ID H0Z408_TAEGU Unreviewed; 144 AA. AC H0Z408; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-MAR-2016, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTGUP00000005302}; DE Flags: Fragment; GN Name=UBE2D1 {ECO:0000313|Ensembl:ENSTGUP00000005302}; 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; OC Estrildidae; Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000005302, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Ensembl:ENSTGUP00000005302, 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., RA London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B., RA Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., RA Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M., RA Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P., RA Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T., RA Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A., RA Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E., RA Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D., RA Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H., RA Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J., RA 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} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC {ECO:0000256|RuleBase:RU362109}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTGUP00000005302}. 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 EMBL; ABQF01048110; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 59729.ENSTGUP00000005302; -. DR Ensembl; ENSTGUT00000005355; ENSTGUP00000005302; ENSTGUG00000005149. DR eggNOG; KOG0417; Eukaryota. DR eggNOG; COG5078; LUCA. DR GeneTree; ENSGT00760000119012; -. DR InParanoid; H0Z408; -. DR OMA; QEIAREW; -. DR OrthoDB; EOG7PCJGX; -. DR TreeFam; TF101108; -. DR Reactome; R-TGU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha. DR Reactome; R-TGU-141430; Inactivation of APC/C via direct inhibition of the APC/C complex. DR Reactome; R-TGU-174048; APC/C:Cdc20 mediated degradation of Cyclin B. DR Reactome; R-TGU-174084; Autodegradation of Cdh1 by Cdh1:APC/C. DR Reactome; R-TGU-174154; APC/C:Cdc20 mediated degradation of Securin. DR Reactome; R-TGU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1. DR Reactome; R-TGU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A. DR Reactome; R-TGU-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase. DR Reactome; R-TGU-176408; Regulation of APC/C activators between G1/S and early anaphase. DR Reactome; R-TGU-176409; APC/C:Cdc20 mediated degradation of mitotic proteins. DR Reactome; R-TGU-176412; Phosphorylation of the APC/C. DR Reactome; R-TGU-179409; APC-Cdc20 mediated degradation of Nek2A. DR Reactome; R-TGU-2467813; Separation of Sister Chromatids. DR Reactome; R-TGU-2559582; Senescence-Associated Secretory Phenotype (SASP). DR Proteomes; UP000007754; Chromosome 6. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:Ensembl. DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl. DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl. DR Gene3D; 3.10.110.10; -; 1. DR InterPro; IPR000608; UBQ-conjugat_E2. DR InterPro; IPR023313; UBQ-conjugating_AS. DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD. DR Pfam; PF00179; UQ_con; 1. DR SUPFAM; SSF54495; SSF54495; 1. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU362109}; KW Complete proteome {ECO:0000313|Proteomes:UP000007754}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU362109}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}; KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU362109, KW ECO:0000256|SAAS:SAAS00497539}. FT DOMAIN 1 133 UBIQUITIN_CONJUGAT_2. FT {ECO:0000259|PROSITE:PS50127}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSTGUP00000005302}. SQ SEQUENCE 144 AA; 16287 MW; 388FF758ED2F5E80 CRC64; KRIQKELSDL QRDPPAHCSA GPVGDDLFHW QATIMGPPDS AYQGGVFFLT VHFPTDYPFK PPKIAFTTKI YHPNINSNGS ICLDILRSQW SPALTVSKVL LSICSLLCDP NPDDPLVPDI AQIYKSDKEK YNRHAREWTQ KYAM //