ID HA11_MOUSE Reviewed; 362 AA. AC P01899; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 2. DT 02-SEP-2026, entry version 223. DE RecName: Full=H-2 class I histocompatibility antigen, D-B alpha chain; DE Short=H-2D(B); DE Flags: Precursor; GN Name=H2-D1; 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]. RC STRAIN=C3H/HeJ; RX PubMed=3680952; DOI=10.4049/jimmunol.139.11.3878; RA Watts S., Vogel J.M., Harriman W.D., Itoh T., Stauss H.J., Goodenow R.S.; RT "DNA sequence analysis of the C3H H-2Kk and H-2Dk loci. Evolutionary RT relationships to H-2 genes from four other mouse strains."; RL J. Immunol. 139:3878-3885(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=NOD/LT; RA Girgis K.R., Capra D.J., Stroynowski I.; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/10; RX PubMed=9869916; RA Wang M., Stepkowski S.M., Hebert J.S., Tian L., Yu J., Kahan B.D.; RT "Nucleotide sequences of three H-2K and three H-2D complementary DNA clones RT coding mouse class I MHC heavy chain proteins."; RL Ann. Transplant. 1:26-31(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 105-362. RX PubMed=7118211; DOI=10.1007/bf00364437; RA Reyes A.A., Schold M., Wallace R.B.; RT "The complete amino acid sequence of the murine transplantation antigen H- RT 2Db as deduced by molecular cloning."; RL Immunogenetics 16:1-9(1982). RN [5] RP PROTEIN SEQUENCE OF 25-122. RX PubMed=7225204; DOI=10.1016/s0021-9258(19)69694-8; RA Maloy W.L., Nathenson S.G., Coligan J.E.; RT "Primary structure of murine major histocompatibility complex alloantigens. RT Amino acid sequence of the NH2-terminal ninety-eight residues of the H-2Db RT glycoprotein."; RL J. Biol. Chem. 256:2863-2872(1981). RN [6] RP PROTEIN SEQUENCE OF 253-308 AND 332-358. RX PubMed=7118212; DOI=10.1007/bf00364438; RA Maloy W.L., Coligan J.E.; RT "Primary structure of the H-2Db alloantigen. II. Additional amino acid RT sequence information, localization of a third site of glycosylation and RT evidence for K and D region specific sequences."; RL Immunogenetics 16:11-22(1982). RN [7] RP GLYCOSYLATION AT ASN-110 AND ASN-280. RX PubMed=3980466; DOI=10.1016/s0021-9258(18)89229-8; RA Swiedler S.J., Freed J.H., Tarentino A.L., Plummer T.H. Jr., Hart G.W.; RT "Oligosaccharide microheterogeneity of the murine major histocompatibility RT antigens. Reproducible site-specific patterns of sialylation and branching RT in asparagine-linked oligosaccharides."; RL J. Biol. Chem. 260:4046-4054(1985). RN [8] RP UBIQUITINATION, INTERACTION WITH MURID HERPESVIRUS 4 K3, AND MUTAGENESIS OF RP LYS-55; LYS-92; LYS-155; LYS-170; LYS-197; LYS-210; LYS-220; LYS-267; RP LYS-277; LYS-332; THR-337; LYS-340; 350-SER--SER-356 AND 360-CYS-LYS-361. RX PubMed=17502423; DOI=10.1083/jcb.200611063; RA Wang X., Herr R.A., Chua W.J., Lybarger L., Wiertz E.J., Hansen T.H.; RT "Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic RT tail can induce ERAD of MHC-I by viral E3 ligase mK3."; RL J. Cell Biol. 177:613-624(2007). RN [9] RP UBIQUITINATION AT SER-353, INTERACTION WITH MURID HERPESVIRUS 4 K3, AND RP MUTAGENESIS OF LYS-332; THR-337; LYS-340; 350-SER--SER-352; SER-356 AND RP 360-CYS-LYS-361. RX PubMed=19951915; DOI=10.1083/jcb.200908036; RA Wang X., Herr R.A., Rabelink M., Hoeben R.C., Wiertz E.J., Hansen T.H.; RT "Ube2j2 ubiquitinates hydroxylated amino acids on ER-associated degradation RT substrates."; RL J. Cell Biol. 187:655-668(2009). RN [10] RP UBIQUITINATION, INTERACTION WITH MURID HERPESVIRUS 4 K3, AND MUTAGENESIS OF RP LYS-332; THR-337; LYS-340; 350-SER--SER-352; SER-356 AND 360-CYS-LYS-361. RX PubMed=19531064; DOI=10.1111/j.1600-0854.2009.00946.x; RA Herr R.A., Harris J., Fang S., Wang X., Hansen T.H.; RT "Role of the RING-CH domain of viral ligase mK3 in ubiquitination of non- RT lysine and lysine MHC I residues."; RL Traffic 10:1301-1317(2009). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 25-296. RX PubMed=7506996; DOI=10.1016/0092-8674(94)90171-6; RA Young A.C.M., Zhang W., Sacchettini J.C., Nathenson S.G.; RT "The three-dimensional structure of H-2Db at 2.4-A resolution: implications RT for antigen-determinant selection."; RL Cell 76:39-50(1994). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 24-304, AND DISULFIDE BONDS. RX PubMed=10993729; DOI=10.1006/jmbi.2000.4501; RA Tissot A.C., Ciatto C., Mittl P.R., Grutter M.G., Pluckthun A.; RT "Viral escape at the molecular level explained by quantitative T-cell RT receptor/peptide/MHC interactions and the crystal structure of a RT peptide/MHC complex."; RL J. Mol. Biol. 302:873-885(2000). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with murid herpesvirus 4 protein K3 (mK3). CC {ECO:0000269|PubMed:17502423, ECO:0000269|PubMed:19531064, CC ECO:0000269|PubMed:19951915}. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. CC -!- PTM: Polyubiquitinated in case of infection by murid herpesvirus 4, by CC the viral E3 ligase K3 (mK3). This modification causes the protein to CC be targeted for rapid degradation by the endoplasmic reticulum- CC associated degradation (ERAD) system. Ubiquitination occurs on lysine, CC as well as serine and threonine residues present in the cytoplasmic CC tail. Serine and threonine residues are subject to ubiquitination via CC ester bonds instead of the usual isopeptide linkage. CC {ECO:0000269|PubMed:17502423, ECO:0000269|PubMed:19531064, CC ECO:0000269|PubMed:19951915}. CC -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA39580.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M18523; AAA53200.1; -; Genomic_DNA. DR EMBL; L36068; AAA89206.1; -; mRNA. DR EMBL; U47325; AAB17603.1; -; mRNA. DR EMBL; K00129; AAA39580.1; ALT_INIT; mRNA. DR CCDS; CCDS57074.1; -. DR PIR; B60854; B60854. DR PIR; I56002; HLMSDB. DR RefSeq; NP_034510.3; NM_010380.3. DR PDB; 1BZ9; X-ray; 2.80 A; A=26-299. DR PDB; 1CE6; X-ray; 2.90 A; A=25-298. DR PDB; 1FFN; X-ray; 2.70 A; A/D=26-298. DR PDB; 1FFO; X-ray; 2.65 A; A/D=26-298. DR PDB; 1FFP; X-ray; 2.60 A; A/D=26-298. DR PDB; 1FG2; X-ray; 2.75 A; A/D/G/J=25-304. DR PDB; 1HOC; X-ray; 2.40 A; A=25-296. DR PDB; 1INQ; X-ray; 2.20 A; A=25-299. DR PDB; 1JPF; X-ray; 2.18 A; A=25-304. DR PDB; 1JPG; X-ray; 2.20 A; A=25-304. DR PDB; 1JUF; X-ray; 2.00 A; A=25-300. DR PDB; 1N3N; X-ray; 3.00 A; A/C/E/G=25-304. DR PDB; 1N5A; X-ray; 2.85 A; A/D/G/J=25-300. DR PDB; 1QLF; X-ray; 2.65 A; A=25-300. DR PDB; 1S7U; X-ray; 2.20 A; A/D/G/J=25-362. DR PDB; 1S7V; X-ray; 2.20 A; A/D=25-362. DR PDB; 1S7W; X-ray; 2.40 A; A/D/G/J=25-362. DR PDB; 1S7X; X-ray; 2.41 A; A/D/G/J=25-362. DR PDB; 1WBX; X-ray; 1.90 A; A=25-300. DR PDB; 1WBY; X-ray; 2.30 A; A=25-300. DR PDB; 1YN6; X-ray; 2.20 A; A=26-298. DR PDB; 1YN7; X-ray; 2.20 A; A=26-298. DR PDB; 1ZHB; X-ray; 2.70 A; A/D/G/J=25-300. DR PDB; 2CII; X-ray; 2.55 A; A=25-299. DR PDB; 2F74; X-ray; 2.70 A; A/D=25-300. DR PDB; 2VE6; X-ray; 2.65 A; A/D/G/J=25-301. DR PDB; 2ZOK; X-ray; 2.10 A; A/C/E/G=25-299. DR PDB; 2ZOL; X-ray; 2.70 A; A/C=25-299. DR PDB; 3BUY; X-ray; 2.60 A; A=26-300. DR PDB; 3CC5; X-ray; 1.91 A; A/D=25-300. DR PDB; 3CCH; X-ray; 2.60 A; A/D/G/J=25-300. DR PDB; 3CH1; X-ray; 2.30 A; A/D/G/J=25-300. DR PDB; 3CPL; X-ray; 2.50 A; A/C=25-299. DR PDB; 3FTG; X-ray; 2.60 A; A=25-304. DR PDB; 3L3H; X-ray; 2.70 A; A=26-300. DR PDB; 3PQY; X-ray; 3.19 A; A/F/K/P=26-300. DR PDB; 3QUK; X-ray; 2.41 A; A/D=25-300. DR PDB; 3QUL; X-ray; 2.00 A; A/D/G/J=25-300. DR PDB; 3TBS; X-ray; 2.49 A; A/D=25-300. DR PDB; 3TBT; X-ray; 2.30 A; A/D/G/J=25-300. DR PDB; 3TBV; X-ray; 2.10 A; A/C/E/G=25-300. DR PDB; 3TBW; X-ray; 2.15 A; A/C/E/G=25-300. DR PDB; 3TBY; X-ray; 2.50 A; A/D/G/J=25-300. DR PDB; 3WS3; X-ray; 2.34 A; A/C=26-298. DR PDB; 3WS6; X-ray; 1.98 A; A/B=26-300. DR PDB; 4HUU; X-ray; 2.00 A; A/D=25-304. DR PDB; 4HUV; X-ray; 2.50 A; A/D=25-304. DR PDB; 4HUW; X-ray; 3.16 A; A/C/E/G=25-304. DR PDB; 4HUX; X-ray; 2.20 A; A=25-304. DR PDB; 4HV8; X-ray; 2.00 A; A/C=25-304. DR PDB; 4IHO; X-ray; 2.80 A; A/D=25-300. DR PDB; 4L8B; X-ray; 2.20 A; A=25-304. DR PDB; 4L8C; X-ray; 2.80 A; A/C/E/G=25-304. DR PDB; 4L8D; X-ray; 1.90 A; A/C=25-304. DR PDB; 4NSK; X-ray; 2.60 A; A=25-300. DR PDB; 4PG2; X-ray; 2.80 A; A=25-299. DR PDB; 5E8N; X-ray; 2.25 A; A/D/G/J=25-300. DR PDB; 5E8O; X-ray; 1.98 A; A/D=25-300. DR PDB; 5E8P; X-ray; 2.00 A; A/D=25-300. DR PDB; 5JWD; X-ray; 2.50 A; A=25-298. DR PDB; 5JWE; X-ray; 2.40 A; A/C/E/G=25-300. DR PDB; 5M00; X-ray; 1.95 A; A=25-300. DR PDB; 5M01; X-ray; 1.95 A; A=25-300. DR PDB; 5M02; X-ray; 1.75 A; A=25-300. DR PDB; 5MZM; X-ray; 2.40 A; A/D=25-300. DR PDB; 5OPI; X-ray; 3.30 A; A=25-300. DR PDB; 5SWS; X-ray; 2.86 A; A=25-304. DR PDB; 5SWZ; X-ray; 2.65 A; A/F/K/P=25-304. DR PDB; 5TIL; X-ray; 2.83 A; A/D=25-300. DR PDB; 5TJE; X-ray; 3.20 A; A/C=25-300. DR PDB; 5WLG; X-ray; 2.10 A; A/F=25-302. DR PDB; 5WLI; X-ray; 2.20 A; A/D/G/J=25-302. DR PDB; 6G9Q; X-ray; 1.89 A; A=25-300. DR PDB; 6G9R; X-ray; 2.70 A; A/C/E/G=25-300. DR PDB; 6GB5; X-ray; 2.30 A; A/C=25-362. DR PDB; 6GB7; X-ray; 2.15 A; A/C/E/G=25-362. DR PDB; 6H6D; X-ray; 2.40 A; A/D=25-362. DR PDB; 6MP0; X-ray; 2.00 A; A=25-300. DR PDB; 6MP1; X-ray; 2.21 A; A=25-300. DR PDB; 6WZY; X-ray; 1.50 A; A=25-302. DR PDB; 6X00; X-ray; 1.55 A; A=25-304. DR PDB; 7JWI; X-ray; 3.02 A; A=1-362. DR PDB; 7JWJ; X-ray; 3.25 A; A=1-362. DR PDB; 7N4K; X-ray; 1.85 A; A=25-301. DR PDB; 7N5C; X-ray; 1.87 A; A=25-300. DR PDB; 7N5P; X-ray; 2.09 A; A=25-301. DR PDB; 7N5Q; X-ray; 1.76 A; A/F=25-305. DR PDB; 7N9J; X-ray; 1.74 A; A=25-304. DR PDB; 7NA5; X-ray; 2.50 A; A=25-304. DR PDB; 7P0A; X-ray; 2.43 A; A/D=25-300. DR PDB; 7P0T; X-ray; 2.60 A; A/D=25-300. DR PDB; 7QNG; X-ray; 2.70 A; C=25-300. DR PDB; 8TQA; X-ray; 2.60 A; A=26-298. DR PDB; 9HY4; X-ray; 2.00 A; A/C=24-203. DR AlphaFoldDB; P01899; -. DR MDRepo; P01899; -. DR SMR; P01899; -. DR BioGRID; 200150; 6. DR DIP; DIP-6121N; -. DR MINT; P01899; -. DR STRING; 10090.ENSMUSP00000134570; -. DR GlyCosmos; P01899; 3 sites, No reported glycans. DR iPTMnet; P01899; -. DR PhosphoSitePlus; P01899; -. DR SwissPalm; P01899; -. DR jPOST; P01899; -. DR PaxDb; 10090-ENSMUSP00000134570; -. DR ProteomicsDB; 270921; -. DR Pumba; P01899; -. DR ABCD; P01899; 1 sequenced antibody. DR DNASU; 14964; -. DR Ensembl; ENSMUST00000172785.8; ENSMUSP00000134570.2; ENSMUSG00000073411.13. DR GeneID; 14964; -. DR KEGG; mmu:14964; -. DR UCSC; uc008chg.1; mouse. DR AGR; MGI:95896; -. DR CTD; 14964; -. DR MGI; MGI:95896; H2-D1. DR VEuPathDB; HostDB:ENSMUSG00000073411; -. DR eggNOG; ENOG502RQEK; Eukaryota. DR GeneTree; ENSGT01120000271826; -. DR HOGENOM; CLU_047501_1_1_1; -. DR OMA; GSHTMQV; -. DR OrthoDB; 77324at9989; -. DR PhylomeDB; P01899; -. DR BioGRID-ORCS; 14964; 7 hits in 84 CRISPR screens. DR EvolutionaryTrace; P01899; -. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; ENSMUSG00000073411; Expressed in peripheral lymph node and 261 other cell types or tissues. DR ExpressionAtlas; P01899; baseline and differential. DR GO; GO:0098553; C:lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR CDD; cd21018; IgC1_MHC_Ia_H2Db_H2Ld; 1. DR CDD; cd12087; TM_EGFR-like; 1. DR FunFam; 2.60.40.10:FF:000014; H-2 class I histocompatibility antigen, alpha chain; 1. DR FunFam; 3.30.500.10:FF:000001; H-2 class I histocompatibility antigen, alpha chain; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 3.30.500.10; MHC class I-like antigen recognition-like; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR050208; MHC_class-I_related. DR InterPro; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR037055; MHC_I-like_Ag-recog_sf. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR001039; MHC_I_a_a1/a2. DR InterPro; IPR010579; MHC_I_a_C. DR PANTHER; PTHR16675:SF251; HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, C ALPHA CHAIN; 1. DR PANTHER; PTHR16675; MHC CLASS I-RELATED; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR SUPFAM; SSF54452; MHC antigen-recognition domain; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. DR PDBsum; 1BZ9; -. DR PDBsum; 1CE6; -. DR PDBsum; 1FFN; -. DR PDBsum; 1FFO; -. DR PDBsum; 1FFP; -. DR PDBsum; 1FG2; -. DR PDBsum; 1HOC; -. DR PDBsum; 1INQ; -. DR PDBsum; 1JPF; -. DR PDBsum; 1JPG; -. DR PDBsum; 1JUF; -. DR PDBsum; 1N3N; -. DR PDBsum; 1N5A; -. DR PDBsum; 1QLF; -. DR PDBsum; 1S7U; -. DR PDBsum; 1S7V; -. DR PDBsum; 1S7W; -. DR PDBsum; 1S7X; -. DR PDBsum; 1WBX; -. DR PDBsum; 1WBY; -. DR PDBsum; 1YN6; -. DR PDBsum; 1YN7; -. DR PDBsum; 1ZHB; -. DR PDBsum; 2CII; -. DR PDBsum; 2F74; -. DR PDBsum; 2VE6; -. DR PDBsum; 2ZOK; -. DR PDBsum; 2ZOL; -. DR PDBsum; 3BUY; -. DR PDBsum; 3CC5; -. DR PDBsum; 3CCH; -. DR PDBsum; 3CH1; -. DR PDBsum; 3CPL; -. DR PDBsum; 3FTG; -. DR PDBsum; 3L3H; -. DR PDBsum; 3PQY; -. DR PDBsum; 3QUK; -. DR PDBsum; 3QUL; -. DR PDBsum; 3TBS; -. DR PDBsum; 3TBT; -. DR PDBsum; 3TBV; -. DR PDBsum; 3TBW; -. DR PDBsum; 3TBY; -. DR PDBsum; 3WS3; -. DR PDBsum; 3WS6; -. DR PDBsum; 4HUU; -. DR PDBsum; 4HUV; -. DR PDBsum; 4HUW; -. DR PDBsum; 4HUX; -. DR PDBsum; 4HV8; -. DR PDBsum; 4IHO; -. DR PDBsum; 4L8B; -. DR PDBsum; 4L8C; -. DR PDBsum; 4L8D; -. DR PDBsum; 4NSK; -. DR PDBsum; 4PG2; -. DR PDBsum; 5E8N; -. DR PDBsum; 5E8O; -. DR PDBsum; 5E8P; -. DR PDBsum; 5JWD; -. DR PDBsum; 5JWE; -. DR PDBsum; 5M00; -. DR PDBsum; 5M01; -. DR PDBsum; 5M02; -. DR PDBsum; 5MZM; -. DR PDBsum; 5OPI; -. DR PDBsum; 5SWS; -. DR PDBsum; 5SWZ; -. DR PDBsum; 5TIL; -. DR PDBsum; 5TJE; -. DR PDBsum; 5WLG; -. DR PDBsum; 5WLI; -. DR PDBsum; 6G9Q; -. DR PDBsum; 6G9R; -. DR PDBsum; 6GB5; -. DR PDBsum; 6GB7; -. DR PDBsum; 6H6D; -. DR PDBsum; 6MP0; -. DR PDBsum; 6MP1; -. DR PDBsum; 6WZY; -. DR PDBsum; 6X00; -. DR PDBsum; 7JWI; -. DR PDBsum; 7JWJ; -. DR PDBsum; 7N4K; -. DR PDBsum; 7N5C; -. DR PDBsum; 7N5P; -. DR PDBsum; 7N5Q; -. DR PDBsum; 7N9J; -. DR PDBsum; 7NA5; -. DR PDBsum; 7P0A; -. DR PDBsum; 7P0T; -. DR PDBsum; 7QNG; -. DR PDBsum; 8TQA; -. DR PDBsum; 9HY4; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Immunity; Membrane; MHC I; Phosphoprotein; Reference proteome; Signal; KW Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1..24 FT /evidence="ECO:0000269|PubMed:7225204" FT CHAIN 25..362 FT /note="H-2 class I histocompatibility antigen, D-B alpha FT chain" FT /id="PRO_0000018923" FT TOPO_DOM 25..309 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 310..331 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 332..362 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 209..297 FT /note="Ig-like C1-type" FT REGION 25..114 FT /note="Alpha-1" FT REGION 115..206 FT /note="Alpha-2" FT REGION 207..298 FT /note="Alpha-3" FT REGION 299..309 FT /note="Connecting peptide" FT REGION 340..362 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 353 FT /note="Phosphoserine; alternate" FT /evidence="ECO:0000250|UniProtKB:P01900" FT MOD_RES 356 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P01900" FT CARBOHYD 110 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:3980466, FT ECO:0000269|PubMed:7118212" FT CARBOHYD 200 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000305" FT CARBOHYD 280 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:3980466" FT DISULFID 125..188 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:10993729" FT DISULFID 227..283 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:10993729" FT CROSSLNK 353 FT /note="Glycyl serine ester (Ser-Gly) (interchain with G- FT Cter in ubiquitin); alternate" FT /evidence="ECO:0000305|PubMed:19951915" FT MUTAGEN 55 FT /note="K->R: In K-less, no effect on ubiquitination; when FT associated with R-92, R-155, R-170, R-197, R-210, R-220, FT R-267 and R-277." FT /evidence="ECO:0000269|PubMed:17502423" FT MUTAGEN 92 FT /note="K->R: In K-less, no effect on ubiquitination; when FT associated with R-55, R-155, R-170, R-197, R-210, R-220, FT R-267 and R-277." FT /evidence="ECO:0000269|PubMed:17502423" FT MUTAGEN 155 FT /note="K->R: In K-less, no effect on ubiquitination; when FT associated with R-55, R-92, R-170, R-197, R-210, R-220, FT R-267 and R-277." FT /evidence="ECO:0000269|PubMed:17502423" FT MUTAGEN 170 FT /note="K->R: In K-less, no effect on ubiquitination; when FT associated with R-55, R-92, R-155, R-197, R-210, R-220, FT R-267 and R-277." FT /evidence="ECO:0000269|PubMed:17502423" FT MUTAGEN 197 FT /note="K->R: In K-less, no effect on ubiquitination; when FT associated with R-55, R-92, R-155, R-170, R-210, R-220, FT R-267 and R-277." FT /evidence="ECO:0000269|PubMed:17502423" FT MUTAGEN 210 FT /note="K->R: In K-less, no effect on ubiquitination; when FT associated with R-55, R-92, R-155, R-170, R-197, R-220, FT R-267 and R-277." FT /evidence="ECO:0000269|PubMed:17502423" FT MUTAGEN 220 FT /note="K->R: In K-less, no effect on ubiquitination; when FT associated with R-55, R-92, R-155, R-170, R-197, R-210, FT R-267 and R-277." FT /evidence="ECO:0000269|PubMed:17502423" FT MUTAGEN 267 FT /note="K->R: In K-less, no effect on ubiquitination; when FT associated with R-55, R-92, R-155, R-170, R-197, R-210, FT R-220 and R-277." FT /evidence="ECO:0000269|PubMed:17502423" FT MUTAGEN 277 FT /note="K->R: In K-less, no effect on ubiquitination; when FT associated with R-55, R-92, R-155, R-170, R-197, R-210, FT R-220 and R-267." FT /evidence="ECO:0000269|PubMed:17502423" FT MUTAGEN 332 FT /note="K->R: In Ld KCST-less, strongly impairs FT ubiquitination; when associated with I-337; R-340; FT 350-A--A-356 and 360-R-R-361. In Ld tail 1S, restores FT ubiquitination; when associated I-337; R-340; 350-A--A-352; FT A-356 and 360-R-R-361." FT /evidence="ECO:0000269|PubMed:17502423, FT ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915" FT MUTAGEN 337 FT /note="T->I: In Ld KCST-less, strongly impairs FT ubiquitination; when associated with R-332; R-340; FT 350-A--A-356 and 360-R-R-361. In Ld tail 1S, restores FT ubiquitination; when associated R-332; R-340; 350-A--A-352; FT A-356 and 360-R-R-361." FT /evidence="ECO:0000269|PubMed:17502423, FT ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915" FT MUTAGEN 340 FT /note="K->R: In Ld KCST-less, strongly impairs FT ubiquitination; when associated with R-332; I-337; FT 350-A--A-356 and 360-R-R-361. In Ld tail 1S, restores FT ubiquitination; when associated R-332; I-337; 350-A--A-352; FT A-356 and 360-R-R-361." FT /evidence="ECO:0000269|PubMed:17502423, FT ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915" FT MUTAGEN 350..356 FT /note="SQSSEMS->AQGAEMA: In Ld KCST-less, strongly impairs FT ubiquitination; when associated with R-332; I-337 and FT 360-R-R-361." FT /evidence="ECO:0000269|PubMed:17502423" FT MUTAGEN 350..352 FT /note="SQS->AQG: In Ld tail 1S, restores ubiquitination; FT when associated R-332; I-337; R-340; A-356 and FT 360-R-R-361." FT /evidence="ECO:0000269|PubMed:19531064, FT ECO:0000269|PubMed:19951915" FT MUTAGEN 356 FT /note="S->A: In Ld tail 1S, restores ubiquitination; when FT associated R-332; I-337; R-340 and A-356." FT /evidence="ECO:0000269|PubMed:19531064, FT ECO:0000269|PubMed:19951915" FT MUTAGEN 360..361 FT /note="CK->RR: In Ld KCST-less, strongly impairs FT ubiquitination; when associated with R-332; I-337; R-340 FT and 350-A--A-356. In Ld tail 1S, restores ubiquitination; FT when associated R-332; I-337; R-340; 350-A--A-352; A-356 FT and 360-R-R-361." FT /evidence="ECO:0000269|PubMed:17502423, FT ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915" FT STRAND 28..36 FT /evidence="ECO:0007829|PDB:6WZY" FT STRAND 39..41 FT /evidence="ECO:0007829|PDB:6WZY" FT HELIX 42..44 FT /evidence="ECO:0007829|PDB:6WZY" FT STRAND 45..52 FT /evidence="ECO:0007829|PDB:6WZY" FT STRAND 55..61 FT /evidence="ECO:0007829|PDB:6WZY" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:6WZY" FT STRAND 70..73 FT /evidence="ECO:0007829|PDB:6WZY" FT HELIX 74..78 FT /evidence="ECO:0007829|PDB:6WZY" FT HELIX 81..108 FT /evidence="ECO:0007829|PDB:6WZY" FT TURN 109..111 FT /evidence="ECO:0007829|PDB:7N4K" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:6G9Q" FT STRAND 118..127 FT /evidence="ECO:0007829|PDB:6WZY" FT STRAND 131..142 FT /evidence="ECO:0007829|PDB:6WZY" FT STRAND 145..150 FT /evidence="ECO:0007829|PDB:6WZY" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:6WZY" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:1BZ9" FT HELIX 164..174 FT /evidence="ECO:0007829|PDB:6WZY" FT HELIX 176..183 FT /evidence="ECO:0007829|PDB:6WZY" FT HELIX 184..188 FT /evidence="ECO:0007829|PDB:6WZY" FT HELIX 189..198 FT /evidence="ECO:0007829|PDB:6WZY" FT HELIX 200..203 FT /evidence="ECO:0007829|PDB:6WZY" FT HELIX 207..209 FT /evidence="ECO:0007829|PDB:5E8N" FT STRAND 210..217 FT /evidence="ECO:0007829|PDB:6WZY" FT STRAND 219..221 FT /evidence="ECO:0007829|PDB:7N5Q" FT STRAND 222..235 FT /evidence="ECO:0007829|PDB:6WZY" FT STRAND 238..243 FT /evidence="ECO:0007829|PDB:6WZY" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:3CC5" FT HELIX 249..251 FT /evidence="ECO:0007829|PDB:7N9J" FT STRAND 252..254 FT /evidence="ECO:0007829|PDB:5M02" FT HELIX 255..257 FT /evidence="ECO:0007829|PDB:6WZY" FT STRAND 261..263 FT /evidence="ECO:0007829|PDB:6WZY" FT STRAND 265..274 FT /evidence="ECO:0007829|PDB:6WZY" FT HELIX 278..280 FT /evidence="ECO:0007829|PDB:6WZY" FT STRAND 281..286 FT /evidence="ECO:0007829|PDB:6WZY" FT STRAND 290..292 FT /evidence="ECO:0007829|PDB:6WZY" FT STRAND 294..296 FT /evidence="ECO:0007829|PDB:6WZY" FT HELIX 298..300 FT /evidence="ECO:0007829|PDB:7N4K" SQ SEQUENCE 362 AA; 40836 MW; 6EE6AEF97263FA71 CRC64; MGAMAPRTLL LLLAAALAPT QTRAGPHSMR YFETAVSRPG LEEPRYISVG YVDNKEFVRF DSDAENPRYE PRAPWMEQEG PEYWERETQK AKGQEQWFRV SLRNLLGYYN QSAGGSHTLQ QMSGCDLGSD WRLLRGYLQF AYEGRDYIAL NEDLKTWTAA DMAAQITRRK WEQSGAAEHY KAYLEGECVE WLHRYLKNGN ATLLRTDSPK AHVTHHPRSK GEVTLRCWAL GFYPADITLT WQLNGEELTQ DMELVETRPA GDGTFQKWAS VVVPLGKEQN YTCRVYHEGL PEPLTLRWEP PPSTDSYMVI VAVLGVLGAM AIIGAVVAFV MKRRRNTGGK GGDYALAPGS QSSEMSLRDC KA //