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C3H26_ARATH
ID   C3H26_ARATH             Reviewed;         453 AA.
AC   O48772;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Zinc finger CCCH domain-containing protein 26;
DE            Short=AtC3H26;
DE   AltName: Full=Zinc finger CCCH domain-containing protein ZFN2;
GN   Name=ZFN2; OrderedLocusNames=At2g32930; ORFNames=T21L14.13;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Choi S., Lee J., Yi H., Shin B., Choi G.;
RT   "Characterization of zinc finger protein ZFN-2 in Arabidopsis thaliana.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NOMENCLATURE.
RX   PubMed=18221561; DOI=10.1186/1471-2164-9-44;
RA   Wang D., Guo Y., Wu C., Yang G., Li Y., Zheng C.;
RT   "Genome-wide analysis of CCCH zinc finger family in Arabidopsis and rice.";
RL   BMC Genomics 9:44-44(2008).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=O48772-1; Sequence=Displayed;
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DR   EMBL; AF138744; AAD33770.1; -; mRNA.
DR   EMBL; AC003033; AAB91975.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08763.1; -; Genomic_DNA.
DR   PIR; T01114; T01114.
DR   RefSeq; NP_565758.1; NM_128853.2. [O48772-1]
DR   AlphaFoldDB; O48772; -.
DR   BioGRID; 3202; 2.
DR   STRING; 3702.AT2G32930.2; -.
DR   iPTMnet; O48772; -.
DR   PaxDb; O48772; -.
DR   PRIDE; O48772; -.
DR   ProteomicsDB; 240573; -. [O48772-1]
DR   EnsemblPlants; AT2G32930.1; AT2G32930.1; AT2G32930. [O48772-1]
DR   GeneID; 817855; -.
DR   Gramene; AT2G32930.1; AT2G32930.1; AT2G32930. [O48772-1]
DR   KEGG; ath:AT2G32930; -.
DR   Araport; AT2G32930; -.
DR   eggNOG; KOG1677; Eukaryota.
DR   HOGENOM; CLU_033292_2_0_1; -.
DR   InParanoid; O48772; -.
DR   PhylomeDB; O48772; -.
DR   PRO; PR:O48772; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O48772; baseline and differential.
DR   Genevisible; O48772; AT.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   Pfam; PF00642; zf-CCCH; 5.
DR   SMART; SM00356; ZnF_C3H1; 5.
DR   SUPFAM; SSF90229; SSF90229; 4.
DR   PROSITE; PS50103; ZF_C3H1; 5.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..453
FT                   /note="Zinc finger CCCH domain-containing protein 26"
FT                   /id="PRO_0000213913"
FT   ZN_FING         44..72
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         95..112
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         129..157
FT                   /note="C3H1-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         261..289
FT                   /note="C3H1-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         307..335
FT                   /note="C3H1-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..410
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..453
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   453 AA;  49747 MW;  B5FC49D5FDE5EBA6 CRC64;
     MSETQQQVQN STGSIRSPDK IEDTFRRMKV NEDNMEQSSP YPDRPGERDC QFFLRTGQCG
     YGNSCRYNHP LTNLPQGIIY YRDQLPERVG QPDCETGACK YGPTCKYHHP KDRNGAGPVL
     FNVLGLPMRQ GEKPCPYYMQ TGLCRFGVAC KFHHPHPHSQ PSNGHSAYAM SSFPSVGFPY
     ASGMTMVSLP PATYGAIPRP QVPQSQAYMP YMVAPSQGLL PPQGWATYMT ASNPIYNMKT
     QLDSSSSASV AVTVTSHHHS FSERAECRFF MNTGTCKYGD DCKYSHPKER LLQSPPTLLN
     PIVLPARPGQ PACGNFKAYG FCKFGANCKF DHSMLLNPYN NTGLAMSSLP TPYPYAPPVS
     TNLRISSPPS PSDMTTLSNG KPAAAEAQSL ETEKQDDSPT EPEKSEVEDS LPPNGSDSTS
     LPNDKPDAET EKQDDDSAEL DSSKVQDSSD KST
 
 
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