UBA1Y_MOUSE
ID UBA1Y_MOUSE Reviewed; 1058 AA.
AC P31254; Q60639; Q8CDH7; Q9QYS4; Q9QZX2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 1 Y;
DE EC=6.2.1.45 {ECO:0000250|UniProtKB:P22314};
DE AltName: Full=Ubiquitin-activating enzyme E1;
DE AltName: Full=Ubiquitin-activating enzyme E1 Y;
GN Name=Uba1y; Synonyms=Sby, Ube1ay, Ube1y, Ube1y1;
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 [GENOMIC DNA / MRNA].
RC STRAIN=C3H/HeJ, and C57BL/6J;
RX PubMed=10656933; DOI=10.1007/s003350010031;
RA Levy N., Navarro A., Bishop C.E., Mitchell M.J.;
RT "The ubiquitin-activating enzyme E1 homologous genes on the mouse Y
RT Chromosome represent one functional gene and six partial pseudogenes.";
RL Mamm. Genome 11:164-168(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 617-1058.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=1684224; DOI=10.1038/354483a0;
RA Mitchell M.J., Woods D.R., Tucker P.K., Opp J.S., Bishop C.E.;
RT "Homology of a candidate spermatogenic gene from the mouse Y chromosome to
RT the ubiquitin-activating enzyme E1.";
RL Nature 354:483-487(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 654-762.
RC STRAIN=BALB/c AnCr; TISSUE=Liver;
RX PubMed=7714913; DOI=10.1007/bf00166597;
RA Chang B.H.-J., Li W.H.;
RT "Estimating the intensity of male-driven evolution in rodents by using X-
RT linked and Y-linked Ube 1 genes and pseudogenes.";
RL J. Mol. Evol. 40:70-77(1995).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8948595; DOI=10.1006/dbio.1996.0305;
RA Odorisio T., Mahadevaiah S.K., McCarrey J.R., Burgoyne P.S.;
RT "Transcriptional analysis of the candidate spermatogenesis gene Ube1y and
RT of the closely related Ube1x shows that they are coexpressed in
RT spermatogonia and spermatids but are repressed in pachytene
RT spermatocytes.";
RL Dev. Biol. 180:336-343(1996).
RN [6]
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: Activates ubiquitin by first adenylating its C-terminal
CC glycine residue with ATP, and thereafter linking this residue to the
CC side chain of a cysteine residue in E1, yielding a ubiquitin-E1
CC thioester and free AMP (By similarity). The Y chromosome form could be
CC involved in the survival and proliferation of differentiating
CC spermatogonia. {ECO:0000250|UniProtKB:P22314, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
CC = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-
CC L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000250|UniProtKB:P22314};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:P22314}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in testis in A spermatogonia and
CC spermatids but not (or at very low levels) in pachytene spermatocytes.
CC Also expressed in Y-bearing ovaries and at very low levels in adrenal
CC gland. {ECO:0000269|PubMed:8948595}.
CC -!- DEVELOPMENTAL STAGE: In testis, expression detected at 12.5 days post
CC coitum (dpc) and peaking at 14.5 dpc, with expression dropping to low
CC levels at the day of birth. After birth, levels increase 4-fold to a
CC peak at 10 days post partum (dpp) and fall again thereafter.
CC {ECO:0000269|PubMed:8948595}.
CC -!- MISCELLANEOUS: There are two active sites within the E1 molecule,
CC allowing it to accommodate two ubiquitin moieties at a time, with a new
CC ubiquitin forming an adenylate intermediate as the previous one is
CC transferred to the thiol site. {ECO:0000250|UniProtKB:P22314}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF127490; AAD56603.1; -; Genomic_DNA.
DR EMBL; AF127483; AAD56603.1; JOINED; Genomic_DNA.
DR EMBL; AF127484; AAD56603.1; JOINED; Genomic_DNA.
DR EMBL; AF127485; AAD56603.1; JOINED; Genomic_DNA.
DR EMBL; AF127486; AAD56603.1; JOINED; Genomic_DNA.
DR EMBL; AF127487; AAD56603.1; JOINED; Genomic_DNA.
DR EMBL; AF127488; AAD56603.1; JOINED; Genomic_DNA.
DR EMBL; AF127489; AAD56603.1; JOINED; Genomic_DNA.
DR EMBL; AF150963; AAF00149.1; -; mRNA.
DR EMBL; AK030031; BAC26749.1; -; mRNA.
DR EMBL; X62581; CAA44466.1; -; mRNA.
DR EMBL; U09052; AAC52170.1; -; Genomic_DNA.
DR CCDS; CCDS30540.1; -.
DR PIR; I49011; I49011.
DR PIR; S19712; S19712.
DR RefSeq; NP_035797.1; NM_011667.2.
DR RefSeq; XP_006531645.1; XM_006531582.2.
DR AlphaFoldDB; P31254; -.
DR SMR; P31254; -.
DR BioGRID; 204411; 5.
DR STRING; 10090.ENSMUSP00000111560; -.
DR iPTMnet; P31254; -.
DR PhosphoSitePlus; P31254; -.
DR SwissPalm; P31254; -.
DR jPOST; P31254; -.
DR MaxQB; P31254; -.
DR PaxDb; P31254; -.
DR PeptideAtlas; P31254; -.
DR PRIDE; P31254; -.
DR ProteomicsDB; 297779; -.
DR DNASU; 22202; -.
DR Ensembl; ENSMUST00000115894; ENSMUSP00000111560; ENSMUSG00000069053.
DR Ensembl; ENSMUST00000190013; ENSMUSP00000140543; ENSMUSG00000069053.
DR UCSC; uc009uyw.1; mouse.
DR MGI; MGI:98891; Uba1y.
DR VEuPathDB; HostDB:ENSMUSG00000069053; -.
DR eggNOG; KOG2012; Eukaryota.
DR GeneTree; ENSGT00940000158975; -.
DR HOGENOM; CLU_002556_0_0_1; -.
DR InParanoid; P31254; -.
DR OMA; ERMDRKM; -.
DR OrthoDB; 91748at2759; -.
DR PhylomeDB; P31254; -.
DR TreeFam; TF300586; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 22202; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Uba1y-ps1; mouse.
DR PRO; PR:P31254; -.
DR Proteomes; UP000000589; Chromosome Y.
DR RNAct; P31254; protein.
DR Bgee; ENSMUSG00000069053; Expressed in spermatid and 11 other tissues.
DR Genevisible; P31254; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IMP:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.10.2660; -; 1.
DR Gene3D; 2.40.30.180; -; 1.
DR Gene3D; 3.10.290.60; -; 1.
DR Gene3D; 3.50.50.80; -; 1.
DR InterPro; IPR032420; E1_4HB.
DR InterPro; IPR032418; E1_FCCH.
DR InterPro; IPR042302; E1_FCCH_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR018965; Ub-activating_enz_E1_C.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR038252; UBA_E1_C_sf.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR018075; UBQ-activ_enz_E1.
DR InterPro; IPR018074; UBQ-activ_enz_E1_CS.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF16190; E1_FCCH; 1.
DR Pfam; PF09358; E1_UFD; 1.
DR Pfam; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_e1_thiolCys; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; SSF69572; 2.
DR TIGRFAMs; TIGR01408; Ube1; 1.
DR PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..1058
FT /note="Ubiquitin-like modifier-activating enzyme 1 Y"
FT /id="PRO_0000194939"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 631
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT BINDING 477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 503
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 514
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 527
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 575..576
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT CONFLICT 93
FT /note="G -> C (in Ref. 1; AAF00149)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="E -> V (in Ref. 2; BAC26749)"
FT /evidence="ECO:0000305"
FT CONFLICT 635
FT /note="N -> Y (in Ref. 3; CAA44466)"
FT /evidence="ECO:0000305"
FT CONFLICT 713
FT /note="W -> R (in Ref. 4; AAC52170)"
FT /evidence="ECO:0000305"
FT CONFLICT 947
FT /note="Y -> F (in Ref. 3; CAA44466)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1058 AA; 118038 MW; B5C5AD66534B0350 CRC64;
MSSSVLSKKR KVSGPDSSLD SSWSPTYSVM FGVPPGPTNE MSKNKEMDID ESLYSRQLYV
LGHEAMKHLQ ASSVLISGLQ GLGVEIAKNI ILGGVKAVTL HDQGIAQWAD LSSQFCLREE
DIGKNRAEIS QPRLAELNSY VPVFAYTGPL IEEFLSGFQV VVLTNTPLEY QLQVGEFCHS
HGIKLVVADT RGLVGQLFCD FGEEMILTDS NGEQPLSAMV SMITKENPGI VTCLEDSRHG
FESGDFISFT EVQGMSELNG IGPIEIKVLG PYTFSICDTS SFSEYIRGGI VSQVKVPRKI
NFKPLLASLA EPEFVVTDFA KCCHPAQLHI GFQALHQFCT QHSRPPRPHN EEDAEELVTL
AQSVNAQALP AVQQDCLDID LIRKLAYVAA GDLAPMNAFF GGLAAQEVMK ACSGKFMPIR
QWLYFDALEC LPEHRVAFME DKCLPHQNRY DGQVAVFGSD LQEKLGKQKY FLVGAGAIGC
ELLKNFAMIG LGCGEDGEIT VTDMDTIEKS NLNRQFLFRP WDITKLKSET AAAAVRDINP
HIRIFSHQNR VGPETEHVYD DDFFQKLDGV ANALDNVDAR LYVDRRCVYY RKPLLESGTL
GTKGNVQVVV PFLTESYSSS QDPPEKSIPI CTLKNFPNAI EHTVQWARDE FEGLFKQSAE
NVNQYLTDPK FMERTLQLAG TQPLEVLEAI HCSLVLQRPQ TWADCVTWAY QHWHTQYSHN
IQQLLHNFPP AQLTSSGALF WSGPKRCPHP LTFDINNPLH LDYVMAAANL FAQTYGLGGS
QDCAVVAKLL QSLPVPKFAP KSGIRIHVSE QELQSTSATT IDDSHLEELK TALPTPDKLL
GFKMYPIDFE KDDDSNFHMD FIVAASNLRA ENYGISPADR HKSKLIAGKI IPAIATTTSA
IVGLVCLELY KVVQGHQQLE SYKNSFINLA LPLFSFSAPL APECHQYYDQ EWTLWDRFDV
QGLQPSGEEM TLKQFLDYFK TEHKLEVIML SQGVSMLYSV FMPASKLKER LDQPMTEIVS
CVSKQKLGHH VKSLVFELCC NSDSGDDIEV PYVRYIIR
