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ZN142_MOUSE
ID   ZN142_MOUSE             Reviewed;        1843 AA.
AC   G5E869; E9PY67; Q3V1C1; Q8BWJ0; Q8BWL4; Q8CHH6;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Zinc finger protein 142 {ECO:0000305};
GN   Name=Znf142 {ECO:0000250|UniProtKB:P52746};
GN   Synonyms=Kiaa0236 {ECO:0000303|PubMed:12465718},
GN   Zfp142 {ECO:0000312|MGI:MGI:1924514};
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).
RC   TISSUE=Brain;
RX   PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT   The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Heart;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
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.
CC   -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=G5E869-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=G5E869-2; Sequence=VSP_060317;
CC       Name=3;
CC         IsoId=G5E869-3; Sequence=VSP_060316;
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41402.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB093218; BAC41402.1; ALT_INIT; mRNA.
DR   EMBL; AK052201; BAC34881.1; -; mRNA.
DR   EMBL; AK052359; BAC34956.1; -; mRNA.
DR   EMBL; AK132550; BAE21230.1; -; mRNA.
DR   EMBL; AC117610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466548; EDL00334.1; -; Genomic_DNA.
DR   CCDS; CCDS35618.1; -. [G5E869-2]
DR   CCDS; CCDS78619.1; -. [G5E869-1]
DR   RefSeq; NP_001297597.1; NM_001310668.1. [G5E869-1]
DR   RefSeq; NP_084164.1; NM_029888.3. [G5E869-2]
DR   RefSeq; XP_006496381.1; XM_006496318.2. [G5E869-1]
DR   RefSeq; XP_006496382.1; XM_006496319.2. [G5E869-1]
DR   RefSeq; XP_006496384.1; XM_006496321.2.
DR   AlphaFoldDB; G5E869; -.
DR   STRING; 10090.ENSMUSP00000109366; -.
DR   iPTMnet; G5E869; -.
DR   PhosphoSitePlus; G5E869; -.
DR   jPOST; G5E869; -.
DR   MaxQB; G5E869; -.
DR   ProteomicsDB; 339071; -.
DR   ProteomicsDB; 341149; -. [G5E869-1]
DR   ProteomicsDB; 352915; -.
DR   Antibodypedia; 56468; 26 antibodies from 10 providers.
DR   Ensembl; ENSMUST00000027315; ENSMUSP00000027315; ENSMUSG00000026135. [G5E869-1]
DR   Ensembl; ENSMUST00000066986; ENSMUSP00000065149; ENSMUSG00000026135. [G5E869-3]
DR   Ensembl; ENSMUST00000113737; ENSMUSP00000109366; ENSMUSG00000026135. [G5E869-2]
DR   GeneID; 77264; -.
DR   KEGG; mmu:77264; -.
DR   UCSC; uc007bmm.1; mouse.
DR   UCSC; uc007bmn.1; mouse. [G5E869-1]
DR   CTD; 77264; -.
DR   MGI; MGI:1924514; Zfp142.
DR   VEuPathDB; HostDB:ENSMUSG00000026135; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000163074; -.
DR   HOGENOM; CLU_001774_0_0_1; -.
DR   InParanoid; G5E869; -.
DR   OMA; LCEFRCR; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; G5E869; -.
DR   TreeFam; TF327469; -.
DR   BioGRID-ORCS; 77264; 3 hits in 58 CRISPR screens.
DR   PRO; PR:G5E869; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; G5E869; protein.
DR   Bgee; ENSMUSG00000026135; Expressed in animal zygote and 240 other tissues.
DR   ExpressionAtlas; G5E869; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 41.
DR   SUPFAM; SSF57667; SSF57667; 12.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 20.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 21.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..1843
FT                   /note="Zinc finger protein 142"
FT                   /id="PRO_0000447987"
FT   ZN_FING         103..127
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         164..186
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         363..385
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         391..413
FT                   /note="C2H2-type 4; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         453..475
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         543..566
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         601..623
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         629..651
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         657..679
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         685..707
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         744..767
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1331..1354
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1388..1411
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1446..1469
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1514..1537
FT                   /note="C2H2-type 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1608..1630
FT                   /note="C2H2-type 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1636..1658
FT                   /note="C2H2-type 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1664..1686
FT                   /note="C2H2-type 18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1692..1715
FT                   /note="C2H2-type 19"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1721..1743
FT                   /note="C2H2-type 20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1749..1771
FT                   /note="C2H2-type 21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          294..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          819..888
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1103..1177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1795..1843
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        860..874
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1151..1167
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1828..1843
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         354
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52746"
FT   CROSSLNK        794
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52746"
FT   CROSSLNK        1353
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52746"
FT   CROSSLNK        1402
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52746"
FT   CROSSLNK        1747
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52746"
FT   VAR_SEQ         94..294
FT                   /note="Missing (in isoform 3)"
FT                   /id="VSP_060316"
FT   VAR_SEQ         94..196
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_060317"
FT   CONFLICT        1764
FT                   /note="L -> M (in Ref. 2; BAC34881)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1843 AA;  206230 MW;  3A35EF70A8E226B6 CRC64;
     MTDPVLASQL ANGTGEMDGL CSELLLIPPP LSNHGILGPV QNTCASGELA PLPADPGCLL
     VEATATEEGP GNMEIIVEAV TGTLSPGAPE ETSGVLVKVV EVYFCERCEQ SFAEPTLLSV
     HQCTETHIQA VQDLSSPPCS VELPPSNLAL RGPLQDPSLP DSPLPCPVCR QEFVQPQALK
     SHFKIHRVTP NMFSCPESGC VFSAEDRKGL QNHLRQTHKA VPVPCSFRGC SLLFGSQQGM
     ELHRQAHYPF HCSHCSFMGS NVKLFRQHQR SHGASARGEL SAAVQGLPSQ ELLPAAKLPP
     GHREPSEEAS TPLPGQESAE EEDAEEEESV TQKDSQKVMD KSQGAQQLEG HVGSGTESLF
     KTHMCPECKR CFKKRTHLVE HLHLHFPDPS LQCPNCQKFF TSKSKLKTHL LRELGEKAHR
     CPLCHYSAVE RNALNRHMAS MHEDISNFYS DTYACPVCRE EFRLSQALKE HLKSHTAAAA
     AEPLPLHCFQ EGCTYVAPDR KAFLKHLKEI HGVRAVECRH HSCPMLFATA EAMEAHHKSH
     YAFHCPHCDF ACSNKHLFRK HKKQGHPGSE ELRCTFCPFA TFNPVAYQDH VGKMHAYEKI
     HQCSECNFAT AHKRVLIRHM LLHTGEKPHK CELCDFTCRD VSYLSKHMLT HSNTKDYMCT
     ECGYVTKWKH YLSVHMRKHA GDLRYQCNQC SYRCHRADQL SSHKLRHQGK SLMCEVCAFA
     CKRKYELQKH MASQHHPGTP APLYPCRYCS YQSRHKQALL SHENCKHTHL REFHCALCDY
     RTFSNTTLFF HKRKVHGYMP GDQVWQFCNA SQELEGARQC LAPPSDSGPS SQLSAQPERE
     DREHEIVANS NMDQALPETN EEASPKRQDG IEAPQEDDQV DSPSLGEVEE GGCTLHLEAL
     RVELEPETEP LPLEELTETA TVEFRPLDPS GPLGTERPGG LEEPALSSFD SIETPALVAE
     EEPVVEKLAS EPPRNPLISE EAPNTFKAAL TAETVPLPPF PESESLLKAM RRQDKEQAEA
     LVLEGRVQMV VIQGEGRAFR CPHCPFITRR EKALTLHSKS GCQGRREPLL CPECGASFKQ
     QRGLSTHMMK KCPVLLKKNK ALPKPVSPTL HPQLPDNQAS QDAESRKPPP LPSKVELLLP
     KDAPSDLPGG PGVEEPLPTP SDFPTSPPEN SLPTGTSEKF HFEQGKFHCS SCTFLCSRLS
     SITSHVTEGC RGGRGQKRKR GRPQTHAVVL PLNNGDSTLL NTGSTESSPS DGDTAVVQKQ
     KGALFSCPTC PFSCQQERTL RTHQTQGCPL KSGDLHCGLC PFTAPAAAAL RLHQKRRHPT
     ASPASGPRPL LQCGDCGFTC KQSRCLQQHR RLKHEGVKPH QCPFCDFSTT RRYRLEAHQS
     RHTGVGRIPC SSCPQTFGTN SKLRLHQLRV HDKTPTHFCP LCDYSGYLRH DITRHVNSCH
     QGTPSFSCTQ CEAQFSSETA LKQHALRRHP EPTPPSSGCP VEVTEGPLHC SHCGLLCPSP
     ASLRGHTRKQ HPRLECGACQ ESFPNRPALD EHRRQHHFSH RCQLCSFAAR ERVGLVKHYL
     EQHEESSTAP SDGDAGQPSL CCPFCDFACR HQLVLDHHVK GHGGTRLYKC TDCAYSTKNR
     QKITWHSRIH TGEKPYHCHL CAYACADPSR LKYHMRIHKE ERKYLCPECG YKCKWVNQLK
     YHMTKHTGLK PYQCPECEYC TNRADALRVH RETRHREARA FMCEQCGKAF KTRFLLRTHL
     RKHSEAKPYV CNVCHRAFRW AAGLRHHALT HTDRHPFFCR LCSYKAKQKF QVVKHVRRHH
     PDQADPNQGV GKDPTTPTVH LHDVKLEDPS PPAPPAPSTG PEG
 
 
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