ID   UB2J2_HUMAN             Reviewed;         259 AA.
AC   Q8N2K1; Q96N26; Q96T84;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 2.
DT   25-NOV-2008, entry version 55.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 J2;
DE            EC=6.3.2.19;
DE   AltName: Full=Non-canonical ubiquitin-conjugating enzyme 2;
DE            Short=NCUBE2;
GN   Name=UBE2J2; Synonyms=NCUBE2;
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] (ISOFORM 1).
RX   MEDLINE=21238294; PubMed=11278356; DOI=10.1074/jbc.M007640200;
RA   Tiwari S., Weissman A.M.;
RT   "Endoplasmic reticulum (ER)-associated degradation of T cell receptor
RT   subunits. Involvement of ER-associated ubiquitin-conjugating enzymes
RT   (E2s).";
RL   J. Biol. Chem. 276:16193-16200(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Ovary;
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).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Seems to function in the selective degradation of
CC       misfolded membrane proteins from the endoplasmic reticulum (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type IV membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8N2K1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8N2K1-2; Sequence=VSP_011572;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
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DR   EMBL; AF296658; AAK52609.1; -; mRNA.
DR   EMBL; AK056065; BAB71086.1; -; mRNA.
DR   EMBL; AK075017; BAC11355.1; -; mRNA.
DR   RefSeq; NP_477515.2; -.
DR   RefSeq; NP_919440.1; -.
DR   UniGene; Hs.191987; -.
DR   PDB; 2F4W; X-ray; 2.00 A; A/B=1-185.
DR   PDBsum; 2F4W; -.
DR   SMR; Q8N2K1; 11-171.
DR   Ensembl; ENSG00000160087; Homo sapiens.
DR   GeneID; 118424; -.
DR   KEGG; hsa:118424; -.
DR   HGNC; HGNC:19268; UBE2J2.
DR   PharmGKB; PA134882268; -.
DR   HOVERGEN; Q8N2K1; -.
DR   NextBio; 80253; -.
DR   ArrayExpress; Q8N2K1; -.
DR   CleanEx; HS_UBE2J2; -.
DR   GermOnline; ENSG00000160087; Homo sapiens.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
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   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-KW.
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; FALSE_NEG.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Endoplasmic reticulum; Ligase;
KW   Membrane; Transmembrane; Ubl conjugation pathway.
FT   CHAIN         1    259       Ubiquitin-conjugating enzyme E2 J2.
FT                                /FTId=PRO_0000082596.
FT   TOPO_DOM      1    226       Cytoplasmic (Potential).
FT   TRANSMEM    227    247       Anchor for type IV membrane protein
FT                                (Potential).
FT   TOPO_DOM    248    259       Lumenal (Potential).
FT   ACT_SITE     94     94       Glycyl thioester intermediate (By
FT                                similarity).
FT   VAR_SEQ       1     44       MNSTSSKRAPTTATQRLKQDYLRIKKDPVPYICAEPLPSNI
FT                                LEW -> MWPQDIAGR (in isoform 2).
FT                                /FTId=VSP_011572.
FT   CONFLICT      2      2       N -> S (in Ref. 1; AAK52609).
FT   CONFLICT    100    100       F -> S (in Ref. 2; BAC11355).
FT   CONFLICT    214    238       PNLAGLQQANRHHGLLGGALANLFV -> QTSQGSSRPTGT
FT                                TDSGWRPGELVC (in Ref. 1; AAK52609).
FT   HELIX        13     26
FT   STRAND       32     37
FT   STRAND       40     49
FT   TURN         55     58
FT   STRAND       60     66
FT   TURN         69     72
FT   STRAND       77     80
FT   STRAND       85     87
FT   HELIX       111    123
FT   HELIX       136    151
FT   HELIX       154    159
FT   HELIX       161    167
SQ   SEQUENCE   259 AA;  28925 MW;  7DB1023D294C177E CRC64;
     MNSTSSKRAP TTATQRLKQD YLRIKKDPVP YICAEPLPSN ILEWHYVVRG PEMTPYEGGY
     YHGKLIFPRE FPFKPPSIYM ITPNGRFKCN TRLCLSITDF HPDTWNPAWS VSTILTGLLS
     FMVEKGPTLG SIETSDFTKR QLAVQSLAFN LKDKVFCELF PEVVEEIKQK QKAQDELSSR
     PQTLPLPDVV PDGETHLVQN GIQLLNGHAP GAVPNLAGLQ QANRHHGLLG GALANLFVIV
     GFAAFAYTVK YVLRSIAQE
//