ID RANG_MOUSE STANDARD; PRT; 203 AA. AC P34022; P34023; Q9D894; Q9DCA3; DT 01-FEB-1994 (Rel. 28, Created) DT 15-JUN-2004 (Rel. 44, Last sequence update) DT 15-JUN-2004 (Rel. 44, Last annotation update) DE Ran-specific GTPase-activating protein (Ran binding protein 1) DE (RANBP1). GN RANBP1 OR HTF9A OR HTF9-A. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94077185; PubMed=8255297; 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 SEQUENCE FROM N.A. RC STRAIN=C57BL/6; RX MEDLINE=91365246; PubMed=1889746; 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 SEQUENCE FROM N.A. RC STRAIN=C57BL/6; RA Lavia P.; RL Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=C57BL/6J; TISSUE=Brain, Small intestine, and Thymus; RX MEDLINE=22354683; PubMed=12466851; DOI=10.1038/nature01266; RA Okazaki Y., Furuno M., Kasukawa T., Adachi J., Bono H., Kondo S., RA Nikaido I., Osato N., Saito R., Suzuki H., Yamanaka I., Kiyosawa H., RA Yagi K., Tomaru Y., Hasegawa Y., Nogami A., Schonbach C., Gojobori T., RA Baldarelli R., Hill D.P., Bult C., Hume D.A., Quackenbush J., RA Schriml L.M., Kanapin A., Matsuda H., Batalov S., Beisel K.W., RA Blake J.A., Bradt D., Brusic V., Chothia C., Corbani L.E., Cousins S., RA Dalla E., Dragani T.A., Fletcher C.F., Forrest A., Frazer K.S., RA Gaasterland T., Gariboldi M., Gissi C., Godzik A., Gough J., RA Grimmond S., Gustincich S., Hirokawa N., Jackson I.J., Jarvis E.D., RA Kanai A., Kawaji H., Kawasawa Y., Kedzierski R.M., King B.L., RA Konagaya A., Kurochkin I.V., Lee Y., Lenhard B., Lyons P.A., RA Maglott D.R., Maltais L., Marchionni L., McKenzie L., Miki H., RA Nagashima T., Numata K., Okido T., Pavan W.J., Pertea G., Pesole G., RA Petrovsky N., Pillai R., Pontius J.U., Qi D., Ramachandran S., RA Ravasi T., Reed J.C., Reed D.J., Reid J., Ring B.Z., Ringwald M., RA Sandelin A., Schneider C., Semple C.A., Setou M., Shimada K., RA Sultana R., Takenaka Y., Taylor M.S., Teasdale R.D., Tomita M., RA Verardo R., Wagner L., Wahlestedt C., Wang Y., Watanabe Y., Wells C., RA Wilming L.G., Wynshaw-Boris A., Yanagisawa M., Yang I., Yang L., RA Yuan Z., Zavolan M., Zhu Y., Zimmer A., Carninci P., Hayatsu N., RA Hirozane-Kishikawa T., Konno H., Nakamura M., Sakazume N., Sato K., RA Shiraki T., Waki K., Kawai J., Aizawa K., Arakawa T., Fukuda S., RA Hara A., Hashizume W., Imotani K., Ishii Y., Itoh M., Kagawa I., RA Miyazaki A., Sakai K., Sasaki D., Shibata K., Shinagawa A., RA Yasunishi A., Yoshino M., Waterston R., Lander E.S., Rogers J., RA Birney E., Hayashizaki Y.; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [5] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length RT human and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [6] RP PHOSPHORYLATION SITE SER-60. RX PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200; RA Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; RT "Identification of phosphoproteins and their phosphorylation sites in RT the WEHI-231 B lymphoma cell line."; RL Mol. Cell. Proteomics 3:279-286(2004). 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 -!- SIMILARITY: Contains 1 RanBD1 domain. 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; -. DR EMBL; L25255; AAA16195.1; -. DR EMBL; X56045; CAA39516.1; -. DR EMBL; AK002989; BAB22501.1; -. DR EMBL; AK008276; BAB25569.1; -. DR EMBL; AK088781; BAC40569.1; -. DR EMBL; BC061140; AAH61140.1; -. DR PIR; JQ1973; JQ1973. DR HSSP; P43487; 1K5D. DR MGD; MGI:96269; Ranbp1. DR GO; GO:0005813; C:centrosome; IDA. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0046604; P:positive regulation of centrosome separation; IDA. DR GO; GO:0007051; P:spindle assembly; IDA. DR InterPro; IPR000697; EVH1. DR InterPro; IPR000156; Ran_BP1. DR Pfam; PF00638; Ran_BP1; 1. DR SMART; SM00160; RanBD; 1. DR PROSITE; PS50196; RANBD1; 1. KW GTPase activation; Phosphorylation. FT DOMAIN 26 164 RanBD1. FT MOD_RES 60 60 Phosphoserine. FT CONFLICT 9 9 E -> A (in Ref. 2). FT CONFLICT 22 24 NHD -> TTH (in Ref. 2). FT CONFLICT 33 33 L -> V (in Ref. 1 and 2). FT CONFLICT 67 67 W -> R (in Ref. 4; BAB25569). FT CONFLICT 70 72 RGT -> PRH (in Ref. 2). FT CONFLICT 85 85 T -> P (in Ref. 4; BAB25569). FT CONFLICT 126 126 A -> T (in Ref. 2 and 3). 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 //