ZRAB2_MOUSE
ID ZRAB2_MOUSE Reviewed; 330 AA.
AC Q9R020; Q3TI29; Q3TLF5; Q3TUB7; Q3UD16;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
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 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] (ISOFORMS 1 AND 2).
RC STRAIN=BALB/cJ, and C57BL/6J;
RC TISSUE=Amnion, Brain, Embryo, Embryonic stomach, Erythroblast, and
RC Macrophage;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-327 (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=10773668; DOI=10.1159/000015487;
RA Adams D.J., van der Weyden L., Kovacic A., Lovicu F.J., Copeland N.G.,
RA Gilbert D.J., Jenkins N.A., Ioannou P.A., Morris B.J.;
RT "Chromosome localization and characterization of the mouse and human zinc
RT finger protein 265 gene.";
RL Cytogenet. Cell Genet. 88:68-73(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-153 AND SER-188, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-18; LYS-54 AND LYS-92, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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 SNRNP70, the Arg/Ser-
CC rich domain of AKAP17A as well as with U2AF1 and CLK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9R020-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9R020-2; Sequence=VSP_024946;
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=AAF04474.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE36054.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE38837.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE39790.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE40017.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK146275; BAE27034.1; -; mRNA.
DR EMBL; AK150291; BAE29446.1; -; mRNA.
DR EMBL; AK152536; BAE31292.1; -; mRNA.
DR EMBL; AK160862; BAE36054.1; ALT_FRAME; mRNA.
DR EMBL; AK166534; BAE38837.1; ALT_INIT; mRNA.
DR EMBL; AK167756; BAE39790.1; ALT_FRAME; mRNA.
DR EMBL; AK167766; BAE39799.1; -; mRNA.
DR EMBL; AK167862; BAE39880.1; -; mRNA.
DR EMBL; AK167983; BAE39974.1; -; mRNA.
DR EMBL; AK168033; BAE40017.1; ALT_FRAME; mRNA.
DR EMBL; AK168162; BAE40123.1; -; mRNA.
DR EMBL; AK168613; BAE40479.1; -; mRNA.
DR EMBL; AK169114; BAE40895.1; -; mRNA.
DR EMBL; AK169335; BAE41087.1; -; mRNA.
DR EMBL; BC132547; AAI32548.1; -; mRNA.
DR EMBL; AF133818; AAF04474.1; ALT_FRAME; mRNA.
DR CCDS; CCDS51100.1; -. [Q9R020-1]
DR RefSeq; NP_059077.1; NM_017381.2. [Q9R020-1]
DR RefSeq; XP_017175137.1; XM_017319648.1.
DR AlphaFoldDB; Q9R020; -.
DR SMR; Q9R020; -.
DR BioGRID; 207495; 11.
DR IntAct; Q9R020; 1.
DR STRING; 10090.ENSMUSP00000101673; -.
DR iPTMnet; Q9R020; -.
DR PhosphoSitePlus; Q9R020; -.
DR EPD; Q9R020; -.
DR jPOST; Q9R020; -.
DR MaxQB; Q9R020; -.
DR PaxDb; Q9R020; -.
DR PRIDE; Q9R020; -.
DR ProteomicsDB; 275315; -. [Q9R020-1]
DR ProteomicsDB; 275316; -. [Q9R020-2]
DR Antibodypedia; 19679; 296 antibodies from 30 providers.
DR DNASU; 53861; -.
DR Ensembl; ENSMUST00000106058; ENSMUSP00000101673; ENSMUSG00000028180. [Q9R020-1]
DR GeneID; 53861; -.
DR KEGG; mmu:53861; -.
DR UCSC; uc008rve.1; mouse. [Q9R020-1]
DR CTD; 9406; -.
DR MGI; MGI:1858211; Zranb2.
DR VEuPathDB; HostDB:ENSMUSG00000028180; -.
DR eggNOG; KOG1995; Eukaryota.
DR GeneTree; ENSGT00730000111078; -.
DR InParanoid; Q9R020; -.
DR OMA; DLWGDNE; -.
DR BioGRID-ORCS; 53861; 10 hits in 75 CRISPR screens.
DR ChiTaRS; Zranb2; mouse.
DR PRO; PR:Q9R020; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9R020; protein.
DR Bgee; ENSMUSG00000028180; Expressed in undifferentiated genital tubercle and 257 other tissues.
DR ExpressionAtlas; Q9R020; baseline and differential.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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; Alternative splicing; Metal-binding; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..330
FT /note="Zinc finger Ran-binding domain-containing protein 2"
FT /id="PRO_0000066586"
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:0007744|PubMed:23806337"
FT MOD_RES 54
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:21183079"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95218"
FT VAR_SEQ 37..73
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024946"
FT CONFLICT 86
FT /note="N -> D (in Ref. 3; AAF04474)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="N -> S (in Ref. 3; AAF04474)"
FT /evidence="ECO:0000305"
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
