CSRN1_MOUSE
ID CSRN1_MOUSE Reviewed; 583 AA.
AC P59054; Q3USP7;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cysteine/serine-rich nuclear protein 1;
DE Short=CSRNP-1;
DE AltName: Full=Axin-1 up-regulated gene 1 protein;
DE AltName: Full=TGF-beta-induced apoptosis protein 3;
DE Short=TAIP-3;
GN Name=Csrnp1; Synonyms=Axud1, Taip3;
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].
RC STRAIN=BALB/cJ; TISSUE=Lung;
RA Akiyama N., Saitoh S., Yamada H., Kondoh S.K.;
RT "TGF-beta induced apoptosis protein 3 (TAIP-3).";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and 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 [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary gland, and Trophoblast;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=17726538; DOI=10.1371/journal.pone.0000808;
RA Gingras S., Pelletier S., Boyd K., Ihle J.N.;
RT "Characterization of a family of novel cysteine- serine-rich nuclear
RT proteins (CSRNP).";
RL PLoS ONE 2:E808-E808(2007).
CC -!- FUNCTION: Binds to the consensus sequence 5'-AGAGTG-3' and has
CC transcriptional activator activity. May have a tumor-suppressor
CC function. May play a role in apoptosis. {ECO:0000269|PubMed:17726538}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17726538}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in thymus and
CC lung. Low levels detected in naive T-cells.
CC {ECO:0000269|PubMed:17726538}.
CC -!- INDUCTION: By interleukin-2. {ECO:0000269|PubMed:17726538}.
CC -!- DISRUPTION PHENOTYPE: Mice display no obvious defects in development,
CC hematopoiesis or T-cell function. Deletion of Csrnp1, Csrnp2 and Csrnp3
CC together causes partial neonatal lethality, suggesting that they have
CC redundant functions. {ECO:0000269|PubMed:17726538}.
CC -!- SIMILARITY: Belongs to the AXUD1 family. {ECO:0000305}.
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DR EMBL; AB091687; BAC16314.1; -; mRNA.
DR EMBL; AK029893; BAC26661.1; -; mRNA.
DR EMBL; AK140213; BAE24284.1; -; mRNA.
DR EMBL; BC029720; AAH29720.1; -; mRNA.
DR EMBL; BC050066; AAH50066.1; -; mRNA.
DR CCDS; CCDS23620.1; -.
DR RefSeq; NP_695019.1; NM_153287.3.
DR RefSeq; XP_006512100.1; XM_006512037.3.
DR RefSeq; XP_006512101.1; XM_006512038.2.
DR RefSeq; XP_006512103.1; XM_006512040.3.
DR RefSeq; XP_006512104.1; XM_006512041.3.
DR RefSeq; XP_011241256.1; XM_011242954.2.
DR AlphaFoldDB; P59054; -.
DR BioGRID; 229623; 1.
DR STRING; 10090.ENSMUSP00000035101; -.
DR iPTMnet; P59054; -.
DR PhosphoSitePlus; P59054; -.
DR EPD; P59054; -.
DR PaxDb; P59054; -.
DR PRIDE; P59054; -.
DR ProteomicsDB; 285378; -.
DR Antibodypedia; 12159; 149 antibodies from 29 providers.
DR Ensembl; ENSMUST00000035101; ENSMUSP00000035101; ENSMUSG00000032515.
DR Ensembl; ENSMUST00000214058; ENSMUSP00000150628; ENSMUSG00000032515.
DR Ensembl; ENSMUST00000215916; ENSMUSP00000149214; ENSMUSG00000032515.
DR GeneID; 215418; -.
DR KEGG; mmu:215418; -.
DR UCSC; uc009sbu.1; mouse.
DR CTD; 64651; -.
DR MGI; MGI:2387989; Csrnp1.
DR VEuPathDB; HostDB:ENSMUSG00000032515; -.
DR eggNOG; KOG3813; Eukaryota.
DR GeneTree; ENSGT00950000183072; -.
DR HOGENOM; CLU_034103_2_2_1; -.
DR InParanoid; P59054; -.
DR OMA; CHCDRVC; -.
DR OrthoDB; 577123at2759; -.
DR PhylomeDB; P59054; -.
DR TreeFam; TF323969; -.
DR BioGRID-ORCS; 215418; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Csrnp1; mouse.
DR PRO; PR:P59054; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P59054; protein.
DR Bgee; ENSMUSG00000032515; Expressed in granulocyte and 204 other tissues.
DR ExpressionAtlas; P59054; baseline and differential.
DR Genevisible; P59054; MM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0060325; P:face morphogenesis; IMP:MGI.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR InterPro; IPR031972; CSRNP_N.
DR InterPro; IPR023260; Cys/Ser-rich_nuc_prot.
DR PANTHER; PTHR13580; PTHR13580; 1.
DR Pfam; PF16019; CSRNP_N; 1.
DR PRINTS; PR02031; CYSSERRICHNP.
PE 2: Evidence at transcript level;
KW Activator; Apoptosis; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..583
FT /note="Cysteine/serine-rich nuclear protein 1"
FT /id="PRO_0000114787"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 60
FT /note="D -> S (in Ref. 2; BAE24284)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="P -> A (in Ref. 2; BAE24284)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 583 AA; 62525 MW; 9061F7A80404FF27 CRC64;
MTGLLKRKFD QLEEDDSSSS SSSSFSSRLS LSSFPASSAS PAWNSDEEGP GGQAPQSDQD
SCGLQSFTPP SILKRAPRER PGHVAFNGIT VYYFPRCQGF TSVPSRGGCT LGMASRHSTC
RLFSLAEFTQ EQVRARREKL RRRLKEEKLE MLRWKFSVAG VPESGAGVPL TADAIDDASV
EEDLAVAVAN GRLEEANFLQ PHPPRQRRAL LRASGVRRID REEKRELQVL RQSREDCGCH
CDGVCDPETC SCSLAGIKCQ MDHTSFPCGC CREGCENPNG RVEFNQTRVQ THFIHTLTRL
QMEQGAESLG DLESPVEDTP VEQAALSPFP PSKPPVSSEL GDSSCSSDMT DSSTTLSSGS
SEPPNHPAHP SLPGPSFRSG VDEDSLEQIL NFSDSDLGIE EEEEEGGGVG NLDNLSCFHL
ADIFGTGDPG SLASWTHSQS GSSLASGILD ENANLDASCF LNSGLGGLRE GSLPGSSGSP
EGDAVQSSSW DLSLSSCDSF ELLQALPDYS LGPHYTSRRV SGSPDSLETF HPLPSFSPPR
DASTCFLESL VGLSEPVTEV LAPLLESQFE DAALAPLLEP VPV
