM2"
FT HELIX 623..635
FT /evidence="ECO:0007829|PDB:5LM2"
FT HELIX 638..703
FT /evidence="ECO:0007829|PDB:5LM2"
FT TURN 704..707
FT /evidence="ECO:0007829|PDB:5LM2"
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
