ID UB2G2_HUMAN Reviewed; 165 AA. AC P60604; P56554; DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2004, sequence version 1. DT 16-DEC-2008, entry version 59. DE RecName: Full=Ubiquitin-conjugating enzyme E2 G2; DE EC=6.3.2.19; DE AltName: Full=Ubiquitin-protein ligase G2; DE AltName: Full=Ubiquitin carrier protein G2; GN Name=UBE2G2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98360100; PubMed=9693041; DOI=10.1006/geno.1998.5263; RA Katsanis N., Fisher E.M.C.; RT "Identification, expression, and chromosomal localization of ubiquitin RT conjugating enzyme 7 (UBE2G2), a human homologue of the Saccharomyces RT cerevisiae UBC7 gene."; RL Genomics 51:128-131(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=20289799; PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., RA Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS). RX PubMed=16582478; DOI=10.1107/S1744309106009006; RA Arai R., Yoshikawa S., Murayama K., Imai Y., Takahashi R., RA Shirouzu M., Yokoyama S.; RT "Structure of human ubiquitin-conjugating enzyme E2 G2 RT (UBE2G2/UBC7)."; RL Acta Crystallogr. F 62:330-334(2006). CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other CC proteins. Involved in endoplasmic reticulum-associated degradation CC (ERAD). CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP + CC diphosphate + protein N-ubiquityllysine. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- INTERACTION: CC Q2TAA5:ALG11; NbExp=1; IntAct=EBI-1051028, EBI-1048799; CC Q9UKV5:AMFR; NbExp=1; IntAct=EBI-1051028, EBI-1046367; CC P31146:CORO1A; NbExp=1; IntAct=EBI-1051028, EBI-1046676; CC Q9UDY8:MALT1; NbExp=1; IntAct=EBI-1051028, EBI-1047372; CC Q9Y4E8:USP15; NbExp=1; IntAct=EBI-1051028, EBI-1043104; CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF032456; AAC32312.1; -; mRNA. DR EMBL; BT006914; AAP35560.1; -; mRNA. DR EMBL; AL163300; CAB90551.1; -; Genomic_DNA. DR EMBL; BC001738; AAH01738.1; -; mRNA. DR EMBL; BC008351; AAH08351.1; -; mRNA. DR EMBL; BC011569; AAH11569.1; -; mRNA. DR RefSeq; NP_003334.2; -. DR RefSeq; NP_872630.1; -. DR UniGene; Hs.529420; -. DR UniGene; Hs.701398; -. DR PDB; 2CYX; X-ray; 2.56 A; A/B/C=1-165. DR PDBsum; 2CYX; -. DR IntAct; P60604; 6. DR PRIDE; P60604; -. DR Ensembl; ENSG00000184787; Homo sapiens. DR GeneID; 7327; -. DR KEGG; hsa:7327; -. DR GeneCards; GC21M045013; -. DR H-InvDB; HIX0016172; -. DR HGNC; HGNC:12483; UBE2G2. DR HPA; HPA003332; -. DR MIM; 603124; gene. DR PharmGKB; PA37132; -. DR HOGENOM; P60604; -. DR HOVERGEN; P60604; -. DR NextBio; 28670; -. DR ArrayExpress; P60604; -. DR CleanEx; HS_UBE2G2; -. DR GermOnline; ENSG00000184787; Homo sapiens. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC. DR GO; GO:0043687; P:post-translational protein modification; IEA:InterPro. DR GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro. DR InterPro; IPR016135; UBQ-conjugat/RWD-like. DR InterPro; IPR000608; UBQ-conjugat_E2. DR Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1. DR PANTHER; PTHR11621; UBQ-conjugat_E2; 1. DR Pfam; PF00179; UQ_con; 1. DR ProDom; PD000461; UBQ_conjugat; 1. DR SMART; SM00212; UBCc; 1. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Ligase; Ubl conjugation pathway. FT CHAIN 1 165 Ubiquitin-conjugating enzyme E2 G2. FT /FTId=PRO_0000082483. FT ACT_SITE 89 89 Glycyl thioester intermediate. FT CONFLICT 12 12 E -> V (in Ref. 1; AAC32312). FT CONFLICT 101 107 MGYESSA -> HGLREQP (in Ref. 1; AAC32312). FT HELIX 1 18 FT STRAND 24 30 FT STRAND 36 42 FT TURN 48 51 FT STRAND 53 59 FT TURN 62 65 FT STRAND 70 75 FT STRAND 86 88 FT HELIX 91 93 FT HELIX 105 108 FT HELIX 116 128 FT HELIX 135 137 FT HELIX 138 145 FT HELIX 148 162 SQ SEQUENCE 165 AA; 18566 MW; 74DEC732A79575E3 CRC64; MAGTALKRLM AEYKQLTLNP PEGIVAGPMN EENFFEWEAL IMGPEDTCFE FGVFPAILSF PLDYPLSPPK MRFTCEMFHP NIYPDGRVCI SILHAPGDDP MGYESSAERW SPVQSVEKIL LSVVSMLAEP NDESGANVDA SKMWRDDREQ FYKIAKQIVQ KSLGL //