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 15-MAR-2017, entry version 145. 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; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. 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 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 [7] 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 [8] 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: Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 CC trimeric complex. Increase GTP hydrolysis induced by the Ran CC GTPase activating protein RANGAP1. May act in an intracellular CC signaling pathway which may control the progression through the CC cell cycle by regulating the transport of protein and nucleic CC acids across the nuclear membrane. 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 UniGene; Mm.235287; -. DR ProteinModelPortal; P34022; -. DR BioGrid; 202581; 21. DR IntAct; P34022; 22. DR MINT; MINT-1850829; -. DR STRING; 10090.ENSMUSP00000111309; -. DR iPTMnet; P34022; -. DR PhosphoSitePlus; P34022; -. DR SwissPalm; P34022; -. DR REPRODUCTION-2DPAGE; P34022; -. DR EPD; 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; ENSGT00870000136510; -. DR HOGENOM; HOG000176323; -. DR HOVERGEN; HBG006958; -. DR InParanoid; P34022; -. DR KO; K15306; -. DR OMA; KGPGKND; -. DR OrthoDB; EOG091G0Y8B; -. DR PhylomeDB; P34022; -. DR ChiTaRS; Ranbp1; mouse. DR PRO; PR:P34022; -. DR Proteomes; UP000000589; Chromosome 16. DR Bgee; ENSMUSG00000005732; -. DR CleanEx; MM_RANBP1; -. DR ExpressionAtlas; P34022; baseline and differential. DR Genevisible; P34022; MM. DR GO; GO:1904115; C:axon cytoplasm; IEA:Ensembl. DR GO; GO:0005913; C:cell-cell adherens junction; 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:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; 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; IEA:Ensembl. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central. DR GO; GO:0046604; P:positive regulation of mitotic centrosome separation; IDA:MGI. DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl. DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central. DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl. DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central. DR GO; GO:0007051; P:spindle organization; IDA:MGI. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR Gene3D; 2.30.29.30; -; 1. DR InterPro; IPR011993; PH_dom-like. DR InterPro; IPR000156; Ran_bind_dom. DR Pfam; PF00638; Ran_BP1; 1. DR SMART; SM00160; RanBD; 1. DR SUPFAM; SSF50729; SSF50729; 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 //