ID   UB2Q2_MOUSE             Reviewed;         378 AA.
AC   Q8K2Z8; Q3UBX3; Q3V3A5; Q8BUN2; Q8BVX5;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 2.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 Q2;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme Q2;
DE   AltName: Full=Ubiquitin carrier protein Q2;
DE   AltName: Full=Ubiquitin-protein ligase Q2;
GN   Name=Ube2q2;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Fetal head, Hippocampus, and Thymus;
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] (ISOFORM 1), AND VARIANT THR-235.
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
CC   -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC       covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-
CC       linked polyubiquitination. {ECO:0000250|UniProtKB:Q8WVN8}.
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:0000255|PROSITE-ProRule:PRU00388};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WVN8}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K2Z8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K2Z8-2; Sequence=VSP_017300;
CC   -!- PTM: Auto-ubiquitinated in vitro. {ECO:0000250|UniProtKB:Q8WVN8}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; AK083216; BAC38813.1; -; mRNA.
DR   EMBL; AK076148; BAC36218.1; -; mRNA.
DR   EMBL; AK042515; BAE20633.1; -; mRNA.
DR   EMBL; AK150776; BAE29841.1; -; mRNA.
DR   EMBL; BC029111; AAH29111.1; -; mRNA.
DR   CCDS; CCDS23201.1; -. [Q8K2Z8-1]
DR   CCDS; CCDS85678.1; -. [Q8K2Z8-2]
DR   RefSeq; NP_001333587.1; NM_001346658.1. [Q8K2Z8-2]
DR   RefSeq; NP_850931.2; NM_180600.3. [Q8K2Z8-1]
DR   AlphaFoldDB; Q8K2Z8; -.
DR   SMR; Q8K2Z8; -.
DR   BioGRID; 224579; 1.
DR   STRING; 10090.ENSMUSP00000059798; -.
DR   iPTMnet; Q8K2Z8; -.
DR   PhosphoSitePlus; Q8K2Z8; -.
DR   EPD; Q8K2Z8; -.
DR   MaxQB; Q8K2Z8; -.
DR   PaxDb; 10090-ENSMUSP00000059798; -.
DR   PeptideAtlas; Q8K2Z8; -.
DR   ProteomicsDB; 297775; -. [Q8K2Z8-1]
DR   ProteomicsDB; 297776; -. [Q8K2Z8-2]
DR   Antibodypedia; 27387; 228 antibodies from 28 providers.
DR   DNASU; 109161; -.
DR   Ensembl; ENSMUST00000059555.15; ENSMUSP00000059798.9; ENSMUSG00000032307.17. [Q8K2Z8-1]
DR   Ensembl; ENSMUST00000122441.2; ENSMUSP00000112745.2; ENSMUSG00000032307.17. [Q8K2Z8-2]
DR   GeneID; 109161; -.
DR   KEGG; mmu:109161; -.
DR   UCSC; uc009psb.2; mouse. [Q8K2Z8-1]
DR   AGR; MGI:2388672; -.
DR   CTD; 92912; -.
DR   MGI; MGI:2388672; Ube2q2.
DR   VEuPathDB; HostDB:ENSMUSG00000032307; -.
DR   eggNOG; KOG0897; Eukaryota.
DR   GeneTree; ENSGT00940000155357; -.
DR   HOGENOM; CLU_053863_0_0_1; -.
DR   InParanoid; Q8K2Z8; -.
DR   OMA; XDIEDLD; -.
DR   OrthoDB; 37924at2759; -.
DR   PhylomeDB; Q8K2Z8; -.
DR   TreeFam; TF313338; -.
DR   Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 109161; 0 hits in 77 CRISPR screens.
DR   ChiTaRS; Ube2q2; mouse.
DR   PRO; PR:Q8K2Z8; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q8K2Z8; Protein.
DR   Bgee; ENSMUSG00000032307; Expressed in superior cervical ganglion and 223 other cell types or tissues.
DR   ExpressionAtlas; Q8K2Z8; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 2.
DR   InterPro; IPR006575; RWD_dom.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF05773; RWD; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 2.
DR   PROSITE; PS50127; UBC_2; 1.
DR   Genevisible; Q8K2Z8; MM.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Nucleotide-binding;
KW   Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN           1..378
FT                   /note="Ubiquitin-conjugating enzyme E2 Q2"
FT                   /id="PRO_0000223880"
FT   DOMAIN          207..371
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          126..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        307
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   VAR_SEQ         1..123
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_017300"
FT   VARIANT         235
FT                   /note="I -> T (in strain: FVB/N)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT   CONFLICT        246
FT                   /note="L -> Q (in Ref. 1; BAC38813)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   378 AA;  42935 MW;  4A81D0AC4BD302E3 CRC64;
     MSVSGLKAEL KFLASIFDKN HERFRIVSWK LDELHCQFLV PPPPPPPGSS LSPPPPLTLH
     CNITESYPSS SPIWFVDSDD PNLTSVLERL EDTKNNSSLR QQLKWLICDL CRLYNLPKHL
     DVEMLDQPLP TGQNGTTEEV TSEEEEEEEM AEDIEDLDHY EMKEEEPING KKSEDEGIEK
     ENLAILEKIR KTQRQDHLNG AVSGSVQASD RLMKELRDVY RSQSYKAGIY SVELINDSLY
     DWHVKLHKVD SDSPLHSDLQ ILKEKEGIEY ILLNFSFKDN FPFDPPFVRV VLPVLSGGYV
     LGGGALCMEL LTKQGWSSAY SIESVIMQIN ATLVKGKARV QFGANKNQYN LARAQQSYNS
     IVQIHEKNGW YTPPKEDG
//