RANB3_HUMAN
ID RANB3_HUMAN Reviewed; 567 AA.
AC Q9H6Z4; B2RAT8; O60405; O75759; O75760; Q9BT47; Q9UG74;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Ran-binding protein 3;
DE Short=RanBP3;
GN Name=RANBP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., 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 project:
RT 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., Kutay U.;
RT "RanBP3 influences interactions between CRM1 and its nuclear protein export
RT 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 exchange
RT factor.";
RL J. Biol. Chem. 277:17385-17388(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT 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, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA 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 IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT 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 of
RT TGF-beta signaling.";
RL Dev. Cell 16:345-357(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-126; SER-333;
RP SER-353; SER-355 AND SER-372, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75; SER-101; SER-108 AND
RP SER-333, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
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 export,
CC perhaps as export complex scaffolding protein. Bound to XPO1/CRM1,
CC stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound
CC GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to
CC CHC1/RCC1 and increases the guanine nucleotide exchange activity of
CC CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner.
CC Negative regulator of TGF-beta signaling through interaction with the
CC R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export.
CC {ECO:0000269|PubMed:11425870, ECO:0000269|PubMed:11571268,
CC ECO:0000269|PubMed:11932251, ECO:0000269|PubMed:19289081,
CC ECO:0000269|PubMed:9637251}.
CC -!- SUBUNIT: Interacts with CHC1 in a Ran-stimulated manner. Interacts with
CC XPO1. Interacts (via its C-terminal R domain) with SMAD2
CC (dephosphorylated form via its MH1 and MH2 domains); the interaction
CC results in the nuclear export of SMAD2 and termination of the TGF-beta
CC signaling. Interacts (via its C-terminal R domain) with SMAD3
CC (dephosphorylated form via its MH1 domain); the interaction results in
CC the nuclear export of SMAD3 and termination of the TGF-beta signaling.
CC {ECO:0000269|PubMed:11425870, ECO:0000269|PubMed:11571268,
CC ECO:0000269|PubMed:11932251, ECO:0000269|PubMed:19289081,
CC ECO:0000269|PubMed:9637251}.
CC -!- INTERACTION:
CC Q9H6Z4; P35813: PPM1A; NbExp=4; IntAct=EBI-992681, EBI-989143;
CC Q9H6Z4; P18754: RCC1; NbExp=2; IntAct=EBI-992681, EBI-992720;
CC Q9H6Z4; Q15796: SMAD2; NbExp=2; IntAct=EBI-992681, EBI-1040141;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19289081}. Nucleus
CC {ECO:0000269|PubMed:19289081}.
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 and
CC heart. {ECO:0000269|PubMed:9637251}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04349.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=CAB43293.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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 CCDS; CCDS42477.1; -. [Q9H6Z4-3]
DR CCDS; CCDS42478.1; -. [Q9H6Z4-1]
DR CCDS; CCDS45935.1; -. [Q9H6Z4-2]
DR PIR; T08778; T08778.
DR RefSeq; NP_001287794.1; NM_001300865.1.
DR RefSeq; NP_003615.2; NM_003624.2. [Q9H6Z4-2]
DR RefSeq; NP_015559.2; NM_007320.2. [Q9H6Z4-3]
DR RefSeq; NP_015561.1; NM_007322.2. [Q9H6Z4-1]
DR PDB; 2CRF; NMR; -; A=380-516.
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 PDB; 5XZX; X-ray; 3.00 A; B=99-128.
DR PDBsum; 2CRF; -.
DR PDBsum; 2Y8F; -.
DR PDBsum; 2Y8G; -.
DR PDBsum; 5XZX; -.
DR AlphaFoldDB; Q9H6Z4; -.
DR SMR; Q9H6Z4; -.
DR BioGRID; 114070; 79.
DR IntAct; Q9H6Z4; 14.
DR MINT; Q9H6Z4; -.
DR STRING; 9606.ENSP00000341483; -.
DR GlyGen; Q9H6Z4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H6Z4; -.
DR MetOSite; Q9H6Z4; -.
DR PhosphoSitePlus; Q9H6Z4; -.
DR BioMuta; RANBP3; -.
DR DMDM; 51316528; -.
DR EPD; Q9H6Z4; -.
DR jPOST; Q9H6Z4; -.
DR MassIVE; Q9H6Z4; -.
DR MaxQB; Q9H6Z4; -.
DR PaxDb; Q9H6Z4; -.
DR PeptideAtlas; Q9H6Z4; -.
DR PRIDE; Q9H6Z4; -.
DR ProteomicsDB; 81064; -. [Q9H6Z4-1]
DR ProteomicsDB; 81065; -. [Q9H6Z4-2]
DR ProteomicsDB; 81066; -. [Q9H6Z4-3]
DR Antibodypedia; 24035; 268 antibodies from 29 providers.
DR DNASU; 8498; -.
DR Ensembl; ENST00000034275.12; ENSP00000034275.7; ENSG00000031823.14. [Q9H6Z4-3]
DR Ensembl; ENST00000340578.10; ENSP00000341483.5; ENSG00000031823.14. [Q9H6Z4-1]
DR Ensembl; ENST00000439268.6; ENSP00000404837.1; ENSG00000031823.14. [Q9H6Z4-2]
DR GeneID; 8498; -.
DR KEGG; hsa:8498; -.
DR MANE-Select; ENST00000340578.10; ENSP00000341483.5; NM_007322.3; NP_015561.1.
DR UCSC; uc002mdw.4; human. [Q9H6Z4-1]
DR CTD; 8498; -.
DR DisGeNET; 8498; -.
DR GeneCards; RANBP3; -.
DR HGNC; HGNC:9850; RANBP3.
DR HPA; ENSG00000031823; Low tissue specificity.
DR MIM; 603327; gene.
DR neXtProt; NX_Q9H6Z4; -.
DR OpenTargets; ENSG00000031823; -.
DR PharmGKB; PA34211; -.
DR VEuPathDB; HostDB:ENSG00000031823; -.
DR eggNOG; KOG0866; Eukaryota.
DR GeneTree; ENSGT00940000158588; -.
DR InParanoid; Q9H6Z4; -.
DR OMA; HGMGHPE; -.
DR OrthoDB; 918488at2759; -.
DR PhylomeDB; Q9H6Z4; -.
DR TreeFam; TF313181; -.
DR PathwayCommons; Q9H6Z4; -.
DR SignaLink; Q9H6Z4; -.
DR SIGNOR; Q9H6Z4; -.
DR BioGRID-ORCS; 8498; 138 hits in 1089 CRISPR screens.
DR ChiTaRS; RANBP3; human.
DR EvolutionaryTrace; Q9H6Z4; -.
DR GeneWiki; RANBP3; -.
DR GenomeRNAi; 8498; -.
DR Pharos; Q9H6Z4; Tbio.
DR PRO; PR:Q9H6Z4; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9H6Z4; protein.
DR Bgee; ENSG00000031823; Expressed in sural nerve and 188 other tissues.
DR ExpressionAtlas; Q9H6Z4; baseline and differential.
DR Genevisible; Q9H6Z4; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0070412; F:R-SMAD binding; IPI:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:GO_Central.
DR GO; GO:0006611; P:protein export from nucleus; IBA:GO_Central.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR PANTHER; PTHR23138; PTHR23138; 1.
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; Cytoplasm; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..567
FT /note="Ran-binding protein 3"
FT /id="PRO_0000097165"
FT DOMAIN 378..518
FT /note="RanBD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REGION 1..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CT10"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CT10"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 27..94
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9637251"
FT /id="VSP_011163"
FT VAR_SEQ 226..230
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9637251"
FT /id="VSP_011162"
FT VARIANT 314
FT /note="A -> V (in dbSNP:rs10417885)"
FT /id="VAR_051303"
FT CONFLICT 358..359
FT /note="SS -> PF (in Ref. 1; CAA69956)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="E -> G (in Ref. 1; CAA69957)"
FT /evidence="ECO:0000305"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:2CRF"
FT STRAND 399..412
FT /evidence="ECO:0007829|PDB:2Y8G"
FT TURN 413..416
FT /evidence="ECO:0007829|PDB:2Y8G"
FT STRAND 417..432
FT /evidence="ECO:0007829|PDB:2Y8G"
FT TURN 434..436
FT /evidence="ECO:0007829|PDB:2Y8G"
FT STRAND 439..447
FT /evidence="ECO:0007829|PDB:2Y8G"
FT TURN 448..450
FT /evidence="ECO:0007829|PDB:2Y8G"
FT STRAND 453..458
FT /evidence="ECO:0007829|PDB:2Y8G"
FT STRAND 465..469
FT /evidence="ECO:0007829|PDB:2Y8G"
FT STRAND 472..476
FT /evidence="ECO:0007829|PDB:2Y8G"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:2Y8G"
FT HELIX 494..519
FT /evidence="ECO:0007829|PDB:2Y8G"
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
