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Ubiquitin-conjugating enzyme E2 R1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme R1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme R1) (Ubiquitin-conjugating enzyme E2-32 kDa complementing) (Ubiquitin-conjugating enzyme E2-CDC34) (Ubiquitin-protein ligase R1)

 UB2R1_HUMAN             Reviewed;         236 AA.
P49427; A8K689;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
25-OCT-2017, entry version 170.
RecName: Full=Ubiquitin-conjugating enzyme E2 R1;
EC=2.3.2.23 {ECO:0000269|PubMed:12037680, ECO:0000269|PubMed:17698585, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:20347421};
AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme R1;
EC=2.3.2.24 {ECO:0000269|PubMed:17588522};
AltName: Full=E2 ubiquitin-conjugating enzyme R1;
AltName: Full=Ubiquitin-conjugating enzyme E2-32 kDa complementing;
AltName: Full=Ubiquitin-conjugating enzyme E2-CDC34;
AltName: Full=Ubiquitin-protein ligase R1;
Name=CDC34; Synonyms=UBCH3, UBE2R1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8248134; DOI=10.1073/pnas.90.22.10484;
Plon S.E., Leppig K.A., Do H.N., Groudine M.;
"Cloning of the human homolog of the CDC34 cell cycle gene by
complementation in yeast.";
Proc. Natl. Acad. Sci. U.S.A. 90:10484-10488(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-227.
NIEHS SNPs program;
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, AND MUTAGENESIS OF CYS-93.
PubMed=10329681; DOI=10.1074/jbc.274.21.14823;
Gonen H., Bercovich B., Orian A., Carrano A., Takizawa C.,
Yamanaka K., Pagano M., Iwai K., Ciechanover A.;
"Identification of the ubiquitin carrier proteins, E2s, involved in
signal-induced conjugation and subsequent degradation of
IkappaBalpha.";
J. Biol. Chem. 274:14823-14830(1999).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10373550; DOI=10.1128/MCB.19.7.5001;
Pati D., Meistrich M.L., Plon S.E.;
"Human Cdc34 and Rad6B ubiquitin-conjugating enzymes target repressors
of cyclic AMP-induced transcription for proteolysis.";
Mol. Cell. Biol. 19:5001-5013(1999).
[9]
SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=10769200;
Reymond F., Wirbelauer C., Krek W.;
"Association of human ubiquitin-conjugating enzyme CDC34 with the
mitotic spindle in anaphase.";
J. Cell Sci. 113:1687-1694(2000).
[10]
FUNCTION.
PubMed=10871850; DOI=10.1038/sj.onc.1203618;
Charrasse S., Carena I., Brondani V., Klempnauer K.H., Ferrari S.;
"Degradation of B-Myb by ubiquitin-mediated proteolysis: involvement
of the Cdc34-SCF(p45Skp2) pathway.";
Oncogene 19:2986-2995(2000).
[11]
INTERACTION WITH SCF COMPLEX.
PubMed=10918611; DOI=10.1038/sj.onc.1203647;
Strack P., Caligiuri M., Pelletier M., Boisclair M., Theodoras A.,
Beer-Romero P., Glass S., Parsons T., Copeland R.A., Auger K.R.,
Benfield P., Brizuela L., Rolfe M.;
"SCF(beta-TRCP) and phosphorylation dependent ubiquitination of I
kappa B alpha catalyzed by Ubc3 and Ubc4.";
Oncogene 19:3529-3536(2000).
[12]
INTERACTION WITH CSNK2B, PHOSPHORYLATION AT SER-203; SER-222; SER-231;
THR-233 AND SER-236, MUTAGENESIS OF SER-203; SER-222; SER-231; THR-233
AND SER-236, AND SUBCELLULAR LOCATION.
PubMed=11546811; DOI=10.1074/jbc.M106453200;
Block K., Boyer T.G., Yew P.R.;
"Phosphorylation of the human ubiquitin-conjugating enzyme, CDC34, by
casein kinase 2.";
J. Biol. Chem. 276:41049-41058(2001).
[13]
INTERACTION WITH HUMAN HERPESVIRUS 1 PROTEIN ICP0, AND ASSOCIATION
WITH THE PROTEASOME.
PubMed=11447293; DOI=10.1073/pnas.161283098;
Van Sant C., Hagglund R., Lopez P., Roizman B.;
"The infected cell protein 0 of herpes simplex virus 1 dynamically
interacts with proteasomes, binds and activates the cdc34 E2
ubiquitin-conjugating enzyme, and possesses in vitro E3 ubiquitin
ligase activity.";
Proc. Natl. Acad. Sci. U.S.A. 98:8815-8820(2001).
[14]
INTERACTION WITH SCF COMPLEX, FUNCTION, AND ENZYME REGULATION.
PubMed=11675391; DOI=10.1074/jbc.M108008200;
Wu K., Chen A., Tan P., Pan Z.Q.;
"The Nedd8-conjugated ROC1-CUL1 core ubiquitin ligase utilizes Nedd8
charged surface residues for efficient polyubiquitin chain assembly
catalyzed by Cdc34.";
J. Biol. Chem. 277:516-527(2002).
[15]
CATALYTIC ACTIVITY, FUNCTION, INTERACTION WITH BTRC, PHOSPHORYLATION
AT SER-231, AND MUTAGENESIS OF CYS-93; LEU-97 AND SER-231.
PubMed=12037680; DOI=10.1038/sj.onc.1205574;
Semplici F., Meggio F., Pinna L.A., Oliviero S.;
"CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme
UBC3B induces its interaction with beta-TrCP and enhances beta-catenin
degradation.";
Oncogene 21:3978-3987(2002).
[16]
INTERACTION WITH HUMAN HERPES VIRUS 1 PROTEIN ICP0, AND
AUTOUBIQUITINATION.
PubMed=11805320; DOI=10.1073/pnas.022531599;
Hagglund R., Van Sant C., Lopez P., Roizman B.;
"Herpes simplex virus 1-infected cell protein 0 contains two E3
ubiquitin ligase sites specific for different E2 ubiquitin-conjugating
enzymes.";
Proc. Natl. Acad. Sci. U.S.A. 99:631-636(2002).
[17]
INTERACTION WITH HUMAN HERPES VIRUS 1 PROTEIN ICP0, AND
AUTOUBIQUITINATION.
PubMed=12060736; DOI=10.1073/pnas.122246999;
Hagglund R., Roizman B.;
"Characterization of the novel E3 ubiquitin ligase encoded in exon 3
of herpes simplex virus-1-infected cell protein 0.";
Proc. Natl. Acad. Sci. U.S.A. 99:7889-7894(2002).
[18]
FUNCTION.
PubMed=15652359; DOI=10.1016/j.yexcr.2004.10.008;
Butz N., Ruetz S., Natt F., Hall J., Weiler J., Mestan J., Ducarre M.,
Grossenbacher R., Hauser P., Kempf D., Hofmann F.;
"The human ubiquitin-conjugating enzyme Cdc34 controls cellular
proliferation through regulation of p27Kip1 protein levels.";
Exp. Cell Res. 303:482-493(2005).
[19]
PHOSPHORYLATION AT SER-203; SER-222 AND SER-231, AND FUNCTION.
PubMed=17461777; DOI=10.1042/BJ20061812;
Sadowski M., Mawson A., Baker R., Sarcevic B.;
"Cdc34 C-terminal tail phosphorylation regulates Skp1/cullin/F-box
(SCF)-mediated ubiquitination and cell cycle progression.";
Biochem. J. 405:569-581(2007).
[20]
CATALYTIC ACTIVITY AS E3-INDEPENDENT E2 UBIQUITIN-CONJUGATING ENZYME.
PubMed=17588522; DOI=10.1016/j.molcel.2007.05.014;
Hoeller D., Hecker C.M., Wagner S., Rogov V., Doetsch V., Dikic I.;
"E3-independent monoubiquitination of ubiquitin-binding proteins.";
Mol. Cell 26:891-898(2007).
[21]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASN-85; TYR-87;
SER-95; ASP-102; ASP-103; GLU-108; GLU-112; SER-138; ASP-143; MET-147;
ARG-149; LYS-150 AND GLU-153.
PubMed=17698585; DOI=10.1128/MCB.00812-07;
Gazdoiu S., Yamoah K., Wu K., Pan Z.Q.;
"Human Cdc34 employs distinct sites to coordinate attachment of
ubiquitin to a substrate and assembly of polyubiquitin chains.";
Mol. Cell. Biol. 27:7041-7052(2007).
[22]
INTERACTION WITH SCF COMPLEX.
PubMed=18851830; DOI=10.1016/j.molcel.2008.08.021;
Saha A., Deshaies R.J.;
"Multimodal activation of the ubiquitin ligase SCF by Nedd8
conjugation.";
Mol. Cell 32:21-31(2008).
[23]
FUNCTION, INTERACTION WITH SCF COMPLEX, DOMAIN, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=19945379; DOI=10.1016/j.cell.2009.10.030;
Kleiger G., Saha A., Lewis S., Kuhlman B., Deshaies R.J.;
"Rapid E2-E3 assembly and disassembly enable processive ubiquitylation
of cullin-RING ubiquitin ligase substrates.";
Cell 139:957-968(2009).
[24]
IDENTIFICATION IN A UBIQUITIN LIGASE COMPLEX WITH HINT1 AND RBX1, AND
FUNCTION.
PubMed=19112177; DOI=10.1074/jbc.M804531200;
Cen B., Li H., Weinstein I.B.;
"Histidine triad nucleotide-binding protein 1 up-regulates cellular
levels of p27KIP1 by targeting ScfSKP2 ubiquitin ligase and Src.";
J. Biol. Chem. 284:5265-5276(2009).
[25]
INDUCTION, AND FUNCTION.
PubMed=19126550; DOI=10.1074/jbc.C900002200;
Legesse-Miller A., Elemento O., Pfau S.J., Forman J.J., Tavazoie S.,
Coller H.A.;
"let-7 Overexpression leads to an increased fraction of cells in G2/M,
direct down-regulation of Cdc34, and stabilization of Wee1 kinase in
primary fibroblasts.";
J. Biol. Chem. 284:6605-6609(2009).
[26]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=20061386; DOI=10.1074/jbc.M109.089003;
David Y., Ziv T., Admon A., Navon A.;
"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
preferred lysines.";
J. Biol. Chem. 285:8595-8604(2010).
[27]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=20347421; DOI=10.1016/j.molcel.2010.02.025;
Wu K., Kovacev J., Pan Z.Q.;
"Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for
polyubiquitination on a SCF substrate.";
Mol. Cell 37:784-796(2010).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[29]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 7-184.
Structural genomics consortium (SGC);
"Human ubiquitin-conjugating enzyme cdc34.";
Submitted (FEB-2009) to the PDB data bank.
[30] {ECO:0000244|PDB:3RZ3}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 7-184 IN COMPLEX WITH
INHIBITOR 4,5-DIDEOXY-5-(3',5'-DICHLOROBIPHENYL-4-YL)-4-
[(METHOXYACETYL)AMINO]-L-ARABINONIC ACID.
PubMed=21683433; DOI=10.1016/j.cell.2011.05.039;
Ceccarelli D.F., Tang X., Pelletier B., Orlicky S., Xie W.,
Plantevin V., Neculai D., Chou Y.C., Ogunjimi A., Al-Hakim A.,
Varelas X., Koszela J., Wasney G.A., Vedadi M., Dhe-Paganon S.,
Cox S., Xu S., Lopez-Girona A., Mercurio F., Wrana J., Durocher D.,
Meloche S., Webb D.R., Tyers M., Sicheri F.;
"An allosteric inhibitor of the human Cdc34 ubiquitin-conjugating
enzyme.";
Cell 145:1075-1087(2011).
[31] {ECO:0000244|PDB:2OB4}
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 7-184, FUNCTION, AND
AUTOUBIQUITINATION.
PubMed=22496338; DOI=10.1074/mcp.O111.013706;
Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J.,
Avvakumov G.V., Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K.,
Arrowsmith C.H., Raught B., Dhe-Paganon S.;
"A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-
function screen.";
Mol. Cell. Proteomics 11:329-341(2012).
[32] {ECO:0000244|PDB:4MDK}
X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 7-184 IN COMPLEX WITH
INHIBITOR 4,5-DIDEOXY-5-(3',5'-DICHLOROBIPHENYL-4-YL)-4-
[(METHOXYACETYL)AMINO]-L-ARABINONIC ACID, INTERACTION WITH RBX1, AND
MUTAGENESIS OF TYR-70; THR-117; SER-129 AND GLU-133.
PubMed=24316736; DOI=10.1038/nchembio.1412;
Huang H., Ceccarelli D.F., Orlicky S., St-Cyr D.J., Ziemba A.,
Garg P., Plamondon S., Auer M., Sidhu S., Marinier A., Kleiger G.,
Tyers M., Sicheri F.;
"E2 enzyme inhibition by stabilization of a low-affinity interface
with ubiquitin.";
Nat. Chem. Biol. 10:156-163(2014).
-!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
covalent attachment to other proteins. In vitro catalyzes 'Lys-
48'-linked polyubiquitination (PubMed:22496338). Cooperates with
the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the
polyubiquitination of NFKBIA leading to its subsequent proteasomal
degradation. Performs ubiquitin chain elongation building
ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin.
UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA
target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin.
Cooperates with the SCF(SKP2) E3 ligase complex to regulate cell
proliferation through ubiquitination and degradation of MYBL2 and
KIP1. Involved in ubiquitin conjugation and degradation of CREM
isoform ICERIIgamma and ATF15 resulting in abrogation of
ICERIIgamma- and ATF5-mediated repression of cAMP-induced
transcription during both meiotic and mitotic cell cycles.
Involved in the regulation of the cell cycle G2/M phase through
its targeting of the WEE1 kinase for ubiquitination and
degradation. Also involved in the degradation of beta-catenin. Is
target of human herpes virus 1 protein ICP0, leading to ICP0-
dependent dynamic interaction with proteasomes (PubMed:10329681,
PubMed:10373550, PubMed:10871850, PubMed:11675391,
PubMed:12037680, PubMed:15652359, PubMed:17461777,
PubMed:17698585, PubMed:19112177, PubMed:19126550,
PubMed:19945379, PubMed:20061386, PubMed:20347421).
{ECO:0000269|PubMed:10329681, ECO:0000269|PubMed:10373550,
ECO:0000269|PubMed:10871850, ECO:0000269|PubMed:11675391,
ECO:0000269|PubMed:12037680, ECO:0000269|PubMed:15652359,
ECO:0000269|PubMed:17461777, ECO:0000269|PubMed:17698585,
ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:19126550,
ECO:0000269|PubMed:19945379, ECO:0000269|PubMed:20061386,
ECO:0000269|PubMed:20347421, ECO:0000269|PubMed:22496338}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
= [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2
ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE-
ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133,
ECO:0000269|PubMed:12037680, ECO:0000269|PubMed:17698585,
ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:20347421}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-
activating enzyme]-L-cysteine + N(6)-monoubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:17588522}.
-!- ENZYME REGULATION: CDC34-catalyzed polyubiquitin chain assembly
activity is stimulated by the conjugation of NEDD8 to the CUL1 SCF
E3 ligase complex subunit. {ECO:0000269|PubMed:11675391}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.11 uM for beta-catenin-monoubiquin
{ECO:0000269|PubMed:19945379};
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SUBUNIT: Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin
ligase complex. Identified in a SCF (SKP1-CUL1-F-box protein) E3
ubiquitin ligase complex together with HINT1 and RBX1. When cullin
is neddylated, the interaction between the E2 and the SCF complex
is strengthened (PubMed:10918611, PubMed:11675391,
PubMed:18851830, PubMed:19945379, PubMed:19112177,
PubMed:24316736). When phosphorylated, interacts with beta-TrCP
(BTRC) (PubMed:12037680). Interacts with human herpes virus 1
protein ICP0 and associates with the proteasome for degradation
(PubMed:11447293, PubMed:11805320, PubMed:12060736). Interacts
with casein kinase subunit CSNK2B (PubMed:11546811).
{ECO:0000269|PubMed:10918611, ECO:0000269|PubMed:11447293,
ECO:0000269|PubMed:11546811, ECO:0000269|PubMed:11675391,
ECO:0000269|PubMed:11805320, ECO:0000269|PubMed:12037680,
ECO:0000269|PubMed:12060736, ECO:0000269|PubMed:18851830,
ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:19945379,
ECO:0000269|PubMed:24316736}.
-!- INTERACTION:
Q13616:CUL1; NbExp=3; IntAct=EBI-975634, EBI-359390;
O00560:SDCBP; NbExp=5; IntAct=EBI-975634, EBI-727004;
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-975634, EBI-747107;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=The phosphorylation
of the C-terminal tail plays an important role in mediating
nuclear localization. Colocalizes with beta-tubulin on mitotic
spindles in anaphase.
-!- TISSUE SPECIFICITY: Expressed in testes during spermatogenesis to
regulate repression of cAMP-induced transcription.
{ECO:0000269|PubMed:10373550}.
-!- INDUCTION: Negatively regulated by the let-7 microRNA.
{ECO:0000269|PubMed:19126550}.
-!- DOMAIN: The C-terminal acidic tail is required for nuclear
localization and is involved in the binding to SCF E3 ligase
complexes, and more specifically with the CUL1 subunit.
{ECO:0000269|PubMed:10769200, ECO:0000269|PubMed:19945379}.
-!- PTM: Autoubiquitinated (PubMed:22496338, PubMed:11805320,
PubMed:12060736). Autoubiquitination is promoted by the human
herpes virus 1 protein ICP0 and leads to degradation by the
Ubiquitin-proteasomal pathway (PubMed:11805320, PubMed:12060736).
{ECO:0000269|PubMed:11805320, ECO:0000269|PubMed:12060736,
ECO:0000269|PubMed:22496338}.
-!- PTM: Phosphorylated by CK2. Phosphorylation of the C-terminal tail
by CK2 controles the nuclear localization.
{ECO:0000269|PubMed:11546811, ECO:0000269|PubMed:12037680,
ECO:0000269|PubMed:17461777}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SEQUENCE CAUTION:
Sequence=AAC37534.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdc34/";
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EMBL; L22005; AAC37534.1; ALT_INIT; mRNA.
EMBL; BT006659; AAP35305.1; -; mRNA.
EMBL; AY650399; AAT46688.1; -; Genomic_DNA.
EMBL; AK291554; BAF84243.1; -; mRNA.
EMBL; CH471242; EAW61190.1; -; Genomic_DNA.
EMBL; BC009850; AAH09850.1; -; mRNA.
EMBL; BC018143; AAH18143.1; -; mRNA.
EMBL; BC023979; AAH23979.1; -; mRNA.
CCDS; CCDS12030.1; -.
PIR; A49630; A49630.
RefSeq; NP_004350.1; NM_004359.1.
UniGene; Hs.514997; -.
PDB; 2OB4; X-ray; 2.40 A; A=7-184.
PDB; 3RZ3; X-ray; 2.30 A; A/B/C/D=7-184.
PDB; 4MDK; X-ray; 2.61 A; A/B/C/D=7-184.
PDBsum; 2OB4; -.
PDBsum; 3RZ3; -.
PDBsum; 4MDK; -.
ProteinModelPortal; P49427; -.
SMR; P49427; -.
BioGrid; 107432; 62.
CORUM; P49427; -.
DIP; DIP-37783N; -.
IntAct; P49427; 19.
MINT; MINT-238910; -.
STRING; 9606.ENSP00000215574; -.
iPTMnet; P49427; -.
PhosphoSitePlus; P49427; -.
BioMuta; CDC34; -.
DMDM; 2507505; -.
EPD; P49427; -.
MaxQB; P49427; -.
PaxDb; P49427; -.
PeptideAtlas; P49427; -.
PRIDE; P49427; -.
DNASU; 997; -.
Ensembl; ENST00000215574; ENSP00000215574; ENSG00000099804.
GeneID; 997; -.
KEGG; hsa:997; -.
UCSC; uc002lov.4; human.
CTD; 997; -.
DisGeNET; 997; -.
EuPathDB; HostDB:ENSG00000099804.8; -.
GeneCards; CDC34; -.
HGNC; HGNC:1734; CDC34.
HPA; CAB005109; -.
HPA; CAB047311; -.
HPA; HPA002382; -.
MIM; 116948; gene.
neXtProt; NX_P49427; -.
OpenTargets; ENSG00000099804; -.
PharmGKB; PA26265; -.
eggNOG; KOG0425; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00730000110436; -.
HOGENOM; HOG000233454; -.
HOVERGEN; HBG063308; -.
InParanoid; P49427; -.
KO; K02207; -.
OMA; CVKTKTP; -.
OrthoDB; EOG091G0O9F; -.
PhylomeDB; P49427; -.
TreeFam; TF101107; -.
BRENDA; 2.3.2.B6; 2681.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; P49427; -.
SIGNOR; P49427; -.
UniPathway; UPA00143; -.
EvolutionaryTrace; P49427; -.
GeneWiki; CDC34; -.
GenomeRNAi; 997; -.
PRO; PR:P49427; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000099804; -.
CleanEx; HS_CDC34; -.
ExpressionAtlas; P49427; baseline and differential.
Genevisible; P49427; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; NAS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0006464; P:cellular protein modification process; NAS:UniProtKB.
GO; GO:0035458; P:cellular response to interferon-beta; IMP:UniProtKB.
GO; GO:0006270; P:DNA replication initiation; NAS:UniProtKB.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; NAS:UniProtKB.
GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IDA:UniProtKB.
GO; GO:0090261; P:positive regulation of inclusion body assembly; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0070848; P:response to growth factor; IEA:Ensembl.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR023313; UBQ-conjugating_AS.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF00179; UQ_con; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell cycle; Complete proteome; Cytoplasm;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transferase; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 236 Ubiquitin-conjugating enzyme E2 R1.
/FTId=PRO_0000082451.
REGION 190 236 SCF-binding.
COMPBIAS 200 236 Asp/Glu-rich (acidic).
ACT_SITE 93 93 Glycyl thioester intermediate.
MOD_RES 203 203 Phosphoserine; by CK2.
{ECO:0000269|PubMed:11546811,
ECO:0000269|PubMed:17461777}.
MOD_RES 222 222 Phosphoserine; by CK2.
{ECO:0000269|PubMed:11546811,
ECO:0000269|PubMed:17461777}.
MOD_RES 231 231 Phosphoserine; by CK2.
{ECO:0000269|PubMed:11546811,
ECO:0000269|PubMed:12037680,
ECO:0000269|PubMed:17461777}.
MOD_RES 233 233 Phosphothreonine; by CK2.
{ECO:0000269|PubMed:11546811}.
MOD_RES 236 236 Phosphoserine; by CK2.
{ECO:0000269|PubMed:11546811}.
VARIANT 227 227 D -> H (in dbSNP:rs16990650).
{ECO:0000269|Ref.3}.
/FTId=VAR_021277.
MUTAGEN 70 70 Y->R: Loss of RBX1-binding.
{ECO:0000269|PubMed:24316736}.
MUTAGEN 85 85 N->Q: Inhibits both mono and
polyubiquitination of NFKBIA.
{ECO:0000269|PubMed:17698585}.
MUTAGEN 87 87 Y->A: Decreases polyubiquitination of
NFKBIA. {ECO:0000269|PubMed:17698585}.
MUTAGEN 93 93 C->S,A: Loss of function.
{ECO:0000269|PubMed:10329681,
ECO:0000269|PubMed:12037680}.
MUTAGEN 95 95 S->D: Inhibits both mono and
polyubiquitination of NFKBIA.
{ECO:0000269|PubMed:17698585}.
MUTAGEN 97 97 L->S: Loss of function.
{ECO:0000269|PubMed:12037680}.
MUTAGEN 102 102 D->A: Inhibits polyubiquitination of
NFKBIA; when associated with A-103.
{ECO:0000269|PubMed:17698585}.
MUTAGEN 103 103 D->A: Inhibits polyubiquitination of
NFKBIA; when associated with A-102.
{ECO:0000269|PubMed:17698585}.
MUTAGEN 108 108 E->A: Inhibits both mono and
polyubiquitination of NFKBIA; when
associated with A-112.
{ECO:0000269|PubMed:17698585}.
MUTAGEN 112 112 E->A: Inhibits both mono
andpolyubiquitination of NFKBIA; when
associated with A-108.
{ECO:0000269|PubMed:17698585}.
MUTAGEN 117 117 T->E: Loss of RBX1-binding.
{ECO:0000269|PubMed:24316736}.
MUTAGEN 129 129 S->L: No effect on activity, when assayed
in a Sic1-SCF-cdc4 ubiquitination assay.
{ECO:0000269|PubMed:24316736}.
MUTAGEN 129 129 S->R: Complete loss of activity, when
assayed in a Sic1-SCF-cdc4 ubiquitination
assay. {ECO:0000269|PubMed:24316736}.
MUTAGEN 133 133 E->R: No effect on activity, when assayed
in a Sic1-SCF-cdc4 ubiquitination assay.
{ECO:0000269|PubMed:24316736}.
MUTAGEN 138 138 S->A: Decreases monoubiquitination of
NFKBIA and inhibits polyubiquitination of
NFKBIA. {ECO:0000269|PubMed:17698585}.
MUTAGEN 143 143 D->A: Inhibits polyubiquitination of
NFKBIA; when associated with A-147; A-
149; A-150 and A-153.
{ECO:0000269|PubMed:17698585}.
MUTAGEN 147 147 M->A: Inhibits polyubiquitination of
NFKBIA; when associated with A-143; A-
149; A-150 and A-153.
{ECO:0000269|PubMed:17698585}.
MUTAGEN 149 149 R->A: Inhibits polyubiquitination of
NFKBIA; when associated with A-147; A-
147; A-150 and A-153.
{ECO:0000269|PubMed:17698585}.
MUTAGEN 150 150 K->A: Inhibits polyubiquitination of
NFKBIA; when associated with A-143; A-
147; A-149 and A-153.
{ECO:0000269|PubMed:17698585}.
MUTAGEN 153 153 E->A: Inhibits polyubiquitination of
NFKBIA; when associated with A-143; A-
147; A-149 and A-150.
{ECO:0000269|PubMed:17698585}.
MUTAGEN 203 203 S->A: Abolishes phosphorylation by CK2.
Impairs nuclear localization; when
associated with A-222; A-231; A-233 and
A-236. {ECO:0000269|PubMed:11546811}.
MUTAGEN 222 222 S->A: Abolishes phosphorylation by CK2.
Impairs nuclear localization; when
associated with A-203; A-231; A-233 and
A-236. {ECO:0000269|PubMed:11546811}.
MUTAGEN 231 231 S->A: Abolishes phosphorylation by CK2.
Impairs nuclear localization; when
associated with A-203; A-222; A-233 and
A-236. {ECO:0000269|PubMed:11546811,
ECO:0000269|PubMed:12037680}.
MUTAGEN 233 233 T->A: Abolishes phosphorylation by CK2.
Impairs nuclear localization; when
associated with A-203; A-222; A-231 and
A-236. {ECO:0000269|PubMed:11546811}.
MUTAGEN 236 236 S->A: Abolishes phosphorylation by CK2.
Impairs nuclear localization; when
associated with A-203; A-222; A-231 and
A-233. {ECO:0000269|PubMed:11546811}.
HELIX 8 22 {ECO:0000244|PDB:3RZ3}.
STRAND 28 32 {ECO:0000244|PDB:3RZ3}.
STRAND 40 46 {ECO:0000244|PDB:3RZ3}.
TURN 52 55 {ECO:0000244|PDB:3RZ3}.
STRAND 57 63 {ECO:0000244|PDB:3RZ3}.
TURN 66 69 {ECO:0000244|PDB:3RZ3}.
STRAND 74 79 {ECO:0000244|PDB:3RZ3}.
STRAND 90 92 {ECO:0000244|PDB:3RZ3}.
HELIX 94 97 {ECO:0000244|PDB:2OB4}.
HELIX 120 132 {ECO:0000244|PDB:3RZ3}.
HELIX 142 153 {ECO:0000244|PDB:3RZ3}.
TURN 154 156 {ECO:0000244|PDB:3RZ3}.
HELIX 160 178 {ECO:0000244|PDB:3RZ3}.
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


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