ID A0A8B9XM57_BOSMU Unreviewed; 942 AA. AC A0A8B9XM57; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 02-OCT-2024, entry version 15. DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569}; DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569}; GN Name=WWP1 {ECO:0000313|Ensembl:ENSBGRP00000021359.1}; OS Bos mutus grunniens (Wild yak) (Bos grunniens). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=30521 {ECO:0000313|Ensembl:ENSBGRP00000021359.1, ECO:0000313|Proteomes:UP000694520}; RN [1] {ECO:0000313|Ensembl:ENSBGRP00000021359.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2023) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885, CC ECO:0000256|PIRNR:PIRNR001569}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}. 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 Ensembl; ENSBGRT00000024636.1; ENSBGRP00000021359.1; ENSBGRG00000013430.1. DR GeneTree; ENSGT00940000154635; -. DR UniPathway; UPA00143; -. DR Proteomes; UP000694520; Chromosome 18. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro. DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR CDD; cd04021; C2_E3_ubiquitin_ligase; 1. DR CDD; cd00078; HECTc; 1. DR CDD; cd00201; WW; 4. DR Gene3D; 2.20.70.10; -; 3. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1. DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1. DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR024928; E3_ub_ligase_SMURF1. DR InterPro; IPR050409; E3_ubiq-protein_ligase. DR InterPro; IPR000569; HECT_dom. DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase. DR InterPro; IPR001202; WW_dom. DR InterPro; IPR036020; WW_dom_sf. DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1. DR PANTHER; PTHR11254:SF299; NEDD4-LIKE E3 UBIQUITIN-PROTEIN LIGASE WWP1; 1. DR Pfam; PF00168; C2; 1. DR Pfam; PF00632; HECT; 2. DR Pfam; PF00397; WW; 4. DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 2. DR SMART; SM00239; C2; 1. DR SMART; SM00119; HECTc; 1. DR SMART; SM00456; WW; 4. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1. DR SUPFAM; SSF51045; WW domain; 4. DR PROSITE; PS50004; C2; 1. DR PROSITE; PS50237; HECT; 1. DR PROSITE; PS01159; WW_DOMAIN_1; 4. DR PROSITE; PS50020; WW_DOMAIN_2; 4. PE 4: Predicted; KW Reference proteome {ECO:0000313|Proteomes:UP000694520}; KW Transferase {ECO:0000256|PIRNR:PIRNR001569}; KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786, KW ECO:0000256|PIRNR:PIRNR001569}. FT DOMAIN 1..116 FT /note="C2" FT /evidence="ECO:0000259|PROSITE:PS50004" FT DOMAIN 348..381 FT /note="WW" FT /evidence="ECO:0000259|PROSITE:PS50020" FT DOMAIN 380..413 FT /note="WW" FT /evidence="ECO:0000259|PROSITE:PS50020" FT DOMAIN 455..488 FT /note="WW" FT /evidence="ECO:0000259|PROSITE:PS50020" FT DOMAIN 495..528 FT /note="WW" FT /evidence="ECO:0000259|PROSITE:PS50020" FT DOMAIN 587..942 FT /note="HECT" FT /evidence="ECO:0000259|PROSITE:PS50237" FT REGION 153..182 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 212..289 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 305..363 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 164..178 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 231..289 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 305..324 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 335..353 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 910 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1, FT ECO:0000256|PROSITE-ProRule:PRU00104" SQ SEQUENCE 942 AA; 106693 MW; 970A82308D96F1C6 CRC64; MATASPRSDT SNNHSGRLQL QVTVSSAKLK RKKNWFGTAI YTEVAADGES KKTAKSSSSS NPKWDEQLTV NVTPQTTLEF RVWSHHTIKA DALLGRATVD LKQALLIHNR KLERVKEQLK LCLETKNGVV QTGELTVVLD GLVIEQENIT NGSSSPAIEV QQNGDALHED REPSARTTTR LAAEDTNGID NCVPTNTVVQ NSCCSYVVNG DNTPSPSQVA ARPKNTPAPK PLTSEPANDT VNGDSPSSVP TDNASSTGTA IGSGEPALSS NCTSTPVEDP PVQETLTSSE NNECIVSNSA AFGSEAQSTL DPSTSSSASS SAFEAAKLRQ PDGCVEPVQQ QSGGANTETL PSGWEQRKDP HGRTYYVDHN TRTTTWERPQ PLPPGWERRV DDRGRVYYVD HNTRTTTWQR PTMESVRNFE QWQSQRSQLQ GAMQQFNQRY LYSASMLAAE NDPYGPLPPG WEKRVDSTDR VYFVNHNTKT TQWEDPRTQG LQNEEPLPEG WEIRYTREGV RYFVDHNTRT TTFKDPRNGK SSVTKGGPQI AYERSFRWKL AHFRYLCQSN ALPSHVKINV SRQTLFEDSF QQIMALKPYD LRRRLYVIFR GEEGLDYGGL AREWFFLLSH EVLNPMYCLF EYAGKNNYCL QINPASTINP DHLSYFCFIG RFIAMALFHG KFIDTGFSLP FYKRMLSKKL TIKDLESIDT EFYNSLIWIR DNNIEECGLE MYFSVDMEIL GKVTSHDLKL GGSNILVTEE NKDEYIGLMT EWRFSRGVQE QTKAFLDGFN EVVPLQWLQY FDEKELEVML CGMQEVDLAD WQRNTVYRHY TRNSKQIIWF WQNKWGRERR ASAGDSADAA PGKFVKETDN EVRMRLLQFV TGTCRLPLGG FAELMGSNGP QKFCIEKVGK DTWLPRSHTC FNRLDLPPYK SYEQLKEKLL FAIEETEGFG QE //