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CSRN3_MOUSE
ID   CSRN3_MOUSE             Reviewed;         597 AA.
AC   P59055; A3F6Q4; Q8BUT9; Q8BYL1;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Cysteine/serine-rich nuclear protein 3;
DE            Short=CSRNP-3;
DE   AltName: Full=Protein FAM130A2;
DE   AltName: Full=TGF-beta-induced apoptosis protein 2;
DE            Short=TAIP-2;
GN   Name=Csrnp3; Synonyms=Fam130a2, Mbu1, Taip2;
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).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=17433858; DOI=10.1016/j.gene.2007.03.005;
RA   Yang H.L., Cho E.Y., Han K.H., Kim H., Kim S.J.;
RT   "Characterization of a novel mouse brain gene (mbu-1) identified by digital
RT   differential display.";
RL   Gene 395:144-150(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; TISSUE=Fetal brain;
RX   PubMed=18291095; DOI=10.1016/j.bbrc.2008.02.041;
RA   Yamada K., Akiyama N., Yamada S., Tanaka H., Saito S., Hiraoka M.,
RA   Kizaka-Kondoh S.;
RT   "Taip2 is a novel cell death-related gene expressed in the brain during
RT   development.";
RL   Biochem. Biophys. Res. Commun. 369:426-431(2008).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Hypothalamus, and Visual cortex;
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   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   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   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. Plays a role in apoptosis.
CC       {ECO:0000269|PubMed:17726538, ECO:0000269|PubMed:18291095}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17726538,
CC       ECO:0000269|PubMed:18291095}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P59055-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P59055-2; Sequence=VSP_034260;
CC   -!- TISSUE SPECIFICITY: Detected only in the brain of 15 dpc, 18 dpc,
CC       newborn and P6 mice (at protein level). {ECO:0000269|PubMed:17726538,
CC       ECO:0000269|PubMed:18291095}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during embryonic development and also
CC       detected a week after birth. Expression decreases by 14 days after
CC       birth and is not detected in the adult (at protein level).
CC   -!- DISRUPTION PHENOTYPE: Mice display no obvious defects in development,
CC       hematopoiesis or T-cell function. Deletion of Axud1, Csnrp2 and Csnrp3
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABN14256.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC30257.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; EF210820; ABN14256.1; ALT_INIT; mRNA.
DR   EMBL; AB091688; BAC16315.1; -; mRNA.
DR   EMBL; AK039150; BAC30257.1; ALT_INIT; mRNA.
DR   EMBL; AK082649; BAC38559.1; -; mRNA.
DR   EMBL; AK158873; BAE34706.1; -; mRNA.
DR   EMBL; AL929230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL935061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS16074.2; -. [P59055-1]
DR   CCDS; CCDS71060.1; -. [P59055-2]
DR   RefSeq; NP_001277594.1; NM_001290665.1. [P59055-2]
DR   RefSeq; NP_700458.3; NM_153409.5. [P59055-1]
DR   RefSeq; NP_848749.2; NM_178634.2. [P59055-1]
DR   RefSeq; XP_006500465.1; XM_006500402.2. [P59055-2]
DR   RefSeq; XP_006500466.1; XM_006500403.3.
DR   AlphaFoldDB; P59055; -.
DR   STRING; 10090.ENSMUSP00000117533; -.
DR   PhosphoSitePlus; P59055; -.
DR   MaxQB; P59055; -.
DR   PaxDb; P59055; -.
DR   PRIDE; P59055; -.
DR   ProteomicsDB; 283962; -. [P59055-1]
DR   ProteomicsDB; 283963; -. [P59055-2]
DR   Antibodypedia; 19202; 127 antibodies from 23 providers.
DR   Ensembl; ENSMUST00000053910; ENSMUSP00000055719; ENSMUSG00000044647. [P59055-1]
DR   Ensembl; ENSMUST00000112394; ENSMUSP00000108013; ENSMUSG00000044647. [P59055-2]
DR   Ensembl; ENSMUST00000122912; ENSMUSP00000117533; ENSMUSG00000044647. [P59055-1]
DR   Ensembl; ENSMUST00000145598; ENSMUSP00000135605; ENSMUSG00000044647. [P59055-2]
DR   Ensembl; ENSMUST00000176109; ENSMUSP00000135019; ENSMUSG00000044647. [P59055-2]
DR   GeneID; 77771; -.
DR   KEGG; mmu:77771; -.
DR   UCSC; uc008jwq.2; mouse. [P59055-1]
DR   CTD; 80034; -.
DR   MGI; MGI:1925021; Csrnp3.
DR   VEuPathDB; HostDB:ENSMUSG00000044647; -.
DR   eggNOG; KOG3813; Eukaryota.
DR   GeneTree; ENSGT00950000183072; -.
DR   HOGENOM; CLU_034103_1_0_1; -.
DR   InParanoid; P59055; -.
DR   OMA; MEGLGTH; -.
DR   OrthoDB; 577123at2759; -.
DR   PhylomeDB; P59055; -.
DR   TreeFam; TF323969; -.
DR   BioGRID-ORCS; 77771; 0 hits in 58 CRISPR screens.
DR   ChiTaRS; Csrnp3; mouse.
DR   PRO; PR:P59055; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P59055; protein.
DR   Bgee; ENSMUSG00000044647; Expressed in subparaventricular zone and 142 other tissues.
DR   ExpressionAtlas; P59055; baseline and differential.
DR   Genevisible; P59055; 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:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Activator; Alternative splicing; Apoptosis; DNA-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..597
FT                   /note="Cysteine/serine-rich nuclear protein 3"
FT                   /id="PRO_0000114789"
FT   REGION          22..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..403
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..12
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072,
FT                   ECO:0000303|PubMed:18291095"
FT                   /id="VSP_034260"
FT   CONFLICT        246
FT                   /note="C -> R (in Ref. 2; BAC16315)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        304
FT                   /note="H -> R (in Ref. 2; BAC16315)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   597 AA;  66121 MW;  20AEA5E37793E522 CRC64;
     MRSQGTCDNA AAMSGILKRK FEDVDASSPC SSARESDDEV SSSESADSGD SVNPSTSNHF
     TPSSILKREK RLRTKNVHFS CVTVYYFTRR QGFTSVPSQG GSTLGMSSRH NSVRQYTLGE
     FAREQERLHR EMLREHLREE KLNSLKLKMT KNGTVESEEA STLTVDDISD DDIDLDNTEV
     DEYFFLQPLP TKKRRALLRA SGVKKIDVDE KHELRAIRLS REDCGCDCRV FCDPETCTCS
     LAGIKCQVDR MSFPCGCTKE GCSNTAGRIE FNPIRVRTHF LHTIMKLELE KNREQQTPTL
     NGCHGEISAH GPSMGPVAHS VEYSIADNFE IETEPQAAVL HLQEELDCQG DEEEEEEDGS
     SFCSGATDSS TQSLAPSESD EEEEEEEEEE EEEEEDDDDD KGDGFVEGLG AHTEVVPLPS
     VLCYSDGTAV HESHTKNASF YASSSTLYYQ IDSHIPGTPS QLSDNYSERD TVKNGALSLV
     PYAMTPERFV DYARQAEEAY GASHYPAANP SVIVCCPTSE NDSGVPCNPL YPEHRSNLPQ
     VEFHSYLKGP AQEGFVSTLN GDSHISEHPA ENPLSLAEKS RLHEECIQSP VVETVPV
 
 
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