eF-site ID 1r4n-ABCDEFGHIJKL PDB Code 1r4n Chain A, B, C, D, E, F, G, H, I, J, K, L Title APPBP1-UBA3-NEDD8, an E1-ubiquitin-like protein complex with ATP Classification CELL CYCLE Compound amyloid beta precursor protein-binding protein 1 Source Homo sapiens (Human) (NEDD8_HUMAN) Sequence A:  KLLKEQKYDRQLRLWGDHGQEALESAHVCLINATATGTEI LKNLVLPGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNR AEAAMEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTV VVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRII IKEHPVIESHPDNALEDLRLDKPFPELREHFQSYDHSHTP WIVIIAKYLAQWYSETNGRIPKTYKEKEDFRDLIRQGILK PEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINIT KQTPSFWILARALKEFVAKEGQGNLPVRGTIPDMIADSGK YIKLQNVYREKAKKDAAAVGNHVAKLLQSIGQAPESISEK ELKLLCSNSAFLRVVRCRSLAEEYGLDTINKDEIISSMDN PDNEIVLYLMLRAVDRFHKQQGRYPGVSNYQVEEDIGKLK SCLTGFLQEYGLSVMVKDDYVHEFCRYGAAEPHTIAAFLG GAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATFQL B:  DWEGRWNHVKKFLERSGPFTHPDFEPSTESLQFLLDTCKV LVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQ FLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN DTFYRQFHIIVCGLDSIIARRWINGMLISLLNYEDGVLDP SSIVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQV NFPMATIASMPRLPEHCIEYVRMLQWPKEQPFGEGVPLDG DDPEHIQWIFQKSLERASQYNIRGVTYRLTQGVVKRIIPA VASTNAVIAAVCATEVFKIATSAYIPLNNYLVFNDVDGLY TYTFEAERKENCPACSQLPQNIQFSPSAKLQEVLDYLTNS ASLQMKSPAITATNRTLYLQSVTSIEERTRKELGLVDGQE AVADVTTPQTVLFKLHFT C:  KLLKEQKYDRQLRLWGDHGQEALESAHVCLINATATGTEI LKNLVLPGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNR AEAAMEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTV VVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRII IKEHPVIESHPDNALEDLRLDKPFPELREHFQSYDHSHTP WIVIIAKYLAQWYSETNGRIPKTYKEKEDFRDLIRQGILK PEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINIT KQTPSFWILARALKEFVAKEGQGNLPVRGTIPDMIADSGK YIKLQNVYREKAKKDAAAVGNHVAKLLQSIGQAPESISEK ELKLLCSNSAFLRVVRCRSLAEEYGLDTINKDEIISSMDN PDNEIVLYLMLRAVDRFHKQQGRYPGVSNYQVEEDIGKLK SCLTGFLQEYGLSVMVKDDYVHEFCRYGAAEPHTIAAFLG GAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATFQL D:  DWEGRWNHVKKFLERSGPFTHPDFEPSTESLQFLLDTCKV LVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQ FLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN DTFYRQFHIIVCGLDSIIARRWINGMLISLLNYEDGVLDP SSIVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQV NFPMATIASMPRLPEHCIEYVRMLQWPKEQPFGEGVPLDG DDPEHIQWIFQKSLERASQYNIRGVTYRLTQGVVKRIIPA VASTNAVIAAVCATEVFKIATSAYIPLNNYLVFNDVDGLY TYTFEAERKENCPACSQLPQNIQFSPSAKLQEVLDYLTNS ASLQMKSPAITATNRTLYLQSVTSIEERTRKELGLVDGQE AVADVTTPQTVLFKLHFT E:  KLLKEQKYDRQLRLWGDHGQEALESAHVCLINATATGTEI LKNLVLPGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNR AEAAMEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTV VVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRII IKEHPVIESHPDNALEDLRLDKPFPELREHFQSYDHSHTP WIVIIAKYLAQWYSETNGRIPKTYKEKEDFRDLIRQGILK PEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINIT KQTPSFWILARALKEFVAKEGQGNLPVRGTIPDMIADSGK YIKLQNVYREKAKKDAAAVGNHVAKLLQSIGQAPESISEK ELKLLCSNSAFLRVVRCRSLAEEYGLDTINKDEIISSMDN PDNEIVLYLMLRAVDRFHKQQGRYPGVSNYQVEEDIGKLK SCLTGFLQEYGLSVMVKDDYVHEFCRYGAAEPHTIAAFLG GAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATFQL F:  DWEGRWNHVKKFLERSGPFTHPDFEPSTESLQFLLDTCKV LVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQ FLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN DTFYRQFHIIVCGLDSIIARRWINGMLISLLNYEDGVLDP SSIVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQV NFPMATIASMPRLPEHCIEYVRMLQWPKEQPFGEGVPLDG DDPEHIQWIFQKSLERASQYNIRGVTYRLTQGVVKRIIPA VASTNAVIAAVCATEVFKIATSAYIPLNNYLVFNDVDGLY TYTFEAERKENCPACSQLPQNIQFSPSAKLQEVLDYLTNS ASLQMKSPAITATNRTLYLQSVTSIEERTRKELGLVDGQE AVADVTTPQTVLFKLHFT G:  KLLKEQKYDRQLRLWGDHGQEALESAHVCLINATATGTEI LKNLVLPGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNR AEAAMEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTV VVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRII IKEHPVIESHPDNALEDLRLDKPFPELREHFQSYDHSHTP WIVIIAKYLAQWYSETNGRIPKTYKEKEDFRDLIRQGILK PEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINIT KQTPSFWILARALKEFVAKEGQGNLPVRGTIPDMIADSGK YIKLQNVYREKAKKDAAAVGNHVAKLLQSIGQAPESISEK ELKLLCSNSAFLRVVRCRSLAEEYGLDTINKDEIISSMDN PDNEIVLYLMLRAVDRFHKQQGRYPGVSNYQVEEDIGKLK SCLTGFLQEYGLSVMVKDDYVHEFCRYGAAEPHTIAAFLG GAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATFQL H:  DWEGRWNHVKKFLERSGPFTHPDFEPSTESLQFLLDTCKV LVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQ FLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN DTFYRQFHIIVCGLDSIIARRWINGMLISLLNYEDGVLDP SSIVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQV NFPMATIASMPRLPEHCIEYVRMLQWPKEQPFGEGVPLDG DDPEHIQWIFQKSLERASQYNIRGVTYRLTQGVVKRIIPA VASTNAVIAAVCATEVFKIATSAYIPLNNYLVFNDVDGLY TYTFEAERKENCPACSQLPQNIQFSPSAKLQEVLDYLTNS ASLQMKSPAITATNRTLYLQSVTSIEERTRKELGLVDGQE AVADVTTPQTVLFKLHFT I:  MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQ QRLIYSGKQMNDEKTAADYKILGGSVLHLVLALRGG J:  MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQ QRLIYSGKQMNDEKTAADYKILGGSVLHLVLALRGG K:  MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQ QRLIYSGKQMNDEKTAADYKILGGSVLHLVLALRGG L:  MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQ QRLIYSGKQMNDEKTAADYKILGGSVLHLVLALRGG Description Functional site 1) chain H residue 199 type sequence C description BINDING SITE FOR RESIDUE ZN H 1 source : AC1 2) chain H residue 202 type sequence C description BINDING SITE FOR RESIDUE ZN H 1 source : AC1 3) chain H residue 343 type sequence C description BINDING SITE FOR RESIDUE ZN H 1 source : AC1 4) chain H residue 346 type sequence C description BINDING SITE FOR RESIDUE ZN H 1 source : AC1 5) chain D residue 338 type sequence E description BINDING SITE FOR RESIDUE ZN J 2 source : AC2 6) chain J residue 148 type sequence K description BINDING SITE FOR RESIDUE ZN J 2 source : AC2 7) chain F residue 199 type sequence C description BINDING SITE FOR RESIDUE ZN F 3 source : AC3 8) chain F residue 202 type sequence C description BINDING SITE FOR RESIDUE ZN F 3 source : AC3 9) chain F residue 343 type sequence C description BINDING SITE FOR RESIDUE ZN F 3 source : AC3 10) chain F residue 346 type sequence C description BINDING SITE FOR RESIDUE ZN F 3 source : AC3 11) chain H residue 340 type sequence K description BINDING SITE FOR RESIDUE ZN H 4 source : AC4 12) chain H residue 373 type sequence S description BINDING SITE FOR RESIDUE ZN H 4 source : AC4 13) chain A residue 15 type sequence R description BINDING SITE FOR RESIDUE ATP B 5 source : AC5 14) chain B residue 56 type sequence A description BINDING SITE FOR RESIDUE ATP B 5 source : AC5 15) chain B residue 57 type sequence G description BINDING SITE FOR RESIDUE ATP B 5 source : AC5 16) chain B residue 79 type sequence D description BINDING SITE FOR RESIDUE ATP B 5 source : AC5 17) chain B residue 80 type sequence M description BINDING SITE FOR RESIDUE ATP B 5 source : AC5 18) chain B residue 81 type sequence D description BINDING SITE FOR RESIDUE ATP B 5 source : AC5 19) chain B residue 90 type sequence R description BINDING SITE FOR RESIDUE ATP B 5 source : AC5 20) chain B residue 91 type sequence Q description BINDING SITE FOR RESIDUE ATP B 5 source : AC5 21) chain B residue 103 type sequence K description BINDING SITE FOR RESIDUE ATP B 5 source : AC5 22) chain B residue 126 type sequence K description BINDING SITE FOR RESIDUE ATP B 5 source : AC5 23) chain B residue 127 type sequence I description BINDING SITE FOR RESIDUE ATP B 5 source : AC5 24) chain B residue 145 type sequence L description BINDING SITE FOR RESIDUE ATP B 5 source : AC5 25) chain B residue 146 type sequence D description BINDING SITE FOR RESIDUE ATP B 5 source : AC5 26) chain B residue 150 type sequence A description BINDING SITE FOR RESIDUE ATP B 5 source : AC5 27) chain I residue 176 type sequence G description BINDING SITE FOR RESIDUE ATP B 5 source : AC5 28) chain C residue 15 type sequence R description BINDING SITE FOR RESIDUE ATP D 6 source : AC6 29) chain D residue 56 type sequence A description BINDING SITE FOR RESIDUE ATP D 6 source : AC6 30) chain D residue 57 type sequence G description BINDING SITE FOR RESIDUE ATP D 6 source : AC6 31) chain D residue 79 type sequence D description BINDING SITE FOR RESIDUE ATP D 6 source : AC6 32) chain D residue 80 type sequence M description BINDING SITE FOR RESIDUE ATP D 6 source : AC6 33) chain D residue 81 type sequence D description BINDING SITE FOR RESIDUE ATP D 6 source : AC6 34) chain D residue 90 type sequence R description BINDING SITE FOR RESIDUE ATP D 6 source : AC6 35) chain D residue 91 type sequence Q description BINDING SITE FOR RESIDUE ATP D 6 source : AC6 36) chain D residue 103 type sequence K description BINDING SITE FOR RESIDUE ATP D 6 source : AC6 37) chain D residue 125 type sequence N description BINDING SITE FOR RESIDUE ATP D 6 source : AC6 38) chain D residue 126 type sequence K description BINDING SITE FOR RESIDUE ATP D 6 source : AC6 39) chain D residue 127 type sequence I description BINDING SITE FOR RESIDUE ATP D 6 source : AC6 40) chain D residue 128 type sequence Q description BINDING SITE FOR RESIDUE ATP D 6 source : AC6 41) chain D residue 145 type sequence L description BINDING SITE FOR RESIDUE ATP D 6 source : AC6 42) chain D residue 146 type sequence D description BINDING SITE FOR RESIDUE ATP D 6 source : AC6 43) chain J residue 176 type sequence G description BINDING SITE FOR RESIDUE ATP D 6 source : AC6 44) chain E residue 15 type sequence R description BINDING SITE FOR RESIDUE ATP F 7 source : AC7 45) chain F residue 56 type sequence A description BINDING SITE FOR RESIDUE ATP F 7 source : AC7 46) chain F residue 57 type sequence G description BINDING SITE FOR RESIDUE ATP F 7 source : AC7 47) chain F residue 79 type sequence D description BINDING SITE FOR RESIDUE ATP F 7 source : AC7 48) chain F residue 80 type sequence M description BINDING SITE FOR RESIDUE ATP F 7 source : AC7 49) chain F residue 81 type sequence D description BINDING SITE FOR RESIDUE ATP F 7 source : AC7 50) chain F residue 87 type sequence N description BINDING SITE FOR RESIDUE ATP F 7 source : AC7 51) chain F residue 90 type sequence R description BINDING SITE FOR RESIDUE ATP F 7 source : AC7 52) chain F residue 91 type sequence Q description BINDING SITE FOR RESIDUE ATP F 7 source : AC7 53) chain F residue 103 type sequence K description BINDING SITE FOR RESIDUE ATP F 7 source : AC7 54) chain F residue 125 type sequence N description BINDING SITE FOR RESIDUE ATP F 7 source : AC7 55) chain F residue 126 type sequence K description BINDING SITE FOR RESIDUE ATP F 7 source : AC7 56) chain F residue 127 type sequence I description BINDING SITE FOR RESIDUE ATP F 7 source : AC7 57) chain F residue 128 type sequence Q description BINDING SITE FOR RESIDUE ATP F 7 source : AC7 58) chain F residue 145 type sequence L description BINDING SITE FOR RESIDUE ATP F 7 source : AC7 59) chain F residue 146 type sequence D description BINDING SITE FOR RESIDUE ATP F 7 source : AC7 60) chain K residue 176 type sequence G description BINDING SITE FOR RESIDUE ATP F 7 source : AC7 61) chain G residue 15 type sequence R description BINDING SITE FOR RESIDUE ATP H 8 source : AC8 62) chain H residue 57 type sequence G description BINDING SITE FOR RESIDUE ATP H 8 source : AC8 63) chain H residue 79 type sequence D description BINDING SITE FOR RESIDUE ATP H 8 source : AC8 64) chain H residue 80 type sequence M description BINDING SITE FOR RESIDUE ATP H 8 source : AC8 65) chain H residue 81 type sequence D description BINDING SITE FOR RESIDUE ATP H 8 source : AC8 66) chain H residue 87 type sequence N description BINDING SITE FOR RESIDUE ATP H 8 source : AC8 67) chain H residue 90 type sequence R description BINDING SITE FOR RESIDUE ATP H 8 source : AC8 68) chain H residue 91 type sequence Q description BINDING SITE FOR RESIDUE ATP H 8 source : AC8 69) chain H residue 103 type sequence K description BINDING SITE FOR RESIDUE ATP H 8 source : AC8 70) chain H residue 125 type sequence N description BINDING SITE FOR RESIDUE ATP H 8 source : AC8 71) chain H residue 126 type sequence K description BINDING SITE FOR RESIDUE ATP H 8 source : AC8 72) chain H residue 127 type sequence I description BINDING SITE FOR RESIDUE ATP H 8 source : AC8 73) chain H residue 128 type sequence Q description BINDING SITE FOR RESIDUE ATP H 8 source : AC8 74) chain H residue 145 type sequence L description BINDING SITE FOR RESIDUE ATP H 8 source : AC8 75) chain H residue 146 type sequence D description BINDING SITE FOR RESIDUE ATP H 8 source : AC8 76) chain L residue 176 type sequence G description BINDING SITE FOR RESIDUE ATP H 8 source : AC8 77) chain I residue 108 type SITE sequence L description Interaction with UBE1C => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI1 78) chain I residue 144 type SITE sequence I description Interaction with UBE1C => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI1 79) chain J residue 108 type SITE sequence L description Interaction with UBE1C => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI1 80) chain J residue 144 type SITE sequence I description Interaction with UBE1C => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI1 81) chain K residue 108 type SITE sequence L description Interaction with UBE1C => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI1 82) chain K residue 144 type SITE sequence I description Interaction with UBE1C => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI1 83) chain L residue 108 type SITE sequence L description Interaction with UBE1C => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI1 84) chain L residue 144 type SITE sequence I description Interaction with UBE1C => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI1 85) chain I residue 140 type MOD_RES sequence Q description (Microbial infection) Deamidated glutamine => ECO:0000269|PubMed:20688984, ECO:0000269|PubMed:21903097, ECO:0000269|PubMed:23175788, ECO:0000269|PubMed:23589306, ECO:0000269|PubMed:26632597 source Swiss-Prot : SWS_FT_FI2 86) chain J residue 140 type MOD_RES sequence Q description (Microbial infection) Deamidated glutamine => ECO:0000269|PubMed:20688984, ECO:0000269|PubMed:21903097, ECO:0000269|PubMed:23175788, ECO:0000269|PubMed:23589306, ECO:0000269|PubMed:26632597 source Swiss-Prot : SWS_FT_FI2 87) chain K residue 140 type MOD_RES sequence Q description (Microbial infection) Deamidated glutamine => ECO:0000269|PubMed:20688984, ECO:0000269|PubMed:21903097, ECO:0000269|PubMed:23175788, ECO:0000269|PubMed:23589306, ECO:0000269|PubMed:26632597 source Swiss-Prot : SWS_FT_FI2 88) chain L residue 140 type MOD_RES sequence Q description (Microbial infection) Deamidated glutamine => ECO:0000269|PubMed:20688984, ECO:0000269|PubMed:21903097, ECO:0000269|PubMed:23175788, ECO:0000269|PubMed:23589306, ECO:0000269|PubMed:26632597 source Swiss-Prot : SWS_FT_FI2 89) chain F residue 79 type MOD_RES sequence D description (Microbial infection) Deamidated glutamine => ECO:0000269|PubMed:20688984, ECO:0000269|PubMed:21903097, ECO:0000269|PubMed:23175788, ECO:0000269|PubMed:23589306, ECO:0000269|PubMed:26632597 source Swiss-Prot : SWS_FT_FI2 90) chain F residue 127 type MOD_RES sequence I description (Microbial infection) Deamidated glutamine => ECO:0000269|PubMed:20688984, ECO:0000269|PubMed:21903097, ECO:0000269|PubMed:23175788, ECO:0000269|PubMed:23589306, ECO:0000269|PubMed:26632597 source Swiss-Prot : SWS_FT_FI2 91) chain H residue 79 type MOD_RES sequence D description (Microbial infection) Deamidated glutamine => ECO:0000269|PubMed:20688984, ECO:0000269|PubMed:21903097, ECO:0000269|PubMed:23175788, ECO:0000269|PubMed:23589306, ECO:0000269|PubMed:26632597 source Swiss-Prot : SWS_FT_FI2 92) chain H residue 127 type MOD_RES sequence I description (Microbial infection) Deamidated glutamine => ECO:0000269|PubMed:20688984, ECO:0000269|PubMed:21903097, ECO:0000269|PubMed:23175788, ECO:0000269|PubMed:23589306, ECO:0000269|PubMed:26632597 source Swiss-Prot : SWS_FT_FI2 93) chain I residue 148 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29595 source Swiss-Prot : SWS_FT_FI3 94) chain J residue 148 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29595 source Swiss-Prot : SWS_FT_FI3 95) chain K residue 148 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29595 source Swiss-Prot : SWS_FT_FI3 96) chain L residue 148 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29595 source Swiss-Prot : SWS_FT_FI3 97) chain I residue 176 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI4 98) chain C residue 346 type CROSSLNK sequence Y description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI4 99) chain J residue 176 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI4 100) chain G residue 346 type CROSSLNK sequence Y description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI4 101) chain K residue 176 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI4 102) chain L residue 176 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI4 103) chain I residue 127-152 type prosite sequence KERVEEKEGIPPQQQRLIYSGKQMND description UBIQUITIN_1 Ubiquitin domain signature. KerVeEkegIPpqqQrLIYsGkqmnD source prosite : PS00299

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