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SRTD1_MOUSE
ID   SRTD1_MOUSE             Reviewed;         236 AA.
AC   Q9JL10; Q925E6; Q9D888;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=SERTA domain-containing protein 1;
DE   AltName: Full=CDK4-binding protein p34SEI1;
DE            Short=SEI-1;
DE   AltName: Full=Transcriptional regulator interacting with the PHD-bromodomain 1;
DE            Short=TRIP-Br1;
GN   Name=Sertad1; Synonyms=Sei1;
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].
RA   Ohtani N., Hara E.;
RT   "Cloning of mouse SEI-1 cDNA.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH E2F1 AND TFDP1,
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=11331592; DOI=10.1093/emboj/20.9.2273;
RA   Hsu S.-I., Yang C.M., Sim K.G., Hentschel D.M., O'Leary E., Bonventre J.V.;
RT   "TRIP-Br: a novel family of PHD zinc finger- and bromodomain-interacting
RT   proteins that regulate the transcriptional activity of E2F-1/DP-1.";
RL   EMBO J. 20:2273-2285(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Small intestine;
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 MRNA].
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).
CC   -!- FUNCTION: Acts at E2F-responsive promoters as coregulator to integrate
CC       signals provided by PHD- and/or bromodomain-containing transcription
CC       factors. Stimulates E2F1/TFDP1 transcriptional activity. Renders the
CC       activity of cyclin D1/CDK4 resistant to the inhibitory effects of
CC       CDKN2A/p16INK4A. {ECO:0000269|PubMed:11331592}.
CC   -!- SUBUNIT: Interacts with the PHD-bromodomain of TIF1, TRIM28/TIF1B and
CC       p300/CBP. Interacts with E2F1 and TFDP1; modulates transactivation
CC       activity of TFDP1/E2F complexes. Also interacts with CDK4.
CC       {ECO:0000269|PubMed:11331592}.
CC   -!- TISSUE SPECIFICITY: Detected at in testis, lung and, at lower levels,
CC       in muscle, liver, spleen, brain and heart.
CC       {ECO:0000269|PubMed:11331592}.
CC   -!- DEVELOPMENTAL STAGE: Detected as early as 7 dpc and persist until, at
CC       least, 17 dpc. {ECO:0000269|PubMed:11331592}.
CC   -!- PTM: Polyubiquitinated, which promotes proteasomal degradation.
CC       {ECO:0000250}.
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DR   EMBL; AF218291; AAF27653.1; -; mRNA.
DR   EMBL; AF366400; AAK52829.1; -; mRNA.
DR   EMBL; AF366401; AAK52830.1; -; mRNA.
DR   EMBL; AK004022; BAB23130.1; -; mRNA.
DR   EMBL; AK008303; BAB25588.1; -; mRNA.
DR   EMBL; BC016077; AAH16077.1; -; mRNA.
DR   CCDS; CCDS21022.1; -.
DR   RefSeq; NP_061290.1; NM_018820.4.
DR   RefSeq; XP_006540280.1; XM_006540217.3.
DR   AlphaFoldDB; Q9JL10; -.
DR   BioGRID; 207738; 12.
DR   CORUM; Q9JL10; -.
DR   IntAct; Q9JL10; 7.
DR   STRING; 10090.ENSMUSP00000008528; -.
DR   PaxDb; Q9JL10; -.
DR   PRIDE; Q9JL10; -.
DR   Antibodypedia; 16970; 193 antibodies from 31 providers.
DR   DNASU; 55942; -.
DR   Ensembl; ENSMUST00000008528; ENSMUSP00000008528; ENSMUSG00000008384.
DR   GeneID; 55942; -.
DR   KEGG; mmu:55942; -.
DR   UCSC; uc009fwh.1; mouse.
DR   CTD; 29950; -.
DR   MGI; MGI:1913438; Sertad1.
DR   VEuPathDB; HostDB:ENSMUSG00000008384; -.
DR   eggNOG; ENOG502S52T; Eukaryota.
DR   GeneTree; ENSGT00940000154733; -.
DR   HOGENOM; CLU_1229598_0_0_1; -.
DR   InParanoid; Q9JL10; -.
DR   OMA; LAVDTWW; -.
DR   OrthoDB; 1466590at2759; -.
DR   PhylomeDB; Q9JL10; -.
DR   TreeFam; TF101069; -.
DR   BioGRID-ORCS; 55942; 4 hits in 71 CRISPR screens.
DR   PRO; PR:Q9JL10; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q9JL10; protein.
DR   Bgee; ENSMUSG00000008384; Expressed in granulocyte and 243 other tissues.
DR   ExpressionAtlas; Q9JL10; baseline and differential.
DR   Genevisible; Q9JL10; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0016528; C:sarcoplasm; IDA:MGI.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR   InterPro; IPR009263; SERTA_dom.
DR   Pfam; PF06031; SERTA; 1.
DR   PROSITE; PS51053; SERTA; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..236
FT                   /note="SERTA domain-containing protein 1"
FT                   /id="PRO_0000191612"
FT   DOMAIN          38..85
FT                   /note="SERTA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00396"
FT   REGION          190..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        9..10
FT                   /note="KR -> NG (in Ref. 3; BAB25588)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        12
FT                   /note="E -> K (in Ref. 2; AAK52829)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   236 AA;  25136 MW;  989ADF8299DE84C5 CRC64;
     MLSKGLKRKR EEEETMEALS VDSCWLDPSH PAVAQTPPTV ASSSLFDLSV VKLHHSLRQS
     EPDLRHLVLV VNTLRRIQAS MEPAPVLPPE PIQPPAPSVA DSLLASSDAG LSASMASLLE
     DLNHIEDLNQ APQPQADEGP PGRSIGGISP NLGALDLLGP ATGCLLDDGL EGLFEDIDTS
     MYDSELWLPA SEGLKPGPEN GPAKEEPPEL DEAELDYLMD VLVGTQALER PPGPGR
 
 
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