ESS2_MOUSE
ID ESS2_MOUSE Reviewed; 479 AA.
AC O70279; Q91YX1;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Splicing factor ESS-2 homolog;
DE AltName: Full=ES2 protein;
DE AltName: Full=Expressed sequence 2 embryonic lethal;
GN Name=Ess2; Synonyms=Dgcr14, Dgsi, Es2, Es2el;
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].
RC TISSUE=Embryo;
RX PubMed=9037598; DOI=10.1101/gr.7.1.17;
RA Galili N., Baldwin H.S., Lund J., Reeves R., Gong W., Wang Z., Roe B.A.,
RA Emanuel B.S., Nayak S., Mickanin C., Budarf M.L., Buck C.A.;
RT "A region of mouse chromosome 16 is syntenic to the DiGeorge,
RT velocardiofacial syndrome minimal critical region.";
RL Genome Res. 7:17-26(1997).
RN [2]
RP ERRATUM OF PUBMED:9037598.
RX PubMed=9110179;
RA Galili N., Baldwin H.S., Lund J., Reeves R., Gong W., Wang Z., Roe B.A.,
RA Emanuel B.S., Nayak S., Mickanin C., Budarf M.L., Buck C.A.;
RL Genome Res. 7:399-399(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=9499415; DOI=10.1093/hmg/7.4.629;
RA Lindsay E.A., Harvey E.L., Scambler P.J., Baldini A.B.;
RT "ES2, a gene deleted in DiGeorge syndrome, encodes a nuclear protein and is
RT expressed during early mouse development, where it shares an expression
RT domain with a Goosecoid-like gene.";
RL Hum. Mol. Genet. 7:629-635(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Kidney;
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: May be involved in pre-mRNA splicing.
CC {ECO:0000250|UniProtKB:P34420}.
CC -!- SUBUNIT: Identified in the spliceosome C complex.
CC {ECO:0000250|UniProtKB:Q96DF8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P34420}.
CC -!- TISSUE SPECIFICITY: In the adult, widely expressed with highest
CC expression in the testis and brain. Also widely expressed in the embryo
CC with highest levels in the anterior pons.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during embryogenesis from 7 dpc
CC onwards.
CC -!- SIMILARITY: Belongs to the ESS2 family. {ECO:0000305}.
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DR EMBL; AC004412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF037256; AAC40077.1; -; mRNA.
DR EMBL; AK088520; BAC40400.1; -; mRNA.
DR EMBL; BC013711; AAH13711.1; -; mRNA.
DR CCDS; CCDS88893.1; -.
DR RefSeq; NP_001075102.1; NM_001081633.1.
DR AlphaFoldDB; O70279; -.
DR STRING; 10090.ENSMUSP00000003621; -.
DR iPTMnet; O70279; -.
DR PhosphoSitePlus; O70279; -.
DR EPD; O70279; -.
DR jPOST; O70279; -.
DR MaxQB; O70279; -.
DR PaxDb; O70279; -.
DR PeptideAtlas; O70279; -.
DR PRIDE; O70279; -.
DR ProteomicsDB; 275479; -.
DR Antibodypedia; 245; 110 antibodies from 18 providers.
DR DNASU; 27886; -.
DR Ensembl; ENSMUST00000232423; ENSMUSP00000156085; ENSMUSG00000003527.
DR GeneID; 27886; -.
DR KEGG; mmu:27886; -.
DR UCSC; uc007ymn.1; mouse.
DR CTD; 8220; -.
DR MGI; MGI:107854; Ess2.
DR VEuPathDB; HostDB:ENSMUSG00000003527; -.
DR eggNOG; KOG2627; Eukaryota.
DR GeneTree; ENSGT00390000009387; -.
DR InParanoid; O70279; -.
DR BioGRID-ORCS; 27886; 16 hits in 75 CRISPR screens.
DR ChiTaRS; Dgcr14; mouse.
DR PRO; PR:O70279; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; O70279; protein.
DR Bgee; ENSMUSG00000003527; Expressed in animal zygote and 210 other tissues.
DR ExpressionAtlas; O70279; baseline and differential.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR019148; Nuclear_protein_DGCR14_ESS-2.
DR PANTHER; PTHR12940; PTHR12940; 1.
DR Pfam; PF09751; Es2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome; Ubl conjugation.
FT CHAIN 1..479
FT /note="Splicing factor ESS-2 homolog"
FT /id="PRO_0000079877"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96DF8"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96DF8"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96DF8"
FT MOD_RES 389
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96DF8"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96DF8"
FT CROSSLNK 145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96DF8"
FT CONFLICT 84
FT /note="R -> P (in Ref. 3; AAC40077)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="D -> DA (in Ref. 3; AAC40077)"
FT /evidence="ECO:0000305"
FT CONFLICT 416..417
FT /note="AL -> PV (in Ref. 3; AAC40077)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="S -> F (in Ref. 4; BAC40400)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 52604 MW; A7BC852063D146A1 CRC64;
MGTPGTSAGA LFLSSASAPS RKRAAGEAGE AGVARSRQRV LDEEEYIEGL QTVIQRDFFP
DVEKLQAQKE YLEAEENGDL ERMRQIAIKF GSALGKISRE PPPPYVTPAT FETPEVHPGS
AVLGNKPRPQ GRDLDDGEAG EEEEKEPLPS LDVFLSQYTS EDNASFQEIM EVAKEKSHAR
HAWLYQAEEE FEKRQKDNLE LPSAEHQAIE SSQAGVETWK YKAKNSLMYY PEGVPDEEQL
FKKPRQIVHK NTRFLRDPFS QALSRSQLQQ AAALNAQHKQ GKVGPDGKEL IPQESPRVGG
FGFVATPSPA PGVNESPLMT WGEVENTPLR VEGSESPYVD RTPGPTFKIL EPGRRERLGL
KMANEAAAKN RAKKQEALRR VTENLASLTP KGLSPAMSPA LQRLVSRTAS KYTDRALRAS
YTPSPARSSH LKTPAGGPQT PTSTPAPGSA TRTPLTQDPA SITDNLLQLP ARRKASDFF
