K1C18_MOUSE
ID K1C18_MOUSE Reviewed; 423 AA.
AC P05784; Q3TIX1; Q3TJH6; Q3TJW7; Q61766;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 5.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Keratin, type I cytoskeletal 18;
DE AltName: Full=Cytokeratin endo B;
DE Short=Keratin D;
DE AltName: Full=Cytokeratin-18;
DE Short=CK-18;
DE AltName: Full=Keratin-18;
DE Short=K18;
GN Name=Krt18; Synonyms=Kerd, Krt1-18;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Endoderm;
RX PubMed=2416755; DOI=10.1016/s0021-9258(17)36125-2;
RA Singer P.A., Trevor K., Oshima R.G.;
RT "Molecular cloning and characterization of the Endo B cytokeratin expressed
RT in preimplantation mouse embryos.";
RL J. Biol. Chem. 261:538-547(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Teratocarcinoma;
RA Alonso A., Weber T., Jorcano J.L.;
RT "Cloning and characterization of keratin D, a murine endodermal
RT cytoskeletal protein induced during in vitro differentiation of F9
RT teratocarcinoma cells.";
RL Roux's Arch. Dev. Biol. 196:16-21(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ; TISSUE=Liver;
RX PubMed=2467843; DOI=10.1016/0378-1119(88)90107-2;
RA Ichinose Y., Morita T., Zhang F., Srimahasongcram S., Tondella M.L.C.,
RA Matsumoto M., Nozaki M., Matsushiro A.;
RT "Nucleotide sequence and structure of the mouse cytokeratin endoB gene.";
RL Gene 70:85-95(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Blastocyst, Embryo, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-132, AND TISSUE SPECIFICITY.
RX PubMed=2454868; DOI=10.1101/gad.2.5.505;
RA Oshima R.G., Trevor K., Shevinsky L.H., Ryder O.A., Cecena G.;
RT "Identification of the gene coding for the Endo B murine cytokeratin and
RT its methylated, stable inactive state in mouse nonepithelial cells.";
RL Genes Dev. 2:505-516(1988).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=7504637; DOI=10.1006/dbio.1993.1326;
RA Thorey I.S., Meneses J.J., Neznanov N., Kulesh D.A., Pedersen R.A.,
RA Oshima R.G.;
RT "Embryonic expression of human keratin 18 and K18-beta-galactosidase fusion
RT genes in transgenic mice.";
RL Dev. Biol. 160:519-534(1993).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=7507912;
RA Dixon M.J., Robinson V., White A., Ferguson M.W.;
RT "Monoclonal antibodies recognising stage and region specific epitopes in
RT embryonic mouse palatal epithelial cells.";
RL J. Anat. 183:423-438(1993).
RN [9]
RP CLEAVAGE BY CASPASES.
RX PubMed=9298992; DOI=10.1083/jcb.138.6.1379;
RA Caulin C., Salvesen G.S., Oshima R.G.;
RT "Caspase cleavage of keratin 18 and reorganization of intermediate
RT filaments during epithelial cell apoptosis.";
RL J. Cell Biol. 138:1379-1394(1997).
RN [10]
RP DEVELOPMENTAL STAGE.
RX PubMed=16973199; DOI=10.1016/j.tice.2006.07.001;
RA Erman A., Veranic P., Psenicnik M., Jezernik K.;
RT "Superficial cell differentiation during embryonic and postnatal
RT development of mouse urothelium.";
RL Tissue Cell 38:293-301(2006).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, AND INDUCTION.
RX PubMed=17213200; DOI=10.1074/jbc.m604068200;
RA Wang L., Srinivasan S., Theiss A.L., Merlin D., Sitaraman S.V.;
RT "Interleukin-6 induces keratin expression in intestinal epithelial cells:
RT potential role of keratin-8 in interleukin-6-induced barrier function
RT alterations.";
RL J. Biol. Chem. 282:8219-8227(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-32; SER-35 AND
RP SER-316, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-32; SER-35; TYR-37;
RP SER-43; SER-57; SER-137; SER-316; SER-384 AND SER-391, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP PHOSPHORYLATION AT SER-52 BY MAPKAPK2 AND MAPKAPK3.
RX PubMed=20724476; DOI=10.1074/jbc.m110.132357;
RA Menon M.B., Schwermann J., Singh A.K., Franz-Wachtel M., Pabst O.,
RA Seidler U., Omary M.B., Kotlyarov A., Gaestel M.;
RT "p38 MAP kinase and MAPKAP kinases MK2/3 cooperatively phosphorylate
RT epithelial keratins.";
RL J. Biol. Chem. 285:33242-33251(2010).
RN [15]
RP IDENTIFICATION IN A COMPLEX WITH KRT8, AND INTERACTION WITH KRT8 AND PLEC.
RX PubMed=24940650; DOI=10.1038/jid.2014.255;
RA Bouameur J.E., Favre B., Fontao L., Lingasamy P., Begre N., Borradori L.;
RT "Interaction of plectin with keratins 5 and 14: dependence on several
RT plectin domains and keratin quaternary structure.";
RL J. Invest. Dermatol. 134:2776-2783(2014).
RN [16]
RP INTERACTION WITH EPPK1.
RX PubMed=25617501; DOI=10.1016/j.jhep.2015.01.007;
RA Szabo S., Woegenstein K.L., Oesterreicher C.H., Guldiken N., Chen Y.,
RA Doler C., Wiche G., Boor P., Haybaeck J., Strnad P., Fuchs P.;
RT "Epiplakin attenuates experimental mouse liver injury by chaperoning
RT keratin reorganization.";
RL J. Hepatol. 62:1357-1366(2015).
CC -!- FUNCTION: When phosphorylated, plays a role in filament reorganization.
CC Involved in the delivery of mutated CFTR to the plasma membrane.
CC Involved in the uptake of thrombin-antithrombin complexes by hepatic
CC cells (By similarity). Together with KRT8, is involved in interleukin-6
CC (IL-6)-mediated barrier protection. {ECO:0000250,
CC ECO:0000269|PubMed:17213200}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins. KRT18
CC associates with KRT8 (PubMed:24940650). Interacts with PLEC isoform 1C,
CC when in a heterodimer with KRT8 (PubMed:24940650). Interacts with PNN
CC and mutated CFTR. Interacts with YWHAE, YWHAH and YWHAZ only when
CC phosphorylated. Interacts with the thrombin-antithrombin complex.
CC Interacts with DNAJB6, TCHP and TRADD (By similarity). Interacts with
CC FAM83H (By similarity). Interacts with EPPK1 (PubMed:25617501).
CC {ECO:0000250, ECO:0000250|UniProtKB:P05783,
CC ECO:0000269|PubMed:24940650, ECO:0000269|PubMed:25617501}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:Q5BJY9}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05783}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:P05783}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q5BJY9}.
CC -!- TISSUE SPECIFICITY: Expressed in endoderm, intestinal epithelial cells
CC and in most extraembryonic tissues. {ECO:0000269|PubMed:17213200,
CC ECO:0000269|PubMed:2416755, ECO:0000269|PubMed:2454868,
CC ECO:0000269|PubMed:7504637}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis, expressed in a complex
CC spatial and temporal pattern in various embryonic epithelia. In 7.5 and
CC 13.5 day old embryo, expressed in most endodermal epithelia, ectodermal
CC and nascent mesodermal tissues. When the neural plate forms, expression
CC begins in the cells of skin ectoderm, head process/notochord, periderm,
CC whisker buds, choroid plexus and the epithelia of auditory duct and
CC inner ear. High expression in the lining endodermal cells when the
CC foregut and hindgut invaginations form. Expression in all three layers
CC of the urothelium starts at day 15 in the embryo and is not visible
CC after day 18. By day 11 and 12, the entire embryonic palatal epithelium
CC shows expression as well as the nasal passages and the roof of the
CC mouth; which disappears progresively from day 13 to 15.
CC {ECO:0000269|PubMed:16973199, ECO:0000269|PubMed:7504637,
CC ECO:0000269|PubMed:7507912}.
CC -!- INDUCTION: By retinoic acid and IL-6. {ECO:0000269|PubMed:17213200,
CC ECO:0000269|PubMed:2416755}.
CC -!- PTM: Phosphorylation increases by IL-6. {ECO:0000269|PubMed:17213200,
CC ECO:0000269|PubMed:20724476}.
CC -!- PTM: Proteolytically cleaved by caspases during epithelial cell
CC apoptosis. Cleavage occurs at Asp-231 by either caspase-3, caspas-6 or
CC caspase-7. {ECO:0000269|PubMed:9298992}.
CC -!- PTM: O-GlcNAcylation increases solubility, and decreases stability by
CC inducing proteasomal degradation. {ECO:0000250}.
CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; M11686; AAA39390.1; -; mRNA.
DR EMBL; M36376; AAA39373.1; -; mRNA.
DR EMBL; M22832; AAA37552.1; -; Genomic_DNA.
DR EMBL; AK145413; BAE26424.1; -; mRNA.
DR EMBL; AK167072; BAE39232.1; -; mRNA.
DR EMBL; AK167265; BAE39378.1; -; mRNA.
DR EMBL; AK167432; BAE39519.1; -; mRNA.
DR EMBL; AK167469; BAE39553.1; -; mRNA.
DR EMBL; AK167676; BAE39725.1; -; mRNA.
DR EMBL; BC089022; AAH89022.1; -; mRNA.
DR EMBL; Y00217; CAA68365.1; -; Genomic_DNA.
DR CCDS; CCDS27869.1; -.
DR PIR; I59463; I59463.
DR RefSeq; NP_034794.2; NM_010664.2.
DR AlphaFoldDB; P05784; -.
DR SMR; P05784; -.
DR BioGRID; 201023; 10.
DR ComplexPortal; CPX-5868; Keratin-8 - Keratin-18 dimer complex.
DR IntAct; P05784; 2.
DR MINT; P05784; -.
DR STRING; 10090.ENSMUSP00000023803; -.
DR GlyGen; P05784; 3 sites.
DR iPTMnet; P05784; -.
DR PhosphoSitePlus; P05784; -.
DR SWISS-2DPAGE; P05784; -.
DR EPD; P05784; -.
DR jPOST; P05784; -.
DR PaxDb; P05784; -.
DR PeptideAtlas; P05784; -.
DR PRIDE; P05784; -.
DR ProteomicsDB; 269138; -.
DR Antibodypedia; 271; 3642 antibodies from 57 providers.
DR DNASU; 16668; -.
DR Ensembl; ENSMUST00000023803; ENSMUSP00000023803; ENSMUSG00000023043.
DR GeneID; 16668; -.
DR KEGG; mmu:16668; -.
DR UCSC; uc007xuj.2; mouse.
DR CTD; 3875; -.
DR MGI; MGI:96692; Krt18.
DR VEuPathDB; HostDB:ENSMUSG00000023043; -.
DR eggNOG; ENOG502QUS8; Eukaryota.
DR GeneTree; ENSGT00940000153309; -.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; P05784; -.
DR OMA; TSFQGSM; -.
DR OrthoDB; 711591at2759; -.
DR PhylomeDB; P05784; -.
DR TreeFam; TF332742; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 16668; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Krt18; mouse.
DR PRO; PR:P05784; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P05784; protein.
DR Bgee; ENSMUSG00000023043; Expressed in urinary bladder urothelium and 224 other tissues.
DR Genevisible; P05784; MM.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005882; C:intermediate filament; IDA:MGI.
DR GO; GO:0045095; C:keratin filament; IDA:MGI.
DR GO; GO:0005815; C:microtubule organizing center; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0043000; P:Golgi to plasma membrane CFTR protein transport; ISO:MGI.
DR GO; GO:0097284; P:hepatocyte apoptotic process; IMP:MGI.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IGI:MGI.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR027695; Keratin-18.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; PTHR23239; 1.
DR PANTHER; PTHR23239:SF349; PTHR23239:SF349; 1.
DR Pfam; PF00038; Filament; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Glycoprotein; Intermediate filament;
KW Isopeptide bond; Keratin; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT CHAIN 2..423
FT /note="Keratin, type I cytoskeletal 18"
FT /id="PRO_0000063667"
FT DOMAIN 72..384
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..71
FT /note="Head"
FT REGION 62..366
FT /note="Necessary for interaction with PNN"
FT /evidence="ECO:0000250"
FT REGION 69..121
FT /note="Interaction with TRADD"
FT /evidence="ECO:0000250"
FT REGION 72..107
FT /note="Coil 1A"
FT REGION 108..125
FT /note="Linker 1"
FT REGION 126..217
FT /note="Coil 1B"
FT REGION 218..241
FT /note="Linker 12"
FT REGION 236..384
FT /note="Interaction with DNAJB6"
FT /evidence="ECO:0000250"
FT REGION 242..380
FT /note="Coil 2"
FT REGION 381..423
FT /note="Tail"
FT SITE 231..232
FT /note="Cleavage; by caspase-3, caspase-6 or caspase-7"
FT SITE 264
FT /note="Stutter"
FT SITE 324
FT /note="Stutter"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT MOD_RES 31
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 32
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 37
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 46
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT MOD_RES 50
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT MOD_RES 52
FT /note="Phosphoserine; by MAPKAPK2 and MAPKAPK3"
FT /evidence="ECO:0000269|PubMed:20724476"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT MOD_RES 124
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT MOD_RES 295
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT MOD_RES 397
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT CARBOHYD 31
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 32
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 50
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 73
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT CROSSLNK 240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT CROSSLNK 363
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT CROSSLNK 365
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT CONFLICT 134
FT /note="F -> L (in Ref. 1; AAA39390 and 2; AAA39373)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="V -> A (in Ref. 4; BAE26424/BAE39378)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="D -> N (in Ref. 2; AAA39373)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="A -> G (in Ref. 2; AAA39373)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="E -> G (in Ref. 4; BAE39725)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 47538 MW; A67ACD6814A02118 CRC64;
MSFTTRSTTF STNYRSLGSV RTPSQRVRPA SSAASVYAGA GGSGSRISVS RSVWGGSVGS
AGLAGMGGIQ TEKETMQDLN DRLASYLDKV KSLETENRRL ESKIREHLEK KGPQGVRDWG
HYFKIIEDLR AQIFANSVDN ARIVLQIDNA RLAADDFRVK YETELAMRQS VESDIHGLRK
VVDDTNITRL QLETEIEALK EELLFMKKNH EEEVQGLEAQ IASSGLTVEV DAPKSQDLSK
IMADIRAQYE ALAQKNREEL DKYWSQQIEE STTVVTTKSA EIRDAETTLT ELRRTLQTLE
IDLDSMKNQN INLENSLGDV EARYKAQMEQ LNGVLLHLES ELAQTRAEGQ RQAQEYEALL
NIKVKLEAEI ATYRRLLEDG EDFSLNDALD SSNSMQTVQK TTTRKIVDGR VVSETNDTRV
LRH
