ID H0Z408_TAEGU Unreviewed; 147 AA. AC H0Z408; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 2. DT 24-JUL-2024, entry version 78. DE RecName: Full=E2 ubiquitin-conjugating enzyme {ECO:0000256|ARBA:ARBA00012486}; DE EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486}; GN Name=UBE2D1 {ECO:0000313|Ensembl:ENSTGUP00000005302.2}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae; OC Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000005302.2, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Ensembl:ENSTGUP00000005302.2, ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E., RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P., RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O., RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L., RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C., RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K., RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A., RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000005302.2} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2024) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin- CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin- CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23; CC Evidence={ECO:0000256|ARBA:ARBA00000485}; CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC {ECO:0000256|RuleBase:RU362109}. 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 RefSeq; XP_002188503.1; XM_002188467.2. DR AlphaFoldDB; H0Z408; -. DR SMR; H0Z408; -. DR STRING; 59729.ENSTGUP00000005302; -. DR Ensembl; ENSTGUT00000005355.2; ENSTGUP00000005302.2; ENSTGUG00000005149.2. DR GeneID; 100221279; -. DR KEGG; tgu:100221279; -. DR CTD; 7321; -. DR GeneTree; ENSGT00940000155109; -. DR HOGENOM; CLU_030988_13_3_1; -. DR InParanoid; H0Z408; -. DR OMA; FCELNRE; -. DR OrthoDB; 5478564at2759; -. DR TreeFam; TF101108; -. DR Proteomes; UP000007754; Chromosome 6. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter. DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:Ensembl. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl. DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IEA:Ensembl. DR GO; GO:1902916; P:positive regulation of protein polyubiquitination; IEA:Ensembl. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl. DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl. DR CDD; cd00195; UBCc; 1. DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1. DR InterPro; IPR000608; UBQ-conjugat_E2. DR InterPro; IPR023313; UBQ-conjugating_AS. DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD. DR PANTHER; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 1. DR PANTHER; PTHR24068:SF36; UBIQUITIN-CONJUGATING ENZYME E2 D1; 1. DR Pfam; PF00179; UQ_con; 1. DR SMART; SM00212; UBCc; 1. DR SUPFAM; SSF54495; UBC-like; 1. DR PROSITE; PS00183; UBC_1; 1. DR PROSITE; PS50127; UBC_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU362109}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU362109}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786, KW ECO:0000256|RuleBase:RU362109}. FT DOMAIN 1..147 FT /note="UBC core" FT /evidence="ECO:0000259|PROSITE:PS50127" FT ACT_SITE 85 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10133" SQ SEQUENCE 147 AA; 16602 MW; 2E96FD0179EE119D CRC64; MALKRIQKEL SDLQRDPPAH CSAGPVGDDL FHWQATIMGP PDSAYQGGVF FLTVHFPTDY PFKPPKIAFT TKIYHPNINS NGSICLDILR SQWSPALTVS KVLLSICSLL CDPNPDDPLV PDIAQIYKSD KEKYNRHARE WTQKYAM //