ID RANG_MOUSE STANDARD; PRT; 203 AA. AC P34022; P34023; Q9D894; Q9DCA3; DT 01-FEB-1994 (Rel. 28, Created) DT 05-JUL-2004 (Rel. 44, Last sequence update) DT 01-MAY-2005 (Rel. 47, Last annotation update) DE Ran-specific GTPase-activating protein (Ran binding protein 1) DE (RANBP1) (HpaII tiny fragments locus 9a protein). 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 Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=94077185; 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. RC STRAIN=C57BL/6; RX MEDLINE=91365246; 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. RC STRAIN=C57BL/6; 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=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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 human RT 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 -!- 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: 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 SMR; P34022; 22-167. 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 mitotic centrosome s...; IDA. DR GO; GO:0007051; P:spindle organization and biogenesis; 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 //