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Zinc finger protein 382 (KRAB/zinc finger suppressor protein 1) (KS1) (Multiple zinc finger and krueppel-associated box protein KS1)

 ZN382_MOUSE             Reviewed;         579 AA.
B2RXC5; Q3UYY9;
20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
01-JUL-2008, sequence version 1.
31-JAN-2018, entry version 85.
RecName: Full=Zinc finger protein 382;
AltName: Full=KRAB/zinc finger suppressor protein 1;
Short=KS1;
AltName: Full=Multiple zinc finger and krueppel-associated box protein KS1;
Name=Znf382; Synonyms=Zfp382;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-578.
STRAIN=C57BL/6J; TISSUE=Forelimb;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
INTERACTION WITH TRIM28.
PubMed=11154279; DOI=10.1128/MCB.21.3.928-939.2001;
Gebelein B., Urrutia R.;
"Sequence-specific transcriptional repression by KS1, a multiple-zinc-
finger-Kruppel-associated box protein.";
Mol. Cell. Biol. 21:928-939(2001).
-!- FUNCTION: Functions as a sequence-specific transcriptional
repressor. {ECO:0000250}.
-!- SUBUNIT: Interacts with TRIM28; enhances the transcriptional
repressor activity. {ECO:0000269|PubMed:11154279}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-37 is the initiator.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CH466593; EDL24044.1; -; Genomic_DNA.
EMBL; BC151163; AAI51164.1; -; mRNA.
EMBL; AK134263; BAE22072.1; -; mRNA.
CCDS; CCDS39877.1; -.
RefSeq; NP_001074476.1; NM_001081007.1.
UniGene; Mm.443484; -.
ProteinModelPortal; B2RXC5; -.
SMR; B2RXC5; -.
STRING; 10090.ENSMUSP00000096196; -.
PhosphoSitePlus; B2RXC5; -.
MaxQB; B2RXC5; -.
PaxDb; B2RXC5; -.
PRIDE; B2RXC5; -.
Ensembl; ENSMUST00000098596; ENSMUSP00000096196; ENSMUSG00000074220.
GeneID; 233060; -.
KEGG; mmu:233060; -.
UCSC; uc009gdf.1; mouse.
CTD; 233060; -.
MGI; MGI:3588204; Zfp382.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00900000140826; -.
HOGENOM; HOG000234617; -.
HOVERGEN; HBG018163; -.
InParanoid; B2RXC5; -.
KO; K09228; -.
OMA; HNECEKS; -.
OrthoDB; EOG091G02KC; -.
PhylomeDB; B2RXC5; -.
TreeFam; TF337898; -.
PRO; PR:B2RXC5; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000074220; -.
ExpressionAtlas; B2RXC5; baseline and differential.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003700; F:DNA binding transcription factor activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd07765; KRAB_A-box; 1.
InterPro; IPR001909; KRAB.
InterPro; IPR036051; KRAB_dom_sf.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF01352; KRAB; 1.
SMART; SM00349; KRAB; 1.
SMART; SM00355; ZnF_C2H2; 9.
SUPFAM; SSF109640; SSF109640; 1.
SUPFAM; SSF57667; SSF57667; 5.
PROSITE; PS50805; KRAB; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
1: Evidence at protein level;
Complete proteome; DNA-binding; Metal-binding; Nucleus;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 579 Zinc finger protein 382.
/FTId=PRO_0000361567.
DOMAIN 42 113 KRAB. {ECO:0000255|PROSITE-
ProRule:PRU00119}.
ZN_FING 241 263 C2H2-type 1; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 325 347 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 353 375 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 381 403 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 409 431 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 437 459 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 465 487 C2H2-type 7. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 493 515 C2H2-type 8. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 521 543 C2H2-type 9. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 549 571 C2H2-type 10. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 12 135 Mediates interaction with TRIM28.
{ECO:0000250}.
REGION 40 81 Represses transcription. {ECO:0000250}.
REGION 105 240 Represses transcription. {ECO:0000250}.
REGION 325 579 Required for transcriptional repression
activity; probably mediates sequence-
specific DNA-binding. {ECO:0000250}.
CONFLICT 576 576 M -> T (in Ref. 3; BAE22072).
{ECO:0000305}.
SEQUENCE 579 AA; 66547 MW; 9FF4EAAFA05A3FF7 CRC64;
MGRPGRKPRG RARPGLFPFP KEELRQGGSS PANLNAMSKG PVSFKDVTVD FTQEEWQRLD
PAQKALYRDV MLENYCHFIS VGFHITKPDM IRKLEQGEEL WTERIFPSQS YLEEEEVLVK
FSDYQDKPPK SIVIIKHKKL IKERSSVYGE ALGKNRVVSK TLFEYKSDGK VLKNISEFIS
RDINPAMGKL GGSKEWEGSI LTSKQEKTHP ASILHKQIGR ALSSEWDLAQ HQKTQIPEQR
FEYNKCDSSF LMTGVEFPHG RAHRGGGNFN YSKDDITLFE KSDLGIHPHD LMEKKCSSYN
KYGELLCRKS VFVMHPSSQM DERPFQCPYC GNSFRRKSYL IEHERIHTGE KPYICCQCGR
AFRQKTALTL HEKTHTEGKP YLCVDCGKSF RQKATLTRHH KAHTGEKAYE CTQCGSAFGK
KSYLIDHQRT HTGEKPYQCT ECGKAFIQKT TLTVHQRTHT GEKPYICSEC GKSFCQKTTL
TLHQRIHTGE KPYICSDCGK SFRQKAILTV HYRIHTGEKS NGCPQCGKAF SRKSNLIRHQ
KIHTGEKPYE CQECGKFFSC KSNLITHQKT HKTETMRFQ


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