K2C8_MOUSE
ID K2C8_MOUSE Reviewed; 490 AA.
AC P11679; Q3KQK5; Q3TGI1; Q3TJE1; Q3TKY7; Q61463; Q61518; Q61519;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Keratin, type II cytoskeletal 8;
DE AltName: Full=Cytokeratin endo A;
DE AltName: Full=Cytokeratin-8;
DE Short=CK-8;
DE AltName: Full=Keratin-8;
DE Short=K8;
DE AltName: Full=Type-II keratin Kb8;
GN Name=Krt8; Synonyms=Krt2-8;
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 [GENOMIC DNA / MRNA].
RX PubMed=2454862; DOI=10.1111/j.1432-0436.1988.tb00794.x;
RA Semat A., Vasseur M., Maillet L., Brulet P., Darmon Y.M.;
RT "Sequence analysis of murine cytokeratin endo A (no. 8) cDNA. Evidence for
RT mRNA species initiated upstream of the normal 5' end in PCC4 cells.";
RL Differentiation 37:40-46(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2464527; DOI=10.1016/0378-1119(88)90604-x;
RA Morita T., Tondella M.L.C., Takemoto Y., Hashido K., Ichinose Y.,
RA Nozaki M., Matsushiro A.;
RT "Nucleotide sequence of mouse EndoA cytokeratin cDNA reveals polypeptide
RT characteristics of the type-II keratin subfamily.";
RL Gene 68:109-117(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2467842; DOI=10.1016/0378-1119(88)90106-0;
RA Ouellet T., Levac P., Royal A.;
RT "Complete sequence of the mouse type-II keratin EndoA: its amino-terminal
RT region resembles mitochondrial signal peptides.";
RL Gene 70:75-84(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=1717348; DOI=10.1016/0378-1119(91)90247-9;
RA Tamai Y., Takemoto Y., Matsumoto M., Morita T., Matsushiro A., Nozaki M.;
RT "Sequence of the EndoA gene encoding mouse cytokeratin and its methylation
RT state in the CpG-rich region.";
RL Gene 104:169-176(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Amnion, Blastocyst, Embryo, Placenta, Stomach, and Thymus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Colon, and Mammary tumor;
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 [7]
RP PROTEIN SEQUENCE OF 103-114, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [8]
RP INTERACTION WITH KRT20, AND TISSUE SPECIFICITY.
RX PubMed=12857878; DOI=10.1091/mbc.e03-02-0059;
RA Zhou Q., Toivola D.M., Feng N., Greenberg H.B., Franke W.W., Omary M.B.;
RT "Keratin 20 helps maintain intermediate filament organization in intestinal
RT epithelia.";
RL Mol. Biol. Cell 14:2959-2971(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-482 AND SER-489, AND
RP 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-259; SER-482; SER-485
RP AND SER-489, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, and Spleen;
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 [12]
RP PHOSPHORYLATION AT SER-80 BY MAPK.
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 [13]
RP IDENTIFICATION IN A COMPLEX WITH KRT18, AND INTERACTION WITH KRT18 AND
RP 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 [14]
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: Together with KRT19, helps to link the contractile apparatus
CC to dystrophin at the costameres of striated muscle. {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins
CC (PubMed:24940650). Forms a heterodimer with KRT18 (PubMed:24940650).
CC Associates with KRT20 (PubMed:12857878). Interacts with PLEC isoform
CC 1C, when in a heterodimer with KRT18 (PubMed:24940650). Interacts with
CC PNN (By similarity). When associated with KRT19, interacts with DMD.
CC Interacts with TCHP (By similarity). Interacts with APEX1 (By
CC similarity). Interacts with GPER1 (By similarity). Interacts with EPPK1
CC (PubMed:25617501). {ECO:0000250|UniProtKB:P05787,
CC ECO:0000269|PubMed:12857878, ECO:0000269|PubMed:24940650,
CC ECO:0000269|PubMed:25617501}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q10758}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q10758}. Nucleus matrix
CC {ECO:0000250|UniProtKB:Q10758}.
CC -!- TISSUE SPECIFICITY: Expressed in abundance in the epithelia of colon,
CC bladder, ileum, and stomach, with lower expression observed in earskin
CC (at protein level). Also expressed in pancreas, liver, dudenum and
CC jejunum. {ECO:0000269|PubMed:12857878}.
CC -!- PTM: Phosphorylation on serine residues is enhanced during EGF
CC stimulation and mitosis. Ser-80 phosphorylation plays an important role
CC in keratin filament reorganization (By similarity). {ECO:0000250}.
CC -!- PTM: O-glycosylated. O-GlcNAcylation at multiple sites increases
CC solubility, and decreases stability by inducing proteasomal degradation
CC (By similarity). {ECO:0000250}.
CC -!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
CC {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37551.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X12789; CAA31278.1; -; mRNA.
DR EMBL; X15662; CAA33697.1; -; Genomic_DNA.
DR EMBL; M21836; AAA37550.1; -; mRNA.
DR EMBL; M21836; AAA37551.1; ALT_INIT; mRNA.
DR EMBL; M22831; AAA37548.1; -; mRNA.
DR EMBL; D90360; BAA14375.1; -; Genomic_DNA.
DR EMBL; AK077597; BAC36888.1; -; mRNA.
DR EMBL; AK145546; BAE26499.1; -; mRNA.
DR EMBL; AK145679; BAE26585.1; -; mRNA.
DR EMBL; AK145777; BAE26646.1; -; mRNA.
DR EMBL; AK146948; BAE27557.1; -; mRNA.
DR EMBL; AK147044; BAE27630.1; -; mRNA.
DR EMBL; AK166737; BAE38980.1; -; mRNA.
DR EMBL; AK166768; BAE39006.1; -; mRNA.
DR EMBL; AK166854; BAE39072.1; -; mRNA.
DR EMBL; AK166960; BAE39143.1; -; mRNA.
DR EMBL; AK166993; BAE39172.1; -; mRNA.
DR EMBL; AK167120; BAE39268.1; -; mRNA.
DR EMBL; AK167269; BAE39382.1; -; mRNA.
DR EMBL; AK167471; BAE39554.1; -; mRNA.
DR EMBL; AK168522; BAE40401.1; -; mRNA.
DR EMBL; AK168540; BAE40418.1; -; mRNA.
DR EMBL; AK168561; BAE40434.1; -; mRNA.
DR EMBL; AK168726; BAE40567.1; -; mRNA.
DR EMBL; AK168910; BAE40723.1; -; mRNA.
DR EMBL; AK169136; BAE40915.1; -; mRNA.
DR EMBL; AK169691; BAE41308.1; -; mRNA.
DR EMBL; BC094009; AAH94009.1; -; mRNA.
DR EMBL; BC106154; AAI06155.1; -; mRNA.
DR CCDS; CCDS27868.1; -.
DR PIR; JS0658; JS0658.
DR PIR; JT0407; JT0407.
DR PIR; S05474; S05474.
DR RefSeq; NP_112447.2; NM_031170.2.
DR AlphaFoldDB; P11679; -.
DR SMR; P11679; -.
DR BioGRID; 201037; 19.
DR ComplexPortal; CPX-5868; Keratin-8 - Keratin-18 dimer complex.
DR IntAct; P11679; 3.
DR MINT; P11679; -.
DR STRING; 10090.ENSMUSP00000023952; -.
DR iPTMnet; P11679; -.
DR PhosphoSitePlus; P11679; -.
DR SWISS-2DPAGE; P11679; -.
DR EPD; P11679; -.
DR jPOST; P11679; -.
DR MaxQB; P11679; -.
DR PaxDb; P11679; -.
DR PeptideAtlas; P11679; -.
DR PRIDE; P11679; -.
DR ProteomicsDB; 269446; -.
DR Antibodypedia; 3437; 3611 antibodies from 52 providers.
DR DNASU; 16691; -.
DR Ensembl; ENSMUST00000023952; ENSMUSP00000023952; ENSMUSG00000049382.
DR GeneID; 16691; -.
DR KEGG; mmu:16691; -.
DR UCSC; uc007xui.1; mouse.
DR CTD; 3856; -.
DR MGI; MGI:96705; Krt8.
DR VEuPathDB; HostDB:ENSMUSG00000049382; -.
DR eggNOG; ENOG502QURK; Eukaryota.
DR GeneTree; ENSGT00940000153339; -.
DR HOGENOM; CLU_012560_5_4_1; -.
DR InParanoid; P11679; -.
DR OMA; AEMWYKQ; -.
DR OrthoDB; 824246at2759; -.
DR PhylomeDB; P11679; -.
DR TreeFam; TF317854; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 16691; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Krt8; mouse.
DR PRO; PR:P11679; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P11679; protein.
DR Bgee; ENSMUSG00000049382; Expressed in ileum and 120 other tissues.
DR Genevisible; P11679; MM.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0043034; C:costamere; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; ISO:MGI.
DR GO; GO:0005882; C:intermediate filament; IDA:MGI.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0045095; C:keratin filament; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR GO; GO:0060706; P:cell differentiation involved in embryonic placenta development; IGI:MGI.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0097284; P:hepatocyte apoptotic process; IMP:MGI.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR GO; GO:0051599; P:response to hydrostatic pressure; ISO:MGI.
DR GO; GO:0051707; P:response to other organism; IMP:MGI.
DR GO; GO:0045214; P:sarcomere organization; ISO:MGI.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:MGI.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR032444; Keratin_2_head.
DR InterPro; IPR003054; Keratin_II.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF16208; Keratin_2_head; 1.
DR PRINTS; PR01276; TYPE2KERATIN.
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 CHAIN 1..490
FT /note="Keratin, type II cytoskeletal 8"
FT /id="PRO_0000063741"
FT DOMAIN 97..408
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..96
FT /note="Head"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..132
FT /note="Coil 1A"
FT REGION 133..149
FT /note="Linker 1"
FT REGION 150..241
FT /note="Coil 1B"
FT REGION 242..265
FT /note="Linker 12"
FT REGION 266..403
FT /note="Coil 2"
FT REGION 267..387
FT /note="Necessary for interaction with PNN"
FT /evidence="ECO:0000250"
FT REGION 404..490
FT /note="Tail"
FT SITE 347
FT /note="Stutter"
FT MOD_RES 9
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 23
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 24
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 26
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q10758"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 32
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10758"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 40
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10758"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10758"
FT MOD_RES 49
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 49
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10758"
FT MOD_RES 80
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000269|PubMed:20724476"
FT MOD_RES 107
FT /note="N6-malonyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 213
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 301
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 331
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10758"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10758"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10758"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 128
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 291
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 301
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 310
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 331
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 399
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 479
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 479
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CONFLICT 12..35
FT /note="MSTSGPRAFSSRSFTSGPGARISS -> NVYSVGLLASARSGSWTGSASTA
FT (in Ref. 3; AAA37548)"
FT /evidence="ECO:0000305"
FT CONFLICT 40..58
FT /note="RVGSSSSSFRGSMGTGVGL -> GRACQLGSSFGEAWHGVS (in Ref.
FT 3; AAA37548)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="M -> L (in Ref. 6; AAI06155)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="N -> D (in Ref. 3; AAA37548)"
FT /evidence="ECO:0000305"
FT CONFLICT 83..87
FT /note="KLEVD -> QLSL (in Ref. 3; AAA37548)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="F -> L (in Ref. 5; BAE39554)"
FT /evidence="ECO:0000305"
FT CONFLICT 190..191
FT /note="NK -> QQ (in Ref. 1; CAA31278)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="E -> G (in Ref. 5; BAE40567)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="Missing (in Ref. 1; CAA31278)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="R -> P (in Ref. 1; CAA31278)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="N -> K (in Ref. 5; BAE38980/BAE39006)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 54565 MW; C0C79590F0C28502 CRC64;
MSIRVTQKSY KMSTSGPRAF SSRSFTSGPG ARISSSSFSR VGSSSSSFRG SMGTGVGLGG
FGGAGVGGIT AVTVNQSLLS PLKLEVDPNI QAVRTQEKEQ IKSLNNKFAS FIDKVRFLEQ
QNKMLETKWS LLQQQKTSRS NMDNMFESYI NNLRRQLEAL GQEKLKLEAE LGNMQGLVED
FKNKYEDEIN KRTEMENEFV LIKKDVDEAY MNKVELESRL EGLTDEINFL RQIHEEEIRE
LQSQISDTSV VLSMDNSRSL DMDGIIAEVR AQYEDIANRS RAEAETMYQI KYEELQTLAG
KHGDDLRRTK TEISEMNRNI NRLQAEIEAL KGQRASLEAA IADAEQRGEM AIKDAQTKLA
ELEAALQRAK QDMARQLREY QELMNVKLAL DIEITTYRKL LEGEESRLES GMQNMSIHTK
TTSGYSGGLS SSYGGLTSPG FSYGMSSFQP GFGSAGGSNT FSRTTKAVVV KKIETRDGKL
VSESSDVVSK
