ID UB2R1_HUMAN Reviewed; 236 AA. AC P49427; A8K689; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 153. DE RecName: Full=Ubiquitin-conjugating enzyme E2 R1; DE EC=2.3.2.23 {ECO:0000269|PubMed:12037680, ECO:0000269|PubMed:17698585, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:20347421}; DE AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme R1; DE EC=2.3.2.24 {ECO:0000269|PubMed:17588522}; DE AltName: Full=E2 ubiquitin-conjugating enzyme R1; DE AltName: Full=Ubiquitin-conjugating enzyme E2-32 kDa complementing; DE AltName: Full=Ubiquitin-conjugating enzyme E2-CDC34; DE AltName: Full=Ubiquitin-protein ligase R1; GN Name=CDC34; Synonyms=UBCH3, UBE2R1; 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]. RX PubMed=8248134; DOI=10.1073/pnas.90.22.10484; RA Plon S.E., Leppig K.A., Do H.N., Groudine M.; RT "Cloning of the human homolog of the CDC34 cell cycle gene by RT complementation in yeast."; RL Proc. Natl. Acad. Sci. U.S.A. 90:10484-10488(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-227. RG NIEHS SNPs program; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 [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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Lung; 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 FUNCTION, AND MUTAGENESIS OF CYS-93. RX PubMed=10329681; DOI=10.1074/jbc.274.21.14823; RA Gonen H., Bercovich B., Orian A., Carrano A., Takizawa C., RA Yamanaka K., Pagano M., Iwai K., Ciechanover A.; RT "Identification of the ubiquitin carrier proteins, E2s, involved in RT signal-induced conjugation and subsequent degradation of RT IkappaBalpha."; RL J. Biol. Chem. 274:14823-14830(1999). RN [8] RP INTERACTION WITH ATF5 AND CREM, FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=10373550; RA Pati D., Meistrich M.L., Plon S.E.; RT "Human Cdc34 and Rad6B ubiquitin-conjugating enzymes target repressors RT of cyclic AMP-induced transcription for proteolysis."; RL Mol. Cell. Biol. 19:5001-5013(1999). RN [9] RP SUBCELLULAR LOCATION, AND DOMAIN. RX PubMed=10769200; RA Reymond F., Wirbelauer C., Krek W.; RT "Association of human ubiquitin-conjugating enzyme CDC34 with the RT mitotic spindle in anaphase."; RL J. Cell Sci. 113:1687-1694(2000). RN [10] RP FUNCTION. RX PubMed=10871850; DOI=10.1038/sj.onc.1203618; RA Charrasse S., Carena I., Brondani V., Klempnauer K.H., Ferrari S.; RT "Degradation of B-Myb by ubiquitin-mediated proteolysis: involvement RT of the Cdc34-SCF(p45Skp2) pathway."; RL Oncogene 19:2986-2995(2000). RN [11] RP INTERACTION WITH SCF COMPLEX. RX PubMed=10918611; DOI=10.1038/sj.onc.1203647; RA Strack P., Caligiuri M., Pelletier M., Boisclair M., Theodoras A., RA Beer-Romero P., Glass S., Parsons T., Copeland R.A., Auger K.R., RA Benfield P., Brizuela L., Rolfe M.; RT "SCF(beta-TRCP) and phosphorylation dependent ubiquitination of I RT kappa B alpha catalyzed by Ubc3 and Ubc4."; RL Oncogene 19:3529-3536(2000). RN [12] RP INTERACTION WITH CSNK2B, PHOSPHORYLATION AT SER-203; SER-222; SER-231; RP THR-233 AND SER-236, MUTAGENESIS OF SER-203; SER-222; SER-231; THR-233 RP AND SER-236, AND SUBCELLULAR LOCATION. RX PubMed=11546811; DOI=10.1074/jbc.M106453200; RA Block K., Boyer T.G., Yew P.R.; RT "Phosphorylation of the human ubiquitin-conjugating enzyme, CDC34, by RT casein kinase 2."; RL J. Biol. Chem. 276:41049-41058(2001). RN [13] RP INTERACTION WITH HUMAN HERPESVIRUS 1 PROTEIN ICP0, AND ASSOCIATION RP WITH THE PROTEASOME. RX PubMed=11447293; DOI=10.1073/pnas.161283098; RA Van Sant C., Hagglund R., Lopez P., Roizman B.; RT "The infected cell protein 0 of herpes simplex virus 1 dynamically RT interacts with proteasomes, binds and activates the cdc34 E2 RT ubiquitin-conjugating enzyme, and possesses in vitro E3 ubiquitin RT ligase activity."; RL Proc. Natl. Acad. Sci. U.S.A. 98:8815-8820(2001). RN [14] RP INTERACTION WITH SCF COMPLEX, FUNCTION, AND ENZYME REGULATION. RX PubMed=11675391; DOI=10.1074/jbc.M108008200; RA Wu K., Chen A., Tan P., Pan Z.Q.; RT "The Nedd8-conjugated ROC1-CUL1 core ubiquitin ligase utilizes Nedd8 RT charged surface residues for efficient polyubiquitin chain assembly RT catalyzed by Cdc34."; RL J. Biol. Chem. 277:516-527(2002). RN [15] RP CATALYTIC ACTIVITY, FUNCTION, INTERACTION WITH BTRC, PHOSPHORYLATION RP AT SER-231, AND MUTAGENESIS OF CYS-93; LEU-97 AND SER-231. RX PubMed=12037680; DOI=10.1038/sj.onc.1205574; RA Semplici F., Meggio F., Pinna L.A., Oliviero S.; RT "CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme RT UBC3B induces its interaction with beta-TrCP and enhances beta-catenin RT degradation."; RL Oncogene 21:3978-3987(2002). RN [16] RP INTERACTION WITH HUMAN HERPES VIRUS 1 PROTEIN ICP0, AND RP AUTOUBIQUITINATION. RX PubMed=11805320; DOI=10.1073/pnas.022531599; RA Hagglund R., Van Sant C., Lopez P., Roizman B.; RT "Herpes simplex virus 1-infected cell protein 0 contains two E3 RT ubiquitin ligase sites specific for different E2 ubiquitin-conjugating RT enzymes."; RL Proc. Natl. Acad. Sci. U.S.A. 99:631-636(2002). RN [17] RP INTERACTION WITH HUMAN HERPES VIRUS 1 PROTEIN ICP0, AND RP AUTOUBIQUITINATION. RX PubMed=12060736; DOI=10.1073/pnas.122246999; RA Hagglund R., Roizman B.; RT "Characterization of the novel E3 ubiquitin ligase encoded in exon 3 RT of herpes simplex virus-1-infected cell protein 0."; RL Proc. Natl. Acad. Sci. U.S.A. 99:7889-7894(2002). RN [18] RP FUNCTION. RX PubMed=15652359; DOI=10.1016/j.yexcr.2004.10.008; RA Butz N., Ruetz S., Natt F., Hall J., Weiler J., Mestan J., Ducarre M., RA Grossenbacher R., Hauser P., Kempf D., Hofmann F.; RT "The human ubiquitin-conjugating enzyme Cdc34 controls cellular RT proliferation through regulation of p27Kip1 protein levels."; RL Exp. Cell Res. 303:482-493(2005). RN [19] RP PHOSPHORYLATION AT SER-203; SER-222 AND SER-231, AND FUNCTION. RX PubMed=17461777; DOI=10.1042/BJ20061812; RA Sadowski M., Mawson A., Baker R., Sarcevic B.; RT "Cdc34 C-terminal tail phosphorylation regulates Skp1/cullin/F-box RT (SCF)-mediated ubiquitination and cell cycle progression."; RL Biochem. J. 405:569-581(2007). RN [20] RP CATALYTIC ACTIVITY AS E3-INDEPENDENT E2 UBIQUITIN-CONJUGATING ENZYME. RX PubMed=17588522; DOI=10.1016/j.molcel.2007.05.014; RA Hoeller D., Hecker C.M., Wagner S., Rogov V., Doetsch V., Dikic I.; RT "E3-independent monoubiquitination of ubiquitin-binding proteins."; RL Mol. Cell 26:891-898(2007). RN [21] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASN-85; TYR-87; RP SER-95; ASP-102; ASP-103; GLU-108; GLU-112; SER-138; ASP-143; MET-147; RP ARG-149; LYS-150 AND GLU-153. RX PubMed=17698585; DOI=10.1128/MCB.00812-07; RA Gazdoiu S., Yamoah K., Wu K., Pan Z.Q.; RT "Human Cdc34 employs distinct sites to coordinate attachment of RT ubiquitin to a substrate and assembly of polyubiquitin chains."; RL Mol. Cell. Biol. 27:7041-7052(2007). RN [22] RP INTERACTION WITH SCF COMPLEX. RX PubMed=18851830; DOI=10.1016/j.molcel.2008.08.021; RA Saha A., Deshaies R.J.; RT "Multimodal activation of the ubiquitin ligase SCF by Nedd8 RT conjugation."; RL Mol. Cell 32:21-31(2008). RN [23] RP FUNCTION, INTERACTION WITH SCF COMPLEX, DOMAIN, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=19945379; DOI=10.1016/j.cell.2009.10.030; RA Kleiger G., Saha A., Lewis S., Kuhlman B., Deshaies R.J.; RT "Rapid E2-E3 assembly and disassembly enable processive ubiquitylation RT of cullin-RING ubiquitin ligase substrates."; RL Cell 139:957-968(2009). RN [24] RP IDENTIFICATION IN A UBIQUITIN LIGASE COMPLEX WITH HINT1 AND RBX1, AND RP FUNCTION. RX PubMed=19112177; DOI=10.1074/jbc.M804531200; RA Cen B., Li H., Weinstein I.B.; RT "Histidine triad nucleotide-binding protein 1 up-regulates cellular RT levels of p27KIP1 by targeting ScfSKP2 ubiquitin ligase and Src."; RL J. Biol. Chem. 284:5265-5276(2009). RN [25] RP INDUCTION, AND FUNCTION. RX PubMed=19126550; DOI=10.1074/jbc.C900002200; RA Legesse-Miller A., Elemento O., Pfau S.J., Forman J.J., Tavazoie S., RA Coller H.A.; RT "let-7 Overexpression leads to an increased fraction of cells in G2/M, RT direct down-regulation of Cdc34, and stabilization of Wee1 kinase in RT primary fibroblasts."; RL J. Biol. Chem. 284:6605-6609(2009). RN [26] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=20061386; DOI=10.1074/jbc.M109.089003; RA David Y., Ziv T., Admon A., Navon A.; RT "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to RT preferred lysines."; RL J. Biol. Chem. 285:8595-8604(2010). RN [27] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=20347421; DOI=10.1016/j.molcel.2010.02.025; RA Wu K., Kovacev J., Pan Z.Q.; RT "Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for RT polyubiquitination on a SCF substrate."; RL Mol. Cell 37:784-796(2010). RN [28] 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 [29] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 7-184. RG Structural genomics consortium (SGC); RT "Human ubiquitin-conjugating enzyme cdc34."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its CC covalent attachment to other proteins. In vitro catalyzes 'Lys- CC 48'-linked polyubiquitination. Cooperates with the E2 UBCH5C and CC the SCF(FBXW11) E3 ligase complex for the polyubiquitination of CC NFKBIA leading to its subsequent proteasomal degradation. Performs CC ubiquitin chain elongation building ubiquitin chains from the CC UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator CC E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' CC and/or 'Lys-22' with a monoubiquitin. Cooperates with the CC SCF(SKP2) E3 ligase complex to regulate cell proliferation through CC ubiquitination and degradation of MYBL2 and KIP1. Involved in CC ubiquitin conjugation and degradation of CREM isoform ICERIIgamma CC and ATF15 resulting in abrogation of ICERIIgamma- and ATF5- CC mediated repression of cAMP-induced transcription during both CC meiotic and mitotic cell cycles. Involved in the regulation of the CC cell cycle G2/M phase through its targeting of the WEE1 kinase for CC ubiquitination and degradation. Also involved in the degradation CC of beta-catenin. Is target of human herpes virus 1 protein ICP0, CC leading to ICP0-dependent dynamic interaction with proteasomes. CC {ECO:0000269|PubMed:10329681, ECO:0000269|PubMed:10373550, CC ECO:0000269|PubMed:10871850, ECO:0000269|PubMed:11675391, CC ECO:0000269|PubMed:12037680, ECO:0000269|PubMed:15652359, CC ECO:0000269|PubMed:17461777, ECO:0000269|PubMed:17698585, CC ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:19126550, CC ECO:0000269|PubMed:19945379, ECO:0000269|PubMed:20061386, CC ECO:0000269|PubMed:20347421}. 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, ECO:0000255|PROSITE-ProRule:PRU10133, CC ECO:0000269|PubMed:12037680, ECO:0000269|PubMed:17698585, CC ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:20347421}. CC -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating CC enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin- CC activating enzyme]-L-cysteine + N(6)-monoubiquitinyl-[acceptor CC protein]-L-lysine. {ECO:0000269|PubMed:17588522}. CC -!- ENZYME REGULATION: CDC34-catalyzed polyubiquitin chain assembly CC activity is stimulated by the conjugation of NEDD8 to the CUL1 SCF CC E3 ligase complex subunit. {ECO:0000269|PubMed:11675391}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.11 uM for beta-catenin-monoubiquin CC {ECO:0000269|PubMed:19945379}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. CC -!- SUBUNIT: Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin CC ligase complex. Identified in a SCF (SKP1-CUL1-F-box protein) E3 CC ubiquitin ligase complex together with HINT1 and RBX1. When cullin CC is neddylated, the interaction between the E2 and the SCF complex CC is strengthened. When phosphorylated, interacts with beta-TrCP CC (BTRC). Interacts with human herpes virus 1 protein ICP0 and CC associates with the proteasome for degradation. Interacts with CC casein kinase subunit CSNK2B. {ECO:0000269|PubMed:10373550, CC ECO:0000269|PubMed:10918611, ECO:0000269|PubMed:11447293, CC ECO:0000269|PubMed:11546811, ECO:0000269|PubMed:11675391, CC ECO:0000269|PubMed:11805320, ECO:0000269|PubMed:12037680, CC ECO:0000269|PubMed:12060736, ECO:0000269|PubMed:18851830, CC ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:19945379}. CC -!- INTERACTION: CC Q13616:CUL1; NbExp=3; IntAct=EBI-975634, EBI-359390; CC O00560:SDCBP; NbExp=3; IntAct=EBI-975634, EBI-727004; CC Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-975634, EBI-747107; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=The phosphorylation CC of the C-terminal tail plays an important role in mediating CC nuclear localization. Colocalizes with beta-tubulin on mitotic CC spindles in anaphase. CC -!- TISSUE SPECIFICITY: Expressed in testes during spermatogenesis to CC regulate repression of cAMP-induced transcription. CC {ECO:0000269|PubMed:10373550}. CC -!- INDUCTION: Negatively regulated by the let-7 microRNA. CC {ECO:0000269|PubMed:19126550}. CC -!- DOMAIN: The C-terminal acidic tail is required for nuclear CC localization and is involved in the binding to SCF E3 ligase CC complexes, and more specifically with the CUL1 subunit. CC {ECO:0000269|PubMed:10769200, ECO:0000269|PubMed:19945379}. CC -!- PTM: Autoubiquitinated. Autoubiquitination is promoted by the CC human herpes virus 1 protein ICP0 and leads to degradation by the CC Ubiquitin-proteasomal pathway. {ECO:0000269|PubMed:11805320, CC ECO:0000269|PubMed:12060736}. CC -!- PTM: Phosphorylated by CK2. Phosphorylation of the C-terminal tail CC by CK2 controles the nuclear localization. CC {ECO:0000269|PubMed:11546811, ECO:0000269|PubMed:12037680, CC ECO:0000269|PubMed:17461777}. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC37534.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/cdc34/"; 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; L22005; AAC37534.1; ALT_INIT; mRNA. DR EMBL; BT006659; AAP35305.1; -; mRNA. DR EMBL; AY650399; AAT46688.1; -; Genomic_DNA. DR EMBL; AK291554; BAF84243.1; -; mRNA. DR EMBL; CH471242; EAW61190.1; -; Genomic_DNA. DR EMBL; BC009850; AAH09850.1; -; mRNA. DR EMBL; BC018143; AAH18143.1; -; mRNA. DR EMBL; BC023979; AAH23979.1; -; mRNA. DR CCDS; CCDS12030.1; -. DR PIR; A49630; A49630. DR RefSeq; NP_004350.1; NM_004359.1. DR UniGene; Hs.514997; -. DR PDB; 2OB4; X-ray; 2.40 A; A=7-184. DR PDB; 3RZ3; X-ray; 2.30 A; A/B/C/D=7-184. DR PDB; 4MDK; X-ray; 2.61 A; A/B/C/D=7-184. DR PDBsum; 2OB4; -. DR PDBsum; 3RZ3; -. DR PDBsum; 4MDK; -. DR ProteinModelPortal; P49427; -. DR SMR; P49427; 7-184. DR BioGrid; 107432; 56. DR DIP; DIP-37783N; -. DR IntAct; P49427; 15. DR MINT; MINT-238910; -. DR STRING; 9606.ENSP00000215574; -. DR PhosphoSite; P49427; -. DR BioMuta; CDC34; -. DR DMDM; 2507505; -. DR MaxQB; P49427; -. DR PaxDb; P49427; -. DR PeptideAtlas; P49427; -. DR PRIDE; P49427; -. DR DNASU; 997; -. DR Ensembl; ENST00000215574; ENSP00000215574; ENSG00000099804. DR GeneID; 997; -. DR KEGG; hsa:997; -. DR UCSC; uc002lov.3; human. DR CTD; 997; -. DR GeneCards; CDC34; -. DR HGNC; HGNC:1734; CDC34. DR HPA; CAB005109; -. DR HPA; CAB047311; -. DR HPA; HPA002382; -. DR MIM; 116948; gene. DR neXtProt; NX_P49427; -. DR PharmGKB; PA26265; -. DR eggNOG; KOG0425; Eukaryota. DR eggNOG; COG5078; LUCA. DR GeneTree; ENSGT00730000110436; -. DR HOGENOM; HOG000233454; -. DR HOVERGEN; HBG063308; -. DR InParanoid; P49427; -. DR KO; K02207; -. DR OMA; CFGEDED; -. DR OrthoDB; EOG7VB2HT; -. DR PhylomeDB; P49427; -. DR TreeFam; TF101107; -. DR BRENDA; 2.3.2.B6; 2681. DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation. DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; P49427; -. DR UniPathway; UPA00143; -. DR EvolutionaryTrace; P49427; -. DR GeneWiki; CDC34; -. DR GenomeRNAi; 997; -. DR NextBio; 4188; -. DR PRO; PR:P49427; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; P49427; -. DR CleanEx; HS_CDC34; -. DR ExpressionAtlas; P49427; baseline and differential. DR Genevisible; P49427; HS. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0006464; P:cellular protein modification process; NAS:UniProtKB. DR GO; GO:0035458; P:cellular response to interferon-beta; IMP:UniProtKB. DR GO; GO:0006270; P:DNA replication initiation; NAS:UniProtKB. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; NAS:UniProtKB. DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IDA:UniProtKB. DR GO; GO:0090261; P:positive regulation of inclusion body assembly; IEA:Ensembl. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB. DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR GO; GO:0070848; P:response to growth factor; IEA:Ensembl. DR Gene3D; 3.10.110.10; -; 1. DR InterPro; IPR000608; UBQ-conjugat_E2. DR InterPro; IPR023313; UBQ-conjugating_AS. DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD. DR Pfam; PF00179; UQ_con; 1. DR SUPFAM; SSF54495; SSF54495; 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; Cell cycle; Complete proteome; Cytoplasm; KW Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; KW Reference proteome; Transferase; Ubl conjugation; KW Ubl conjugation pathway. FT CHAIN 1 236 Ubiquitin-conjugating enzyme E2 R1. FT /FTId=PRO_0000082451. FT REGION 190 236 SCF-binding. FT COMPBIAS 200 236 Asp/Glu-rich (acidic). FT ACT_SITE 93 93 Glycyl thioester intermediate. FT MOD_RES 203 203 Phosphoserine; by CK2. FT {ECO:0000269|PubMed:11546811, FT ECO:0000269|PubMed:17461777}. FT MOD_RES 222 222 Phosphoserine; by CK2. FT {ECO:0000269|PubMed:11546811, FT ECO:0000269|PubMed:17461777}. FT MOD_RES 231 231 Phosphoserine; by CK2. FT {ECO:0000269|PubMed:11546811, FT ECO:0000269|PubMed:12037680, FT ECO:0000269|PubMed:17461777}. FT MOD_RES 233 233 Phosphothreonine; by CK2. FT {ECO:0000269|PubMed:11546811}. FT MOD_RES 236 236 Phosphoserine; by CK2. FT {ECO:0000269|PubMed:11546811}. FT VARIANT 227 227 D -> H (in dbSNP:rs16990650). FT {ECO:0000269|Ref.3}. FT /FTId=VAR_021277. FT MUTAGEN 85 85 N->Q: Inhibits both mono and FT polyubiquitination of NFKBIA. FT {ECO:0000269|PubMed:17698585}. FT MUTAGEN 87 87 Y->A: Decreases polyubiquitination of FT NFKBIA. {ECO:0000269|PubMed:17698585}. FT MUTAGEN 93 93 C->S,A: Loss of function. FT {ECO:0000269|PubMed:10329681, FT ECO:0000269|PubMed:12037680}. FT MUTAGEN 95 95 S->D: Inhibits both mono and FT polyubiquitination of NFKBIA. FT {ECO:0000269|PubMed:17698585}. FT MUTAGEN 97 97 L->S: Loss of function. FT {ECO:0000269|PubMed:12037680}. FT MUTAGEN 102 102 D->A: Inhibits polyubiquitination of FT NFKBIA; when associated with A-103. FT {ECO:0000269|PubMed:17698585}. FT MUTAGEN 103 103 D->A: Inhibits polyubiquitination of FT NFKBIA; when associated with A-102. FT {ECO:0000269|PubMed:17698585}. FT MUTAGEN 108 108 E->A: Inhibits both mono and FT polyubiquitination of NFKBIA; when FT associated with A-112. FT {ECO:0000269|PubMed:17698585}. FT MUTAGEN 112 112 E->A: Inhibits both mono FT andpolyubiquitination of NFKBIA; when FT associated with A-108. FT {ECO:0000269|PubMed:17698585}. FT MUTAGEN 138 138 S->A: Decreases monoubiquitination of FT NFKBIA and inhibits polyubiquitination of FT NFKBIA. {ECO:0000269|PubMed:17698585}. FT MUTAGEN 143 143 D->A: Inhibits polyubiquitination of FT NFKBIA; when associated with A-147; A- FT 149; A-150 and A-153. FT {ECO:0000269|PubMed:17698585}. FT MUTAGEN 147 147 M->A: Inhibits polyubiquitination of FT NFKBIA; when associated with A-143; A- FT 149; A-150 and A-153. FT {ECO:0000269|PubMed:17698585}. FT MUTAGEN 149 149 R->A: Inhibits polyubiquitination of FT NFKBIA; when associated with A-147; A- FT 147; A-150 and A-153. FT {ECO:0000269|PubMed:17698585}. FT MUTAGEN 150 150 K->A: Inhibits polyubiquitination of FT NFKBIA; when associated with A-143; A- FT 147; A-149 and A-153. FT {ECO:0000269|PubMed:17698585}. FT MUTAGEN 153 153 E->A: Inhibits polyubiquitination of FT NFKBIA; when associated with A-143; A- FT 147; A-149 and A-150. FT {ECO:0000269|PubMed:17698585}. FT MUTAGEN 203 203 S->A: Abolishes phosphorylation by CK2. FT Impairs nuclear localization; when FT associated with A-222; A-231; A-233 and FT A-236. {ECO:0000269|PubMed:11546811}. FT MUTAGEN 222 222 S->A: Abolishes phosphorylation by CK2. FT Impairs nuclear localization; when FT associated with A-203; A-231; A-233 and FT A-236. {ECO:0000269|PubMed:11546811}. FT MUTAGEN 231 231 S->A: Abolishes phosphorylation by CK2. FT Impairs nuclear localization; when FT associated with A-203; A-222; A-233 and FT A-236. {ECO:0000269|PubMed:11546811, FT ECO:0000269|PubMed:12037680}. FT MUTAGEN 233 233 T->A: Abolishes phosphorylation by CK2. FT Impairs nuclear localization; when FT associated with A-203; A-222; A-231 and FT A-236. {ECO:0000269|PubMed:11546811}. FT MUTAGEN 236 236 S->A: Abolishes phosphorylation by CK2. FT Impairs nuclear localization; when FT associated with A-203; A-222; A-231 and FT A-233. {ECO:0000269|PubMed:11546811}. FT HELIX 8 22 {ECO:0000244|PDB:3RZ3}. FT STRAND 28 32 {ECO:0000244|PDB:3RZ3}. FT STRAND 40 46 {ECO:0000244|PDB:3RZ3}. FT TURN 52 55 {ECO:0000244|PDB:3RZ3}. FT STRAND 57 63 {ECO:0000244|PDB:3RZ3}. FT TURN 66 69 {ECO:0000244|PDB:3RZ3}. FT STRAND 74 79 {ECO:0000244|PDB:3RZ3}. FT STRAND 90 92 {ECO:0000244|PDB:3RZ3}. FT HELIX 94 97 {ECO:0000244|PDB:2OB4}. FT HELIX 120 132 {ECO:0000244|PDB:3RZ3}. FT HELIX 142 153 {ECO:0000244|PDB:3RZ3}. FT TURN 154 156 {ECO:0000244|PDB:3RZ3}. FT HELIX 160 178 {ECO:0000244|PDB:3RZ3}. SQ SEQUENCE 236 AA; 26737 MW; 258960666B589DB3 CRC64; MARPLVPSSQ KALLLELKGL QEEPVEGFRV TLVDEGDLYN WEVAIFGPPN TYYEGGYFKA RLKFPIDYPY SPPAFRFLTK MWHPNIYETG DVCISILHPP VDDPQSGELP SERWNPTQNV RTILLSVISL LNEPNTFSPA NVDASVMYRK WKESKGKDRE YTDIIRKQVL GTKVDAERDG VKVPTTLAEY CVKTKAPAPD EGSDLFYDDY YEDGEVEEEA DSCFGDDEDD SGTEES //