ZCH18_RAT
ID ZCH18_RAT Reviewed; 947 AA.
AC Q6TQE1; Q6TQE2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Zinc finger CCCH domain-containing protein 18;
DE AltName: Full=Nuclear protein NHN1;
GN Name=Zc3h18; Synonyms=Nhn1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC STRAIN=Wistar;
RA Hidalgo de Quintana J., Ponnambalam S., Walker J.H.;
RT "Nhn1, a novel highly conserved nuclear protein.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-57; SER-63; SER-70;
RP SER-74; SER-79; SER-91; SER-529; SER-846 AND SER-887, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- SUBUNIT: Interacts with ZFC3H1 in a RNase-insensitive manner.
CC {ECO:0000250|UniProtKB:Q86VM9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q6TQE1-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q6TQE1-2; Sequence=VSP_029458;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY389807; AAR92226.1; -; mRNA.
DR EMBL; AY389808; AAR92227.1; -; mRNA.
DR RefSeq; NP_958819.1; NM_201416.1. [Q6TQE1-2]
DR RefSeq; XP_006255823.1; XM_006255761.2. [Q6TQE1-2]
DR AlphaFoldDB; Q6TQE1; -.
DR STRING; 10116.ENSRNOP00000048376; -.
DR iPTMnet; Q6TQE1; -.
DR PhosphoSitePlus; Q6TQE1; -.
DR PaxDb; Q6TQE1; -.
DR PeptideAtlas; Q6TQE1; -.
DR PRIDE; Q6TQE1; -.
DR GeneID; 292067; -.
DR KEGG; rno:292067; -.
DR UCSC; RGD:1303257; rat. [Q6TQE1-1]
DR CTD; 124245; -.
DR RGD; 1303257; Zc3h18.
DR VEuPathDB; HostDB:ENSRNOG00000028501; -.
DR eggNOG; ENOG502R7WP; Eukaryota.
DR HOGENOM; CLU_012901_0_0_1; -.
DR InParanoid; Q6TQE1; -.
DR PRO; PR:Q6TQE1; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000028501; Expressed in skeletal muscle tissue and 18 other tissues.
DR ExpressionAtlas; Q6TQE1; baseline and differential.
DR Genevisible; Q6TQE1; RN.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140262; F:mRNA cap binding complex binding; ISO:RGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:RGD.
DR GO; GO:0050779; P:RNA destabilization; ISO:RGD.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..947
FT /note="Zinc finger CCCH domain-containing protein 18"
FT /id="PRO_0000311244"
FT ZN_FING 214..240
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 915..944
FT /evidence="ECO:0000255"
FT COMPBIAS 1..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..136
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..204
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..539
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..620
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..648
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q86VM9"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VM9"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VM9"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86VM9"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VM9"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VM9"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VM9"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VM9"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VM9"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VM9"
FT MOD_RES 809
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q0P678"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VM9"
FT MOD_RES 846
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 862
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VM9"
FT MOD_RES 887
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VM9"
FT CROSSLNK 505
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86VM9"
FT CROSSLNK 617
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86VM9"
FT CROSSLNK 656
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86VM9"
FT CROSSLNK 812
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86VM9"
FT CROSSLNK 902
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86VM9"
FT VAR_SEQ 223
FT /note="M -> MKDVVTPLSTLLPPIPNSIPLRGQV (in isoform B)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_029458"
SQ SEQUENCE 947 AA; 105537 MW; 4A8513A205131AE4 CRC64;
MDVAESPELE PHSPDEEQPA LSDDDILRES GSEQDLDGAG ERASDLEEEE NATRVQSQEE
IHSDEEDQAS EPKSQDQDSE AHELSRGPAG SPCEEGDDAE EDGTSDLRDE ASSVTRELDE
HELDYDEEVP EEPAPAAQEE EAEKAGAEEE EEKGEGAPGE EGKPDVQSVG EKEPTEAAKE
KKKEDDDGEI DDGEIDDDDL EEGEVKDPSD RKVRPRPTCR FFMKGNCTWG MNCRFIHPGV
NDKGNYSLIT KAEPFPPNGA PPLGPHPLMP ANPWGGPVVD EILPPPPPEP PTESAWERGL
RHAKEVLKKA TIRKEQEPDF EEKRFTVTIG EDDREFDKEN EVFRDWNSRV PRDVRDTTLE
PYADPYYDYE IERFWRGGQY ENFRVQYTEA EPYHNYRDRE RERERENRQR ERERDRERDR
ERERRQRERE RERERERDKE RQRRKEEWER ERAKRDEKDR QHRDRDRDKD RDKDKEKPKP
RSPQPPSRQA EPPKKETASV GPQVKRADEW KDPWRRSKSP KKKLGVSVSP SRARRRRKTS
ASSASASNSS RSSSRSSSYS GSGSSRSRSR SSSYSSYSSR SSRRSSFSGS RSRSRSFSSS
PSPSPTPSPH RPPVRTKGEP APPPGKAGEK SIKKPAPPPA PPQATKTTAP APEPAKPGDL
REARRKERQT RTPPRRRTLS GSGSGSGSSY SGSSSRSRSL SVSSVSSVSS ATSSSSSVHS
VDSDDMYADL ASPVSSASSR SPTPAQTKKE RGKSKKEDGV REEKRKRDPS AQPPKSSKAP
AGGKASQQAA APQQAAPGQP QQGSFVAHKE IKLTLLNKAA EKGSRKRYEP SDKDRQSPPA
KKANLSPDRG SRDRKSGGRM GSPKPERQRG QNAKAPAAPA DRKRPLSPQS KSSSKVTSVP
GKATDTATAG TKSGKASTLS RREELLKQLK AVEDAIARKR AKIPGKV
