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   24-JAN-2024, entry version 141.
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; 2.
DR   STRING; 10090.ENSMUSP00000037939; -.
DR   iPTMnet; Q7TSS2; -.
DR   PhosphoSitePlus; Q7TSS2; -.
DR   EPD; Q7TSS2; -.
DR   MaxQB; Q7TSS2; -.
DR   PaxDb; 10090-ENSMUSP00000037939; -.
DR   PeptideAtlas; Q7TSS2; -.
DR   ProteomicsDB; 298174; -. [Q7TSS2-1]
DR   ProteomicsDB; 298175; -. [Q7TSS2-2]
DR   Pumba; Q7TSS2; -.
DR   Antibodypedia; 34155; 181 antibodies from 23 providers.
DR   DNASU; 70093; -.
DR   Ensembl; ENSMUST00000038356.13; ENSMUSP00000037939.9; ENSMUSG00000042572.13. [Q7TSS2-1]
DR   Ensembl; ENSMUST00000196726.2; ENSMUSP00000143422.2; ENSMUSG00000042572.13. [Q7TSS2-2]
DR   GeneID; 70093; -.
DR   KEGG; mmu:70093; -.
DR   UCSC; uc008qad.2; mouse. [Q7TSS2-1]
DR   AGR; MGI:1917343; -.
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; 37924at2759; -.
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 78 CRISPR screens.
DR   PRO; PR:Q7TSS2; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q7TSS2; Protein.
DR   Bgee; ENSMUSG00000042572; Expressed in dorsal pancreas and 229 other cell types or tissues.
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; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
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; Q7TSS2; MM.
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
//