ID UB2E2_HUMAN Reviewed; 201 AA. AC Q96LR5; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 07-JUL-2009, entry version 72. DE RecName: Full=Ubiquitin-conjugating enzyme E2 E2; DE EC=6.3.2.19; DE AltName: Full=Ubiquitin-protein ligase E2; DE AltName: Full=Ubiquitin carrier protein E2; DE AltName: Full=UbcH8; GN Name=UBE2E2; Synonyms=UBCH8; 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], AND FUNCTION. RX PubMed=9371400; RA Kimura M., Hattori T., Matsuda Y., Yoshioka T., Sumi N., Umeda Y., RA Nakashima S., Okano Y.; RT "cDNA cloning, characterization, and chromosome mapping of UBE2E2 RT encoding a human ubiquitin-conjugating E2 enzyme."; RL Cytogenet. Cell Genet. 78:107-111(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Prostate; 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 [4] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other CC proteins (Probable). CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP + CC diphosphate + protein N-ubiquityllysine. CC -!- PATHWAY: Protein modification; protein ubiquitination. 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; AK057886; BAB71605.1; -; mRNA. DR EMBL; BC022332; AAH22332.1; -; mRNA. DR IPI; IPI00102173; -. DR RefSeq; NP_689866.1; -. DR UniGene; Hs.475688; -. DR UniGene; Hs.595802; -. DR PDB; 1Y6L; X-ray; 1.85 A; A/B/C=55-201. DR PDBsum; 1Y6L; -. DR PhosphoSite; Q96LR5; -. DR PRIDE; Q96LR5; -. DR Ensembl; ENSG00000182247; Homo sapiens. DR GeneID; 7325; -. DR KEGG; hsa:7325; -. DR UCSC; uc003ccg.1; human. DR GeneCards; GC03P023221; -. DR H-InvDB; HIX0018506; -. DR HGNC; HGNC:12478; UBE2E2. DR HPA; HPA003303; -. DR MIM; 602163; gene. DR PharmGKB; PA37128; -. DR HOGENOM; Q96LR5; -. DR HOVERGEN; Q96LR5; -. DR OMA; Q96LR5; NASDCSA. DR BRENDA; 6.3.2.19; 247. DR NextBio; 28662; -. DR ArrayExpress; Q96LR5; -. DR Bgee; Q96LR5; -. DR CleanEx; HS_UBE2E2; -. DR GermOnline; ENSG00000182247; Homo sapiens. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042296; F:ISG15 ligase activity; IDA:HGNC. DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC. DR GO; GO:0032020; P:ISG15-protein conjugation; IDA:HGNC. DR GO; GO:0019941; P:modification-dependent protein catabolic pr...; IEA:UniProtKB-KW. 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 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; ATP-binding; Complete proteome; Ligase; KW Nucleotide-binding; Ubl conjugation pathway. FT CHAIN 1 201 Ubiquitin-conjugating enzyme E2 E2. FT /FTId=PRO_0000082472. FT ACT_SITE 139 139 Glycyl thioester intermediate (By FT similarity). FT HELIX 55 69 FT STRAND 75 82 FT STRAND 86 92 FT TURN 98 101 FT STRAND 103 109 FT TURN 112 115 FT STRAND 120 125 FT HELIX 141 143 FT TURN 144 146 FT HELIX 153 165 FT HELIX 175 183 FT HELIX 185 199 SQ SEQUENCE 201 AA; 22255 MW; 3286FB51E2B9CD3E CRC64; MSTEAQRVDD SPSTSGGSSD GDQRESVQQE PEREQVQPKK KEGKISSKTA AKLSTSAKRI QKELAEITLD PPPNCSAGPK GDNIYEWRST ILGPPGSVYE GGVFFLDITF SPDYPFKPPK VTFRTRIYHC NINSQGVICL DILKDNWSPA LTISKVLLSI CSLLTDCNPA DPLVGSIATQ YMTNRAEHDR MARQWTKRYA T //