eF-site ID 3jsv-ABCD PDB Code 3jsv Chain A, B, C, D click to enlarge Title Crystal structure of mouse NEMO CoZi in complex with Lys63-linked di-ubiquitin Classification SIGNALING PROTEIN/TRANSCRIPTION Compound Ubiquitin Source null (NEMO_MOUSE) Sequence A:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQRESTLHLVLRLRGG B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGD C:  QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETV PVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQR EFN D:  LRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLK AQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNK LKVGCH Description Functional site 1) chain B residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106 source Swiss-Prot : SWS_FT_FI12 2) chain B residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 3) chain B residue 76 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 4) chain B residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603 source Swiss-Prot : SWS_FT_FI6 5) chain B residue 76 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI7 6) chain B residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 7) chain B residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 8) chain A residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 9) chain B residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 10) chain B residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577 source Swiss-Prot : SWS_FT_FI11 11) chain B residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127 source Swiss-Prot : SWS_FT_FI10 12) chain B residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860 source Swiss-Prot : SWS_FT_FI9 13) chain C residue 314 type SITE sequence K description Essential for function source Swiss-Prot : SWS_FT_FI2 14) chain C residue 318 type SITE sequence K description Essential for function source Swiss-Prot : SWS_FT_FI2 15) chain C residue 319 type SITE sequence K description Essential for function source Swiss-Prot : SWS_FT_FI2 16) chain D residue 278 type SITE sequence K description Essential for function source Swiss-Prot : SWS_FT_FI2 17) chain D residue 314 type SITE sequence K description Essential for function source Swiss-Prot : SWS_FT_FI2 18) chain D residue 318 type SITE sequence K description Essential for function source Swiss-Prot : SWS_FT_FI2 19) chain D residue 319 type SITE sequence K description Essential for function source Swiss-Prot : SWS_FT_FI2 20) chain B residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 21) chain C residue 278 type SITE sequence K description Essential for function source Swiss-Prot : SWS_FT_FI2 22) chain B residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 23) chain D residue 270 type SITE sequence K description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 24) chain D residue 302 type SITE sequence K description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 25) chain B residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 26) chain C residue 285 type MOD_RES sequence K description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 27) chain C residue 295 type MOD_RES sequence K description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 28) chain D residue 276 type MOD_RES sequence K description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 29) chain D residue 285 type MOD_RES sequence K description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 30) chain D residue 295 type MOD_RES sequence K description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 31) chain B residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3

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