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 08-MAY-2019, entry version 159. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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 RT regulatory 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; RC 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: 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; RA Goerlich D., Pante N., Kutay U., Aebi U., Bischoff F.R.; RT "Identification of different roles for RanGDP and RanGTP in nuclear RT protein import."; RL EMBO J. 15:5584-5594(1996). RN [8] RP FUNCTION, INTERACTION WITH RAN, AND SUBUNIT. RX PubMed=9428644; RA Bischoff F.R., Goerlich D.; RT "RanBP1 is crucial for the release of RanGTP from importin beta- RT related 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 RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, 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 RT expression."; RL Cell 143:1174-1189(2010). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-150 AND LYS-182, RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-150, AND IDENTIFICATION BY RP 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., RA Zhang Y., 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 CC transport. Alleviates the TNPO1-dependent inhibition of RAN GTPase CC activity and mediates the dissociation of RAN from proteins CC involved in transport into the nucleus (PubMed:9428644). Induces a CC conformation change in the complex formed by XPO1 and RAN that CC triggers the release of the nuclear export signal of cargo CC proteins (By similarity). Promotes the disassembly of the complex CC formed by RAN and importin beta. Promotes dissociation of RAN from CC a complex with KPNA2 and CSE1L (PubMed:9428644). Required for CC normal mitotic spindle assembly and normal progress through CC mitosis via its effect on RAN (By similarity). Does not increase CC the RAN GTPase activity by itself, but increases GTP hydrolysis CC mediated by RANGAP1 (PubMed:9428644). Inhibits RCC1-dependent CC 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 CC not with GDP-bound RAN (PubMed:8255297, PubMed:7891706, CC PubMed:8896452). Identified in a complex composed of RAN, RANGAP1 CC and RANBP1 (By similarity). Identified in a complex that contains CC TNPO1, RAN and RANBP1 (PubMed:9428644). Identified in a complex CC that contains CSE1L, KPNA2, RAN and RANBP1 (PubMed:9428644). CC Identified in a complex with nucleotide-free RAN and RCC1 (By CC similarity). {ECO:0000250|UniProtKB:P43487, CC ECO:0000269|PubMed:7891706, ECO:0000269|PubMed:8255297, CC ECO:0000269|PubMed:8896452, ECO:0000269|PubMed:9428644}. CC -!- MISCELLANEOUS: Htf9a (RanBP1) and Htf9c are transcribed with CC opposite polarity from complementary DNA strands from a shared CC bidirectional TATA-less promoter. CC -!- SIMILARITY: Belongs to the RANBP1 family. {ECO:0000305}. 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; 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 BioGrid; 202581; 21. DR IntAct; P34022; 22. DR MINT; P34022; -. DR STRING; 10090.ENSMUSP00000111309; -. DR iPTMnet; P34022; -. DR PhosphoSitePlus; P34022; -. DR SwissPalm; P34022; -. DR REPRODUCTION-2DPAGE; P34022; -. DR EPD; P34022; -. DR jPOST; P34022; -. DR MaxQB; P34022; -. DR PaxDb; P34022; -. DR PeptideAtlas; P34022; -. DR PRIDE; P34022; -. DR TopDownProteomics; P34022; -. DR Ensembl; ENSMUST00000115645; ENSMUSP00000111309; ENSMUSG00000005732. DR Ensembl; ENSMUST00000183528; ENSMUSP00000139059; ENSMUSG00000099164. DR GeneID; 19385; -. DR KEGG; mmu:19385; -. DR UCSC; uc007ymy.1; mouse. DR CTD; 5902; -. DR MGI; MGI:96269; Ranbp1. DR eggNOG; KOG0864; Eukaryota. DR eggNOG; COG5171; LUCA. DR GeneTree; ENSGT00900000141073; -. DR HOGENOM; HOG000176323; -. DR InParanoid; P34022; -. DR KO; K15306; -. DR OMA; EEADVHF; -. DR OrthoDB; 1573143at2759; -. DR PhylomeDB; P34022; -. DR ChiTaRS; Ranbp1; mouse. DR PRO; PR:P34022; -. DR Proteomes; UP000000589; Chromosome 16. DR Bgee; ENSMUSG00000005732; Expressed in 274 organ(s), highest expression level in maxillary prominence. 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:0008536; F:Ran GTPase binding; IBA:GO_Central. DR GO; GO:0035690; P:cellular response to drug; IEA:Ensembl. DR GO; GO:0072750; P:cellular response to leptomycin B; ISO:MGI. DR GO; GO:0046907; P:intracellular 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:0051592; P:response to calcium ion; IEA:Ensembl. DR GO; GO:0007051; P:spindle organization; IDA:MGI. DR Gene3D; 2.30.29.30; -; 1. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR000156; Ran_bind_dom. DR Pfam; PF00638; Ran_BP1; 1. DR SMART; SM00160; RanBD; 1. DR PROSITE; PS50196; RANBD1; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; GTPase activation; Phosphoprotein; KW Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P43487}. FT CHAIN 2 203 Ran-specific GTPase-activating protein. FT /FTId=PRO_0000213668. FT DOMAIN 26 164 RanBD1. {ECO:0000255|PROSITE- FT ProRule:PRU00164}. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000250|UniProtKB:P43487}. FT MOD_RES 13 13 Phosphothreonine. FT {ECO:0000250|UniProtKB:P43487}. FT MOD_RES 21 21 Phosphoserine. FT {ECO:0000250|UniProtKB:P43487}. FT MOD_RES 60 60 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 150 150 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 150 150 N6-succinyllysine; alternate. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 182 182 N6-acetyllysine. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 187 187 Phosphoserine. FT {ECO:0000250|UniProtKB:P43487}. FT CONFLICT 9 9 E -> A (in Ref. 2). {ECO:0000305}. FT CONFLICT 22 24 NHD -> TTH (in Ref. 2). {ECO:0000305}. FT CONFLICT 33 33 L -> V (in Ref. 1 and 2). {ECO:0000305}. FT CONFLICT 67 67 W -> R (in Ref. 4; BAB25569). FT {ECO:0000305}. FT CONFLICT 70 72 RGT -> PRH (in Ref. 2). {ECO:0000305}. FT CONFLICT 85 85 T -> P (in Ref. 4; BAB25569). FT {ECO:0000305}. FT CONFLICT 126 126 A -> T (in Ref. 2 and 3). {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 //