CALX_HUMAN
ID CALX_HUMAN Reviewed; 592 AA.
AC P27824; B2R5V8; B4DGP8; B4E2T8; D3DWQ3; D6R9K3;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 235.
DE RecName: Full=Calnexin;
DE AltName: Full=IP90;
DE AltName: Full=Major histocompatibility complex class I antigen-binding protein p88;
DE AltName: Full=p90;
DE Flags: Precursor;
GN Name=CANX;
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] (ISOFORM 1).
RX PubMed=8486646; DOI=10.1016/s0021-9258(18)98391-2;
RA David V., Hochstenbach F., Rajagopalan S., Brenner M.B.;
RT "Interaction with newly synthesized and retained proteins in the
RT endoplasmic reticulum suggests a chaperone function for human integral
RT membrane protein IP90 (calnexin).";
RL J. Biol. Chem. 268:9585-9592(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lymph, and Placenta;
RX PubMed=8136357; DOI=10.1021/bi00177a013;
RA Tjoelker L.W., Seyfried C.E., Eddy R.L. Jr., Shows T.B. Jr., Calderon J.,
RA Schreiber R.B., Gray P.W.;
RT "Human, mouse, and rat calnexin cDNA cloning: identification of potential
RT calcium binding motifs and gene localization to human chromosome 5.";
RL Biochemistry 33:3229-3236(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Keratinocyte;
RX PubMed=8055875; DOI=10.1002/elps.1150150166;
RA Honore B., Rasmussen H.H., Celis A., Leffers H., Madsen P., Celis J.E.;
RT "The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin exhibit
RT strikingly different levels in quiescent keratinocytes as compared to their
RT proliferating normal and transformed counterparts: cDNA cloning and
RT expression of calnexin.";
RL Electrophoresis 15:482-490(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fibroblast;
RA Hansen J.J., Jorgensen M.M., Bolund L., Gregersen N.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, Cerebellum, and Trachea;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [9]
RP PROTEIN SEQUENCE OF 62-77; 171-193; 200-205; 221-227; 401-415; 517-525 AND
RP 574-582, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 237-592 (ISOFORM 1).
RX PubMed=1326756; DOI=10.1073/pnas.89.18.8452;
RA Galvin K., Krishna S., Ponchel F., Frohlich M., Cummings D.E., Carlson R.,
RA Wands J.R., Isselbacher K.J., Pillai S., Ozturk M.;
RT "The major histocompatibility complex class I antigen-binding protein p88
RT is the product of the calnexin gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8452-8456(1992).
RN [11]
RP PROTEIN SEQUENCE OF 275-286; 293-313; 383-398 AND 516-523.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [12]
RP INTERACTION WITH HBV LARGE ENVELOPE PROTEIN ISOFORM L (MICROBIAL
RP INFECTION).
RX PubMed=9188622; DOI=10.1128/jvi.71.7.5487-5494.1997;
RA Xu Z., Bruss V., Yen T.S.;
RT "Formation of intracellular particles by hepatitis B virus large surface
RT protein.";
RL J. Virol. 71:5487-5494(1997).
RN [13]
RP INTERACTION WITH HBV LARGE ENVELOPE PROTEIN ISOFORM M (MICROBIAL
RP INFECTION).
RX PubMed=9420286; DOI=10.1128/jvi.72.1.778-782.1998;
RA Werr M., Prange R.;
RT "Role for calnexin and N-linked glycosylation in the assembly and secretion
RT of hepatitis B virus middle envelope protein particles.";
RL J. Virol. 72:778-782(1998).
RN [14]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J.,
RA Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F.,
RA Appella E.;
RT "Proteomic analysis of early melanosomes: identification of novel
RT melanosomal proteins.";
RL J. Proteome Res. 2:69-79(2003).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-583, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [16]
RP INTERACTION WITH KCNH2.
RX PubMed=16361248; DOI=10.1074/jbc.m511765200;
RA Gong Q., Jones M.A., Zhou Z.;
RT "Mechanisms of pharmacological rescue of trafficking-defective hERG mutant
RT channels in human long QT syndrome.";
RL J. Biol. Chem. 281:4069-4074(2006).
RN [17]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-583, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-583, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-564, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564, 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 [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [25]
RP INTERACTION WITH PPIB.
RX PubMed=20801878; DOI=10.1074/jbc.m110.160101;
RA Kozlov G., Bastos-Aristizabal S., Maattanen P., Rosenauer A., Zheng F.,
RA Killikelly A., Trempe J.F., Thomas D.Y., Gehring K.;
RT "Structural basis of cyclophilin B binding by the calnexin/calreticulin P-
RT domain.";
RL J. Biol. Chem. 285:35551-35557(2010).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; SER-564 AND SER-583, AND
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 [27]
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 [28]
RP INTERACTION WITH ZNRF4, AND UBIQUITINATION.
RX PubMed=21205830; DOI=10.1074/jbc.m110.197459;
RA Neutzner A., Neutzner M., Benischke A.S., Ryu S.W., Frank S., Youle R.J.,
RA Karbowski M.;
RT "A systematic search for endoplasmic reticulum (ER) membrane-associated
RT RING finger proteins identifies Nixin/ZNRF4 as a regulator of calnexin
RT stability and ER homeostasis.";
RL J. Biol. Chem. 286:8633-8643(2011).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; THR-562 AND SER-583, AND
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 [30]
RP PALMITOYLATION AT CYS-502 AND CYS-503 BY DHHC6, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH SSR1.
RX PubMed=22314232; DOI=10.1038/emboj.2012.15;
RA Lakkaraju A.K., Abrami L., Lemmin T., Blaskovic S., Kunz B., Kihara A.,
RA Dal Peraro M., van der Goot F.G.;
RT "Palmitoylated calnexin is a key component of the ribosome-translocon
RT complex.";
RL EMBO J. 31:1823-1835(2012).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; THR-562; SER-564 AND
RP SER-583, AND IDENTIFICATION BY 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 [32]
RP INTERACTION WITH SERPINA2P AND SERPINA1, AND SUBCELLULAR LOCATION.
RX PubMed=23826168; DOI=10.1371/journal.pone.0066889;
RA Marques P.I., Ferreira Z., Martins M., Figueiredo J., Silva D.I.,
RA Castro P., Morales-Hojas R., Simoes-Correia J., Seixas S.;
RT "SERPINA2 is a novel gene with a divergent function from SERPINA1.";
RL PLoS ONE 8:E66889-E66889(2013).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; THR-562; SER-564 AND
RP SER-583, AND 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 [34]
RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-20, AND
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 [35]
RP INTERACTION WITH SMIM22.
RX PubMed=29765154; DOI=10.1038/s41388-018-0281-5;
RA Polycarpou-Schwarz M., Gross M., Mestdagh P., Schott J., Grund S.E.,
RA Hildenbrand C., Rom J., Aulmann S., Sinn H.P., Vandesompele J.,
RA Diederichs S.;
RT "The cancer-associated microprotein CASIMO1 controls cell proliferation and
RT interacts with squalene epoxidase modulating lipid droplet formation.";
RL Oncogene 37:4750-4768(2018).
RN [36]
RP INTERACTION WITH TMX2.
RX PubMed=31735293; DOI=10.1016/j.ajhg.2019.10.009;
RA Vandervore L.V., Schot R., Milanese C., Smits D.J., Kasteleijn E.,
RA Fry A.E., Pilz D.T., Brock S., Boerklue-Yuecel E., Post M.,
RA Bahi-Buisson N., Sanchez-Soler M.J., van Slegtenhorst M., Keren B.,
RA Afenjar A., Coury S.A., Tan W.H., Oegema R., de Vries L.S., Fawcett K.A.,
RA Nikkels P.G.J., Bertoli-Avella A., Al Hashem A., Alwabel A.A.,
RA Tlili-Graiess K., Efthymiou S., Zafar F., Rana N., Bibi F., Houlden H.,
RA Maroofian R., Person R.E., Crunk A., Savatt J.M., Turner L., Doosti M.,
RA Karimiani E.G., Saadi N.W., Akhondian J., Lequin M.H., Kayserili H.,
RA van der Spek P.J., Jansen A.C., Kros J.M., Verdijk R.M., Milosevic N.J.,
RA Fornerod M., Mastroberardino P.G., Mancini G.M.S.;
RT "TMX2 is a crucial regulator of cellular redox state, and its dysfunction
RT causes severe brain developmental abnormalities.";
RL Am. J. Hum. Genet. 105:1126-1147(2019).
RN [37]
RP INTERACTION WITH CHRNA7.
RX PubMed=32783947; DOI=10.1016/j.celrep.2020.108025;
RA Kweon H.J., Gu S., Witham E., Dhara M., Yu H., Mandon E.D., Jawhari A.,
RA Bredt D.S.;
RT "NACHO Engages N-Glycosylation ER Chaperone Pathways for alpha7 Nicotinic
RT Receptor Assembly.";
RL Cell Rep. 32:108025-108025(2020).
CC -!- FUNCTION: Calcium-binding protein that interacts with newly synthesized
CC monoglucosylated glycoproteins in the endoplasmic reticulum. It may act
CC in assisting protein assembly and/or in the retention within the ER of
CC unassembled protein subunits. It seems to play a major role in the
CC quality control apparatus of the ER by the retention of incorrectly
CC folded proteins. Associated with partial T-cell antigen receptor
CC complexes that escape the ER of immature thymocytes, it may function as
CC a signaling complex regulating thymocyte maturation. Additionally it
CC may play a role in receptor-mediated endocytosis at the synapse.
CC -!- SUBUNIT: Interacts with MAPK3/ERK1 (By similarity). Interacts with
CC KCNH2 (PubMed:16361248). Associates with ribosomes (By similarity).
CC Interacts with SGIP1; involved in negative regulation of endocytosis
CC (By similarity). The palmitoylated form interacts with the ribosome-
CC translocon complex component SSR1, promoting efficient folding of
CC glycoproteins (PubMed:22314232). Interacts with SERPINA2P/SERPINA2 and
CC with the S and Z variants of SERPINA1 (PubMed:23826168). Interacts with
CC PPIB (PubMed:20801878). Interacts with ZNRF4 (PubMed:21205830).
CC Interacts with SMIM22 (PubMed:29765154). Interacts with TMX2
CC (PubMed:31735293). Interacts with TMEM35A/NACHO (By similarity).
CC Interacts with CHRNA7 (PubMed:32783947). {ECO:0000250|UniProtKB:P35564,
CC ECO:0000250|UniProtKB:P35565, ECO:0000269|PubMed:16361248,
CC ECO:0000269|PubMed:20801878, ECO:0000269|PubMed:21205830,
CC ECO:0000269|PubMed:22314232, ECO:0000269|PubMed:23826168,
CC ECO:0000269|PubMed:29765154, ECO:0000269|PubMed:31735293,
CC ECO:0000269|PubMed:32783947}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HBV large envelope
CC protein, isoform L. {ECO:0000269|PubMed:9188622}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HBV large envelope
CC protein, isoform M; this association may be essential for isoform M
CC proper secretion. {ECO:0000269|PubMed:9188622}.
CC -!- INTERACTION:
CC P27824; O95477: ABCA1; NbExp=8; IntAct=EBI-355947, EBI-784112;
CC P27824; P13569: CFTR; NbExp=13; IntAct=EBI-355947, EBI-349854;
CC P27824; Q7LFX5: CHST15; NbExp=2; IntAct=EBI-355947, EBI-11123530;
CC P27824; Q9UHC6-1: CNTNAP2; NbExp=2; IntAct=EBI-355947, EBI-16594440;
CC P27824; Q92597: NDRG1; NbExp=2; IntAct=EBI-355947, EBI-716486;
CC P27824; P41143: OPRD1; NbExp=2; IntAct=EBI-355947, EBI-2624456;
CC P27824; P30050: RPL12; NbExp=3; IntAct=EBI-355947, EBI-352743;
CC P27824; P61619: SEC61A1; NbExp=4; IntAct=EBI-355947, EBI-358919;
CC P27824; P43307: SSR1; NbExp=6; IntAct=EBI-355947, EBI-714168;
CC P27824; P11607: ATP2A2; Xeno; NbExp=2; IntAct=EBI-355947, EBI-8004986;
CC P27824; P04578: env; Xeno; NbExp=3; IntAct=EBI-355947, EBI-6163496;
CC P27824-2; P05067: APP; NbExp=3; IntAct=EBI-25890990, EBI-77613;
CC P27824-2; P04271: S100B; NbExp=3; IntAct=EBI-25890990, EBI-458391;
CC P27824-2; P43405-2: SYK; NbExp=3; IntAct=EBI-25890990, EBI-25892332;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22314232}; Single-pass type I membrane protein
CC {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:22314232}.
CC Melanosome {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}.
CC Note=Identified by mass spectrometry in melanosome fractions from stage
CC I to stage IV (PubMed:12643545, PubMed:17081065). The palmitoylated
CC form preferentially localizes to the perinuclear rough ER
CC (PubMed:22314232). {ECO:0000269|PubMed:12643545,
CC ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:22314232}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P27824-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P27824-2; Sequence=VSP_055516;
CC Name=3;
CC IsoId=P27824-3; Sequence=VSP_055515;
CC -!- PTM: Phosphorylated at Ser-564 by MAPK3/ERK1. phosphorylation by
CC MAPK3/ERK1 increases its association with ribosomes (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Palmitoylation by DHHC6 leads to the preferential localization to
CC the perinuclear rough ER. It mediates the association of calnexin with
CC the ribosome-translocon complex (RTC) which is required for efficient
CC folding of glycosylated proteins. {ECO:0000269|PubMed:22314232}.
CC -!- PTM: Ubiquitinated, leading to proteasomal degradation. Probably
CC ubiquitinated by ZNRF4. {ECO:0000269|PubMed:21205830}.
CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Calnexin entry;
CC URL="https://en.wikipedia.org/wiki/Calnexin";
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DR EMBL; L10284; AAA36125.1; -; mRNA.
DR EMBL; L18887; AAA21013.1; -; mRNA.
DR EMBL; M94859; AAA21749.1; -; mRNA.
DR EMBL; M98452; AAA35696.1; -; mRNA.
DR EMBL; AK294702; BAG57859.1; -; mRNA.
DR EMBL; AK304420; BAG65250.1; -; mRNA.
DR EMBL; AK312334; BAG35255.1; -; mRNA.
DR EMBL; AC113426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC136604; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471165; EAW53802.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53803.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53805.1; -; Genomic_DNA.
DR EMBL; BC003552; AAH03552.1; -; mRNA.
DR EMBL; BC042843; AAH42843.1; -; mRNA.
DR EMBL; AJ271880; CAB72137.1; -; mRNA.
DR CCDS; CCDS4447.1; -. [P27824-1]
DR PIR; A46164; A46164.
DR PIR; A46673; A46673.
DR PIR; I53260; I53260.
DR RefSeq; NP_001019820.1; NM_001024649.1. [P27824-1]
DR RefSeq; NP_001737.1; NM_001746.3. [P27824-1]
DR RefSeq; XP_011532967.1; XM_011534665.2. [P27824-1]
DR AlphaFoldDB; P27824; -.
DR SMR; P27824; -.
DR BioGRID; 107271; 932.
DR CORUM; P27824; -.
DR DIP; DIP-457N; -.
DR IntAct; P27824; 566.
DR MINT; P27824; -.
DR STRING; 9606.ENSP00000247461; -.
DR BindingDB; P27824; -.
DR ChEMBL; CHEMBL2719; -.
DR DrugBank; DB00025; Antihemophilic factor, human recombinant.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR DrugBank; DB06245; Lanoteplase.
DR DrugBank; DB13998; Lonoctocog alfa.
DR DrugBank; DB13999; Moroctocog alfa.
DR DrugBank; DB00031; Tenecteplase.
DR TCDB; 8.A.165.1.1; the calnexin (calnexin) family.
DR GlyGen; P27824; 4 sites, 3 O-linked glycans (4 sites).
DR iPTMnet; P27824; -.
DR PhosphoSitePlus; P27824; -.
DR SwissPalm; P27824; -.
DR BioMuta; CANX; -.
DR DMDM; 543920; -.
DR EPD; P27824; -.
DR jPOST; P27824; -.
DR MassIVE; P27824; -.
DR MaxQB; P27824; -.
DR PaxDb; P27824; -.
DR PeptideAtlas; P27824; -.
DR PRIDE; P27824; -.
DR ProteomicsDB; 54425; -. [P27824-1]
DR ProteomicsDB; 5850; -.
DR TopDownProteomics; P27824-1; -. [P27824-1]
DR ABCD; P27824; 1 sequenced antibody.
DR Antibodypedia; 2421; 1151 antibodies from 46 providers.
DR DNASU; 821; -.
DR Ensembl; ENST00000247461.9; ENSP00000247461.4; ENSG00000127022.16. [P27824-1]
DR Ensembl; ENST00000452673.6; ENSP00000391646.2; ENSG00000127022.16. [P27824-1]
DR Ensembl; ENST00000502296.6; ENSP00000424745.2; ENSG00000127022.16. [P27824-1]
DR Ensembl; ENST00000504734.5; ENSP00000424063.1; ENSG00000127022.16. [P27824-1]
DR Ensembl; ENST00000506654.6; ENSP00000426555.2; ENSG00000127022.16. [P27824-3]
DR Ensembl; ENST00000509563.2; ENSP00000421434.2; ENSG00000127022.16. [P27824-1]
DR Ensembl; ENST00000513246.6; ENSP00000421813.2; ENSG00000127022.16. [P27824-1]
DR Ensembl; ENST00000638425.1; ENSP00000492372.1; ENSG00000283777.2. [P27824-1]
DR Ensembl; ENST00000638706.2; ENSP00000492868.1; ENSG00000283777.2. [P27824-1]
DR Ensembl; ENST00000639938.1; ENSP00000491760.1; ENSG00000283777.2. [P27824-1]
DR Ensembl; ENST00000680006.1; ENSP00000505129.1; ENSG00000127022.16. [P27824-3]
DR Ensembl; ENST00000680013.1; ENSP00000506078.1; ENSG00000127022.16. [P27824-1]
DR Ensembl; ENST00000680042.1; ENSP00000505960.1; ENSG00000127022.16. [P27824-1]
DR Ensembl; ENST00000680092.1; ENSP00000505202.1; ENSG00000127022.16. [P27824-1]
DR Ensembl; ENST00000680618.1; ENSP00000506583.1; ENSG00000127022.16. [P27824-1]
DR Ensembl; ENST00000680827.1; ENSP00000506051.1; ENSG00000127022.16. [P27824-3]
DR Ensembl; ENST00000681072.1; ENSP00000505526.1; ENSG00000127022.16. [P27824-1]
DR Ensembl; ENST00000681168.1; ENSP00000506021.1; ENSG00000127022.16. [P27824-1]
DR Ensembl; ENST00000681476.1; ENSP00000506003.1; ENSG00000127022.16. [P27824-1]
DR Ensembl; ENST00000681674.1; ENSP00000505013.1; ENSG00000127022.16. [P27824-1]
DR Ensembl; ENST00000681712.1; ENSP00000506061.1; ENSG00000127022.16. [P27824-1]
DR Ensembl; ENST00000681733.1; ENSP00000506568.1; ENSG00000127022.16. [P27824-1]
DR Ensembl; ENST00000681903.1; ENSP00000506509.1; ENSG00000127022.16. [P27824-1]
DR GeneID; 821; -.
DR KEGG; hsa:821; -.
DR MANE-Select; ENST00000247461.9; ENSP00000247461.4; NM_001746.4; NP_001737.1.
DR UCSC; uc003mkk.4; human. [P27824-1]
DR CTD; 821; -.
DR DisGeNET; 821; -.
DR GeneCards; CANX; -.
DR HGNC; HGNC:1473; CANX.
DR HPA; ENSG00000127022; Low tissue specificity.
DR MIM; 114217; gene.
DR neXtProt; NX_P27824; -.
DR OpenTargets; ENSG00000127022; -.
DR PharmGKB; PA26055; -.
DR VEuPathDB; HostDB:ENSG00000127022; -.
DR eggNOG; KOG0675; Eukaryota.
DR GeneTree; ENSGT00950000182915; -.
DR HOGENOM; CLU_018224_2_0_1; -.
DR InParanoid; P27824; -.
DR OMA; ANPKCEA; -.
DR OrthoDB; 775337at2759; -.
DR PhylomeDB; P27824; -.
DR TreeFam; TF300618; -.
DR PathwayCommons; P27824; -.
DR Reactome; R-HSA-168316; Assembly of Viral Components at the Budding Site.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-8984722; Interleukin-35 Signalling.
DR Reactome; R-HSA-901042; Calnexin/calreticulin cycle.
DR Reactome; R-HSA-9020956; Interleukin-27 signaling.
DR Reactome; R-HSA-9683686; Maturation of spike protein.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR SignaLink; P27824; -.
DR BioGRID-ORCS; 821; 17 hits in 1085 CRISPR screens.
DR ChiTaRS; CANX; human.
DR GeneWiki; Calnexin; -.
DR GenomeRNAi; 821; -.
DR Pharos; P27824; Tbio.
DR PRO; PR:P27824; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P27824; protein.
DR Bgee; ENSG00000127022; Expressed in stromal cell of endometrium and 112 other tissues.
DR ExpressionAtlas; P27824; baseline and differential.
DR Genevisible; P27824; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:AgBase.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005840; C:ribosome; IEA:Ensembl.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0034185; F:apolipoprotein binding; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; TAS:Reactome.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; TAS:ParkinsonsUK-UCL.
DR GO; GO:0009306; P:protein secretion; TAS:ProtInc.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR Gene3D; 2.10.250.10; -; 1.
DR InterPro; IPR001580; Calret/calnex.
DR InterPro; IPR018124; Calret/calnex_CS.
DR InterPro; IPR009033; Calreticulin/calnexin_P_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR PANTHER; PTHR11073; PTHR11073; 1.
DR Pfam; PF00262; Calreticulin; 1.
DR PRINTS; PR00626; CALRETICULIN.
DR SUPFAM; SSF49899; SSF49899; 2.
DR SUPFAM; SSF63887; SSF63887; 1.
DR PROSITE; PS00803; CALRETICULIN_1; 1.
DR PROSITE; PS00804; CALRETICULIN_2; 1.
DR PROSITE; PS00805; CALRETICULIN_REPEAT; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calcium; Chaperone;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Host-virus interaction; Lectin; Lipoprotein; Membrane; Metal-binding;
KW Palmitate; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255, ECO:0007744|PubMed:25944712"
FT CHAIN 21..592
FT /note="Calnexin"
FT /id="PRO_0000004198"
FT TOPO_DOM 21..481
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 278..290
FT /note="1-1"
FT REPEAT 295..307
FT /note="1-2"
FT REPEAT 314..326
FT /note="1-3"
FT REPEAT 333..345
FT /note="1-4"
FT REPEAT 348..358
FT /note="2-1"
FT REPEAT 367..377
FT /note="2-2"
FT REPEAT 381..391
FT /note="2-3"
FT REPEAT 395..405
FT /note="2-4"
FT REGION 260..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..409
FT /note="P domain (Extended arm)"
FT /evidence="ECO:0000250"
FT REGION 278..345
FT /note="4 X approximate repeats"
FT REGION 326..359
FT /note="Interaction with PPIB"
FT /evidence="ECO:0000250"
FT REGION 348..405
FT /note="4 X approximate repeats"
FT REGION 503..592
FT /note="Sufficient to mediate interaction with SGIP1"
FT /evidence="ECO:0000250"
FT REGION 511..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..345
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..546
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 166
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 185
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 192
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 425
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 436
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 137
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 562
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 564
FT /note="Phosphoserine; by MAPK3"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT LIPID 502
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:22314232"
FT LIPID 503
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:22314232"
FT DISULFID 160..194
FT /evidence="ECO:0000250"
FT DISULFID 360..366
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..108
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055515"
FT VAR_SEQ 1
FT /note="M -> MADRRTPTPFAGCRLPRQRRARDASQVSAPGTRRIM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055516"
FT CONFLICT 179
FT /note="F -> L (in Ref. 2; AAA21749)"
FT /evidence="ECO:0000305"
FT CONFLICT 431..433
FT /note="SDI -> LTF (in Ref. 10; AAA35696)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="R -> L (in Ref. 10; AAA35696)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 592 AA; 67568 MW; EDE094D9B82261EE CRC64;
MEGKWLLCML LVLGTAIVEA HDGHDDDVID IEDDLDDVIE EVEDSKPDTT APPSSPKVTY
KAPVPTGEVY FADSFDRGTL SGWILSKAKK DDTDDEIAKY DGKWEVEEMK ESKLPGDKGL
VLMSRAKHHA ISAKLNKPFL FDTKPLIVQY EVNFQNGIEC GGAYVKLLSK TPELNLDQFH
DKTPYTIMFG PDKCGEDYKL HFIFRHKNPK TGIYEEKHAK RPDADLKTYF TDKKTHLYTL
ILNPDNSFEI LVDQSVVNSG NLLNDMTPPV NPSREIEDPE DRKPEDWDER PKIPDPEAVK
PDDWDEDAPA KIPDEEATKP EGWLDDEPEY VPDPDAEKPE DWDEDMDGEW EAPQIANPRC
ESAPGCGVWQ RPVIDNPNYK GKWKPPMIDN PSYQGIWKPR KIPNPDFFED LEPFRMTPFS
AIGLELWSMT SDIFFDNFII CADRRIVDDW ANDGWGLKKA ADGAAEPGVV GQMIEAAEER
PWLWVVYILT VALPVFLVIL FCCSGKKQTS GMEYKKTDAP QPDVKEEEEE KEEEKDKGDE
EEEGEEKLEE KQKSDAEEDG GTVSQEEEDR KPKAEEDEIL NRSPRNRKPR RE
