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CXXC5_MOUSE
ID   CXXC5_MOUSE             Reviewed;         317 AA.
AC   Q91WA4; Q3V0R4; Q8CES6; Q8CF49;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=CXXC-type zinc finger protein 5;
GN   Name=Cxxc5;
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 MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Eye, and Salivary 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   [3]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=19001364; DOI=10.1074/jbc.m808119200;
RA   Andersson T., Soedersten E., Duckworth J.K., Cascante A., Fritz N.,
RA   Sacchetti P., Cervenka I., Bryja V., Hermanson O.;
RT   "CXXC5 is a novel BMP4-regulated modulator of Wnt signaling in neural stem
RT   cells.";
RL   J. Biol. Chem. 284:3672-3681(2009).
CC   -!- FUNCTION: May indirectly participate in activation of the NF-kappa-B
CC       and MAPK pathways. Acts as a mediator of BMP4-mediated modulation of
CC       canonical Wnt signaling activity in neural stem cells. Required for DNA
CC       damage-induced ATM phosphorylation, p53 activation and cell cycle
CC       arrest. Involved in myelopoiesis (By similarity). Binds to the oxygen
CC       responsive element of COX4I2 and represses its transcription under
CC       hypoxia conditions (4% oxygen), as well as normoxia conditions (20%
CC       oxygen). May repress COX4I2 transactivation induced by CHCHD2 and RBPJ
CC       (By similarity). Binds preferentially to DNA containing cytidine-
CC       phosphate-guanosine (CpG) dinucleotides over CpH (H=A, T, and C),
CC       hemimethylated-CpG and hemimethylated-hydroxymethyl-CpG (By
CC       similarity). {ECO:0000250|UniProtKB:Q5XIQ3,
CC       ECO:0000250|UniProtKB:Q7LFL8}.
CC   -!- SUBUNIT: Interacts with DVL1 (By similarity). Interacts with RBPJ (By
CC       similarity). {ECO:0000250|UniProtKB:Q5XIQ3,
CC       ECO:0000250|UniProtKB:Q7LFL8}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5XIQ3}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q5XIQ3}. Note=Colocalizes with DVL1 in large
CC       bodies localized just outside the nuclear membrane.
CC       {ECO:0000250|UniProtKB:Q5XIQ3}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in dorsal pallium and in and around the
CC       developing choroid plexus at 10.5 and 12.5 dpc.
CC       {ECO:0000269|PubMed:19001364}.
CC   -!- DOMAIN: The CXXC zinc finger mediates binding to CpG-DNA.
CC       {ECO:0000250|UniProtKB:Q7LFL8}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC25113.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAC25458.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK005364; BAC25113.1; ALT_FRAME; mRNA.
DR   EMBL; AK015150; BAC25458.1; ALT_FRAME; mRNA.
DR   EMBL; AK132950; BAE21439.1; -; mRNA.
DR   EMBL; BC016207; AAH16207.1; -; mRNA.
DR   EMBL; BC089314; AAH89314.1; -; mRNA.
DR   CCDS; CCDS29150.1; -.
DR   RefSeq; NP_598448.1; NM_133687.2.
DR   RefSeq; XP_006526239.1; XM_006526176.3.
DR   RefSeq; XP_006526240.1; XM_006526177.3.
DR   RefSeq; XP_006526241.1; XM_006526178.3.
DR   RefSeq; XP_006526243.1; XM_006526180.2.
DR   RefSeq; XP_006526244.1; XM_006526181.3.
DR   AlphaFoldDB; Q91WA4; -.
DR   SMR; Q91WA4; -.
DR   BioGRID; 212157; 8.
DR   IntAct; Q91WA4; 7.
DR   MINT; Q91WA4; -.
DR   STRING; 10090.ENSMUSP00000054307; -.
DR   iPTMnet; Q91WA4; -.
DR   PhosphoSitePlus; Q91WA4; -.
DR   EPD; Q91WA4; -.
DR   MaxQB; Q91WA4; -.
DR   PaxDb; Q91WA4; -.
DR   PeptideAtlas; Q91WA4; -.
DR   PRIDE; Q91WA4; -.
DR   ProteomicsDB; 284080; -.
DR   Antibodypedia; 49849; 154 antibodies from 30 providers.
DR   DNASU; 67393; -.
DR   Ensembl; ENSMUST00000060722; ENSMUSP00000054307; ENSMUSG00000046668.
DR   GeneID; 67393; -.
DR   KEGG; mmu:67393; -.
DR   UCSC; uc008emx.1; mouse.
DR   CTD; 51523; -.
DR   MGI; MGI:1914643; Cxxc5.
DR   VEuPathDB; HostDB:ENSMUSG00000046668; -.
DR   eggNOG; ENOG502QT2M; Eukaryota.
DR   GeneTree; ENSGT00940000154108; -.
DR   HOGENOM; CLU_074593_0_0_1; -.
DR   InParanoid; Q91WA4; -.
DR   OMA; ANGHDPP; -.
DR   OrthoDB; 946583at2759; -.
DR   PhylomeDB; Q91WA4; -.
DR   TreeFam; TF326617; -.
DR   BioGRID-ORCS; 67393; 3 hits in 71 CRISPR screens.
DR   ChiTaRS; Cxxc5; mouse.
DR   PRO; PR:Q91WA4; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q91WA4; protein.
DR   Bgee; ENSMUSG00000046668; Expressed in choroid plexus epithelium and 256 other tissues.
DR   ExpressionAtlas; Q91WA4; baseline and differential.
DR   Genevisible; Q91WA4; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR   GO; GO:0008327; F:methyl-CpG binding; ISS:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   InterPro; IPR040388; CXXC4/CXXC5.
DR   InterPro; IPR002857; Znf_CXXC.
DR   PANTHER; PTHR13419; PTHR13419; 1.
DR   Pfam; PF02008; zf-CXXC; 1.
DR   PROSITE; PS51058; ZF_CXXC; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; DNA-binding; Metal-binding; Nucleus; Reference proteome; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..317
FT                   /note="CXXC-type zinc finger protein 5"
FT                   /id="PRO_0000317549"
FT   ZN_FING         251..292
FT                   /note="CXXC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   REGION          1..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           252..257
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         258
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         261
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         264
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         273
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         276
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         286
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   CONFLICT        10
FT                   /note="D -> G (in Ref. 1; BAE21439)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        105
FT                   /note="A -> G (in Ref. 1; BAC25458)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   317 AA;  32812 MW;  215B73C8BA2AE031 CRC64;
     MSSLGGGSQD AGGSSSSSNT NSSSGSGQKA GGTDKSTAVA ATTAPTSVAD DAPPPERRNK
     SGIISEPLNK SLRRSRPLSH YSSFGSSGGG GSMMGVESAD KAAAAAASLL ANGHDLAAAM
     AVDKSNPTSK HKSGAVASLL SKAERATELA AEGQLTLQQF AQSTEMLKRV VQEHLPLMSE
     AGAGLPDMEA VAGAEALNGQ SDFPYLGAFP INPGLFIMTP AGVFLAESAL HMAGLAEYPM
     QGELASAISS GKKKRKRCGM CAPCRRRINC EQCSSCRNRK TGHQICKFRK CEELKKKPSA
     ALEKVMLPSG AAFRWFQ
 
 
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