UB2Q1_MOUSE
ID UB2Q1_MOUSE Reviewed; 422 AA.
AC Q7TSS2; Q29ST1; Q3UIY3; Q6P913; Q80UT5; Q8K2T0; Q9D7E1;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 Q1;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme Q1;
DE AltName: Full=Galactosyl transferase-associated protein {ECO:0000303|PubMed:18511602};
DE Short=GTAP {ECO:0000303|PubMed:18511602};
DE AltName: Full=Ubiquitin carrier protein Q1;
DE AltName: Full=Ubiquitin-protein ligase Q1;
GN Name=Ube2q1; Synonyms=Ube2q;
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 [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INTERACTION WITH B4GALT1, AND MUTAGENESIS OF CYS-351.
RX PubMed=18511602; DOI=10.1634/stemcells.2007-1080;
RA Wassler M.J., Shur B.D., Zhou W., Geng Y.J.;
RT "Characterization of a novel ubiquitin-conjugating enzyme that regulates
RT beta1,4-galactosyltransferase-1 in embryonic stem cells.";
RL Stem Cells 26:2006-2018(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 169-422 (ISOFORM 1).
RC TISSUE=Brain, Mammary gland, and Thymus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-422 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Fetal heart, and Tongue;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, and 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).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23108111; DOI=10.1530/rep-12-0054;
RA Grzmil P., Altmann M.E., Adham I.M., Engel U., Jarry H., Schweyer S.,
RA Wolf S., Manz J., Engel W.;
RT "Embryo implantation failure and other reproductive defects in Ube2q1-
RT deficient female mice.";
RL Reproduction 145:45-56(2013).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins (By similarity). Involved in female fertility and embryo
CC implantation (PubMed:23108111). May be involved in hormonal homeostasis
CC in females (PubMed:23108111). Involved in regulation of B4GALT1 cell
CC surface expression, B4GALT1-mediated cell adhesion to laminin and
CC embryoid body formation (PubMed:18511602).
CC {ECO:0000250|UniProtKB:Q7Z7E8, ECO:0000269|PubMed:18511602,
CC ECO:0000269|PubMed:23108111, ECO:0000303|PubMed:23108111}.
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 -!- SUBUNIT: Monomer and homodimer. Only the homodimer is linked to
CC ubiquitin through thiolester activation. Interacts (via N-terminus)
CC with B4GALT1 (via N-terminal cytoplasmic domain); the interaction is
CC direct. {ECO:0000269|PubMed:18511602}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18511602}. Cell
CC projection, filopodium {ECO:0000269|PubMed:18511602}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:18511602}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TSS2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TSS2-2; Sequence=VSP_017297;
CC -!- TISSUE SPECIFICITY: Expressed in liver, brain, heart, spleen, lung,
CC kidney, muscle, ovary, epididymis, testis and placenta
CC (PubMed:23108111). Also expressed in thymus and ES cells
CC (PubMed:18511602). Only expressed in the uterus during pregnancy
CC (PubMed:23108111). Expressed in oocytes and during subsequent embryonic
CC development stages (4-cell stage, blastocyst, 8.5 dpc, 13.5 dpc, 16.5
CC dpc and 18.5 dpc) (PubMed:23108111). {ECO:0000269|PubMed:18511602,
CC ECO:0000269|PubMed:23108111}.
CC -!- PTM: Autoubiquitinated in vitro in the presence of NEDD4L.
CC {ECO:0000250|UniProtKB:Q7Z7E8}.
CC -!- DISRUPTION PHENOTYPE: No reproductive defects in males but females have
CC reduced litter size due to embryo implantation failure, normal
CC ovulation but a longer estrus cycle, reduced levels of serum prolactin
CC at the beginning of lactation, abnormal sexual behavior and show
CC reduced offspring care. {ECO:0000269|PubMed:23108111}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH51487.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB26217.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY945937; AAY23286.1; -; mRNA.
DR EMBL; AY112699; AAM60815.1; -; mRNA.
DR EMBL; AK009324; BAB26217.2; ALT_INIT; mRNA.
DR EMBL; AK146707; BAE27373.1; -; mRNA.
DR EMBL; BC030044; AAH30044.2; -; mRNA.
DR EMBL; BC051487; AAH51487.1; ALT_INIT; mRNA.
DR EMBL; BC060966; AAH60966.1; -; mRNA.
DR EMBL; BC082275; AAH82275.1; -; mRNA.
DR CCDS; CCDS17517.1; -. [Q7TSS2-1]
DR RefSeq; NP_081591.3; NM_027315.4. [Q7TSS2-1]
DR AlphaFoldDB; Q7TSS2; -.
DR SMR; Q7TSS2; -.
DR BioGRID; 213860; 1.
DR STRING; 10090.ENSMUSP00000037939; -.
DR iPTMnet; Q7TSS2; -.
DR PhosphoSitePlus; Q7TSS2; -.
DR EPD; Q7TSS2; -.
DR MaxQB; Q7TSS2; -.
DR PaxDb; Q7TSS2; -.
DR PeptideAtlas; Q7TSS2; -.
DR PRIDE; Q7TSS2; -.
DR ProteomicsDB; 298174; -. [Q7TSS2-1]
DR ProteomicsDB; 298175; -. [Q7TSS2-2]
DR Antibodypedia; 34155; 144 antibodies from 23 providers.
DR DNASU; 70093; -.
DR Ensembl; ENSMUST00000038356; ENSMUSP00000037939; ENSMUSG00000042572. [Q7TSS2-1]
DR Ensembl; ENSMUST00000196726; ENSMUSP00000143422; ENSMUSG00000042572. [Q7TSS2-2]
DR GeneID; 70093; -.
DR KEGG; mmu:70093; -.
DR UCSC; uc008qad.2; mouse. [Q7TSS2-1]
DR CTD; 55585; -.
DR MGI; MGI:1917343; Ube2q1.
DR VEuPathDB; HostDB:ENSMUSG00000042572; -.
DR eggNOG; KOG0897; Eukaryota.
DR GeneTree; ENSGT00940000160166; -.
DR InParanoid; Q7TSS2; -.
DR OMA; NIQENYP; -.
DR OrthoDB; 1214134at2759; -.
DR PhylomeDB; Q7TSS2; -.
DR TreeFam; TF313338; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 70093; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q7TSS2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q7TSS2; protein.
DR Bgee; ENSMUSG00000042572; Expressed in dorsal pancreas and 226 other tissues.
DR Genevisible; Q7TSS2; MM.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; 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:0007566; P:embryo implantation; IMP:MGI.
DR GO; GO:0009566; P:fertilization; IMP:MGI.
DR GO; GO:0007617; P:mating behavior; IMP:MGI.
DR GO; GO:0070459; P:prolactin secretion; IMP:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0061458; P:reproductive system development; IMP:MGI.
DR GO; GO:0001967; P:suckling behavior; IMP:MGI.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cell projection; Cytoplasm;
KW Nucleotide-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..422
FT /note="Ubiquitin-conjugating enzyme E2 Q1"
FT /id="PRO_0000223877"
FT DOMAIN 251..415
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..204
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 351
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z7E8"
FT VAR_SEQ 1..169
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017297"
FT MUTAGEN 351
FT /note="C->A: Loss of ubiquitin binding. Normal dimer
FT formation."
FT /evidence="ECO:0000269|PubMed:18511602"
FT CONFLICT 121
FT /note="V -> G (in Ref. 1; AAM60815)"
FT /evidence="ECO:0000305"
FT CONFLICT 125..126
FT /note="DP -> AL (in Ref. 1; AAM60815)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="K -> R (in Ref. 1; AAM60815)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 46173 MW; 845897861B36971F CRC64;
MQQPQPQGQQ QPGPGQQLGV QGAAPGAGGG PGGGPGPGPC LRRELKLLES IFHRGHERFR
IASACLDELS CEFLLAGAGG AGAGAAPGPH LPSRGSVPGD PVRIHCNITE SYPAVPPIWS
VESDDPNLAA VLERLVDIKK GNTLLLQHLK RIISDLCKLY NLPQHPDVEM LDQPLPAEQC
TQEEVSSEDE DEEMPEDTED LDHYEMKEEE PAEGKKSEDD GIGKENLAIL EKIKKNQRQD
YLNGAVSGSV QATDRLMKEL RDIYRSQSFK GGNYAVELVN DSLYDWNVKL LKVDQDSALH
NDLQILKEKE GADFILLNFS FKDNFPFDPP FVRVVSPVLS GGYVLGGGAI CMELLTKQGW
SSAYSIESVI MQISATLVKG KARVQFGANK SQYSLTRAQQ SYKSLVQIHE KNGWYTPPKE
DG
