K1C18_RAT
ID K1C18_RAT Reviewed; 423 AA.
AC Q5BJY9; Q63278;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Keratin, type I cytoskeletal 18;
DE AltName: Full=Cytokeratin-18;
DE Short=CK-18;
DE AltName: Full=Keratin-18;
DE Short=K18;
GN Name=Krt18 {ECO:0000250|UniProtKB:P05783};
GN Synonyms=Krt1-18 {ECO:0000312|RGD:619935};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAH91275.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus {ECO:0000312|EMBL:AAH91275.1};
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 [2] {ECO:0000305, ECO:0000312|EMBL:CAA57204.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 124-270, AND DEVELOPMENTAL STAGE.
RC STRAIN=Wistar {ECO:0000312|EMBL:CAA57204.1};
RC TISSUE=Fetal gonad {ECO:0000269|PubMed:8541209};
RX PubMed=8541209; DOI=10.1016/0925-4773(95)00401-l;
RA Fridmacher V., le Bert M., Guillou F., Magre S.;
RT "Switch in the expression of the K19/K18 keratin genes as a very early
RT evidence of testicular differentiation in the rat.";
RL Mech. Dev. 52:199-207(1995).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 131-140, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver {ECO:0000269|PubMed:16128803};
RX PubMed=16128803; DOI=10.1111/j.1742-4658.2005.04847.x;
RA Segawa M., Niino K., Mineki R., Kaga N., Murayama K., Sugimoto K.,
RA Watanabe Y., Furukawa K., Horigome T.;
RT "Proteome analysis of a rat liver nuclear insoluble protein fraction and
RT localization of a novel protein, ISP36, to compartments in the
RT interchromatin space.";
RL FEBS J. 272:4327-4338(2005).
RN [4] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=7507868; DOI=10.1111/j.1432-0436.1993.tb00032.x;
RA Frojdman K., Paranko J., Virtanen I., Pelliniemi L.J.;
RT "Intermediate filament proteins and epithelial differentiation in the
RT embryonic ovary of the rat.";
RL Differentiation 55:47-55(1993).
RN [5] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=7514933;
RA Flint N., Pemberton P.W., Lobley R.W., Evans G.S.;
RT "Cytokeratin expression in epithelial cells isolated from the crypt and
RT villus regions of the rodent small intestine.";
RL Epithelial Cell Biol. 3:16-23(1994).
RN [6] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=7517927; DOI=10.1007/bf00315832;
RA Kasper M., Hofer D., Woodcock-Mitchell J., Migheli A., Attanasio A.,
RA Rudolf T., Muller M., Drenckhahn D.;
RT "Colocalization of cytokeratin 18 and villin in type III alveolar cells
RT (brush cells) of the rat lung.";
RL Histochemistry 101:57-62(1994).
RN [7] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=7589899; DOI=10.1046/j.1432-0436.1995.5930155.x;
RA Zhang C., Cotter M., Lawton A., Oakley B., Wong L., Zeng Q.;
RT "Keratin 18 is associated with a subset of older taste cells in the rat.";
RL Differentiation 59:155-162(1995).
RN [8] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8789401; DOI=10.1007/bf02389690;
RA Zeng Q., Lawton A., Oakley B.;
RT "Glycoconjugates and keratin 18 define subsets of taste cells.";
RL Histochem. J. 27:997-1006(1995).
RN [9] {ECO:0000305}
RP DEPHOSPHORYLATION BY ETHANOL.
RX PubMed=8824732;
RX DOI=10.1002/(sici)1097-0169(1996)33:1<30::aid-cm4>3.0.co;2-m;
RA Eckert B.S., Yeagle P.L.;
RT "Site-specificity of ethanol-induced dephosphorylation of rat hepatocyte
RT keratins 8 and 18: a 31P NMR study.";
RL Cell Motil. Cytoskeleton 33:30-37(1996).
RN [10] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH THROMBIN-ANTITHROMBIN
RP COMPLEX.
RX PubMed=9353322; DOI=10.1074/jbc.272.45.28574;
RA Wells M.J., Hatton M.W., Hewlett B., Podor T.J., Sheffield W.P.,
RA Blajchman M.A.;
RT "Cytokeratin 18 is expressed on the hepatocyte plasma membrane surface and
RT interacts with thrombin-antithrombin complexes.";
RL J. Biol. Chem. 272:28574-28581(1997).
RN [11] {ECO:0000305}
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10707864; DOI=10.1016/s0168-8278(00)80069-0;
RA Sanchez A., Alvarez A.M., Pagan R., Roncero C., Vilaro S., Benito M.,
RA Fabregat I.;
RT "Fibronectin regulates morphology, cell organization and gene expression of
RT rat fetal hepatocytes in primary culture.";
RL J. Hepatol. 32:242-250(2000).
RN [12] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11428046; DOI=10.1023/a:1026548020851;
RA Hofer D., Shin D.W., Drenckhahn D.;
RT "Identification of cytoskeletal markers for the different microvilli and
RT cell types of the rat vomeronasal sensory epithelium.";
RL J. Neurocytol. 29:147-156(2000).
RN [13] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14630065; DOI=10.1016/s0887-2333(03)00132-2;
RA Ridd K., Alexander D.J., Reed C.J.;
RT "Foetal rat lung epithelial (FRLE) cells: partial characterisation and
RT response to pneumotoxins.";
RL Toxicol. in Vitro 18:79-88(2004).
RN [14] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=16998620; DOI=10.1007/s10266-005-0059-4;
RA Iwasaki S., Aoyagi H., Asami T.;
RT "Expression of keratin 18 in the periderm cells of the lingual epithelium
RT of fetal rats: visualization by fluorescence immunohistochemistry and
RT differential interference contrast microscopy.";
RL Odontology 94:64-68(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-35, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-35 AND SER-57, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: When phosphorylated, plays a role in filament reorganization.
CC Involved in the delivery of mutated CFTR to the plasma membrane.
CC Together with KRT8, is involved in interleukin-6 (IL-6)-mediated
CC barrier protection (By similarity). Involved in the uptake of thrombin-
CC antithrombin complexes by hepatic cells. {ECO:0000250|UniProtKB:P05783,
CC ECO:0000269|PubMed:9353322}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins. KRT18
CC associates with KRT8 (By similarity). Interacts with PNN and mutated
CC CFTR. Interacts with YWHAE, YWHAH and YWHAZ only when phosphorylated.
CC Interacts with DNAJB6, TCHP and TRADD (By similarity). Interacts with
CC the thrombin-antithrombin complex. Interacts with FAM83H (By
CC similarity). Interacts with EPPK1 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P05783, ECO:0000250|UniProtKB:P05784,
CC ECO:0000269|PubMed:9353322}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:16128803,
CC ECO:0000269|PubMed:16998620}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P05783}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P05783}. Cytoplasm {ECO:0000269|PubMed:16128803,
CC ECO:0000269|PubMed:16998620}.
CC -!- TISSUE SPECIFICITY: Expressed on the plasma membrane of hepatocytes and
CC in the narrow apical portions of supporting cells in the vomeronasal
CC sensory epithelium. Detected in the type III alveolar cells of the
CC lung, in the proliferative crypt epithelium of the small intestine and
CC in the older intragemmal cells of the tongue.
CC {ECO:0000269|PubMed:10707864, ECO:0000269|PubMed:11428046,
CC ECO:0000269|PubMed:14630065, ECO:0000269|PubMed:7514933,
CC ECO:0000269|PubMed:7517927, ECO:0000269|PubMed:8789401,
CC ECO:0000269|PubMed:9353322}.
CC -!- DEVELOPMENTAL STAGE: Expression first detected in the male gonad at
CC 13.5 dpc, at the onset of testicular differentiation, and at 17 dpc in
CC cell aggregates of the early ovary; then only in some cord cells of the
CC older ovary. Expressed in fetal lung epithelium at 20 dpc. Detected at
CC 13 dpc, sparsely distributed throughout the cytoplasm in the single
CC layer of periderm cells covering the dorsal epithelium of the fetal
CC tongue. Expression increases in the lingual periderm cells at 17 dpc
CC and then disappears at 19 dpc coinciding with the disappearance of the
CC periderm cells at the onset of squamous stratification of the lingual
CC epithelium. Expressed at day 2-3 postnatally in older, elongated taste
CC bud cells and at day 5, uniformly distributed throughout the epithelium
CC of villi, intervillus epithelium and developing crypt buds of the small
CC intestine. {ECO:0000269|PubMed:14630065, ECO:0000269|PubMed:16998620,
CC ECO:0000269|PubMed:7507868, ECO:0000269|PubMed:7514933,
CC ECO:0000269|PubMed:7589899, ECO:0000269|PubMed:8541209,
CC ECO:0000269|PubMed:8789401}.
CC -!- INDUCTION: By IL-6 (By similarity). By fibronectin.
CC {ECO:0000250|UniProtKB:P05783, ECO:0000269|PubMed:10707864}.
CC -!- PTM: Phosphorylation increases by IL-6. {ECO:0000250|UniProtKB:P05783}.
CC -!- PTM: Proteolytically cleaved by caspases during epithelial cell
CC apoptosis. Cleavage occurs at Asp-231 by either caspase-3, caspase-6 or
CC caspase-7 (By similarity). {ECO:0000250}.
CC -!- PTM: Dephosphorylated by ethanol. {ECO:0000269|PubMed:8824732}.
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; BC091275; AAH91275.1; -; mRNA.
DR EMBL; X81448; CAA57204.1; -; mRNA.
DR RefSeq; NP_446428.1; NM_053976.1.
DR AlphaFoldDB; Q5BJY9; -.
DR SMR; Q5BJY9; -.
DR BioGRID; 254814; 2.
DR IntAct; Q5BJY9; 2.
DR STRING; 10116.ENSRNOP00000067234; -.
DR GlyGen; Q5BJY9; 3 sites.
DR iPTMnet; Q5BJY9; -.
DR PhosphoSitePlus; Q5BJY9; -.
DR jPOST; Q5BJY9; -.
DR PaxDb; Q5BJY9; -.
DR PRIDE; Q5BJY9; -.
DR Ensembl; ENSRNOT00000073951; ENSRNOP00000067234; ENSRNOG00000047393.
DR GeneID; 294853; -.
DR KEGG; rno:294853; -.
DR CTD; 3875; -.
DR RGD; 619935; Krt18.
DR eggNOG; ENOG502QUS8; Eukaryota.
DR GeneTree; ENSGT00940000153309; -.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; Q5BJY9; -.
DR OMA; YRASSIH; -.
DR OrthoDB; 711591at2759; -.
DR PhylomeDB; Q5BJY9; -.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR PRO; PR:Q5BJY9; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000047393; Expressed in stomach and 17 other tissues.
DR Genevisible; Q5BJY9; RN.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0034451; C:centriolar satellite; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005882; C:intermediate filament; ISO:RGD.
DR GO; GO:0045095; C:keratin filament; IDA:RGD.
DR GO; GO:0005815; C:microtubule organizing center; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:1902488; P:cholangiocyte apoptotic process; IEP:RGD.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0043000; P:Golgi to plasma membrane CFTR protein transport; ISO:RGD.
DR GO; GO:0097284; P:hepatocyte apoptotic process; ISO:RGD.
DR GO; GO:0070365; P:hepatocyte differentiation; IEP:RGD.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISO:RGD.
DR GO; GO:0072497; P:mesenchymal stem cell differentiation; IEP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0009750; P:response to fructose; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:RGD.
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; Direct protein sequencing;
KW Glycoprotein; Intermediate filament; Isopeptide bond; Keratin; Methylation;
KW Nucleus; Phosphoprotein; 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_0000063668"
FT DOMAIN 72..384
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..71
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 62..366
FT /note="Necessary for interaction with PNN"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT REGION 69..121
FT /note="Interaction with TRADD"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT REGION 72..107
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 108..125
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 126..217
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 218..241
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 236..384
FT /note="Interaction with DNAJB6"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT REGION 242..380
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 381..423
FT /note="Tail"
FT /evidence="ECO:0000255"
FT SITE 231..232
FT /note="Cleavage; by caspase-3, caspase-6 or caspase-7"
FT /evidence="ECO:0000250"
FT SITE 264
FT /note="Stutter"
FT /evidence="ECO:0000255"
FT SITE 324
FT /note="Stutter"
FT /evidence="ECO:0000255"
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:0007744|PubMed:16641100"
FT MOD_RES 31
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 32
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05784"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 37
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P05784"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05783"
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:0000250|UniProtKB:P05784"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 124
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05784"
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 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05784"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05783"
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|UniProtKB:P05783"
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 CROSSLNK 410
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT CONFLICT 125
FT /note="T -> I (in Ref. 2; CAA57204)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 47761 MW; 793F0BAA275CCA4E CRC64;
MSFTTRSTTF STNYRSLGSV RTPSQRVRPA SSAASVYAGA GGSGSRISVS RSVWGGSVGS
AGLAGMGGVQ TEKETMQDLN DRLASYLDKV KNLETENRRL ESKIREYLEK RGPQGVRDWG
HYFKTIEDLR AQIFANSVDN ARIVLQIDNA RLAADDFRVK YETELAMRQS VESDIHGLRK
VVDDTNITRL QLETEIEALK EELLFMKKNH EEEVQGLEAQ IASSGLTVEV DAPKSQDLSK
IMADIRAQYE QLAQKNREEL DKYWSQQIEE STTVVTTKSA EIRDAETTLL ELRRTLQTLE
IDLDSMKNQN INLENNLGEV EARYRVQMEQ LNGVLLHLES ELAQTRAEGQ RQTQEYEALL
NIKVKLEAEI ATYRRLLEDG DDFSLNDALD SSNSMQTVQR TTTRKVVDGK VVSETNDTRV
LRH
