QSER1_MOUSE
ID QSER1_MOUSE Reviewed; 1788 AA.
AC A0A338P6K9; A2BIE1; Q3UR75;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Glutamine and serine-rich protein 1 {ECO:0000305};
GN Name=Qser1 {ECO:0000312|MGI:MGI:2138986};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 586-1788.
RC STRAIN=C57BL/6J;
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).
CC -!- FUNCTION: Plays an essential role in the protection and maintenance of
CC transcriptional and developmental programs. Protects many bivalent
CC promoters and poised enhancers from hypermethylation, showing a marked
CC preference for these regulatory elements over other types of promoters
CC or enhancers. Mechanistically, cooperates with TET1 and binds to DNA in
CC a common complex to inhibit the binding of DNMT3A/3B and therefore de
CC novo methylation. {ECO:0000250|UniProtKB:Q2KHR3}.
CC -!- SUBUNIT: Interacts with TET1. {ECO:0000250|UniProtKB:Q2KHR3}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q2KHR3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A0A338P6K9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A338P6K9-2; Sequence=VSP_061204;
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DR EMBL; AK141733; BAE24813.1; -; mRNA.
DR CCDS; CCDS50653.1; -. [A0A338P6K9-2]
DR RefSeq; NP_001116799.1; NM_001123327.2. [A0A338P6K9-2]
DR RefSeq; XP_006500521.1; XM_006500458.2.
DR AlphaFoldDB; A0A338P6K9; -.
DR IntAct; A0A338P6K9; 2.
DR MINT; A0A338P6K9; -.
DR STRING; 10090.ENSMUSP00000114062; -.
DR iPTMnet; A2BIE1; -.
DR jPOST; A0A338P6K9; -.
DR ProteomicsDB; 349126; -.
DR Antibodypedia; 1555; 74 antibodies from 20 providers.
DR Ensembl; ENSMUST00000117237; ENSMUSP00000114062; ENSMUSG00000074994. [A0A338P6K9-2]
DR Ensembl; ENSMUST00000231375; ENSMUSP00000155882; ENSMUSG00000074994. [A0A338P6K9-1]
DR GeneID; 99003; -.
DR KEGG; mmu:99003; -.
DR UCSC; uc008lkg.3; mouse.
DR CTD; 79832; -.
DR MGI; MGI:2138986; Qser1.
DR VEuPathDB; HostDB:ENSMUSG00000074994; -.
DR eggNOG; KOG4805; Eukaryota.
DR GeneTree; ENSGT00440000037417; -.
DR HOGENOM; CLU_000708_2_0_1; -.
DR OMA; LMFLECA; -.
DR OrthoDB; 64109at2759; -.
DR TreeFam; TF333141; -.
DR BioGRID-ORCS; 99003; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Qser1; mouse.
DR Proteomes; UP000000589; Chromosome 2.
DR Bgee; ENSMUSG00000074994; Expressed in external carotid artery and 246 other tissues.
DR ExpressionAtlas; A0A338P6K9; baseline and differential.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR InterPro; IPR025451; DUF4211.
DR Pfam; PF13926; DUF4211; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chromosome; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1788
FT /note="Glutamine and serine-rich protein 1"
FT /id="PRO_0000453804"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1234..1264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1494..1588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1541..1562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2KHR3"
FT MOD_RES 940
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2KHR3"
FT MOD_RES 1003
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q2KHR3"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2KHR3"
FT MOD_RES 1262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2KHR3"
FT MOD_RES 1281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2KHR3"
FT MOD_RES 1282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2KHR3"
FT MOD_RES 1394
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q2KHR3"
FT MOD_RES 1401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2KHR3"
FT CROSSLNK 1112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q2KHR3"
FT CROSSLNK 1137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q2KHR3"
FT VAR_SEQ 1..90
FT /note="Missing (in isoform 2)"
FT /id="VSP_061204"
FT CONFLICT 601
FT /note="Y -> C (in Ref. 2; BAE24813)"
FT /evidence="ECO:0000305"
FT CONFLICT 1397
FT /note="E -> G (in Ref. 2; BAE24813)"
FT /evidence="ECO:0000305"
FT CONFLICT 1787
FT /note="C -> F (in Ref. 2; BAE24813)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1788 AA; 194475 MW; 7B58ECF6B1DD159C CRC64;
MDAHYAPAGF AEPPAPPASA ATQPAAPAWA YEARVPAAAS SPSCSGSSPS LKASYEDGHP
SQSESDVLQR QTFTASHQLP GYATTPQATG MHSSAATELF VAGPLPTTGT LPPPTLSAYQ
HSSTFSNRNF ATTSPLVLQD SSFNTTSNGI LSPHDPLLQI KTSQGTVPTA LAFERLGSSA
LSNSVPPQSS TYRSAQESAP HLLQPQFSLL PSTLGGAQQT PQAYNSALFP SSAASIERAL
LRECSVIKHH QRPSVTQSIQ AQLTGSQHPL HSYLSSASIG NFQEPSRQSS LSCSSVRDST
QVSNGVLPQK TPQVSAELAQ SYSSVIPSSG YLPSATKVDS CSTKQPLTST TIPKPQSVIP
PVQTLNYSKP LHNQSSVISG QAQIYSTAQL PSLLSVSQSQ NYGLVQPHNV PSIVHSQVYR
SSRVEKLPSL YKTLTFSGSS QPVTSENQTL SYSSNQQEVL SLVTNENYPA QTRDLPSVSE
SQNYSSGQSQ GLSPVSQTQV SYSSQSQVLS VVSPSESYAS GQSLTLTAPS LSYSSASRGQ
SLPVSTPTPS YTSMHPSPNA QTQGSSAQPQ EFLPAVQSSF ASSTRGQTLQ SSIPSPDPKS
YAERKLDSSV YTSSKQDEFP VQKLQALQSQ ASLESSSQRL PDGEVNAQES VYKTSKADDR
YSQSVTRNNS HLEDQVVGVA LQGSEQEENM VGSMTQLNQQ SGQSNNAVAT DLKKATNLMQ
TPQVRLNTKD LNQQHSLMHK MHEAKVQQQH DQIMSASSQI QIPNPALGQS HQALPHTSVL
LDSACDLQIL QQAGILQASL GQAKASLQVQ RVQSPQQIVH PFLQMDGHII QSNGEHPQQQ
LHPHNSDIMK LDLPEPSKPL QQLTTKGPFS EANPHDSKNQ FVSLGSICFS EAMLLSDERN
ILSNVDDILA ATAAACGVTP SDFSKSAANE TMQDIESSDS KSHYQQSLNV RHVNSDFNSI
AASVGKPQSI NDISLNGNQV SVSLSSVPTL QSETVLDQPH METPSQTIPT KVPSAMVGLG
QEIQEQSSDP FKKQLTINHE SKEDREIAVD SALSNNRNQE FVSNSRSISG DSVVSERDFT
LVGDDTGVLV NPRRSTLALL AMPQPGDAAS GKTEDEKQDV TYFNLPKEKA KGKEQGKEEE
DNQKQLKRSA QCKRQNPRGT DVYVPYTSPS LESCDEGFQH QEKMRQKIKE VEEKQPEVKT
GFIASFLDFL KCGPKQQFST LAVRVPNRTR RSGIQTTRTF CPPPFAKTSP AAQAPSETGG
VSLSEKVDSE LKTLEQLSSF SSDEEDPGSC GHDIYKNTSA PLTVLDATSD KTKKTVLEAL
PVATPGASAE TAGVAPTAST AVATIKQDLH LTSLTVNTME NANSTESPTA IELDSLPSDQ
LAKGQDTVAI EGFTDEENIE SGGEGQYRER DEFVVKIEDI ETFKEALNTG KEPPAIWKVQ
KALLQKFVPE IRDGQREFAA TNSYLGYFGD AKTKYKRIYV KFIENANKKE YVRVCSKKPR
NKPSQTIRNI PSKPSSISKT SDPPVSKTTT TKTPSTKPKA KQLKIKAEPP PKKRKKWKEE
FSSSQSESSP EVRSSSSEDE GFEPPAPSVT RFLNTRAMKE TFKSYMELLV SIALDPDTMQ
ALEKSNDELL LPHMKKIDGM LNDNRKRLLV NLHLDQPFKN ALESFPELTV ITRDSKAKSG
GSAISKIKMN GKAYNKKTLR TSKTTTKSAQ EFAVDPEKIQ LYSLYHSLHH YKYHVYLICK
NEISSVQKKN EDLGQEEIVQ LCMKNVKWVE DLFEKFGELL NHVQQKCS
