ZRAB2_RAT
ID ZRAB2_RAT Reviewed; 330 AA.
AC O35986; A1A4C8;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Zinc finger Ran-binding domain-containing protein 2;
DE AltName: Full=Zinc finger protein 265;
DE AltName: Full=Zinc finger, splicing;
GN Name=Zranb2; Synonyms=Zfp265, Zis, Znf265;
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 [GENOMIC DNA / MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=9374836; DOI=10.1152/ajprenal.1997.273.5.f731;
RA Karginova E.A., Pentz E.S., Kazakova I.G., Norwood V.F., Carey R.M.,
RA Gomez R.A.;
RT "Zis: a developmentally regulated gene expressed in juxtaglomerular
RT cells.";
RL Am. J. Physiol. 273:F731-F738(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-153 AND SER-188, AND
RP IDENTIFICATION BY 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 -!- FUNCTION: Splice factor required for alternative splicing of
CC TRA2B/SFRS10 transcripts. May interfere with constitutive 5'-splice
CC site selection (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the C-terminal half of SNRP70/U1-70K, the
CC Arg/Ser-rich domain of AKAP17A as well as with U2AF1 and CLK1.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney; more specifically in renal
CC juxtaglomerular (JG) cells.
CC -!- DOMAIN: The RanBP2-type zinc fingers mediate binding to RNA.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ZRANB2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC02295.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC02296.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC02297.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF013965; AAC02295.1; ALT_FRAME; mRNA.
DR EMBL; AF013966; AAC02296.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF013967; AAC02297.1; ALT_FRAME; mRNA.
DR EMBL; BC087012; AAH87012.1; -; mRNA.
DR RefSeq; NP_113804.1; NM_031616.1.
DR RefSeq; XP_017446546.1; XM_017591057.1.
DR AlphaFoldDB; O35986; -.
DR SMR; O35986; -.
DR BioGRID; 248628; 1.
DR STRING; 10116.ENSRNOP00000052134; -.
DR iPTMnet; O35986; -.
DR PhosphoSitePlus; O35986; -.
DR jPOST; O35986; -.
DR PaxDb; O35986; -.
DR PRIDE; O35986; -.
DR Ensembl; ENSRNOT00000098797; ENSRNOP00000093503; ENSRNOG00000009990.
DR GeneID; 58821; -.
DR KEGG; rno:58821; -.
DR CTD; 9406; -.
DR RGD; 61854; Zranb2.
DR eggNOG; KOG1995; Eukaryota.
DR GeneTree; ENSGT00730000111078; -.
DR HOGENOM; CLU_061048_0_0_1; -.
DR InParanoid; O35986; -.
DR OrthoDB; 1224748at2759; -.
DR PhylomeDB; O35986; -.
DR TreeFam; TF105996; -.
DR PRO; PR:O35986; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Genevisible; O35986; RN.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0001530; F:lipopolysaccharide binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR InterPro; IPR017337; ZRANB2.
DR Pfam; PF00641; zf-RanBP; 2.
DR PIRSF; PIRSF037956; UCP037956_ZnF_Ran; 1.
DR SMART; SM00547; ZnF_RBZ; 2.
DR SUPFAM; SSF90209; SSF90209; 2.
DR PROSITE; PS01358; ZF_RANBP2_1; 2.
DR PROSITE; PS50199; ZF_RANBP2_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..330
FT /note="Zinc finger Ran-binding domain-containing protein 2"
FT /id="PRO_0000066587"
FT ZN_FING 9..40
FT /note="RanBP2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 65..94
FT /note="RanBP2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 117..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..324
FT /note="Required for nuclear targeting"
FT /evidence="ECO:0000250"
FT COMPBIAS 117..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..180
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..309
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95218"
FT MOD_RES 18
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R020"
FT MOD_RES 54
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95218"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R020"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95218"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95218"
SQ SEQUENCE 330 AA; 37350 MW; 1FD8F01C7C644F21 CRC64;
MSTKNFRVSD GDWICPDKKC GNVNFARRTS CNRCGREKTT EAKMMKAGGT EIGKTLAEKS
RGLFSANDWQ CKTCSNVNWA RRSECNMCNT PKYAKLEERT GYGGGFNERE NVEYIEREES
DGEYDEFGRK KKKYRGKAVG PASILKEVED KESEGEEEDE DEDLSKYKLD EDEDEDDADL
SKYNLDASEE EDSNKKKSNR RSRSKSRSSH SRSSSRSSSP SSSRSRSRSR SRSSSSSQSR
SHSGSREHSR SRGSKSRSSS RSHRGSSSPR KRSYSSSSSS PERDRKRSRS RPSSPAVRKK
RRTRSRSPER HHRSSSGSTH SGSRSSSKKK
