RANG_MOUSE
ID RANG_MOUSE Reviewed; 203 AA.
AC P34022; P34023; Q3TL81; Q9D894; Q9DCA3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Ran-specific GTPase-activating protein;
DE AltName: Full=HpaII tiny fragments locus 9a protein;
DE AltName: Full=Ran-binding protein 1;
DE Short=RANBP1;
GN Name=Ranbp1; Synonyms=Htf9-a, Htf9a;
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 [MRNA], AND INTERACTION WITH RAN.
RX PubMed=8255297; DOI=10.1038/366585a0;
RA Coutavas E., Ren M., Oppenheim J.D., D'Eustachio P., Rush M.G.;
RT "Characterization of proteins that interact with the cell-cycle regulatory
RT protein Ran/TC4.";
RL Nature 366:585-587(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=1889746; DOI=10.1016/0378-1119(91)90274-f;
RA Bressan A., Somma M.P., Lewis J., Santolamazza C., Copeland N.G.,
RA Gilbert D.J., Jenkins N.A., Lavia P.;
RT "Characterization of the opposite-strand genes from the mouse
RT bidirectionally transcribed HTF9 locus.";
RL Gene 103:201-209(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Lavia P.;
RL Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Brain, Small intestine, and Thymus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [6]
RP INTERACTION WITH RAN.
RX PubMed=7891706; DOI=10.1128/mcb.15.4.2117;
RA Ren M., Villamarin A., Shih A., Coutavas E., Moore M.S., Locurcio M.,
RA Clarke V., Oppenheim J.D., D'Eustachio P., Rush M.G.;
RT "Separate domains of the Ran GTPase interact with different factors to
RT regulate nuclear protein import and RNA processing.";
RL Mol. Cell. Biol. 15:2117-2124(1995).
RN [7]
RP INTERACTION WITH RAN.
RX PubMed=8896452; DOI=10.1002/j.1460-2075.1996.tb00943.x;
RA Goerlich D., Pante N., Kutay U., Aebi U., Bischoff F.R.;
RT "Identification of different roles for RanGDP and RanGTP in nuclear protein
RT import.";
RL EMBO J. 15:5584-5594(1996).
RN [8]
RP FUNCTION, INTERACTION WITH RAN, AND SUBUNIT.
RX PubMed=9428644; DOI=10.1016/s0014-5793(97)01467-1;
RA Bischoff F.R., Goerlich D.;
RT "RanBP1 is crucial for the release of RanGTP from importin beta-related
RT nuclear transport factors.";
RL FEBS Lett. 419:249-254(1997).
RN [9]
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-150 AND LYS-182, SUCCINYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-150, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Plays a role in RAN-dependent nucleocytoplasmic transport.
CC Alleviates the TNPO1-dependent inhibition of RAN GTPase activity and
CC mediates the dissociation of RAN from proteins involved in transport
CC into the nucleus (PubMed:9428644). Induces a conformation change in the
CC complex formed by XPO1 and RAN that triggers the release of the nuclear
CC export signal of cargo proteins (By similarity). Promotes the
CC disassembly of the complex formed by RAN and importin beta. Promotes
CC dissociation of RAN from a complex with KPNA2 and CSE1L
CC (PubMed:9428644). Required for normal mitotic spindle assembly and
CC normal progress through mitosis via its effect on RAN (By similarity).
CC Does not increase the RAN GTPase activity by itself, but increases GTP
CC hydrolysis mediated by RANGAP1 (PubMed:9428644). Inhibits RCC1-
CC dependent exchange of RAN-bound GDP by GTP (By similarity).
CC {ECO:0000250|UniProtKB:P43487, ECO:0000269|PubMed:9428644}.
CC -!- SUBUNIT: Interacts with RAN (via C-terminus of GTP-bound form) but not
CC with GDP-bound RAN (PubMed:8255297, PubMed:7891706, PubMed:8896452).
CC Identified in a complex composed of RAN, RANGAP1 and RANBP1 (By
CC similarity). Identified in a complex that contains TNPO1, RAN and
CC RANBP1 (PubMed:9428644). Identified in a complex that contains CSE1L,
CC KPNA2, RAN and RANBP1 (PubMed:9428644). Identified in a complex with
CC nucleotide-free RAN and RCC1 (By similarity).
CC {ECO:0000250|UniProtKB:P43487, ECO:0000269|PubMed:7891706,
CC ECO:0000269|PubMed:8255297, ECO:0000269|PubMed:8896452,
CC ECO:0000269|PubMed:9428644}.
CC -!- MISCELLANEOUS: Htf9a (RanBP1) and Htf9c are transcribed with opposite
CC polarity from complementary DNA strands from a shared bidirectional
CC TATA-less promoter.
CC -!- SIMILARITY: Belongs to the RANBP1 family. {ECO:0000305}.
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DR EMBL; X56046; CAA39517.1; -; mRNA.
DR EMBL; L25255; AAA16195.1; -; mRNA.
DR EMBL; X56045; CAA39516.1; -; mRNA.
DR EMBL; AK002989; BAB22501.1; -; mRNA.
DR EMBL; AK008276; BAB25569.1; -; mRNA.
DR EMBL; AK088781; BAC40569.1; -; mRNA.
DR EMBL; AK151167; BAE30170.1; -; mRNA.
DR EMBL; AK166642; BAE38911.1; -; mRNA.
DR EMBL; AK167053; BAE39217.1; -; mRNA.
DR EMBL; BC061140; AAH61140.1; -; mRNA.
DR CCDS; CCDS37280.1; -.
DR PIR; JQ1973; JQ1973.
DR RefSeq; NP_035369.2; NM_011239.2.
DR AlphaFoldDB; P34022; -.
DR SMR; P34022; -.
DR BioGRID; 202581; 37.
DR IntAct; P34022; 21.
DR STRING; 10090.ENSMUSP00000111309; -.
DR iPTMnet; P34022; -.
DR PhosphoSitePlus; P34022; -.
DR SwissPalm; P34022; -.
DR REPRODUCTION-2DPAGE; P34022; -.
DR CPTAC; non-CPTAC-3859; -.
DR CPTAC; non-CPTAC-3860; -.
DR EPD; P34022; -.
DR jPOST; P34022; -.
DR MaxQB; P34022; -.
DR PaxDb; P34022; -.
DR PeptideAtlas; P34022; -.
DR PRIDE; P34022; -.
DR ProteomicsDB; 254980; -.
DR TopDownProteomics; P34022; -.
DR Antibodypedia; 23138; 288 antibodies from 36 providers.
DR DNASU; 19385; -.
DR Ensembl; ENSMUST00000115645; ENSMUSP00000111309; ENSMUSG00000005732.
DR GeneID; 19385; -.
DR KEGG; mmu:19385; -.
DR UCSC; uc007ymy.1; mouse.
DR CTD; 5902; -.
DR MGI; MGI:96269; Ranbp1.
DR VEuPathDB; HostDB:ENSMUSG00000005732; -.
DR eggNOG; KOG0864; Eukaryota.
DR GeneTree; ENSGT00900000141073; -.
DR InParanoid; P34022; -.
DR OMA; HLEQTGN; -.
DR OrthoDB; 1573143at2759; -.
DR PhylomeDB; P34022; -.
DR BioGRID-ORCS; 19385; 16 hits in 74 CRISPR screens.
DR ChiTaRS; Ranbp1; mouse.
DR PRO; PR:P34022; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P34022; protein.
DR Bgee; ENSMUSG00000005732; Expressed in yolk sac and 72 other tissues.
DR ExpressionAtlas; P34022; baseline and differential.
DR Genevisible; P34022; MM.
DR GO; GO:1904115; C:axon cytoplasm; ISO:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032838; C:plasma membrane bounded cell projection cytoplasm; ISO:MGI.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0072750; P:cellular response to leptomycin B; ISO:MGI.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IEA:InterPro.
DR GO; GO:0046604; P:positive regulation of mitotic centrosome separation; IDA:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0007051; P:spindle organization; IDA:MGI.
DR CDD; cd13179; RanBD_RanBP1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR InterPro; IPR045256; RanBP1_RanBD.
DR PANTHER; PTHR23138; PTHR23138; 1.
DR Pfam; PF00638; Ran_BP1; 1.
DR SMART; SM00160; RanBD; 1.
DR PROSITE; PS50196; RANBD1; 1.
PE 1: Evidence at protein level;
KW Acetylation; GTPase activation; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P43487"
FT CHAIN 2..203
FT /note="Ran-specific GTPase-activating protein"
FT /id="PRO_0000213668"
FT DOMAIN 26..164
FT /note="RanBD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P43487"
FT MOD_RES 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P43487"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43487"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 150
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 150
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 182
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43487"
FT CONFLICT 9
FT /note="E -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 22..24
FT /note="NHD -> TTH (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="L -> V (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="W -> R (in Ref. 4; BAB25569)"
FT /evidence="ECO:0000305"
FT CONFLICT 70..72
FT /note="RGT -> PRH (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="T -> P (in Ref. 4; BAB25569)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="A -> T (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 203 AA; 23596 MW; 4CA6C21DDF5B6F4F CRC64;
MAAAKDSHED HDTSTENADE SNHDPQFEPI VSLPEQEIKT LEEDEEELFK MRAKLFRFAS
ENDLPEWKER GTGDVKLLKH KEKGTIRLLM RRDKTLKICA NHYITPMMEL KPNAGSDRAW
VWNTHADFAD ECPKPELLAI RFLNAENAQK FKTKFEECRK EIEEREKKGP GKNDNAEKVA
EKLEALSVRE AREEAEEKSE EKQ
