ID   ZRAB2_PONAB             Reviewed;         320 AA.
AC   Q5R580;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Zinc finger Ran-binding domain-containing protein 2;
DE   AltName: Full=Zinc finger protein 265;
GN   Name=ZRANB2 {ECO:0000250|UniProtKB:O95218};
GN   Synonyms=ZNF265 {ECO:0000250|UniProtKB:O95218};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1] {ECO:0000312|EMBL:CAH93086.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex {ECO:0000312|EMBL:CAH93086.1};
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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|UniProtKB:O95218}.
CC   -!- DOMAIN: The RanBP2-type zinc fingers mediate binding to RNA.
CC       {ECO:0000250|UniProtKB:O95218}.
CC   -!- PTM: Phosphorylated on Ser-310 upon DNA damage, probably by ATM or ATR.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ZRANB2 family. {ECO:0000255}.
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DR   EMBL; CR860984; CAH93086.1; -; mRNA.
DR   RefSeq; NP_001127628.1; NM_001134156.1.
DR   AlphaFoldDB; Q5R580; -.
DR   SMR; Q5R580; -.
DR   STRING; 9601.ENSPPYP00000001445; -.
DR   GeneID; 100174707; -.
DR   KEGG; pon:100174707; -.
DR   CTD; 9406; -.
DR   eggNOG; KOG1995; Eukaryota.
DR   InParanoid; Q5R580; -.
DR   OrthoDB; 1399319at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Acetylation; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT   CHAIN           1..320
FT                   /note="Zinc finger Ran-binding domain-containing protein 2"
FT                   /id="PRO_0000285985"
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..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          151..320
FT                   /note="Required for nuclear targeting"
FT                   /evidence="ECO:0000250|UniProtKB:O95218"
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   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:0000250|UniProtKB:O95218"
FT   MOD_RES         153
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95218"
FT   MOD_RES         181
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95218"
FT   MOD_RES         188
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95218"
FT   MOD_RES         193
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95218"
SQ   SEQUENCE   320 AA;  36318 MW;  15F1DFB7CD6CF611 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
     SRSSSRERSR SRGSKSRSSS RSHRGSSSPR KRSYSSSSSS PERNRKRSRS RSSSSGDRKK
     RRTRSRSPES QVIGENTKQP