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   27-MAR-2024, entry version 156.
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 SQSTM1 and
CC       autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced
CC       conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1
CC       ubiquitination and degradation, MDM2-dependent degradation of p53/TP53
CC       and the activation of MAVS in the mitochondria by 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; 10090-ENSMUSP00000072387; -.
DR   PeptideAtlas; Q6ZWY6; -.
DR   ProteomicsDB; 298254; -.
DR   DNASU; 73318; -.
DR   Ensembl; ENSMUST00000072578.8; ENSMUSP00000072387.7; ENSMUSG00000063447.8.
DR   GeneID; 73318; -.
DR   KEGG; mmu:73318; -.
DR   UCSC; uc008yng.2; mouse.
DR   AGR; MGI:1920568; -.
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; PNIASMY; -.
DR   OrthoDB; 5478564at2759; -.
DR   PhylomeDB; Q6ZWY6; -.
DR   TreeFam; TF101108; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 73318; 1 hit in 71 CRISPR screens.
DR   PRO; PR:Q6ZWY6; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q6ZWY6; Protein.
DR   Bgee; ENSMUSG00000063447; Expressed in spermatid and 21 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
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:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; ISO:MGI.
DR   GO; GO:0044314; P:protein K27-linked ubiquitination; ISO:MGI.
DR   GO; GO:0035519; P:protein K29-linked ubiquitination; ISO:MGI.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:MGI.
DR   GO; GO:0085020; P:protein K6-linked ubiquitination; ISO:MGI.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; ISO:MGI.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24068:SF44; UBIQUITIN-CONJUGATING ENZYME E2 D2B; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
DR   Genevisible; Q6ZWY6; MM.
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
//