ID   UB2Q1_HUMAN             Reviewed;         422 AA.
AC   Q7Z7E8; Q3B841; Q5I0X2; Q6IS04; Q6P7P2; Q96MV4; Q9BVX5; Q9UGL6;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   07-JUL-2009, entry version 57.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 Q1;
DE            EC=6.3.2.19;
DE   AltName: Full=Ubiquitin-protein ligase Q1;
DE   AltName: Full=Ubiquitin carrier protein Q1;
DE   AltName: Full=Protein NICE-5;
GN   Name=UBE2Q1; Synonyms=NICE5, UBE2Q; ORFNames=PRO3094;
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).
RA   Altmann M.E., Schulze E., Adham I.M., Koehler M., Engel W.;
RT   "Isolation and characterization of the human UBE2Q gene and its murine
RT   ortholog.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 163-422 (ISOFORM 1).
RC   TISSUE=Cervix, and Uterus;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-422.
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 282-422, AND TISSUE SPECIFICITY.
RC   TISSUE=Keratinocyte;
RX   MEDLINE=21154910; PubMed=11230159; DOI=10.1101/gr.114801;
RA   Marenholz I., Zirra M., Fischer D.F., Backendorf C., Ziegler A.,
RA   Mischke D.;
RT   "Identification of human epidermal differentiation complex (EDC)-
RT   encoded genes by subtractive hybridization of entire YACs to a gridded
RT   keratinocyte cDNA library.";
RL   Genome Res. 11:341-355(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 312-386.
RC   TISSUE=Fetal liver;
RA   Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA   Liu M., He F.;
RT   "Functional prediction of the coding sequences of 121 new genes
RT   deduced by analysis of cDNA clones from human fetal liver.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 352-422.
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   [8]
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- INTERACTION:
CC       Q9UNE7:STUB1; NbExp=2; IntAct=EBI-1783287, EBI-357085;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7Z7E8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7Z7E8-2; Sequence=VSP_017296;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
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; AY112698; AAM60814.1; -; mRNA.
DR   EMBL; AL592078; CAI16186.1; -; Genomic_DNA.
DR   EMBL; BC000848; AAH00848.1; -; mRNA.
DR   EMBL; BC015316; AAH15316.1; ALT_INIT; mRNA.
DR   EMBL; BC061583; AAH61583.1; ALT_INIT; mRNA.
DR   EMBL; BC070158; AAH70158.1; -; mRNA.
DR   EMBL; BC087836; AAH87836.1; ALT_INIT; mRNA.
DR   EMBL; BC107057; AAI07058.1; ALT_INIT; mRNA.
DR   EMBL; AK056388; BAB71173.1; ALT_INIT; mRNA.
DR   EMBL; AJ243666; CAB65097.1; ALT_INIT; mRNA.
DR   EMBL; AF116721; AAF71141.1; ALT_INIT; mRNA.
DR   EMBL; CR457219; CAG33500.1; -; mRNA.
DR   IPI; IPI00333410; -.
DR   IPI; IPI00719397; -.
DR   RefSeq; NP_060052.3; -.
DR   UniGene; Hs.607928; -.
DR   PDB; 2QGX; X-ray; 2.56 A; A/B/C/D=247-414.
DR   PDBsum; 2QGX; -.
DR   IntAct; Q7Z7E8; 1.
DR   PhosphoSite; Q7Z7E8; -.
DR   PRIDE; Q7Z7E8; -.
DR   Ensembl; ENSG00000160714; Homo sapiens.
DR   GeneID; 55585; -.
DR   KEGG; hsa:55585; -.
DR   UCSC; uc001fff.1; human.
DR   GeneCards; GC01M152787; -.
DR   H-InvDB; HIX0087635; -.
DR   HGNC; HGNC:15698; UBE2Q1.
DR   PharmGKB; PA38029; -.
DR   HOVERGEN; Q7Z7E8; -.
DR   OMA; Q7Z7E8; IAPPARD.
DR   BRENDA; 6.3.2.19; 247.
DR   NextBio; 60100; -.
DR   ArrayExpress; Q7Z7E8; -.
DR   Bgee; Q7Z7E8; -.
DR   CleanEx; HS_UBE2Q1; -.
DR   GermOnline; ENSG00000160714; Homo sapiens.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC.
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; FALSE_NEG.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Complete proteome;
KW   Ligase; Nucleotide-binding; Ubl conjugation pathway.
FT   CHAIN         1    422       Ubiquitin-conjugating enzyme E2 Q1.
FT                                /FTId=PRO_0000223876.
FT   COMPBIAS      8     38       Gly-rich.
FT   ACT_SITE    351    351       Glycyl thioester intermediate (By
FT                                similarity).
FT   VAR_SEQ       1    169       Missing (in isoform 2).
FT                                /FTId=VSP_017296.
FT   CONFLICT    287    287       N -> Y (in Ref. 5).
FT   HELIX       250    264
FT   HELIX       267    270
FT   STRAND      273    278
FT   HELIX       279    281
FT   STRAND      285    291
FT   HELIX       298    309
FT   STRAND      315    320
FT   TURN        325    327
FT   STRAND      331    337
FT   STRAND      339    341
FT   STRAND      348    350
FT   TURN        357    359
FT   HELIX       366    379
FT   STRAND      386    388
FT   HELIX       390    392
FT   HELIX       395    405
SQ   SEQUENCE   422 AA;  46127 MW;  106FF7E59DF65555 CRC64;
     MQQPQPQGQQ QPGPGQQLGG QGAAPGAGGG PGGGPGPGPC LRRELKLLES IFHRGHERFR
     IASACLDELS CEFLLAGAGG AGAGAAPGPH LPPRGSVPGD PVRIHCNITE SYPAVPPIWS
     VESDDPNLAA VLERLVDIKK GNTLLLQHLK RIISDLCKLY NLPQHPDVEM LDQPLPAEQC
     TQEDVSSEDE DEEMPEDTED LDHYEMKEEE PAEGKKSEDD GIGKENLAIL EKIKKNQRQD
     YLNGAVSGSV QATDRLMKEL RDIYRSQSFK GGNYAVELVN DSLYDWNVKL LKVDQDSALH
     NDLQILKEKE GADFILLNFS FKDNFPFDPP FVRVVSPVLS GGYVLGGGAI CMELLTKQGW
     SSAYSIESVI MQISATLVKG KARVQFGANK SQYSLTRAQQ SYKSLVQIHE KNGWYTPPKE
     DG
//