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ZSC10_MOUSE
ID   ZSC10_MOUSE             Reviewed;         782 AA.
AC   Q3URR7; B7ZP53; Q20D61; Q20D62; Q20D63;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Zinc finger and SCAN domain-containing protein 10;
DE   AltName: Full=Zinc finger protein 206;
GN   Name=Zscan10; Synonyms=Zfp206;
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] (ISOFORMS 1; 2 AND 3), FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=129S1/Sv;
RX   PubMed=16971461; DOI=10.1093/nar/gkl631;
RA   Zhang W., Walker E., Tamplin O.J., Rossant J., Stanford W.L., Hughes T.R.;
RT   "Zfp206 regulates ES cell gene expression and differentiation.";
RL   Nucleic Acids Res. 34:4780-4790(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=129P2;
RX   PubMed=17628018; DOI=10.1634/stemcells.2007-0085;
RA   Wang Z.X., Kueh J.L., Teh C.H., Rossbach M., Lim L., Li P., Wong K.Y.,
RA   Lufkin T., Robson P., Stanton L.W.;
RT   "Zfp206 is a transcription factor that controls pluripotency of embryonic
RT   stem cells.";
RL   Stem Cells 25:2173-2182(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
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].
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   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   [6]
RP   INDUCTION.
RX   PubMed=17344211; DOI=10.1074/jbc.m611814200;
RA   Wang Z.X., Teh C.H., Kueh J.L., Lufkin T., Robson P., Stanton L.W.;
RT   "Oct4 and Sox2 directly regulate expression of another pluripotency
RT   transcription factor, Zfp206, in embryonic stem cells.";
RL   J. Biol. Chem. 282:12822-12830(2007).
RN   [7]
RP   FUNCTION, DNA-BINDING, AND INTERACTION WITH POU5F1 AND SOX2.
RX   PubMed=19740739; DOI=10.1074/jbc.m109.016162;
RA   Yu H.B., Kunarso G., Hong F.H., Stanton L.W.;
RT   "Zfp206, Oct4, and Sox2 are integrated components of a transcriptional
RT   regulatory network in embryonic stem cells.";
RL   J. Biol. Chem. 284:31327-31335(2009).
CC   -!- FUNCTION: Embryonic stem (ES) cell-specific transcription factor
CC       required to maintain ES cell pluripotency. Can both activate and /or
CC       repress expression of target genes, depending on the context.
CC       Specifically binds the 5'-[GA]CGCNNGCG[CT]-3' DNA consensus sequence.
CC       Regulates expression of POU5F1/OCT4, ZSCAN4 and ALYREF/THOC4.
CC       {ECO:0000269|PubMed:16971461, ECO:0000269|PubMed:17628018,
CC       ECO:0000269|PubMed:19740739}.
CC   -!- SUBUNIT: Interacts with POU5F1/OCT4 and SOX2.
CC       {ECO:0000269|PubMed:19740739}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187,
CC       ECO:0000269|PubMed:16971461, ECO:0000269|PubMed:17628018}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3URR7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3URR7-2; Sequence=VSP_039228;
CC       Name=3;
CC         IsoId=Q3URR7-3; Sequence=VSP_039227;
CC   -!- TISSUE SPECIFICITY: Embryonic stem (ES) cell-specific. Not expressed in
CC       adult, except in testis. {ECO:0000269|PubMed:16971461,
CC       ECO:0000269|PubMed:17628018}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout embryogenesis.
CC       {ECO:0000269|PubMed:16971461}.
CC   -!- INDUCTION: Transcriptionally regulated by POU5F1/OCT4 and SOX2.
CC       {ECO:0000269|PubMed:17344211}.
CC   -!- PTM: Methylated at Gln-485 by N6AMT1. {ECO:0000250|UniProtKB:Q96SZ4}.
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DR   EMBL; DQ323929; ABC54589.1; -; mRNA.
DR   EMBL; DQ323930; ABC54590.1; -; mRNA.
DR   EMBL; DQ323931; ABC54591.1; -; mRNA.
DR   EMBL; EF152498; ABM45916.1; -; mRNA.
DR   EMBL; AK141259; BAE24621.1; -; mRNA.
DR   EMBL; CH466606; EDL22251.1; -; Genomic_DNA.
DR   EMBL; BC145638; AAI45639.1; -; mRNA.
DR   CCDS; CCDS28451.1; -. [Q3URR7-1]
DR   CCDS; CCDS70766.1; -. [Q3URR7-2]
DR   CCDS; CCDS79510.1; -. [Q3URR7-3]
DR   RefSeq; NP_001028597.2; NM_001033425.4. [Q3URR7-1]
DR   RefSeq; NP_001276410.1; NM_001289481.1. [Q3URR7-2]
DR   RefSeq; NP_001276411.1; NM_001289482.1. [Q3URR7-3]
DR   RefSeq; NP_001276412.1; NM_001289483.1.
DR   RefSeq; NP_001276413.1; NM_001289484.1.
DR   PDB; 4E6S; X-ray; 1.85 A; A=36-128.
DR   PDBsum; 4E6S; -.
DR   AlphaFoldDB; Q3URR7; -.
DR   SMR; Q3URR7; -.
DR   BioGRID; 237126; 24.
DR   STRING; 10090.ENSMUSP00000093255; -.
DR   iPTMnet; Q3URR7; -.
DR   PhosphoSitePlus; Q3URR7; -.
DR   PaxDb; Q3URR7; -.
DR   PeptideAtlas; Q3URR7; -.
DR   PRIDE; Q3URR7; -.
DR   ProteomicsDB; 302148; -. [Q3URR7-1]
DR   ProteomicsDB; 302149; -. [Q3URR7-2]
DR   ProteomicsDB; 302150; -. [Q3URR7-3]
DR   Antibodypedia; 58023; 28 antibodies from 11 providers.
DR   DNASU; 332221; -.
DR   Ensembl; ENSMUST00000095595; ENSMUSP00000093255; ENSMUSG00000023902. [Q3URR7-1]
DR   Ensembl; ENSMUST00000115509; ENSMUSP00000111171; ENSMUSG00000023902. [Q3URR7-3]
DR   Ensembl; ENSMUST00000120967; ENSMUSP00000113386; ENSMUSG00000023902. [Q3URR7-2]
DR   GeneID; 332221; -.
DR   KEGG; mmu:332221; -.
DR   UCSC; uc008ask.3; mouse. [Q3URR7-2]
DR   UCSC; uc008asl.2; mouse. [Q3URR7-1]
DR   UCSC; uc008asm.2; mouse. [Q3URR7-3]
DR   CTD; 84891; -.
DR   MGI; MGI:3040700; Zscan10.
DR   VEuPathDB; HostDB:ENSMUSG00000023902; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000162513; -.
DR   HOGENOM; CLU_002678_49_8_1; -.
DR   InParanoid; Q3URR7; -.
DR   OMA; THQLRSH; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q3URR7; -.
DR   TreeFam; TF338010; -.
DR   BioGRID-ORCS; 332221; 3 hits in 71 CRISPR screens.
DR   PRO; PR:Q3URR7; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q3URR7; protein.
DR   Bgee; ENSMUSG00000023902; Expressed in epiblast (generic) and 63 other tissues.
DR   ExpressionAtlas; Q3URR7; baseline and differential.
DR   Genevisible; Q3URR7; MM.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0048863; P:stem cell differentiation; TAS:UniProtKB.
DR   CDD; cd07936; SCAN; 1.
DR   Gene3D; 1.10.4020.10; -; 1.
DR   InterPro; IPR003309; SCAN_dom.
DR   InterPro; IPR038269; SCAN_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00096; zf-C2H2; 12.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 14.
DR   SUPFAM; SSF57667; SSF57667; 8.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; DNA-binding; Metal-binding;
KW   Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..782
FT                   /note="Zinc finger and SCAN domain-containing protein 10"
FT                   /id="PRO_0000394248"
FT   DOMAIN          1..71
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT   ZN_FING         292..315
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         321..343
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         349..371
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         377..399
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         421..443
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         467..489
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         495..517
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         523..545
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         551..573
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         579..601
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         607..629
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         635..657
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         669..691
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         697..719
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..318
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         160
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96SZ4"
FT   MOD_RES         206
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96SZ4"
FT   MOD_RES         485
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96SZ4"
FT   VAR_SEQ         131..240
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16971461"
FT                   /id="VSP_039227"
FT   VAR_SEQ         328..359
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16971461"
FT                   /id="VSP_039228"
FT   CONFLICT        306
FT                   /note="V -> E (in Ref. 1; ABC54589/ABC54590/ABC54591, 2;
FT                   ABM45916 and 4; EDL22251)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        546
FT                   /note="V -> L (in Ref. 3; BAE24621)"
FT                   /evidence="ECO:0000305"
FT   HELIX           39..47
FT                   /evidence="ECO:0007829|PDB:4E6S"
FT   TURN            53..55
FT                   /evidence="ECO:0007829|PDB:4E6S"
FT   HELIX           57..72
FT                   /evidence="ECO:0007829|PDB:4E6S"
FT   TURN            74..76
FT                   /evidence="ECO:0007829|PDB:4E6S"
FT   HELIX           79..93
FT                   /evidence="ECO:0007829|PDB:4E6S"
FT   HELIX           97..100
FT                   /evidence="ECO:0007829|PDB:4E6S"
FT   HELIX           101..103
FT                   /evidence="ECO:0007829|PDB:4E6S"
FT   HELIX           111..116
FT                   /evidence="ECO:0007829|PDB:4E6S"
SQ   SEQUENCE   782 AA;  88355 MW;  B521507A5C617AED CRC64;
     MLAEPVPDAL EQEHPGAVKL EEDEVGEEDP RLAESRPRPE VAHQLFRCFQ YQEDMGPRAS
     LGRLRELCNH WLRPALHTKK QILELLVLEQ FLSVLPPHVL SRLHGQPLRD GEEVVQLLEG
     VPRDISHMGP LDFSFSAGKN APADIISEEQ NSPSQVPSHS PQTELPSEEI PALHPLNELP
     PPQPAPIRPA EPEEWRLAPS SNWPMSPEPQ EILQDPRESN PSQGPSWLEE NSRDQELAAV
     LESLTFEDTS EKRAWPANPL GFGSRMPDNE ELKVEEPKVT TWPVVIGAES QTEKPEVAGE
     PLTQTVGQET SSTGWGGTPA DGSEVVKVRG ASDAPEPQGE MQFICTYCGV NFPEMSHLQA
     HQLQSHPNLQ PHPSSRSFRC LWCGKTFGRS SILKLHMRTH TDERPHACHL CNRRFRQSSH
     LTKHLLTHSS EPAFRCAECN QGFQRRSSLM QHLLAHAQGK NLTPNPEGKT KVPEMAAVLC
     SHCGQTFKRR SSLKRHLRNH AKDKDHLSSE DPGSLSSSQE SNPYVCSDCG KAFRQSEQLM
     IHTRRVHTRE RPFSCQVCGR CFTQNSQLIS HQQIHTGEKP HACPQCSKRF VRRAGLARHL
     LTHGSLRPYH CAQCGKSFRQ MRDLTRHVRC HTGEKPCRCN ECGEGFTQNA HLARHQRIHT
     GEKPHACDIC GHRFRNSSNL ARHRRSHTGE RPYSCPTCGR SFRRNAHLQR HLITHTGSKQ
     EKEVPQECPE CGKSFNRSCN LLRHLLVHTG ARPYSCALCG RSFSRNSHLL RHLRTHARES
     LY
 
 
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