ID   UB2L6_HUMAN             Reviewed;         153 AA.
AC   O14933; A6NDM6; A8MY53; Q8N5D8; Q9UEZ0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 4.
DT   07-JUL-2009, entry version 91.
DE   RecName: Full=Ubiquitin/ISG15-conjugating enzyme E2 L6;
DE            EC=6.3.2.19;
DE   AltName: Full=Ubiquitin-protein ligase L6;
DE   AltName: Full=Ubiquitin carrier protein L6;
DE   AltName: Full=UbcH8;
DE   AltName: Full=Retinoic acid-induced gene B protein;
DE            Short=RIG-B;
GN   Name=UBE2L6; 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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RX   MEDLINE=20355010; PubMed=10894956;
RA   Ardley H.C., Rose S.A., Tan N., Leek J.P., Markham A.F.,
RA   Robinson P.A.;
RT   "Genomic organization of the human ubiquitin-conjugating enzyme gene,
RT   UBE2L6 on chromosome 11q12.";
RL   Cytogenet. Cell Genet. 89:137-140(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Liu T., Mao M., Zhang J., Wu J., Zhang Q., Fu G., Shen Y., Zhou J.,
RA   Yu Y., Wang Z., Chen S., Chen Z.;
RT   "Human retinoic acid induced gene B (RIG-B) mRNA.";
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Thymus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-153 (ISOFORM 1).
RX   MEDLINE=97298053; PubMed=9153201; DOI=10.1074/jbc.272.21.13548;
RA   Kumar S., Kao W.H., Howley P.M.;
RT   "Physical interaction between specific E2 and Hect E3 enzymes
RT   determines functional cooperativity.";
RL   J. Biol. Chem. 272:13548-13554(1997).
RN   [10]
RP   PROTEIN SEQUENCE OF 140-146, FUNCTION IN ISG15 ATTACHMENT, AND
RP   INDUCTION BY INTERFERON BETA.
RX   PubMed=15131269; DOI=10.1073/pnas.0402528101;
RA   Zhao C., Beaudenon S.L., Kelley M.L., Waddell M.B., Yuan W.,
RA   Schulman B.A., Huibregtse J.M., Krug R.M.;
RT   "The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an
RT   IFN-alpha/beta-induced ubiquitin-like protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7578-7582(2004).
RN   [11]
RP   INTERACTION WITH RNF19A.
RX   MEDLINE=21134303; PubMed=11237715; DOI=10.1006/bbrc.2001.4414;
RA   Niwa J., Ishigaki S., Doyu M., Suzuki T., Tanaka K., Sobue G.;
RT   "A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin
RT   ligase activity.";
RL   Biochem. Biophys. Res. Commun. 281:706-713(2001).
RN   [12]
RP   INTERACTION WITH RNF144B.
RX   PubMed=16427630; DOI=10.1016/j.febslet.2005.09.105;
RA   Huang J., Xu L.-G., Liu T., Zhai Z., Shu H.-B.;
RT   "The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent
RT   apoptosis.";
RL   FEBS Lett. 580:940-947(2006).
RN   [13]
RP   INTERACTION WITH RNF19B, AND TISSUE SPECIFICITY.
RX   PubMed=16709802;
RA   Fortier J.M., Kornbluth J.;
RT   "NK lytic-associated molecule, involved in NK cytotoxic function, is
RT   an E3 ligase.";
RL   J. Immunol. 176:6454-6463(2006).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-153.
RA   Mizushima T., Suzuki M., Teshima N., Yamane T., Murata S., Tanaka K.;
RT   "Crystal structure of Ubch8.";
RL   Submitted (MAR-2005) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin or ISG15
CC       to other proteins. Functions in the E6/E6-AP-induced
CC       ubiquitination of p53/TP53.
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with RNF19A, RNF19B and RNF144B.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O14933-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O14933-2; Sequence=VSP_037344;
CC   -!- TISSUE SPECIFICITY: Present in natural killer cells (at protein
CC       level).
CC   -!- INDUCTION: By interferon beta.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
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DR   EMBL; AJ243268; CAB64566.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AJ243269; CAB64566.1; JOINED; Genomic_DNA.
DR   EMBL; AJ243270; CAB64566.1; JOINED; Genomic_DNA.
DR   EMBL; AJ243271; CAB64566.1; JOINED; Genomic_DNA.
DR   EMBL; AF061736; AAD17525.1; -; mRNA.
DR   EMBL; AK315755; BAG38109.1; -; mRNA.
DR   EMBL; CR457126; CAG33407.1; -; mRNA.
DR   EMBL; AK226165; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AP002893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471076; EAW73757.1; -; Genomic_DNA.
DR   EMBL; CH471076; EAW73759.1; -; Genomic_DNA.
DR   EMBL; BC032491; AAH32491.1; -; mRNA.
DR   EMBL; AF031141; AAB86433.1; -; mRNA.
DR   IPI; IPI00329563; -.
DR   RefSeq; NP_004214.1; -.
DR   UniGene; Hs.425777; -.
DR   PDB; 1WZV; X-ray; 2.10 A; A/B=1-152.
DR   PDB; 1WZW; X-ray; 2.40 A; A=1-152.
DR   PDBsum; 1WZV; -.
DR   PDBsum; 1WZW; -.
DR   PRIDE; O14933; -.
DR   Ensembl; ENSG00000156587; Homo sapiens.
DR   GeneID; 9246; -.
DR   KEGG; hsa:9246; -.
DR   GeneCards; GC11M057075; -.
DR   HGNC; HGNC:12490; UBE2L6.
DR   HPA; HPA003328; -.
DR   MIM; 603890; gene.
DR   PharmGKB; PA37139; -.
DR   HOVERGEN; O14933; -.
DR   OMA; O14933; EFTLQFG.
DR   BRENDA; 6.3.2.19; 247.
DR   NextBio; 34661; -.
DR   ArrayExpress; O14933; -.
DR   Bgee; O14933; -.
DR   CleanEx; HS_UBE2L6; -.
DR   GermOnline; ENSG00000156587; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; TAS:ProtInc.
DR   GO; GO:0019941; P:modification-dependent protein catabolic pr...; IEA:UniProtKB-KW.
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   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; Alternative splicing; Complete proteome;
KW   Direct protein sequencing; Ligase; Ubl conjugation pathway.
FT   CHAIN         1    153       Ubiquitin/ISG15-conjugating enzyme E2 L6.
FT                                /FTId=PRO_0000082478.
FT   ACT_SITE     86     86       Glycyl thioester intermediate (By
FT                                similarity).
FT   VAR_SEQ       1     66       Missing (in isoform 2).
FT                                /FTId=VSP_037344.
FT   HELIX         4     16
FT   STRAND       22     27
FT   STRAND       34     39
FT   HELIX        46     48
FT   STRAND       49     56
FT   TURN         59     62
FT   STRAND       67     72
FT   HELIX        88     90
FT   TURN         92     94
FT   HELIX       101    113
FT   STRAND      117    119
FT   HELIX       123    131
FT   HELIX       133    147
SQ   SEQUENCE   153 AA;  17769 MW;  D79768775344EFAE CRC64;
     MMASMRVVKE LEDLQKKPPP YLRNLSSDDA NVLVWHALLL PDQPPYHLKA FNLRISFPPE
     YPFKPPMIKF TTKIYHPNVD ENGQICLPII SSENWKPCTK TCQVLEALNV LVNRPNIREP
     LRMDLADLLT QNPELFRKNA EEFTLRFGVD RPS
//