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UBN1_MOUSE
ID   UBN1_MOUSE              Reviewed;        1135 AA.
AC   Q4G0F8; Q3UUZ4; Q6P9K7; Q8BNC3; Q9CRM4; Q9CS40;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Ubinuclein-1;
DE   AltName: Full=Ubiquitously expressed nuclear protein;
GN   Name=Ubn1;
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] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-197 (ISOFORM 1/2), AND NUCLEOTIDE SEQUENCE [LARGE
RP   SCALE MRNA] OF 557-1135 (ISOFORM 3).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryo, Placenta, Spinal ganglion, Vagina, and Wolffian duct;
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 GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 70-1135 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=18823282; DOI=10.1042/bc20080072;
RA   Aho S., Lupo J., Coly P.-A., Sabine A., Castellazzi M., Morand P.,
RA   Sergeant A., Manet E., Boyer V., Gruffat H.;
RT   "Characterization of the ubinuclein protein as a new member of the nuclear
RT   and adhesion complex components (NACos).";
RL   Biol. Cell 101:319-334(2009).
CC   -!- FUNCTION: Acts as a novel regulator of senescence. Involved in the
CC       formation of senescence-associated heterochromatin foci (SAHF), which
CC       represses expression of proliferation-promoting genes. Binds to
CC       proliferation-promoting genes. May be required for replication-
CC       independent chromatin assembly (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of a complex that includes at least ASF1A, CABIN1,
CC       HIRA, histone H3.3 and UBN1. Interacts with HIRA (via WD repeat
CC       domain); the interaction is direct. Interacts with ASF1A, CEBPA, TJP1,
CC       TJP2 and TJP3 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus, PML
CC       body {ECO:0000250}. Cell junction, tight junction
CC       {ECO:0000269|PubMed:18823282}. Note=Localized as a nuclear speckled-
CC       like pattern in proliferating primary fibroblasts. Colocalizes with
CC       HIRA, PML and SP100 in PML bodies of senescent cells. Colocalizes with
CC       CLDN1. Detected along the upper granular cell layer of epidermis. When
CC       overexpressed, accumulates in the nucleus in cells showing defective
CC       cytokinesis (By similarity). Colocalizes with TJP1. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q4G0F8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q4G0F8-2; Sequence=VSP_036972;
CC       Name=3;
CC         IsoId=Q4G0F8-3; Sequence=VSP_036973;
CC   -!- TISSUE SPECIFICITY: Expressed in bile canaliculi in liver, in
CC       bronchiolar epithelium in lung and in tubular structures of gland ducts
CC       inside the olfactory epithelium and tongue epithelium.
CC       {ECO:0000269|PubMed:18823282}.
CC   -!- SIMILARITY: Belongs to the ubinuclein family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDK97277.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AK019173; BAB31587.1; -; mRNA.
DR   EMBL; AK020146; BAB32010.1; -; mRNA.
DR   EMBL; AK084046; BAC39106.1; -; mRNA.
DR   EMBL; AK137727; BAE23479.1; -; mRNA.
DR   EMBL; AK147571; BAE28001.1; -; mRNA.
DR   EMBL; CH466521; EDK97277.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC060723; AAH60723.1; -; mRNA.
DR   EMBL; BC098372; AAH98372.1; -; mRNA.
DR   CCDS; CCDS27931.1; -. [Q4G0F8-1]
DR   CCDS; CCDS88873.1; -. [Q4G0F8-2]
DR   RefSeq; NP_080942.1; NM_026666.3. [Q4G0F8-1]
DR   RefSeq; XP_006521879.1; XM_006521816.3. [Q4G0F8-1]
DR   RefSeq; XP_006521880.1; XM_006521817.3. [Q4G0F8-1]
DR   RefSeq; XP_006521882.1; XM_006521819.3.
DR   RefSeq; XP_017172375.1; XM_017316886.1. [Q4G0F8-1]
DR   AlphaFoldDB; Q4G0F8; -.
DR   SMR; Q4G0F8; -.
DR   BioGRID; 228360; 2.
DR   STRING; 10090.ENSMUSP00000061843; -.
DR   iPTMnet; Q4G0F8; -.
DR   PhosphoSitePlus; Q4G0F8; -.
DR   EPD; Q4G0F8; -.
DR   jPOST; Q4G0F8; -.
DR   MaxQB; Q4G0F8; -.
DR   PaxDb; Q4G0F8; -.
DR   PeptideAtlas; Q4G0F8; -.
DR   PRIDE; Q4G0F8; -.
DR   ProteomicsDB; 298355; -. [Q4G0F8-1]
DR   ProteomicsDB; 298356; -. [Q4G0F8-2]
DR   ProteomicsDB; 298357; -. [Q4G0F8-3]
DR   Antibodypedia; 11234; 162 antibodies from 35 providers.
DR   DNASU; 170644; -.
DR   Ensembl; ENSMUST00000052449; ENSMUSP00000061843; ENSMUSG00000039473. [Q4G0F8-1]
DR   Ensembl; ENSMUST00000229126; ENSMUSP00000155263; ENSMUSG00000039473. [Q4G0F8-2]
DR   Ensembl; ENSMUST00000230703; ENSMUSP00000155223; ENSMUSG00000039473. [Q4G0F8-1]
DR   GeneID; 170644; -.
DR   KEGG; mmu:170644; -.
DR   UCSC; uc007ybq.1; mouse. [Q4G0F8-1]
DR   UCSC; uc007ybr.1; mouse. [Q4G0F8-2]
DR   UCSC; uc007ybs.1; mouse. [Q4G0F8-3]
DR   CTD; 29855; -.
DR   MGI; MGI:1891307; Ubn1.
DR   VEuPathDB; HostDB:ENSMUSG00000039473; -.
DR   eggNOG; KOG4786; Eukaryota.
DR   GeneTree; ENSGT00940000158857; -.
DR   HOGENOM; CLU_007400_0_0_1; -.
DR   InParanoid; Q4G0F8; -.
DR   OMA; HQDPEPA; -.
DR   OrthoDB; 469344at2759; -.
DR   PhylomeDB; Q4G0F8; -.
DR   TreeFam; TF326088; -.
DR   Reactome; R-MMU-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR   BioGRID-ORCS; 170644; 4 hits in 74 CRISPR screens.
DR   ChiTaRS; Ubn1; mouse.
DR   PRO; PR:Q4G0F8; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q4G0F8; protein.
DR   Bgee; ENSMUSG00000039473; Expressed in lacrimal gland and 244 other tissues.
DR   ExpressionAtlas; Q4G0F8; baseline and differential.
DR   Genevisible; Q4G0F8; MM.
DR   GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR   GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006336; P:DNA replication-independent chromatin assembly; ISO:MGI.
DR   GO; GO:0030216; P:keratinocyte differentiation; TAS:MGI.
DR   InterPro; IPR014840; HRD.
DR   InterPro; IPR026936; Ubinuclein-1.
DR   InterPro; IPR026947; UBN_middle_dom.
DR   PANTHER; PTHR21669:SF12; PTHR21669:SF12; 1.
DR   Pfam; PF08729; HUN; 1.
DR   Pfam; PF14075; UBN_AB; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Cell junction; Chromatin regulator;
KW   Coiled coil; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Tight junction.
FT   CHAIN           1..1135
FT                   /note="Ubinuclein-1"
FT                   /id="PRO_0000370691"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          253..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          603..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          747..985
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1094..1135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          476..539
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..270
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..646
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        807..841
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        857..961
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         166
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPG3"
FT   MOD_RES         173
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPG3"
FT   MOD_RES         175
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPG3"
FT   MOD_RES         222
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPG3"
FT   MOD_RES         323
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPG3"
FT   MOD_RES         336
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPG3"
FT   MOD_RES         338
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPG3"
FT   MOD_RES         493
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPG3"
FT   MOD_RES         660
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPG3"
FT   MOD_RES         677
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPG3"
FT   MOD_RES         1028
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPG3"
FT   VAR_SEQ         1090..1120
FT                   /note="SLLAGLHSSPPHTAPLPHAAVSTHVPQSLPD -> N (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_036972"
FT   VAR_SEQ         1091..1135
FT                   /note="LLAGLHSSPPHTAPLPHAAVSTHVPQSLPDASQLHGKGPVVPRKL -> KFL
FT                   SPASVPMLCAMLGPVCVWCNHGNIPHLWKLHSTRDSCFVPDWSAGCLGL (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_036973"
FT   CONFLICT        184
FT                   /note="K -> N (in Ref. 1; BAB31587)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        681
FT                   /note="A -> G (in Ref. 1; BAC39106)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        801
FT                   /note="G -> A (in Ref. 1; BAC39106)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        969
FT                   /note="A -> P (in Ref. 1; BAC39106)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1135 AA;  122336 MW;  8B5994B86F97E0F7 CRC64;
     MSEPHRVQFT SVPGSLNPAF LKKSRKEEVG GTEQHQDCEP AAAAVRITLT LFEPDHKRCP
     EFFYPELVKN IRGKVKGLHP GDKKKDVLDP FNDEEKERHK VEALARKFEE KYGGKKRRKD
     RIQDLIDMGY GYDESDSFID NSEAYDELVP ASLTTKYGGF YINSGTLQFR QASESEDDFI
     KEKKKKSPKK RKLKEGGEKI KKKKKDDTYD KEKKSKKSKF SKAGFTALNA SKEKKKKKYS
     GSLSVREMLK KFQKEKEAQK KREEEHKPVA VSSIEAQGLR ELEGTSDPLL SLFGSTSDND
     LLQAATAMDS LTDLDLEQLL SESPEGSPFR DMDDGSDSLG VGLDQEFRQP SSFPEGLPIP
     LEKRVKELAQ AARAAEGESK QKFFTQDING ILLDIEVQTR ELTSQIRSGV FAYLASFLPC
     SKDALVKRAR KLHLYEQGGR LKEPLQKLKD AIGRAMPEQV AKYQDECQAH TQAKVAKMLE
     EEKDKEQRER ICSDEEEDEE KGGRRIMGPR KKFQWNDEIR ELLCQVVKIK LESRDLERNS
     KAQAWEDCVK AFLDAEVKPL WPKGWMQART LFKESRRGHG HLTSLLAKKK VIAPSKIKMK
     ESSVKLDKKV SVPSGQHGGP TTLLSEHQGG GLNTGANSRE HPSQATCGLT DSVSVTLEDS
     LDEDLVRNPA SSVDAVSKEL ATLNSRAANS SEFTLPTPSK APTEKVGGVL CTEEKRNFAK
     PSSSAPPPTN ALQSPLNFLA EQALALGQSS QEKKPEGSGF KELSCQGPLS KGVPELHPSK
     AKHHNLPRTS HGPQAAAPVP GPQVKVFHAG TQQQKSFTPP SPFVNKLQGP KATSPQCHRS
     LLQLVKTAAK GQAFHATMPA SSGSSPASSS SAHKTTASNS TTISHPAKLH PTSSVGPSYK
     NNPFAGSVSK HGASSSSPSP GGGAQVQSSV SGASLPGVQS PSAGQSASRA APSSAVKKTP
     VTQKLTLVAP PGGPNGDSGG GTQGVAKLLT SSLKPAAVSS VTSSTSLPKG TGGAVLLSNT
     SSLSLLSSSY KSNNPKLPGA MNSNSLGIIT QFPLHVLSFN ADSSAKAGVS KDAIVTGPAP
     GTFHHGLSHS LLAGLHSSPP HTAPLPHAAV STHVPQSLPD ASQLHGKGPV VPRKL
 
 
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