ID PP1B_HUMAN Reviewed; 327 AA.
AC P62140; B2R5V4; D6W565; P37140; Q5U087; Q6FG45;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 203.
DE RecName: Full=Serine/threonine-protein phosphatase PP1-beta catalytic subunit;
DE Short=PP-1B;
DE Short=PPP1CD;
DE EC=3.1.3.16;
DE EC=3.1.3.53;
GN Name=PPP1CB;
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].
RX PubMed=8312365; DOI=10.1016/0167-4889(94)90138-4;
RA Barker H.M., Brewis N.D., Street A.J., Spurr N.K., Cohen P.T.W.;
RT "Three genes for protein phosphatase 1 map to different human chromosomes:
RT sequence, expression and gene localisation of protein serine/threonine
RT phosphatase 1 beta (PPP1CB).";
RL Biochim. Biophys. Acta 1220:212-218(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7796987; DOI=10.1007/bf00410284;
RA Prochazka M., Mochizuki H., Baier L.J., Cohen P.T.W., Bogardus C.;
RT "Molecular and linkage analysis of type-1 protein phosphatase catalytic
RT beta-subunit gene: lack of evidence for its major role in insulin
RT resistance in Pima Indians.";
RL Diabetologia 38:461-466(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Umbilical vein;
RX PubMed=10906760;
RX DOI=10.1002/1097-4644(2000)79:1<113::aid-jcb110>3.3.co;2-0;
RA Verin A.D., Csortos C., Durbin S.D., Aydanyan A., Wang P., Patterson C.E.,
RA Garcia J.G.;
RT "Characterization of the protein phosphatase 1 catalytic subunit in
RT endothelium: involvement in contractile responses.";
RL J. Cell. Biochem. 79:113-125(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Endometrium;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [9]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [11]
RP PROTEIN SEQUENCE OF 2-14, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [12]
RP INTERACTION WITH PPP1R12C.
RX PubMed=11399775; DOI=10.1074/jbc.m102615200;
RA Tan I., Ng C.H., Lim L., Leung T.;
RT "Phosphorylation of a novel myosin binding subunit of protein phosphatase 1
RT reveals a conserved mechanism in the regulation of actin cytoskeleton.";
RL J. Biol. Chem. 276:21209-21216(2001).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=11739654; DOI=10.1242/jcs.114.23.4219;
RA Trinkle-Mulcahy L., Sleeman J.E., Lamond A.I.;
RT "Dynamic targeting of protein phosphatase 1 within the nuclei of living
RT mammalian cells.";
RL J. Cell Sci. 114:4219-4228(2001).
RN [14]
RP INTERACTION WITH PPP1R15A.
RX PubMed=11564868; DOI=10.1128/mcb.21.20.6841-6850.2001;
RA Connor J.H., Weiser D.C., Li S., Hallenbeck J.M., Shenolikar S.;
RT "Growth arrest and DNA damage-inducible protein GADD34 assembles a novel
RT signaling complex containing protein phosphatase 1 and inhibitor 1.";
RL Mol. Cell. Biol. 21:6841-6850(2001).
RN [15]
RP INTERACTION WITH PPP1R7.
RX PubMed=12226088; DOI=10.1074/jbc.m206838200;
RA Ceulemans H., Vulsteke V., De Maeyer M., Tatchell K., Stalmans W.,
RA Bollen M.;
RT "Binding of the concave surface of the Sds22 superhelix to the alpha
RT 4/alpha 5/alpha 6-triangle of protein phosphatase-1.";
RL J. Biol. Chem. 277:47331-47337(2002).
RN [16]
RP ACTIVITY REGULATION.
RX PubMed=15705855; DOI=10.1126/science.1101902;
RA Boyce M., Bryant K.F., Jousse C., Long K., Harding H.P., Scheuner D.,
RA Kaufman R.J., Ma D., Coen D.M., Ron D., Yuan J.;
RT "A selective inhibitor of eIF2alpha dephosphorylation protects cells from
RT ER stress.";
RL Science 307:935-939(2005).
RN [17]
RP INTERACTION WITH PPP1R16B.
RX PubMed=18586956; DOI=10.1152/ajplung.00325.2007;
RA Csortos C., Czikora I., Bogatcheva N.V., Adyshev D.M., Poirier C., Olah G.,
RA Verin A.D.;
RT "TIMAP is a positive regulator of pulmonary endothelial barrier function.";
RL Am. J. Physiol. 295:L440-L450(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, 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 [19]
RP RETRACTED PAPER.
RX PubMed=19377461; DOI=10.1038/nature07954;
RA Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
RA Kitagawa H., Kato S.;
RT "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced
RT granulopoiesis.";
RL Nature 459:455-459(2009).
RN [20]
RP CAUTION, AND RETRACTION NOTICE OF PUBMED:19377461.
RX PubMed=24336203; DOI=10.1038/nature12896;
RA Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
RA Kitagawa H., Kato S.;
RT "Retraction: GlcNAcylation of a histone methyltransferase in retinoic-acid-
RT induced granulopoiesis.";
RL Nature 505:574-574(2014).
RN [21]
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 [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, 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 [25]
RP IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION, AND
RP INTERACTION WITH PPP1R8.
RX PubMed=20516061; DOI=10.1074/jbc.m110.109801;
RA Lee J.H., You J., Dobrota E., Skalnik D.G.;
RT "Identification and characterization of a novel human PP1 phosphatase
RT complex.";
RL J. Biol. Chem. 285:24466-24476(2010).
RN [26]
RP INTERACTION WITH RRP1B, AND SUBCELLULAR LOCATION.
RX PubMed=20926688; DOI=10.1091/mbc.e10-04-0287;
RA Chamousset D., De Wever V., Moorhead G.B., Chen Y., Boisvert F.M.,
RA Lamond A.I., Trinkle-Mulcahy L.;
RT "RRP1B targets PP1 to mammalian cell nucleoli and is associated with pre-
RT 60S ribosomal subunits.";
RL Mol. Biol. Cell 21:4212-4226(2010).
RN [27]
RP INTERACTION WITH NUAK1 AND PPP1R12A.
RX PubMed=20354225; DOI=10.1126/scisignal.2000616;
RA Zagorska A., Deak M., Campbell D.G., Banerjee S., Hirano M., Aizawa S.,
RA Prescott A.R., Alessi D.R.;
RT "New roles for the LKB1-NUAK pathway in controlling myosin phosphatase
RT complexes and cell adhesion.";
RL Sci. Signal. 3:RA25-RA25(2010).
RN [28]
RP INTERACTION WITH TRIM28.
RX PubMed=20424263; DOI=10.1126/scisignal.2000781;
RA Li X., Lin H.H., Chen H., Xu X., Shih H.M., Ann D.K.;
RT "SUMOylation of the transcriptional co-repressor KAP1 is regulated by the
RT serine and threonine phosphatase PP1.";
RL Sci. Signal. 3:RA32-RA32(2010).
RN [29]
RP FUNCTION IN CIRCADIAN CLOCK.
RX PubMed=21712997; DOI=10.1371/journal.pone.0021325;
RA Schmutz I., Wendt S., Schnell A., Kramer A., Mansuy I.M., Albrecht U.;
RT "Protein phosphatase 1 (PP1) is a post-translational regulator of the
RT mammalian circadian clock.";
RL PLoS ONE 6:E21325-E21325(2011).
RN [30]
RP FUNCTION, INTERACTION WITH FOXP3, AND INDUCTION.
RX PubMed=23396208; DOI=10.1038/nm.3085;
RA Nie H., Zheng Y., Li R., Guo T.B., He D., Fang L., Liu X., Xiao L.,
RA Chen X., Wan B., Chin Y.E., Zhang J.Z.;
RT "Phosphorylation of FOXP3 controls regulatory T cell function and is
RT inhibited by TNF-alpha in rheumatoid arthritis.";
RL Nat. Med. 19:322-328(2013).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [32]
RP INVOLVEMENT IN NSLH2, AND VARIANTS NSLH2 ARG-49 AND PRO-56.
RX PubMed=27264673; DOI=10.1002/ajmg.a.37781;
RA Gripp K.W., Aldinger K.A., Bennett J.T., Baker L., Tusi J.,
RA Powell-Hamilton N., Stabley D., Sol-Church K., Timms A.E., Dobyns W.B.;
RT "A novel rasopathy caused by recurrent de novo missense mutations in PPP1CB
RT closely resembles Noonan syndrome with loose anagen hair.";
RL Am. J. Med. Genet. A 170:2237-2247(2016).
RN [33]
RP INVOLVEMENT IN NSLH2, AND VARIANTS NSLH2 ARG-49; ALA-183; VAL-183; TYR-252
RP AND LYS-274.
RX PubMed=27681385; DOI=10.1007/s00439-016-1731-1;
RA Ma L., Bayram Y., McLaughlin H.M., Cho M.T., Krokosky A., Turner C.E.,
RA Lindstrom K., Bupp C.P., Mayberry K., Mu W., Bodurtha J., Weinstein V.,
RA Zadeh N., Alcaraz W., Powis Z., Shao Y., Scott D.A., Lewis A.M.,
RA White J.J., Jhangiani S.N., Gulec E.Y., Lalani S.R., Lupski J.R.,
RA Retterer K., Schnur R.E., Wentzensen I.M., Bale S., Chung W.K.;
RT "De novo missense variants in PPP1CB are associated with intellectual
RT disability and congenital heart disease.";
RL Hum. Genet. 135:1399-1409(2016).
RN [34]
RP INVOLVEMENT IN NSLH2, AND VARIANT NSLH2 ARG-49.
RX PubMed=27868344; DOI=10.1002/ajmg.a.38056;
RA Zambrano R.M., Marble M., Chalew S.A., Lilje C., Vargas A., Lacassie Y.;
RT "Further evidence that variants in PPP1CB cause a rasopathy similar to
RT Noonan syndrome with loose anagen hair.";
RL Am. J. Med. Genet. A 173:565-567(2017).
RN [35]
RP INVOLVEMENT IN NSLH2, AND VARIANT NSLH2 ARG-49.
RX PubMed=28211982; DOI=10.1002/ajmg.a.38070;
RA Bertola D., Yamamoto G., Buscarilli M., Jorge A., Passos-Bueno M.R.,
RA Kim C.;
RT "The recurrent PPP1CB mutation p.Pro49Arg in an additional Noonan-like
RT syndrome individual: Broadening the clinical phenotype.";
RL Am. J. Med. Genet. A 173:824-828(2017).
RN [36]
RP INTERACTION WITH SERPINE1.
RX PubMed=28296156; DOI=10.1111/jcmm.13127;
RA Yao H., He G., Chen C., Yan S., Lu L., Song L., Vijayan K.V., Li Q.,
RA Xiong L., Miao X., Deng X.;
RT "PAI1: a novel PP1-interacting protein that mediates human plasma's anti-
RT apoptotic effect in endothelial cells.";
RL J. Cell. Mol. Med. 21:2068-2076(2017).
RN [37]
RP VARIANT NSLH2 ARG-49, AND INTERACTION WITH LZTR1.
RX PubMed=30368668; DOI=10.1007/s00439-018-1951-7;
RA Umeki I., Niihori T., Abe T., Kanno S.I., Okamoto N., Mizuno S.,
RA Kurosawa K., Nagasaki K., Yoshida M., Ohashi H., Inoue S.I., Matsubara Y.,
RA Fujiwara I., Kure S., Aoki Y.;
RT "Delineation of LZTR1 mutation-positive patients with Noonan syndrome and
RT identification of LZTR1 binding to RAF1-PPP1CB complexes.";
RL Hum. Genet. 138:21-35(2019).
CC -!- FUNCTION: Protein phosphatase that associates with over 200 regulatory
CC proteins to form highly specific holoenzymes which dephosphorylate
CC hundreds of biological targets. Protein phosphatase (PP1) is essential
CC for cell division, it participates in the regulation of glycogen
CC metabolism, muscle contractility and protein synthesis. Involved in
CC regulation of ionic conductances and long-term synaptic plasticity.
CC Component of the PTW/PP1 phosphatase complex, which plays a role in the
CC control of chromatin structure and cell cycle progression during the
CC transition from mitosis into interphase. In balance with CSNK1D and
CC CSNK1E, determines the circadian period length, through the regulation
CC of the speed and rhythmicity of PER1 and PER2 phosphorylation. May
CC dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418'
CC residue of FOXP3 in regulatory T-cells (Treg) from patients with
CC rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg
CC cells functionally defective (PubMed:23396208).
CC {ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:21712997,
CC ECO:0000269|PubMed:23396208}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[myosin light chain] = L-seryl-[myosin
CC light chain] + phosphate; Xref=Rhea:RHEA:12849, Rhea:RHEA-COMP:13684,
CC Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.53;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[myosin light chain] = L-threonyl-
CC [myosin light chain] + phosphate; Xref=Rhea:RHEA:53988, Rhea:RHEA-
CC COMP:13686, Rhea:RHEA-COMP:13687, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.53;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by the toxins okadaic acid, tautomycin
CC and microcystin Leu-Arg (By similarity). The phosphatase activity of
CC the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited by
CC Salubrinal, a drug that protects cells from endoplasmic reticulum
CC stress. {ECO:0000250, ECO:0000269|PubMed:15705855}.
CC -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC,
CC which is folded into its native form by inhibitor 2 and glycogen
CC synthetase kinase 3, and then complexed to one or several targeting or
CC regulatory subunits. The targeting or regulatory subunits determine the
CC substrate specificity of PP1. PPP1R12A, PPP1R12B and PPP1R12C mediate
CC binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver),
CC PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen.
CC Part of a complex containing PPP1R15B, PP1 and NCK1/2 (By similarity).
CC Interacts with PPP1R7 and PPP1R12C. PPP1R15A and PPP1R15B mediate
CC binding to EIF2S1. Interacts with PPP1R16B. Component of the PTW/PP1
CC phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA
CC or PPP1CB or PPP1CC. Interacts with PPP1R8. Interacts with TRIM28; the
CC interaction is weak. Interacts with PPP1R12A and NUAK1; the interaction
CC is direct. Interacts with FOXP3. Interacts with RRP1B
CC (PubMed:20926688). Interacts with SERPINE1 (PubMed:28296156). Interacts
CC with LZTR1 (PubMed:30368668). {ECO:0000250|UniProtKB:P62141,
CC ECO:0000269|PubMed:11399775, ECO:0000269|PubMed:11564868,
CC ECO:0000269|PubMed:12226088, ECO:0000269|PubMed:18586956,
CC ECO:0000269|PubMed:20354225, ECO:0000269|PubMed:20424263,
CC ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:20926688,
CC ECO:0000269|PubMed:23396208, ECO:0000269|PubMed:28296156,
CC ECO:0000269|PubMed:30368668}.
CC -!- INTERACTION:
CC P62140; P35609: ACTN2; NbExp=3; IntAct=EBI-352350, EBI-77797;
CC P62140; P38398: BRCA1; NbExp=3; IntAct=EBI-352350, EBI-349905;
CC P62140; Q9NX63: CHCHD3; NbExp=3; IntAct=EBI-352350, EBI-743375;
CC P62140; Q96S65: CSRNP1; NbExp=3; IntAct=EBI-352350, EBI-4311573;
CC P62140; Q9H175: CSRNP2; NbExp=7; IntAct=EBI-352350, EBI-5235958;
CC P62140; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-352350, EBI-3867333;
CC P62140; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-352350, EBI-2556193;
CC P62140; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-352350, EBI-16439278;
CC P62140; Q8N912: NRAC; NbExp=3; IntAct=EBI-352350, EBI-12051377;
CC P62140; Q96KR7: PHACTR3; NbExp=3; IntAct=EBI-352350, EBI-717068;
CC P62140; O60927: PPP1R11; NbExp=8; IntAct=EBI-352350, EBI-1048104;
CC P62140; A0A0S2Z4Q8: PPP1R12B; NbExp=3; IntAct=EBI-352350, EBI-16434210;
CC P62140; Q8WUF5: PPP1R13L; NbExp=6; IntAct=EBI-352350, EBI-5550163;
CC P62140; Q96I34: PPP1R16A; NbExp=10; IntAct=EBI-352350, EBI-710402;
CC P62140; Q96T49: PPP1R16B; NbExp=5; IntAct=EBI-352350, EBI-10293968;
CC P62140; Q86WC6: PPP1R27; NbExp=3; IntAct=EBI-352350, EBI-5235602;
CC P62140; Q6NXS1: PPP1R2B; NbExp=8; IntAct=EBI-352350, EBI-10251630;
CC P62140; O14990: PPP1R2C; NbExp=5; IntAct=EBI-352350, EBI-12404293;
CC P62140; Q9UQK1: PPP1R3C; NbExp=9; IntAct=EBI-352350, EBI-2506727;
CC P62140; Q15435: PPP1R7; NbExp=10; IntAct=EBI-352350, EBI-1024281;
CC P62140; Q96SB3: PPP1R9B; NbExp=2; IntAct=EBI-352350, EBI-351275;
CC P62140; Q14684: RRP1B; NbExp=3; IntAct=EBI-352350, EBI-372051;
CC P62140; Q9H788: SH2D4A; NbExp=18; IntAct=EBI-352350, EBI-747035;
CC P62140; Q9H0A9-2: SPATC1L; NbExp=3; IntAct=EBI-352350, EBI-11995806;
CC P62140; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-352350, EBI-5235340;
CC P62140; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-352350, EBI-11952721;
CC P62140; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-352350, EBI-10175039;
CC P62140; O08785: Clock; Xeno; NbExp=2; IntAct=EBI-352350, EBI-79859;
CC P62140; Q76TK5: ORF23; Xeno; NbExp=2; IntAct=EBI-352350, EBI-14033469;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11739654}. Nucleus
CC {ECO:0000269|PubMed:11739654}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:11739654}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:11739654, ECO:0000269|PubMed:20926688}. Note=Highly
CC mobile in cells and can be relocalized through interaction with
CC targeting subunits. In the presence of PPP1R8 relocalizes from the
CC nucleus to nuclear speckles. {ECO:0000269|PubMed:11739654}.
CC -!- INDUCTION: Up-regulated in synovial fluid mononuclear cells and
CC peripheral blood mononuclear cells from patients with rheumatoid
CC arthritis. {ECO:0000269|PubMed:23396208}.
CC -!- DISEASE: Noonan syndrome-like disorder with loose anagen hair 2 (NSLH2)
CC [MIM:617506]: A syndrome characterized by Noonan dysmorphic features
CC such as macrocephaly, high forehead, hypertelorism, palpebral ptosis,
CC low-set and posteriorly rotated ears, short and webbed neck, pectus
CC anomalies, in association with pluckable, sparse, thin and slow-growing
CC hair. {ECO:0000269|PubMed:27264673, ECO:0000269|PubMed:27681385,
CC ECO:0000269|PubMed:27868344, ECO:0000269|PubMed:28211982,
CC ECO:0000269|PubMed:30368668}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be part of the MLL5-L complex, at
CC least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and
CC OGT (PubMed:19377461). However, the corresponding article has been
CC retracted (PubMed:24336203). {ECO:0000269|PubMed:19377461,
CC ECO:0000269|PubMed:24336203}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The things we forget - Issue
CC 32 of March 2003;
CC URL="https://web.expasy.org/spotlight/back_issues/032";
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DR EMBL; X80910; CAA56870.1; -; mRNA.
DR EMBL; U11005; AAA85093.1; -; Genomic_DNA.
DR EMBL; U10998; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; U10999; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; U11000; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; U11001; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; U11002; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; U11003; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; U11004; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; AF092905; AAF01137.1; -; mRNA.
DR EMBL; CR542263; CAG47059.1; -; mRNA.
DR EMBL; CR542285; CAG47080.1; -; mRNA.
DR EMBL; BT019744; AAV38549.1; -; mRNA.
DR EMBL; AK312329; BAG35251.1; -; mRNA.
DR EMBL; BX647970; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC097724; AAY24124.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00527.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00528.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00529.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00530.1; -; Genomic_DNA.
DR EMBL; BC002697; AAH02697.1; -; mRNA.
DR EMBL; BC012045; AAH12045.1; -; mRNA.
DR CCDS; CCDS33169.1; -.
DR PIR; S41052; S41052.
DR RefSeq; NP_002700.1; NM_002709.2.
DR RefSeq; NP_996759.1; NM_206876.1.
DR AlphaFoldDB; P62140; -.
DR SMR; P62140; -.
DR BioGRID; 111494; 461.
DR DIP; DIP-33220N; -.
DR IntAct; P62140; 272.
DR MINT; P62140; -.
DR STRING; 9606.ENSP00000378769; -.
DR ChEMBL; CHEMBL4546; -.
DR DEPOD; PPP1CB; -.
DR GlyGen; P62140; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62140; -.
DR MetOSite; P62140; -.
DR PhosphoSitePlus; P62140; -.
DR SwissPalm; P62140; -.
DR BioMuta; PPP1CB; -.
DR DMDM; 49065814; -.
DR OGP; P37140; -.
DR EPD; P62140; -.
DR jPOST; P62140; -.
DR MassIVE; P62140; -.
DR PaxDb; 9606-ENSP00000378769; -.
DR PeptideAtlas; P62140; -.
DR PRIDE; P62140; -.
DR ProteomicsDB; 57367; -.
DR Pumba; P62140; -.
DR TopDownProteomics; P62140; -.
DR Antibodypedia; 28856; 573 antibodies from 33 providers.
DR DNASU; 5500; -.
DR Ensembl; ENST00000296122.10; ENSP00000296122.6; ENSG00000213639.11.
DR Ensembl; ENST00000395366.3; ENSP00000378769.2; ENSG00000213639.11.
DR Ensembl; ENST00000420282.6; ENSP00000398839.2; ENSG00000213639.11.
DR Ensembl; ENST00000441461.6; ENSP00000414918.2; ENSG00000213639.11.
DR Ensembl; ENST00000703173.1; ENSP00000515219.1; ENSG00000213639.11.
DR GeneID; 5500; -.
DR KEGG; hsa:5500; -.
DR MANE-Select; ENST00000395366.3; ENSP00000378769.2; NM_002709.3; NP_002700.1.
DR AGR; HGNC:9282; -.
DR CTD; 5500; -.
DR DisGeNET; 5500; -.
DR GeneCards; PPP1CB; -.
DR HGNC; HGNC:9282; PPP1CB.
DR HPA; ENSG00000213639; Low tissue specificity.
DR MalaCards; PPP1CB; -.
DR MIM; 600590; gene.
DR MIM; 617506; phenotype.
DR neXtProt; NX_P62140; -.
DR OpenTargets; ENSG00000213639; -.
DR Orphanet; 2701; Noonan syndrome-like disorder with loose anagen hair.
DR PharmGKB; PA33610; -.
DR VEuPathDB; HostDB:ENSG00000213639; -.
DR eggNOG; KOG0374; Eukaryota.
DR GeneTree; ENSGT00940000154644; -.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; P62140; -.
DR OMA; FGEFDNA; -.
DR OrthoDB; 19833at2759; -.
DR PhylomeDB; P62140; -.
DR TreeFam; TF354243; -.
DR BRENDA; 3.1.3.16; 2681.
DR PathwayCommons; P62140; -.
DR Reactome; R-HSA-163560; Triglyceride catabolism.
DR Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
DR Reactome; R-HSA-5625900; RHO GTPases activate CIT.
DR Reactome; R-HSA-5627117; RHO GTPases Activate ROCKs.
DR Reactome; R-HSA-5627123; RHO GTPases activate PAKs.
DR Reactome; R-HSA-5673000; RAF activation.
DR Reactome; R-HSA-9726840; SHOC2 M1731 mutant abolishes MRAS complex function.
DR Reactome; R-HSA-9726842; Gain-of-function MRAS complexes activate RAF signaling.
DR SignaLink; P62140; -.
DR SIGNOR; P62140; -.
DR BioGRID-ORCS; 5500; 739 hits in 1192 CRISPR screens.
DR ChiTaRS; PPP1CB; human.
DR GeneWiki; PPP1CB; -.
DR GenomeRNAi; 5500; -.
DR Pharos; P62140; Tbio.
DR PRO; PR:P62140; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P62140; Protein.
DR Bgee; ENSG00000213639; Expressed in calcaneal tendon and 211 other cell types or tissues.
DR ExpressionAtlas; P62140; baseline and differential.
DR Genevisible; P62140; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; ISS:UniProtKB.
DR GO; GO:0050115; F:myosin-light-chain-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; IDA:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR CDD; cd07414; MPP_PP1_PPKL; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR11668:SF472; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1-BETA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Biological rhythms; Carbohydrate metabolism; Cell cycle;
KW Cell division; Cytoplasm; Direct protein sequencing; Disease variant;
KW Glycogen metabolism; Hydrolase; Manganese; Metal-binding; Nucleus;
KW Phosphoprotein; Protein phosphatase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..327
FT /note="Serine/threonine-protein phosphatase PP1-beta
FT catalytic subunit"
FT /id="PRO_0000058779"
FT REGION 305..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 124
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 316
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 49
FT /note="P -> R (in NSLH2; dbSNP:rs886037952)"
FT /evidence="ECO:0000269|PubMed:27264673,
FT ECO:0000269|PubMed:27681385, ECO:0000269|PubMed:27868344,
FT ECO:0000269|PubMed:28211982, ECO:0000269|PubMed:30368668"
FT /id="VAR_076839"
FT VARIANT 56
FT /note="A -> P (in NSLH2; dbSNP:rs1114167429)"
FT /evidence="ECO:0000269|PubMed:27264673"
FT /id="VAR_076840"
FT VARIANT 183
FT /note="E -> A (in NSLH2; dbSNP:rs886037954)"
FT /evidence="ECO:0000269|PubMed:27681385"
FT /id="VAR_079189"
FT VARIANT 183
FT /note="E -> V (in NSLH2; dbSNP:rs886037954)"
FT /evidence="ECO:0000269|PubMed:27681385"
FT /id="VAR_079190"
FT VARIANT 252
FT /note="D -> Y (in NSLH2; dbSNP:rs886037953)"
FT /evidence="ECO:0000269|PubMed:27681385"
FT /id="VAR_079191"
FT VARIANT 274
FT /note="E -> K (in NSLH2; uncertain significance;
FT dbSNP:rs886037955)"
FT /evidence="ECO:0000269|PubMed:27681385"
FT /id="VAR_079192"
FT CONFLICT 51
FT /note="L -> P (in Ref. 5; AAV38549)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 37187 MW; E8356022E9B94ECD CRC64;
MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI LLELEAPLKI
CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL
RGNHECASIN RIYGFYDECK RRFNIKLWKT FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ
SMEQIRRIMR PTDVPDTGLL CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL
DLICRAHQVV EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK
KAKYQYGGLN SGRPVTPPRT ANPPKKR
//
