Full text data of RANBP3
RANBP3
[Confidence: low (only semi-automatic identification from reviews)]
Ran-binding protein 3; RanBP3
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ran-binding protein 3; RanBP3
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H6Z4
ID RANB3_HUMAN Reviewed; 567 AA.
AC Q9H6Z4; B2RAT8; O60405; O75759; O75760; Q9BT47; Q9UG74;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Ran-binding protein 3;
DE Short=RanBP3;
GN Name=RANBP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH CHC1.
RX PubMed=9637251; DOI=10.1016/S0014-5793(98)00459-1;
RA Mueller L., Cordes V.C., Bischoff F.R., Ponstingl H.;
RT "Human RanBP3, a group of nuclear RanGTP binding proteins.";
RL FEBS Lett. 427:330-336(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Colon, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-418 (ISOFORM 3).
RC TISSUE=Eye;
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 FUNCTION, AND INTERACTION WITH XPO1.
RX PubMed=11571268; DOI=10.1093/embo-reports/kve200;
RA Englmeier L., Fornerod M., Bischoff F.R., Petosa C., Mattaj I.W.,
RA Kutay U.;
RT "RanBP3 influences interactions between CRM1 and its nuclear protein
RT export substrates.";
RL EMBO Rep. 2:926-932(2001).
RN [7]
RP FUNCTION, AND INTERACTION WITH XPO1.
RX PubMed=11425870; DOI=10.1083/jcb.153.7.1391;
RA Lindsay M.E., Holaska J.M., Welch K., Paschal B.M., Macara I.G.;
RT "Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein
RT export.";
RL J. Cell Biol. 153:1391-1402(2001).
RN [8]
RP FUNCTION, AND INTERACTION WITH CHC1.
RX PubMed=11932251; DOI=10.1074/jbc.C100620200;
RA Nemergut M.E., Lindsay M.E., Brownawell A.M., Macara I.G.;
RT "Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide
RT exchange factor.";
RL J. Biol. Chem. 277:17385-17388(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-101; SER-108;
RP THR-124; SER-333; SER-353; SER-355 AND SER-539, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP INTERACTION WITH SMAD2 AND SMAD3, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19289081; DOI=10.1016/j.devcel.2009.01.022;
RA Dai F., Lin X., Chang C., Feng X.H.;
RT "Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination
RT of TGF-beta signaling.";
RL Dev. Cell 16:345-357(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP STRUCTURE BY NMR OF 380-516.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RAN_BP1 domain of RAN-binding protein-3.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Acts as a cofactor for XPO1/CRM1-mediated nuclear
CC export, perhaps as export complex scaffolding protein. Bound to
CC XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the
CC absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the
CC nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine
CC nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to
CC CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF-
CC beta signaling through interaction with the R-SMAD proteins, SMAD2
CC and SMAD3, and mediating their nuclear export.
CC -!- SUBUNIT: Interacts with CHC1 in a Ran-stimulated manner. Interacts
CC with XPO1. Interacts (via its C-terminal R domain) with SMAD2
CC (dephosphorylated form via its MH1 and MH2 domains); the
CC interaction results in the nuclear export of SMAD2 and termination
CC of the TGF-beta signaling. Interacts (via its C-terminal R domain)
CC with SMAD3 (dephosphorylated form via its MH1 domain); the
CC interaction results in the nuclear export of SMAD3 and termination
CC of the TGF-beta signaling.
CC -!- INTERACTION:
CC P35813:PPM1A; NbExp=4; IntAct=EBI-992681, EBI-989143;
CC P18754:RCC1; NbExp=2; IntAct=EBI-992681, EBI-992720;
CC Q15796:SMAD2; NbExp=2; IntAct=EBI-992681, EBI-1040141;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H6Z4-1; Sequence=Displayed;
CC Name=2; Synonyms=Ranbp3-a;
CC IsoId=Q9H6Z4-2; Sequence=VSP_011162;
CC Name=3; Synonyms=Ranbp3-b;
CC IsoId=Q9H6Z4-3; Sequence=VSP_011163;
CC -!- TISSUE SPECIFICITY: Widely expressed with high levels in testis
CC and heart.
CC -!- SIMILARITY: Contains 1 RanBD1 domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04349.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing;
CC Sequence=CAB43293.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; Y08697; CAA69956.1; -; mRNA.
DR EMBL; Y08698; CAA69957.1; -; mRNA.
DR EMBL; AK025300; BAB15106.1; -; mRNA.
DR EMBL; AK314343; BAG36985.1; -; mRNA.
DR EMBL; AL050149; CAB43293.1; ALT_INIT; mRNA.
DR EMBL; AC004602; AAC14485.1; -; Genomic_DNA.
DR EMBL; AC104532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004349; AAH04349.1; ALT_SEQ; mRNA.
DR PIR; T08778; T08778.
DR RefSeq; NP_003615.2; NM_003624.2.
DR RefSeq; NP_015559.2; NM_007320.2.
DR RefSeq; NP_015561.1; NM_007322.2.
DR UniGene; Hs.531752; -.
DR PDB; 2CRF; NMR; -; A=380-511.
DR PDB; 2Y8F; X-ray; 2.10 A; A/B/C/D=388-522.
DR PDB; 2Y8G; X-ray; 1.61 A; A/B=388-522.
DR PDBsum; 2CRF; -.
DR PDBsum; 2Y8F; -.
DR PDBsum; 2Y8G; -.
DR ProteinModelPortal; Q9H6Z4; -.
DR SMR; Q9H6Z4; 390-516.
DR IntAct; Q9H6Z4; 7.
DR MINT; MINT-3068756; -.
DR STRING; 9606.ENSP00000341483; -.
DR PhosphoSite; Q9H6Z4; -.
DR DMDM; 51316528; -.
DR PaxDb; Q9H6Z4; -.
DR PeptideAtlas; Q9H6Z4; -.
DR PRIDE; Q9H6Z4; -.
DR Ensembl; ENST00000034275; ENSP00000034275; ENSG00000031823.
DR Ensembl; ENST00000340578; ENSP00000341483; ENSG00000031823.
DR Ensembl; ENST00000439268; ENSP00000404837; ENSG00000031823.
DR GeneID; 8498; -.
DR KEGG; hsa:8498; -.
DR UCSC; uc002mdv.3; human.
DR CTD; 8498; -.
DR GeneCards; GC19M005916; -.
DR HGNC; HGNC:9850; RANBP3.
DR HPA; HPA043375; -.
DR HPA; HPA043389; -.
DR MIM; 603327; gene.
DR neXtProt; NX_Q9H6Z4; -.
DR PharmGKB; PA34211; -.
DR eggNOG; NOG304969; -.
DR HOVERGEN; HBG061383; -.
DR InParanoid; Q9H6Z4; -.
DR KO; K15304; -.
DR OMA; TSFASPN; -.
DR OrthoDB; EOG7TJ3JQ; -.
DR PhylomeDB; Q9H6Z4; -.
DR SignaLink; Q9H6Z4; -.
DR ChiTaRS; RANBP3; human.
DR EvolutionaryTrace; Q9H6Z4; -.
DR GeneWiki; RANBP3; -.
DR GenomeRNAi; 8498; -.
DR NextBio; 31793; -.
DR PRO; PR:Q9H6Z4; -.
DR ArrayExpress; Q9H6Z4; -.
DR Bgee; Q9H6Z4; -.
DR CleanEx; HS_RANBP3; -.
DR Genevestigator; Q9H6Z4; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0008536; F:Ran GTPase binding; TAS:ProtInc.
DR GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH_like_dom.
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 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Nucleus; Phosphoprotein; Polymorphism; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 567 Ran-binding protein 3.
FT /FTId=PRO_0000097165.
FT DOMAIN 378 518 RanBD1.
FT COMPBIAS 76 81 Poly-Pro.
FT COMPBIAS 537 543 Poly-Asp.
FT MOD_RES 21 21 N6-acetyllysine.
FT MOD_RES 100 100 Phosphoserine.
FT MOD_RES 101 101 Phosphoserine.
FT MOD_RES 108 108 Phosphoserine.
FT MOD_RES 124 124 Phosphothreonine.
FT MOD_RES 219 219 Phosphoserine (By similarity).
FT MOD_RES 333 333 Phosphoserine.
FT MOD_RES 353 353 Phosphoserine.
FT MOD_RES 355 355 Phosphoserine.
FT MOD_RES 539 539 Phosphoserine.
FT VAR_SEQ 27 94 Missing (in isoform 3).
FT /FTId=VSP_011163.
FT VAR_SEQ 226 230 Missing (in isoform 2).
FT /FTId=VSP_011162.
FT VARIANT 314 314 A -> V (in dbSNP:rs10417885).
FT /FTId=VAR_051303.
FT CONFLICT 358 359 SS -> PF (in Ref. 1; CAA69956).
FT CONFLICT 367 367 E -> G (in Ref. 1; CAA69957).
FT TURN 389 391
FT STRAND 399 412
FT TURN 413 416
FT STRAND 417 432
FT TURN 434 436
FT STRAND 439 447
FT TURN 448 450
FT STRAND 453 458
FT STRAND 465 469
FT STRAND 472 476
FT STRAND 487 491
FT HELIX 494 519
SQ SEQUENCE 567 AA; 60210 MW; 203B5A900512743C CRC64;
MADLANEEKP AIAPPVFVFQ KDKGQKSPAE QKNLSDSGEE PRGEAEAPHH GTGHPESAGE
HALEPPAPAG ASASTPPPPA PEAQLPPFPR ELAGRSAGGS SPEGGEDSDR EDGNYCPPVK
RERTSSLTQF PPSQSEERSS GFRLKPPTLI HGQAPSAGLP SQKPKEQQRS VLRPAVLQAP
QPKALSQTVP SSGTNGVSLP ADCTGAVPAA SPDTAAWRSP SEAADEVCAL EEKEPQKNES
SNASEEEACE KKDPATQQAF VFGQNLRDRV KLINESVDEA DMENAGHPSA DTPTATNYFL
QYISSSLENS TNSADASSNK FVFGQNMSER VLSPPKLNEV SSDANRENAA AESGSESSSQ
EATPEKESLA ESAAAYTKAT ARKCLLEKVE VITGEEAESN VLQMQCKLFV FDKTSQSWVE
RGRGLLRLND MASTDDGTLQ SRLVMRTQGS LRLILNTKLW AQMQIDKASE KSIRITAMDT
EDQGVKVFLI SASSKDTGQL YAALHHRILA LRSRVEQEQE AKMPAPEPGA APSNEEDDSD
DDDVLAPSGA TAAGAGDEGD GQTTGST
//
ID RANB3_HUMAN Reviewed; 567 AA.
AC Q9H6Z4; B2RAT8; O60405; O75759; O75760; Q9BT47; Q9UG74;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Ran-binding protein 3;
DE Short=RanBP3;
GN Name=RANBP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH CHC1.
RX PubMed=9637251; DOI=10.1016/S0014-5793(98)00459-1;
RA Mueller L., Cordes V.C., Bischoff F.R., Ponstingl H.;
RT "Human RanBP3, a group of nuclear RanGTP binding proteins.";
RL FEBS Lett. 427:330-336(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Colon, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-418 (ISOFORM 3).
RC TISSUE=Eye;
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 FUNCTION, AND INTERACTION WITH XPO1.
RX PubMed=11571268; DOI=10.1093/embo-reports/kve200;
RA Englmeier L., Fornerod M., Bischoff F.R., Petosa C., Mattaj I.W.,
RA Kutay U.;
RT "RanBP3 influences interactions between CRM1 and its nuclear protein
RT export substrates.";
RL EMBO Rep. 2:926-932(2001).
RN [7]
RP FUNCTION, AND INTERACTION WITH XPO1.
RX PubMed=11425870; DOI=10.1083/jcb.153.7.1391;
RA Lindsay M.E., Holaska J.M., Welch K., Paschal B.M., Macara I.G.;
RT "Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein
RT export.";
RL J. Cell Biol. 153:1391-1402(2001).
RN [8]
RP FUNCTION, AND INTERACTION WITH CHC1.
RX PubMed=11932251; DOI=10.1074/jbc.C100620200;
RA Nemergut M.E., Lindsay M.E., Brownawell A.M., Macara I.G.;
RT "Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide
RT exchange factor.";
RL J. Biol. Chem. 277:17385-17388(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-101; SER-108;
RP THR-124; SER-333; SER-353; SER-355 AND SER-539, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP INTERACTION WITH SMAD2 AND SMAD3, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19289081; DOI=10.1016/j.devcel.2009.01.022;
RA Dai F., Lin X., Chang C., Feng X.H.;
RT "Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination
RT of TGF-beta signaling.";
RL Dev. Cell 16:345-357(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP STRUCTURE BY NMR OF 380-516.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RAN_BP1 domain of RAN-binding protein-3.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Acts as a cofactor for XPO1/CRM1-mediated nuclear
CC export, perhaps as export complex scaffolding protein. Bound to
CC XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the
CC absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the
CC nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine
CC nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to
CC CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF-
CC beta signaling through interaction with the R-SMAD proteins, SMAD2
CC and SMAD3, and mediating their nuclear export.
CC -!- SUBUNIT: Interacts with CHC1 in a Ran-stimulated manner. Interacts
CC with XPO1. Interacts (via its C-terminal R domain) with SMAD2
CC (dephosphorylated form via its MH1 and MH2 domains); the
CC interaction results in the nuclear export of SMAD2 and termination
CC of the TGF-beta signaling. Interacts (via its C-terminal R domain)
CC with SMAD3 (dephosphorylated form via its MH1 domain); the
CC interaction results in the nuclear export of SMAD3 and termination
CC of the TGF-beta signaling.
CC -!- INTERACTION:
CC P35813:PPM1A; NbExp=4; IntAct=EBI-992681, EBI-989143;
CC P18754:RCC1; NbExp=2; IntAct=EBI-992681, EBI-992720;
CC Q15796:SMAD2; NbExp=2; IntAct=EBI-992681, EBI-1040141;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H6Z4-1; Sequence=Displayed;
CC Name=2; Synonyms=Ranbp3-a;
CC IsoId=Q9H6Z4-2; Sequence=VSP_011162;
CC Name=3; Synonyms=Ranbp3-b;
CC IsoId=Q9H6Z4-3; Sequence=VSP_011163;
CC -!- TISSUE SPECIFICITY: Widely expressed with high levels in testis
CC and heart.
CC -!- SIMILARITY: Contains 1 RanBD1 domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04349.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing;
CC Sequence=CAB43293.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; Y08697; CAA69956.1; -; mRNA.
DR EMBL; Y08698; CAA69957.1; -; mRNA.
DR EMBL; AK025300; BAB15106.1; -; mRNA.
DR EMBL; AK314343; BAG36985.1; -; mRNA.
DR EMBL; AL050149; CAB43293.1; ALT_INIT; mRNA.
DR EMBL; AC004602; AAC14485.1; -; Genomic_DNA.
DR EMBL; AC104532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004349; AAH04349.1; ALT_SEQ; mRNA.
DR PIR; T08778; T08778.
DR RefSeq; NP_003615.2; NM_003624.2.
DR RefSeq; NP_015559.2; NM_007320.2.
DR RefSeq; NP_015561.1; NM_007322.2.
DR UniGene; Hs.531752; -.
DR PDB; 2CRF; NMR; -; A=380-511.
DR PDB; 2Y8F; X-ray; 2.10 A; A/B/C/D=388-522.
DR PDB; 2Y8G; X-ray; 1.61 A; A/B=388-522.
DR PDBsum; 2CRF; -.
DR PDBsum; 2Y8F; -.
DR PDBsum; 2Y8G; -.
DR ProteinModelPortal; Q9H6Z4; -.
DR SMR; Q9H6Z4; 390-516.
DR IntAct; Q9H6Z4; 7.
DR MINT; MINT-3068756; -.
DR STRING; 9606.ENSP00000341483; -.
DR PhosphoSite; Q9H6Z4; -.
DR DMDM; 51316528; -.
DR PaxDb; Q9H6Z4; -.
DR PeptideAtlas; Q9H6Z4; -.
DR PRIDE; Q9H6Z4; -.
DR Ensembl; ENST00000034275; ENSP00000034275; ENSG00000031823.
DR Ensembl; ENST00000340578; ENSP00000341483; ENSG00000031823.
DR Ensembl; ENST00000439268; ENSP00000404837; ENSG00000031823.
DR GeneID; 8498; -.
DR KEGG; hsa:8498; -.
DR UCSC; uc002mdv.3; human.
DR CTD; 8498; -.
DR GeneCards; GC19M005916; -.
DR HGNC; HGNC:9850; RANBP3.
DR HPA; HPA043375; -.
DR HPA; HPA043389; -.
DR MIM; 603327; gene.
DR neXtProt; NX_Q9H6Z4; -.
DR PharmGKB; PA34211; -.
DR eggNOG; NOG304969; -.
DR HOVERGEN; HBG061383; -.
DR InParanoid; Q9H6Z4; -.
DR KO; K15304; -.
DR OMA; TSFASPN; -.
DR OrthoDB; EOG7TJ3JQ; -.
DR PhylomeDB; Q9H6Z4; -.
DR SignaLink; Q9H6Z4; -.
DR ChiTaRS; RANBP3; human.
DR EvolutionaryTrace; Q9H6Z4; -.
DR GeneWiki; RANBP3; -.
DR GenomeRNAi; 8498; -.
DR NextBio; 31793; -.
DR PRO; PR:Q9H6Z4; -.
DR ArrayExpress; Q9H6Z4; -.
DR Bgee; Q9H6Z4; -.
DR CleanEx; HS_RANBP3; -.
DR Genevestigator; Q9H6Z4; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0008536; F:Ran GTPase binding; TAS:ProtInc.
DR GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH_like_dom.
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 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Nucleus; Phosphoprotein; Polymorphism; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 567 Ran-binding protein 3.
FT /FTId=PRO_0000097165.
FT DOMAIN 378 518 RanBD1.
FT COMPBIAS 76 81 Poly-Pro.
FT COMPBIAS 537 543 Poly-Asp.
FT MOD_RES 21 21 N6-acetyllysine.
FT MOD_RES 100 100 Phosphoserine.
FT MOD_RES 101 101 Phosphoserine.
FT MOD_RES 108 108 Phosphoserine.
FT MOD_RES 124 124 Phosphothreonine.
FT MOD_RES 219 219 Phosphoserine (By similarity).
FT MOD_RES 333 333 Phosphoserine.
FT MOD_RES 353 353 Phosphoserine.
FT MOD_RES 355 355 Phosphoserine.
FT MOD_RES 539 539 Phosphoserine.
FT VAR_SEQ 27 94 Missing (in isoform 3).
FT /FTId=VSP_011163.
FT VAR_SEQ 226 230 Missing (in isoform 2).
FT /FTId=VSP_011162.
FT VARIANT 314 314 A -> V (in dbSNP:rs10417885).
FT /FTId=VAR_051303.
FT CONFLICT 358 359 SS -> PF (in Ref. 1; CAA69956).
FT CONFLICT 367 367 E -> G (in Ref. 1; CAA69957).
FT TURN 389 391
FT STRAND 399 412
FT TURN 413 416
FT STRAND 417 432
FT TURN 434 436
FT STRAND 439 447
FT TURN 448 450
FT STRAND 453 458
FT STRAND 465 469
FT STRAND 472 476
FT STRAND 487 491
FT HELIX 494 519
SQ SEQUENCE 567 AA; 60210 MW; 203B5A900512743C CRC64;
MADLANEEKP AIAPPVFVFQ KDKGQKSPAE QKNLSDSGEE PRGEAEAPHH GTGHPESAGE
HALEPPAPAG ASASTPPPPA PEAQLPPFPR ELAGRSAGGS SPEGGEDSDR EDGNYCPPVK
RERTSSLTQF PPSQSEERSS GFRLKPPTLI HGQAPSAGLP SQKPKEQQRS VLRPAVLQAP
QPKALSQTVP SSGTNGVSLP ADCTGAVPAA SPDTAAWRSP SEAADEVCAL EEKEPQKNES
SNASEEEACE KKDPATQQAF VFGQNLRDRV KLINESVDEA DMENAGHPSA DTPTATNYFL
QYISSSLENS TNSADASSNK FVFGQNMSER VLSPPKLNEV SSDANRENAA AESGSESSSQ
EATPEKESLA ESAAAYTKAT ARKCLLEKVE VITGEEAESN VLQMQCKLFV FDKTSQSWVE
RGRGLLRLND MASTDDGTLQ SRLVMRTQGS LRLILNTKLW AQMQIDKASE KSIRITAMDT
EDQGVKVFLI SASSKDTGQL YAALHHRILA LRSRVEQEQE AKMPAPEPGA APSNEEDDSD
DDDVLAPSGA TAAGAGDEGD GQTTGST
//
MIM
603327
*RECORD*
*FIELD* NO
603327
*FIELD* TI
*603327 RAN-BINDING PROTEIN 3; RANBP3
*FIELD* TX
CLONING
The RAN GTPase (601179) plays an essential role in the transport of
read moremacromolecules between the cytoplasm and the nucleus. The
nucleotide-bound state of RAN is regulated by RANGAP1 (602362), a
RAN-specific GTPase activating protein, and by RCC1 (CHC1; 179710), a
specific guanine nucleotide exchange factor. Using a yeast 2-hybrid
screen with RCC1 as bait, Mueller et al. (1998) isolated a partial human
lymphocyte cDNA encoding a protein that they designated RANBP3
(RAN-binding protein-3). They used the partial cDNA to screen HeLa cell
libraries and recovered additional cDNAs representing alternatively
spliced transcripts encoding 562-amino acid RANBP3-a and 499-amino acid
RANBP3-b isoforms. The RANBP3 proteins contain FXFG motifs
characteristic of a subgroup of nucleoporins, and a C-terminal domain
showing similarity to RANBP1 (601180). RANBP3-a has a calculated
molecular mass of 60 kD and pI of 4.5. However, the protein has an
apparent molecular mass of 100 kD by SDS-PAGE. Immunofluorescence
studies showed that RANBP3 is localized diffusely in the nucleus of
interphase mammalian cells but is excluded from nucleoli. Northern blot
analysis revealed that RANBP3 is expressed ubiquitously as 1.8- and 3-kb
mRNAs.
GENE FUNCTION
Mueller et al. (1998) found that, in vitro, RANBP3 formed a trimeric
RCC1-RAN-RANBP3 complex, although it did not bind RCC1 directly.
MAPPING
By inclusion within a mapped clone (GenBank GENBANK AC004602), the Joint
Genome Institute mapped the RANBP3 gene to 19p13.3 (Rasooly, 1998).
*FIELD* RF
1. Mueller, L.; Cordes, V. C.; Bischoff, F. R.; Ponstingl, H.: Human
RanBP3, a group of nuclear RanGTP binding proteins. FEBS Lett. 427:
330-336, 1998.
2. Rasooly, R. S.: Personal Communication. Baltimore, Md. 11/30/1998.
*FIELD* CD
Rebekah S. Rasooly: 12/2/1998
*FIELD* ED
carol: 06/22/2012
alopez: 4/30/1999
alopez: 12/7/1998
alopez: 12/4/1998
alopez: 12/2/1998
*RECORD*
*FIELD* NO
603327
*FIELD* TI
*603327 RAN-BINDING PROTEIN 3; RANBP3
*FIELD* TX
CLONING
The RAN GTPase (601179) plays an essential role in the transport of
read moremacromolecules between the cytoplasm and the nucleus. The
nucleotide-bound state of RAN is regulated by RANGAP1 (602362), a
RAN-specific GTPase activating protein, and by RCC1 (CHC1; 179710), a
specific guanine nucleotide exchange factor. Using a yeast 2-hybrid
screen with RCC1 as bait, Mueller et al. (1998) isolated a partial human
lymphocyte cDNA encoding a protein that they designated RANBP3
(RAN-binding protein-3). They used the partial cDNA to screen HeLa cell
libraries and recovered additional cDNAs representing alternatively
spliced transcripts encoding 562-amino acid RANBP3-a and 499-amino acid
RANBP3-b isoforms. The RANBP3 proteins contain FXFG motifs
characteristic of a subgroup of nucleoporins, and a C-terminal domain
showing similarity to RANBP1 (601180). RANBP3-a has a calculated
molecular mass of 60 kD and pI of 4.5. However, the protein has an
apparent molecular mass of 100 kD by SDS-PAGE. Immunofluorescence
studies showed that RANBP3 is localized diffusely in the nucleus of
interphase mammalian cells but is excluded from nucleoli. Northern blot
analysis revealed that RANBP3 is expressed ubiquitously as 1.8- and 3-kb
mRNAs.
GENE FUNCTION
Mueller et al. (1998) found that, in vitro, RANBP3 formed a trimeric
RCC1-RAN-RANBP3 complex, although it did not bind RCC1 directly.
MAPPING
By inclusion within a mapped clone (GenBank GENBANK AC004602), the Joint
Genome Institute mapped the RANBP3 gene to 19p13.3 (Rasooly, 1998).
*FIELD* RF
1. Mueller, L.; Cordes, V. C.; Bischoff, F. R.; Ponstingl, H.: Human
RanBP3, a group of nuclear RanGTP binding proteins. FEBS Lett. 427:
330-336, 1998.
2. Rasooly, R. S.: Personal Communication. Baltimore, Md. 11/30/1998.
*FIELD* CD
Rebekah S. Rasooly: 12/2/1998
*FIELD* ED
carol: 06/22/2012
alopez: 4/30/1999
alopez: 12/7/1998
alopez: 12/4/1998
alopez: 12/2/1998