ID 2.3.2.26 DE HECT-type E3 ubiquitin transferase. AN HECT E3 ligase. AN ubiquitin transferase HECT-E3. CA S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor CA protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- CA ubiquitinyl-[acceptor protein]-L-lysine. CC -!- In the first step the enzyme transfers ubiquitin from the E2 CC ubiquitin-conjugating enzyme (EC 2.3.2.23) to a cysteine residue in CC its HECT domain (which is located in the C-terminal region), forming CC a thioester bond. CC -!- In a subsequent step the enzyme transfers the ubiquitin to an CC acceptor protein, resulting in the formation of an isopeptide bond CC between the C-terminal glycine residue of ubiquitin and the epsilon- CC amino group of an L-lysine residue of the acceptor protein. cf. CC EC 2.3.2.27 and EC 2.3.2.31. DR C6KTB7, ALTH1_PLAF7; O15033, AREL1_HUMAN; Q8CHG5, AREL1_MOUSE; DR O17736, ETC1_CAEEL ; Q5F4A1, G2E3_CHICK ; Q7L622, G2E3_HUMAN ; DR Q4R9C4, G2E3_MACFA ; Q5RJY2, G2E3_MOUSE ; F1N6G5, HACE1_BOVIN; DR E1C656, HACE1_CHICK; F8W2M1, HACE1_DANRE; Q8IYU2, HACE1_HUMAN; DR Q3U0D9, HACE1_MOUSE; D3ZBM7, HACE1_RAT ; Q6DCL5, HACE1_XENLA; DR Q28BK1, HACE1_XENTR; V6CLA2, HECD1_CAEEL; Q9ULT8, HECD1_HUMAN; DR Q69ZR2, HECD1_MOUSE; Q5U5R9, HECD2_HUMAN; Q8CDU6, HECD2_MOUSE; DR Q5RD78, HECD2_PONAB; Q5T447, HECD3_HUMAN; Q3U487, HECD3_MOUSE; DR Q9Y4D8, HECD4_HUMAN; Q09291, HECW1_CAEEL; Q76N89, HECW1_HUMAN; DR Q8K4P8, HECW1_MOUSE; Q9P2P5, HECW2_HUMAN; Q6I6G8, HECW2_MOUSE; DR Q15751, HERC1_HUMAN; Q9VR91, HERC2_DROME; O95714, HERC2_HUMAN; DR Q4U2R1, HERC2_MOUSE; Q15034, HERC3_HUMAN; Q5GLZ8, HERC4_HUMAN; DR Q6PAV2, HERC4_MOUSE; Q5PQN1, HERC4_RAT ; Q8IVU3, HERC6_HUMAN; DR Q757T0, HUL4_EREGS ; P40985, HUL4_YEAST ; P53119, HUL5_YEAST ; DR Q7Z6Z7, HUWE1_HUMAN; Q7TMY8, HUWE1_MOUSE; P51593, HUWE1_RAT ; DR P51592, HYD_DROME ; Q96J02, ITCH_HUMAN ; Q8C863, ITCH_MOUSE ; DR O94275, MUG30_SCHPO; Q96PU5, NED4L_HUMAN; Q8CFI0, NED4L_MOUSE; DR Q5RBF2, NED4L_PONAB; Q9VVI3, NEDD4_DROME; P46934, NEDD4_HUMAN; DR P46935, NEDD4_MOUSE; Q62940, NEDD4_RAT ; O13834, PTR1_SCHPO ; DR Q92462, PUB1_SCHPO ; Q9UTG2, PUB2_SCHPO ; O14326, PUB3_SCHPO ; DR A1CQG2, RSP5_ASPCL ; B0XQ72, RSP5_ASPFC ; B8N7E5, RSP5_ASPFN ; DR Q4WTF3, RSP5_ASPFU ; A2QQ28, RSP5_ASPNC ; Q2UBP1, RSP5_ASPOR ; DR Q0CCL1, RSP5_ASPTN ; G0S9J5, RSP5_CHATD ; Q5BDP1, RSP5_EMENI ; DR A1D3C5, RSP5_NEOFI ; P39940, RSP5_YEAST ; Q9V853, SMUF1_DROME; DR Q9HCE7, SMUF1_HUMAN; Q9CUN6, SMUF1_MOUSE; Q9PUN2, SMUF1_XENLA; DR A9JRZ0, SMUF2_DANRE; Q9HAU4, SMUF2_HUMAN; A2A5Z6, SMUF2_MOUSE; DR Q2TAS2, SMUF2_XENLA; B5EX33, SOPA_SALA4 ; Q57MS9, SOPA_SALCH ; DR B5FM34, SOPA_SALDC ; Q9S4P4, SOPA_SALDU ; B5QZK6, SOPA_SALEP ; DR B4T918, SOPA_SALHS ; B4SX34, SOPA_SALNS ; B4TMK5, SOPA_SALSV ; DR D0ZMG9, SOPA_SALT1 ; C9X8K0, SOPA_SALTD ; Q8ZNR3, SOPA_SALTY ; DR Q8SSY6, SPKUL_DICDI; Q9Y0H4, SUDX_DROME ; Q756G2, TOM1_EREGS ; DR Q9P4Z1, TOM1_NEUCR ; Q03280, TOM1_YEAST ; E1B7Q7, TRIPC_BOVIN; DR F1RCR6, TRIPC_DANRE; Q14669, TRIPC_HUMAN; G5E870, TRIPC_MOUSE; DR F1LP64, TRIPC_RAT ; B4F6W9, TRIPC_XENTR; Q05086, UBE3A_HUMAN; DR O08759, UBE3A_MOUSE; Q7Z3V4, UBE3B_HUMAN; Q9ES34, UBE3B_MOUSE; DR Q08CZ0, UBE3B_XENTR; Q15386, UBE3C_HUMAN; Q80U95, UBE3C_MOUSE; DR Q1JQA1, UBE3D_BOVIN; Q7Z6J8, UBE3D_HUMAN; Q8BX13, UBE3D_MOUSE; DR Q5RFG8, UBE3D_PONAB; Q3T1H6, UBE3D_RAT ; O95071, UBR5_HUMAN ; DR Q80TP3, UBR5_MOUSE ; Q62671, UBR5_RAT ; Q9VL06, UFD4_DROME ; DR P33202, UFD4_YEAST ; Q8GY23, UPL1_ARATH ; Q8H0T4, UPL2_ARATH ; DR Q6WWW4, UPL3_ARATH ; Q9LYZ7, UPL4_ARATH ; Q9SU29, UPL5_ARATH ; DR Q8RWB8, UPL6_ARATH ; Q9SCQ2, UPL7_ARATH ; Q9N2Z7, WWP1_CAEEL ; DR Q9H0M0, WWP1_HUMAN ; Q8BZZ3, WWP1_MOUSE ; O00308, WWP2_HUMAN ; DR Q9DBH0, WWP2_MOUSE ; Q10435, YDE1_SCHPO ; Q1K9C4, YFK7_SCHPO ; //