eF-site ID 1r4m-ABCDEFGHIJKL PDB Code 1r4m Chain A, B, C, D, E, F, G, H, I, J, K, L Title APPBP1-UBA3-NEDD8, an E1-ubiquitin-like protein complex 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 I residue 127-152 type prosite sequence KERVEEKEGIPPQQQRLIYSGKQMND description UBIQUITIN_1 Ubiquitin domain signature. KerVeEkegIPpqqQrLIYsGkqmnD source prosite : PS00299 14) chain B residue 216 type ACT_SITE sequence A description Glycyl thioester intermediate source Swiss-Prot : SWS_FT_FI1 15) chain D residue 216 type ACT_SITE sequence A description Glycyl thioester intermediate source Swiss-Prot : SWS_FT_FI1 16) chain F residue 216 type ACT_SITE sequence A description Glycyl thioester intermediate source Swiss-Prot : SWS_FT_FI1 17) chain H residue 216 type ACT_SITE sequence A description Glycyl thioester intermediate source Swiss-Prot : SWS_FT_FI1 18) chain K residue 108 type ACT_SITE sequence L description Glycyl thioester intermediate source Swiss-Prot : SWS_FT_FI1 19) chain K residue 144 type ACT_SITE sequence I description Glycyl thioester intermediate source Swiss-Prot : SWS_FT_FI1 20) chain L residue 108 type ACT_SITE sequence L description Glycyl thioester intermediate source Swiss-Prot : SWS_FT_FI1 21) chain L residue 144 type ACT_SITE sequence I description Glycyl thioester intermediate source Swiss-Prot : SWS_FT_FI1 22) chain B residue 79 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI2 23) chain B residue 127 type BINDING sequence I description BINDING => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI2 24) chain D residue 79 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI2 25) chain D residue 127 type BINDING sequence I description BINDING => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI2 26) chain F residue 79 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI2 27) chain F residue 127 type BINDING sequence I description BINDING => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI2 28) chain H residue 79 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI2 29) chain H residue 127 type BINDING sequence I description BINDING => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI2 30) chain B residue 190 type SITE sequence R description Determines specificity for NEDD8 source Swiss-Prot : SWS_FT_FI3 31) chain D residue 190 type SITE sequence R description Determines specificity for NEDD8 source Swiss-Prot : SWS_FT_FI3 32) chain F residue 190 type SITE sequence R description Determines specificity for NEDD8 source Swiss-Prot : SWS_FT_FI3 33) chain H residue 190 type SITE sequence R description Determines specificity for NEDD8 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 346 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:Q8VBW6 source Swiss-Prot : SWS_FT_FI4 35) chain C residue 346 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:Q8VBW6 source Swiss-Prot : SWS_FT_FI4 36) chain E residue 346 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:Q8VBW6 source Swiss-Prot : SWS_FT_FI4 37) chain G residue 346 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:Q8VBW6 source Swiss-Prot : SWS_FT_FI4 38) chain K residue 176 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:Q8VBW6 source Swiss-Prot : SWS_FT_FI4 39) chain L residue 176 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:Q8VBW6 source Swiss-Prot : SWS_FT_FI4

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