U2D2B_MOUSE
ID U2D2B_MOUSE Reviewed; 147 AA.
AC Q6ZWY6;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 D2B;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme D2B;
DE AltName: Full=Ubiquitin carrier protein D2B;
DE AltName: Full=Ubiquitin-protein ligase D2B;
GN Name=Ube2d2b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB24345.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAB24345.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16024774; DOI=10.1128/mcb.25.15.6346-6354.2005;
RA Bedard N., Hingamp P., Pang Z., Karaplis A., Morales C., Trasler J.,
RA Cyr D., Gagnon C., Wing S.S.;
RT "Mice lacking the UBC4-testis gene have a delay in postnatal testis
RT development but normal spermatogenesis and fertility.";
RL Mol. Cell. Biol. 25:6346-6354(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. Mediates the selective degradation of short-lived and
CC abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of
CC p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of
CC STUB1 and TRAF6. Involved in the signal-induced conjugation and
CC subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination
CC and degradation, MDM2-dependent degradation of p53/TP53 and the
CC activation of MAVS in the mitochondria by DDX58/RIG-I in response to
CC viral infection (By similarity). Plays a role in early maturation of
CC the testis. {ECO:0000250|UniProtKB:P62837, ECO:0000255|PROSITE-
CC ProRule:PRU00388, ECO:0000269|PubMed:16024774}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000250|UniProtKB:P62837, ECO:0000255|PROSITE-
CC ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Interacts with CNOT4 (via RING domain).
CC {ECO:0000250|UniProtKB:P62837}.
CC -!- TISSUE SPECIFICITY: Testis-specific.
CC -!- DISRUPTION PHENOTYPE: Mice show a delay in postnatal testis development
CC but normal spermatogenesis and fertility.
CC {ECO:0000269|PubMed:16024774}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AK005969; BAB24345.1; -; mRNA.
DR EMBL; AK133385; BAE21627.1; -; mRNA.
DR EMBL; BC050749; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS71632.1; -.
DR RefSeq; NP_001263326.1; NM_001276397.1.
DR AlphaFoldDB; Q6ZWY6; -.
DR SMR; Q6ZWY6; -.
DR STRING; 10090.ENSMUSP00000072387; -.
DR iPTMnet; Q6ZWY6; -.
DR PhosphoSitePlus; Q6ZWY6; -.
DR jPOST; Q6ZWY6; -.
DR MaxQB; Q6ZWY6; -.
DR PaxDb; Q6ZWY6; -.
DR PeptideAtlas; Q6ZWY6; -.
DR PRIDE; Q6ZWY6; -.
DR ProteomicsDB; 298254; -.
DR DNASU; 73318; -.
DR Ensembl; ENSMUST00000072578; ENSMUSP00000072387; ENSMUSG00000063447.
DR GeneID; 73318; -.
DR KEGG; mmu:73318; -.
DR UCSC; uc008yng.2; mouse.
DR CTD; 73318; -.
DR MGI; MGI:1920568; Ube2d2b.
DR VEuPathDB; HostDB:ENSMUSG00000063447; -.
DR eggNOG; KOG0417; Eukaryota.
DR GeneTree; ENSGT00940000164947; -.
DR HOGENOM; CLU_030988_13_3_1; -.
DR InParanoid; Q6ZWY6; -.
DR OMA; ISEANMY; -.
DR OrthoDB; 1337945at2759; -.
DR PhylomeDB; Q6ZWY6; -.
DR TreeFam; TF101108; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 73318; 1 hit in 66 CRISPR screens.
DR PRO; PR:Q6ZWY6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6ZWY6; protein.
DR Bgee; ENSMUSG00000063447; Expressed in spermatid and 19 other tissues.
DR Genevisible; Q6ZWY6; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IBA:GO_Central.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR CDD; cd00195; UBCc; 1.
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; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..147
FT /note="Ubiquitin-conjugating enzyme E2 D2B"
FT /id="PRO_0000283816"
FT DOMAIN 1..147
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 85
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q969T4,
FT ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
FT ProRule:PRU10133"
SQ SEQUENCE 147 AA; 16659 MW; E950720AEC2AB2B2 CRC64;
MALKRIHKEL NDLAQDPPAQ CSAGPVGEDM FHWQATIMGP NDSPYQGGAF FLTIDFPTEY
PFKPPKVEFT TRIYHPNVNS NGSICLDILR SQWSPALTIS KVLLSISSLL CDPNPDDPLV
PEIAQIYKTD RDKYNRTARE WTQKYAM
