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PP1B_HUMAN
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   03-AUG-2022, entry version 194.
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>3.0.co;2-9;
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   CAUTION.
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   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   [21]
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   [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=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   [23]
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   [24]
RP   CAUTION, AND RETRACTION NOTICE OF PUBMED:23186163.
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   [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; 361.
DR   DIP; DIP-33220N; -.
DR   IntAct; P62140; 264.
DR   MINT; P62140; -.
DR   STRING; 9606.ENSP00000378769; -.
DR   ChEMBL; CHEMBL4546; -.
DR   DEPOD; PPP1CB; -.
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; P62140; -.
DR   PeptideAtlas; P62140; -.
DR   PRIDE; P62140; -.
DR   ProteomicsDB; 57367; -.
DR   TopDownProteomics; P62140; -.
DR   Antibodypedia; 28856; 521 antibodies from 33 providers.
DR   DNASU; 5500; -.
DR   Ensembl; ENST00000296122.10; ENSP00000296122.6; ENSG00000213639.10.
DR   Ensembl; ENST00000358506.6; ENSP00000351298.2; ENSG00000213639.10.
DR   Ensembl; ENST00000395366.3; ENSP00000378769.2; ENSG00000213639.10.
DR   GeneID; 5500; -.
DR   KEGG; hsa:5500; -.
DR   MANE-Select; ENST00000395366.3; ENSP00000378769.2; NM_002709.3; NP_002700.1.
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; TVQMSEN; -.
DR   OrthoDB; 766640at2759; -.
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; 692 hits in 1089 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 209 other 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:0005886; C:plasma membrane; IDA:HPA.
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   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   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; SSF56300; 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; unknown pathological 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
 
 
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