UB2Q2_MOUSE
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 03-AUG-2022, entry version 155.
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; 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; Q8K2Z8; -.
DR PeptideAtlas; Q8K2Z8; -.
DR PRIDE; Q8K2Z8; -.
DR ProteomicsDB; 297775; -. [Q8K2Z8-1]
DR ProteomicsDB; 297776; -. [Q8K2Z8-2]
DR Antibodypedia; 27387; 204 antibodies from 28 providers.
DR DNASU; 109161; -.
DR Ensembl; ENSMUST00000059555; ENSMUSP00000059798; ENSMUSG00000032307. [Q8K2Z8-1]
DR Ensembl; ENSMUST00000122441; ENSMUSP00000112745; ENSMUSG00000032307. [Q8K2Z8-2]
DR GeneID; 109161; -.
DR KEGG; mmu:109161; -.
DR UCSC; uc009psb.2; mouse. [Q8K2Z8-1]
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; LHCNITX; -.
DR OrthoDB; 1214134at2759; -.
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 72 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 220 other tissues.
DR ExpressionAtlas; Q8K2Z8; baseline and differential.
DR Genevisible; Q8K2Z8; MM.
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 GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR Gene3D; 3.10.110.10; -; 2.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 2.
DR PROSITE; PS50127; UBC_2; 1.
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
