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Keratin, type II cytoskeletal 8 (Cytokeratin endo A) (Cytokeratin-8) (CK-8) (Keratin-8) (K8) (Type-II keratin Kb8)

 K2C8_MOUSE              Reviewed;         490 AA.
P11679; Q3KQK5; Q3TGI1; Q3TJE1; Q3TKY7; Q61463; Q61518; Q61519;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
30-AUG-2017, entry version 165.
RecName: Full=Keratin, type II cytoskeletal 8;
AltName: Full=Cytokeratin endo A;
AltName: Full=Cytokeratin-8;
Short=CK-8;
AltName: Full=Keratin-8;
Short=K8;
AltName: Full=Type-II keratin Kb8;
Name=Krt8; Synonyms=Krt2-8;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=2454862; DOI=10.1111/j.1432-0436.1988.tb00794.x;
Semat A., Vasseur M., Maillet L., Brulet P., Darmon Y.M.;
"Sequence analysis of murine cytokeratin endo A (no. 8) cDNA. Evidence
for mRNA species initiated upstream of the normal 5' end in PCC4
cells.";
Differentiation 37:40-46(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2464527; DOI=10.1016/0378-1119(88)90604-X;
Morita T., Tondella M.L.C., Takemoto Y., Hashido K., Ichinose Y.,
Nozaki M., Matsushiro A.;
"Nucleotide sequence of mouse EndoA cytokeratin cDNA reveals
polypeptide characteristics of the type-II keratin subfamily.";
Gene 68:109-117(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2467842; DOI=10.1016/0378-1119(88)90106-0;
Ouellet T., Levac P., Royal A.;
"Complete sequence of the mouse type-II keratin EndoA: its amino-
terminal region resembles mitochondrial signal peptides.";
Gene 70:75-84(1988).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv; TISSUE=Liver;
PubMed=1717348; DOI=10.1016/0378-1119(91)90247-9;
Tamai Y., Takemoto Y., Matsumoto M., Morita T., Matsushiro A.,
Nozaki M.;
"Sequence of the EndoA gene encoding mouse cytokeratin and its
methylation state in the CpG-rich region.";
Gene 104:169-176(1991).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Amnion, Blastocyst, Embryo, Placenta, Stomach, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II, and FVB/N; TISSUE=Colon, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 103-114, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[8]
INTERACTION WITH KRT20, AND TISSUE SPECIFICITY.
PubMed=12857878; DOI=10.1091/mbc.E03-02-0059;
Zhou Q., Toivola D.M., Feng N., Greenberg H.B., Franke W.W.,
Omary M.B.;
"Keratin 20 helps maintain intermediate filament organization in
intestinal epithelia.";
Mol. Biol. Cell 14:2959-2971(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-482 AND SER-489,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-259; SER-482;
SER-485 AND SER-489, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Kidney, Liver, Lung, Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
PHOSPHORYLATION AT SER-80 BY MAPK.
PubMed=20724476; DOI=10.1074/jbc.M110.132357;
Menon M.B., Schwermann J., Singh A.K., Franz-Wachtel M., Pabst O.,
Seidler U., Omary M.B., Kotlyarov A., Gaestel M.;
"p38 MAP kinase and MAPKAP kinases MK2/3 cooperatively phosphorylate
epithelial keratins.";
J. Biol. Chem. 285:33242-33251(2010).
[13]
INTERACTION WITH EPPK1.
PubMed=25617501; DOI=10.1016/j.jhep.2015.01.007;
Szabo S., Woegenstein K.L., Oesterreicher C.H., Guldiken N., Chen Y.,
Doler C., Wiche G., Boor P., Haybaeck J., Strnad P., Fuchs P.;
"Epiplakin attenuates experimental mouse liver injury by chaperoning
keratin reorganization.";
J. Hepatol. 62:1357-1366(2015).
-!- FUNCTION: Together with KRT19, helps to link the contractile
apparatus to dystrophin at the costameres of striated muscle.
{ECO:0000250}.
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
KRT8 associates with KRT18. Associates with KRT20. Interacts with
PNN. When associated with KRT19, interacts with DMD. Interacts
with TCHP. Interacts with APEX1 (By similarity). Interacts with
GPER1 (By similarity). Interacts with EPPK1 (PubMed:25617501).
{ECO:0000250, ECO:0000269|PubMed:25617501}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus,
nucleoplasm {ECO:0000250}. Nucleus matrix {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in abundance in the epithelia of
colon, bladder, ileum, and stomach, with lower expression observed
in earskin (at protein level). Also expressed in pancreas, liver,
dudenum and jejunum. {ECO:0000269|PubMed:12857878}.
-!- PTM: Phosphorylation on serine residues is enhanced during EGF
stimulation and mitosis. Ser-80 phosphorylation plays an important
role in keratin filament reorganization (By similarity).
{ECO:0000250}.
-!- PTM: O-glycosylated. O-GlcNAcylation at multiple sites increases
solubility, and decreases stability by inducing proteasomal
degradation (By similarity). {ECO:0000250}.
-!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent
manner. {ECO:0000250}.
-!- MISCELLANEOUS: There are two types of cytoskeletal and
microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to
basic; 56-70 kDa).
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA37551.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; X12789; CAA31278.1; -; mRNA.
EMBL; X15662; CAA33697.1; -; Genomic_DNA.
EMBL; M21836; AAA37550.1; -; mRNA.
EMBL; M21836; AAA37551.1; ALT_INIT; mRNA.
EMBL; M22831; AAA37548.1; -; mRNA.
EMBL; D90360; BAA14375.1; -; Genomic_DNA.
EMBL; AK077597; BAC36888.1; -; mRNA.
EMBL; AK145546; BAE26499.1; -; mRNA.
EMBL; AK145679; BAE26585.1; -; mRNA.
EMBL; AK145777; BAE26646.1; -; mRNA.
EMBL; AK146948; BAE27557.1; -; mRNA.
EMBL; AK147044; BAE27630.1; -; mRNA.
EMBL; AK166737; BAE38980.1; -; mRNA.
EMBL; AK166768; BAE39006.1; -; mRNA.
EMBL; AK166854; BAE39072.1; -; mRNA.
EMBL; AK166960; BAE39143.1; -; mRNA.
EMBL; AK166993; BAE39172.1; -; mRNA.
EMBL; AK167120; BAE39268.1; -; mRNA.
EMBL; AK167269; BAE39382.1; -; mRNA.
EMBL; AK167471; BAE39554.1; -; mRNA.
EMBL; AK168522; BAE40401.1; -; mRNA.
EMBL; AK168540; BAE40418.1; -; mRNA.
EMBL; AK168561; BAE40434.1; -; mRNA.
EMBL; AK168726; BAE40567.1; -; mRNA.
EMBL; AK168910; BAE40723.1; -; mRNA.
EMBL; AK169136; BAE40915.1; -; mRNA.
EMBL; AK169691; BAE41308.1; -; mRNA.
EMBL; BC094009; AAH94009.1; -; mRNA.
EMBL; BC106154; AAI06155.1; -; mRNA.
CCDS; CCDS27868.1; -.
PIR; JS0658; JS0658.
PIR; JT0407; JT0407.
PIR; S05474; S05474.
RefSeq; NP_112447.2; NM_031170.2.
UniGene; Mm.358618; -.
ProteinModelPortal; P11679; -.
SMR; P11679; -.
BioGrid; 201037; 7.
IntAct; P11679; 3.
MINT; MINT-1859050; -.
STRING; 10090.ENSMUSP00000023952; -.
iPTMnet; P11679; -.
PhosphoSitePlus; P11679; -.
SWISS-2DPAGE; P11679; -.
MaxQB; P11679; -.
PaxDb; P11679; -.
PeptideAtlas; P11679; -.
PRIDE; P11679; -.
Ensembl; ENSMUST00000023952; ENSMUSP00000023952; ENSMUSG00000049382.
GeneID; 16691; -.
KEGG; mmu:16691; -.
UCSC; uc007xui.1; mouse.
CTD; 3856; -.
MGI; MGI:96705; Krt8.
eggNOG; ENOG410IG4R; Eukaryota.
eggNOG; ENOG410YY6B; LUCA.
GeneTree; ENSGT00760000118796; -.
HOVERGEN; HBG013015; -.
InParanoid; P11679; -.
KO; K07605; -.
OMA; IQKRTDM; -.
OrthoDB; EOG091G09KR; -.
PhylomeDB; P11679; -.
TreeFam; TF317854; -.
Reactome; R-MMU-6805567; Keratinization.
Reactome; R-MMU-6809371; Formation of the cornified envelope.
PRO; PR:P11679; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000049382; -.
CleanEx; MM_KRT8; -.
Genevisible; P11679; MM.
GO; GO:0016327; C:apicolateral plasma membrane; IDA:UniProtKB.
GO; GO:0071944; C:cell periphery; IDA:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0043034; C:costamere; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005882; C:intermediate filament; IDA:MGI.
GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
GO; GO:0045095; C:keratin filament; IEA:Ensembl.
GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0042383; C:sarcolemma; IDA:MGI.
GO; GO:0030018; C:Z disc; IDA:MGI.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0060706; P:cell differentiation involved in embryonic placenta development; IGI:MGI.
GO; GO:0000904; P:cell morphogenesis involved in differentiation; TAS:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:0097284; P:hepatocyte apoptotic process; IMP:MGI.
GO; GO:0007275; P:multicellular organism development; TAS:UniProtKB.
GO; GO:0051599; P:response to hydrostatic pressure; IEA:Ensembl.
GO; GO:0051707; P:response to other organism; IMP:MGI.
GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:MGI.
InterPro; IPR001664; IF.
InterPro; IPR018039; Intermediate_filament_CS.
InterPro; IPR032444; Keratin_2_head.
InterPro; IPR003054; Keratin_II.
PANTHER; PTHR23239; PTHR23239; 1.
Pfam; PF00038; Filament; 1.
Pfam; PF16208; Keratin_2_head; 1.
PRINTS; PR01276; TYPE2KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Cytoplasm;
Direct protein sequencing; Glycoprotein; Intermediate filament;
Isopeptide bond; Keratin; Methylation; Nucleus; Phosphoprotein;
Reference proteome; Ubl conjugation.
CHAIN 1 490 Keratin, type II cytoskeletal 8.
/FTId=PRO_0000063741.
REGION 1 96 Head.
REGION 97 403 Rod.
REGION 97 132 Coil 1A.
REGION 133 149 Linker 1.
REGION 150 241 Coil 1B.
REGION 242 265 Linker 12.
REGION 266 403 Coil 2.
REGION 267 387 Necessary for interaction with PNN.
{ECO:0000250}.
REGION 404 490 Tail.
COMPBIAS 9 51 Ser-rich.
SITE 347 347 Stutter.
MOD_RES 9 9 Phosphoserine; by PKC/PRKCE.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 23 23 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 24 24 Phosphoserine; by PKC/PRKCE.
{ECO:0000250|UniProtKB:P05787,
ECO:0000305}.
MOD_RES 26 26 Phosphothreonine.
{ECO:0000250|UniProtKB:Q10758}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 32 32 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000250|UniProtKB:Q10758}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 40 40 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000250|UniProtKB:Q10758}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000250|UniProtKB:Q10758}.
MOD_RES 49 49 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 49 49 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 51 51 Phosphoserine.
{ECO:0000250|UniProtKB:Q10758}.
MOD_RES 80 80 Phosphoserine; by MAPK.
{ECO:0000269|PubMed:20724476}.
MOD_RES 107 107 N6-malonyllysine. {ECO:0000250}.
MOD_RES 213 213 N6-acetyllysine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 259 259 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 301 301 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 331 331 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 336 336 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 406 406 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 410 410 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 416 416 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 423 423 Phosphoserine.
{ECO:0000250|UniProtKB:Q10758}.
MOD_RES 430 430 Phosphoserine.
{ECO:0000250|UniProtKB:Q10758}.
MOD_RES 432 432 Phosphoserine.
{ECO:0000250|UniProtKB:Q10758}.
MOD_RES 438 438 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 482 482 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 484 484 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 485 485 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 489 489 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 128 128 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 136 136 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 203 203 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 203 203 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 291 291 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 301 301 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 310 310 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 331 331 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 399 399 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 479 479 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 479 479 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05787}.
CONFLICT 12 35 MSTSGPRAFSSRSFTSGPGARISS -> NVYSVGLLASARS
GSWTGSASTA (in Ref. 3; AAA37548).
{ECO:0000305}.
CONFLICT 40 58 RVGSSSSSFRGSMGTGVGL -> GRACQLGSSFGEAWHGVS
(in Ref. 3; AAA37548). {ECO:0000305}.
CONFLICT 52 52 M -> L (in Ref. 6; AAI06155).
{ECO:0000305}.
CONFLICT 75 75 N -> D (in Ref. 3; AAA37548).
{ECO:0000305}.
CONFLICT 83 87 KLEVD -> QLSL (in Ref. 3; AAA37548).
{ECO:0000305}.
CONFLICT 108 108 F -> L (in Ref. 5; BAE39554).
{ECO:0000305}.
CONFLICT 190 191 NK -> QQ (in Ref. 1; CAA31278).
{ECO:0000305}.
CONFLICT 312 312 E -> G (in Ref. 5; BAE40567).
{ECO:0000305}.
CONFLICT 325 325 Missing (in Ref. 1; CAA31278).
{ECO:0000305}.
CONFLICT 368 368 R -> P (in Ref. 1; CAA31278).
{ECO:0000305}.
CONFLICT 385 385 N -> K (in Ref. 5; BAE38980/BAE39006).
{ECO:0000305}.
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


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