ID UB2Q1_HUMAN Reviewed; 422 AA. AC Q7Z7E8; B4DF92; Q29SN7; Q3B841; Q5I0X2; Q6IS04; Q6P7P2; Q96MV4; AC Q9BVX5; Q9UGL6; DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 09-DEC-2015, entry version 119. DE RecName: Full=Ubiquitin-conjugating enzyme E2 Q1; DE EC=2.3.2.23; DE AltName: Full=E2 ubiquitin-conjugating enzyme Q1; DE AltName: Full=Protein NICE-5; DE AltName: Full=Ubiquitin carrier protein Q1; DE AltName: Full=Ubiquitin-protein ligase Q1; 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 [MRNA]. RA Wassler M., Sagar B., Geng Y.-J.; RT "Cloning and characterization of galactosyl transferase-associated RT protein (GTAP), a human ubiquitin-conjugating enzyme that regulate RT stem cell adhesion, growth and differentiation."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 204-422. RC TISSUE=Cerebellum; 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 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 [5] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 282-422, AND TISSUE SPECIFICITY. RC TISSUE=Keratinocyte; RX 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 [8] 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 [9] 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 [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other CC proteins (Potential). May be involved in hormonal homeostasis in CC females. Involved in regulation of B4GALT1 cell surface CC expression, B4GALT1-mediated cell adhesion to laminin and embryoid CC body formation. {ECO:0000250|UniProtKB:Q7TSS2, CC ECO:0000255|PROSITE-ProRule:PRU00388}. CC -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating CC enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine CC = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 CC ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE- CC ProRule:PRU00388}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. CC -!- SUBUNIT: Monomer and homodimer. Only the homodimer is linked to CC ubiquitin through thiolester activation. Interacts (via N- CC terminus) with B4GALT1 (via N-terminal cytoplasmic domain). The CC interaction is direct. {ECO:0000250|UniProtKB:Q7TSS2}. CC -!- INTERACTION: CC Q13643:FHL3; NbExp=3; IntAct=EBI-10258181, EBI-741101; CC Q9UNE7:STUB1; NbExp=3; IntAct=EBI-1783287, EBI-357085; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7TSS2}. Cell CC projection, filopodium {ECO:0000250|UniProtKB:Q7TSS2}. Cytoplasm, CC cytosol {ECO:0000250|UniProtKB:Q7TSS2}. 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 -!- TISSUE SPECIFICITY: Widely expressed. CC {ECO:0000269|PubMed:11230159}. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF71141.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAH61583.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAH87836.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAI07058.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB71173.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAB65097.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY112698; AAM60814.1; -; mRNA. DR EMBL; AY948200; AAY23342.1; -; mRNA. DR EMBL; AK056388; BAB71173.1; ALT_INIT; mRNA. DR EMBL; AK293986; BAG57353.1; -; mRNA. DR EMBL; AL592078; CAI16186.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53193.1; -; Genomic_DNA. DR EMBL; BC000848; AAH00848.1; -; mRNA. DR EMBL; BC015316; AAH15316.2; -; 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; AJ243666; CAB65097.1; ALT_INIT; mRNA. DR EMBL; AF116721; AAF71141.1; ALT_INIT; mRNA. DR EMBL; CR457219; CAG33500.1; -; mRNA. DR CCDS; CCDS1069.1; -. [Q7Z7E8-1] DR RefSeq; NP_060052.3; NM_017582.6. [Q7Z7E8-1] DR UniGene; Hs.607928; -. DR PDB; 2QGX; X-ray; 2.56 A; A/B/C/D=247-414. DR PDBsum; 2QGX; -. DR ProteinModelPortal; Q7Z7E8; -. DR SMR; Q7Z7E8; 249-409. DR BioGrid; 120732; 15. DR IntAct; Q7Z7E8; 8. DR MINT; MINT-7944200; -. DR STRING; 9606.ENSP00000292211; -. DR PhosphoSite; Q7Z7E8; -. DR BioMuta; UBE2Q1; -. DR DMDM; 74750234; -. DR MaxQB; Q7Z7E8; -. DR PaxDb; Q7Z7E8; -. DR PRIDE; Q7Z7E8; -. DR DNASU; 55585; -. DR Ensembl; ENST00000292211; ENSP00000292211; ENSG00000160714. [Q7Z7E8-1] DR GeneID; 55585; -. DR KEGG; hsa:55585; -. DR UCSC; uc001fff.1; human. [Q7Z7E8-1] DR CTD; 55585; -. DR GeneCards; UBE2Q1; -. DR H-InvDB; HIX0001106; -. DR HGNC; HGNC:15698; UBE2Q1. DR neXtProt; NX_Q7Z7E8; -. DR PharmGKB; PA38029; -. DR eggNOG; KOG0897; Eukaryota. DR eggNOG; ENOG410XRET; LUCA. DR GeneTree; ENSGT00390000018573; -. DR HOVERGEN; HBG061368; -. DR InParanoid; Q7Z7E8; -. DR KO; K10582; -. DR OMA; SSAYTME; -. DR OrthoDB; EOG76DTSS; -. DR PhylomeDB; Q7Z7E8; -. DR TreeFam; TF313338; -. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q29SN7; -. DR SignaLink; Q7Z7E8; -. DR UniPathway; UPA00143; -. DR ChiTaRS; UBE2Q1; human. DR EvolutionaryTrace; Q7Z7E8; -. DR GenomeRNAi; 55585; -. DR NextBio; 60100; -. DR PRO; PR:Q7Z7E8; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; Q7Z7E8; -. DR CleanEx; HS_UBE2Q1; -. DR Genevisible; Q7Z7E8; HS. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:Ensembl. DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl. DR GO; GO:0009566; P:fertilization; IEA:Ensembl. DR GO; GO:0007617; P:mating behavior; IEA:Ensembl. DR GO; GO:0070459; P:prolactin secretion; IEA:Ensembl. DR GO; GO:0061458; P:reproductive system development; IEA:Ensembl. DR GO; GO:0001967; P:suckling behavior; IEA:Ensembl. DR Gene3D; 3.10.110.10; -; 1. DR InterPro; IPR000608; UBQ-conjugat_E2. DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD. DR Pfam; PF00179; UQ_con; 1. DR SUPFAM; SSF54495; SSF54495; 2. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Cell projection; Complete proteome; Cytoplasm; Nucleotide-binding; KW Nucleus; Reference proteome; Transferase; 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. FT {ECO:0000255|PROSITE-ProRule:PRU00388}. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:22223895}. FT VAR_SEQ 1 169 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_017296. FT CONFLICT 287 287 N -> Y (in Ref. 7; CAB65097). FT {ECO:0000305}. FT HELIX 250 264 {ECO:0000244|PDB:2QGX}. FT HELIX 267 270 {ECO:0000244|PDB:2QGX}. FT STRAND 273 278 {ECO:0000244|PDB:2QGX}. FT HELIX 279 281 {ECO:0000244|PDB:2QGX}. FT STRAND 285 291 {ECO:0000244|PDB:2QGX}. FT HELIX 298 309 {ECO:0000244|PDB:2QGX}. FT STRAND 315 320 {ECO:0000244|PDB:2QGX}. FT TURN 325 327 {ECO:0000244|PDB:2QGX}. FT STRAND 331 337 {ECO:0000244|PDB:2QGX}. FT STRAND 339 341 {ECO:0000244|PDB:2QGX}. FT STRAND 348 350 {ECO:0000244|PDB:2QGX}. FT TURN 357 359 {ECO:0000244|PDB:2QGX}. FT HELIX 366 379 {ECO:0000244|PDB:2QGX}. FT STRAND 386 388 {ECO:0000244|PDB:2QGX}. FT HELIX 390 392 {ECO:0000244|PDB:2QGX}. FT HELIX 395 405 {ECO:0000244|PDB:2QGX}. 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 //