ID RNB3L_HUMAN Reviewed; 465 AA. AC Q86VV4; B7Z866; E9PGP9; Q96LK2; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 2. DT 24-JAN-2024, entry version 153. DE RecName: Full=Ran-binding protein 3-like; GN Name=RANBP3L; 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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT RP ARG-70. RC TISSUE=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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-70. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-70. RC TISSUE=Brain; 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 [5] RP INTERACTION WITH SMAD1; SMAD5 AND SMAD8, AND SUBCELLULAR LOCATION. RX PubMed=25755279; DOI=10.1128/mcb.00121-15; RA Chen F., Lin X., Xu P., Zhang Z., Chen Y., Wang C., Han J., Zhao B., RA Xiao M., Feng X.H.; RT "Nuclear export of Smads by RanBP3L regulates bone morphogenetic protein RT signaling and mesenchymal stem cell differentiation."; RL Mol. Cell. Biol. 35:1700-1711(2015). CC -!- FUNCTION: Nuclear export factor for BMP-specific SMAD1/5/8 that plays a CC critical role in terminating BMP signaling and regulating mesenchymal CC stem cell differentiation by blocking osteoblast differentiation to CC promote myogenic differention. Directly recognizes dephosphorylated CC SMAD1/5/8 and mediates their nuclear export in a Ran-dependent manner. CC {ECO:0000250|UniProtKB:Q6PDH4, ECO:0000269|PubMed:25755279}. CC -!- SUBUNIT: Interacts with SMAD1, SMAD5 and SMAD8; the interaction (with CC SMAD at least) increases when SMAD1 is not phosphorylated and mediates CC SMAD1 nuclear export. {ECO:0000250|UniProtKB:Q6PDH4, CC ECO:0000269|PubMed:25755279}. CC -!- INTERACTION: CC Q86VV4; Q08379: GOLGA2; NbExp=3; IntAct=EBI-12028066, EBI-618309; CC Q86VV4; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-12028066, EBI-5916454; CC Q86VV4; Q5T7B8-2: KIF24; NbExp=3; IntAct=EBI-12028066, EBI-10213781; CC Q86VV4; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-12028066, EBI-10172526; CC Q86VV4; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-12028066, EBI-11522433; CC Q86VV4; Q15654: TRIP6; NbExp=3; IntAct=EBI-12028066, EBI-742327; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:25755279}. Cytoplasm CC {ECO:0000305|PubMed:25755279}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q86VV4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q86VV4-2; Sequence=VSP_029893, VSP_029894; CC Name=3; CC IsoId=Q86VV4-3; Sequence=VSP_044463; 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; AK058151; BAB71689.1; -; mRNA. DR EMBL; AK302947; BAH13852.1; -; mRNA. DR EMBL; AC008807; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC114277; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471119; EAW55942.1; -; Genomic_DNA. DR EMBL; CH471119; EAW55943.1; -; Genomic_DNA. DR EMBL; BC047660; AAH47660.1; -; mRNA. DR CCDS; CCDS3918.1; -. [Q86VV4-1] DR CCDS; CCDS54843.1; -. [Q86VV4-3] DR RefSeq; NP_001154901.1; NM_001161429.2. [Q86VV4-3] DR RefSeq; NP_001310202.1; NM_001323273.1. DR RefSeq; NP_001310203.1; NM_001323274.1. DR RefSeq; NP_001310204.1; NM_001323275.1. DR RefSeq; NP_001310205.1; NM_001323276.1. DR RefSeq; NP_001310206.1; NM_001323277.1. DR RefSeq; NP_001310207.1; NM_001323278.1. DR RefSeq; NP_001310208.1; NM_001323279.1. DR RefSeq; NP_001310209.1; NM_001323280.1. DR RefSeq; NP_659437.3; NM_145000.4. [Q86VV4-1] DR AlphaFoldDB; Q86VV4; -. DR SMR; Q86VV4; -. DR BioGRID; 128419; 11. DR IntAct; Q86VV4; 8. DR STRING; 9606.ENSP00000421853; -. DR iPTMnet; Q86VV4; -. DR PhosphoSitePlus; Q86VV4; -. DR BioMuta; RANBP3L; -. DR DMDM; 317373276; -. DR MassIVE; Q86VV4; -. DR PaxDb; 9606-ENSP00000421853; -. DR PeptideAtlas; Q86VV4; -. DR ProteomicsDB; 20364; -. DR ProteomicsDB; 70072; -. [Q86VV4-1] DR ProteomicsDB; 70073; -. [Q86VV4-2] DR Antibodypedia; 43549; 122 antibodies from 19 providers. DR DNASU; 202151; -. DR Ensembl; ENST00000296604.8; ENSP00000296604.3; ENSG00000164188.9. [Q86VV4-1] DR Ensembl; ENST00000502994.5; ENSP00000421853.1; ENSG00000164188.9. [Q86VV4-3] DR Ensembl; ENST00000515759.5; ENSP00000421149.1; ENSG00000164188.9. [Q86VV4-2] DR GeneID; 202151; -. DR KEGG; hsa:202151; -. DR MANE-Select; ENST00000296604.8; ENSP00000296604.3; NM_145000.5; NP_659437.3. DR UCSC; uc003jkh.4; human. [Q86VV4-1] DR AGR; HGNC:26353; -. DR CTD; 202151; -. DR DisGeNET; 202151; -. DR GeneCards; RANBP3L; -. DR HGNC; HGNC:26353; RANBP3L. DR HPA; ENSG00000164188; Tissue enhanced (brain, kidney). DR MIM; 616391; gene. DR neXtProt; NX_Q86VV4; -. DR OpenTargets; ENSG00000164188; -. DR PharmGKB; PA162400660; -. DR VEuPathDB; HostDB:ENSG00000164188; -. DR eggNOG; KOG0866; Eukaryota. DR GeneTree; ENSGT00940000161387; -. DR HOGENOM; CLU_046714_0_0_1; -. DR InParanoid; Q86VV4; -. DR OMA; HSRLIMR; -. DR OrthoDB; 2906517at2759; -. DR PhylomeDB; Q86VV4; -. DR TreeFam; TF313181; -. DR PathwayCommons; Q86VV4; -. DR SignaLink; Q86VV4; -. DR BioGRID-ORCS; 202151; 8 hits in 1141 CRISPR screens. DR GenomeRNAi; 202151; -. DR Pharos; Q86VV4; Tdark. DR PRO; PR:Q86VV4; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q86VV4; Protein. DR Bgee; ENSG00000164188; Expressed in metanephros cortex and 96 other cell types or tissues. DR ExpressionAtlas; Q86VV4; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central. DR GO; GO:0046332; F:SMAD binding; IPI:UniProtKB. DR GO; GO:1901706; P:mesenchymal cell differentiation involved in bone development; ISS:UniProtKB. DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB. DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB. DR GO; GO:0006611; P:protein export from nucleus; IBA:GO_Central. DR CDD; cd13180; RanBD_RanBP3; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR000156; Ran_bind_dom. DR InterPro; IPR045255; RanBP1-like. DR PANTHER; PTHR23138; RAN BINDING PROTEIN; 1. DR PANTHER; PTHR23138:SF88; RAN-BINDING PROTEIN 3-LIKE; 1. DR Pfam; PF00638; Ran_BP1; 1. DR SMART; SM00160; RanBD; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50196; RANBD1; 1. DR Genevisible; Q86VV4; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Nucleus; Reference proteome. FT CHAIN 1..465 FT /note="Ran-binding protein 3-like" FT /id="PRO_0000312749" FT DOMAIN 276..417 FT /note="RanBD1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164" FT VAR_SEQ 89 FT /note="G -> GVSTLSQKQMRCSSVTNLPTFPHSGP (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044463" FT VAR_SEQ 302..321 FT /note="INCKLFIFNKTTQSWIERGR -> VCISCFTLSGSIYILGIKLT (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_029893" FT VAR_SEQ 322..465 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_029894" FT VARIANT 70 FT /note="T -> R (in dbSNP:rs1035480)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15372022, ECO:0000269|PubMed:15489334" FT /id="VAR_037557" FT VARIANT 111 FT /note="A -> D (in dbSNP:rs35433829)" FT /id="VAR_037558" FT VARIANT 271 FT /note="A -> V (in dbSNP:rs16902872)" FT /id="VAR_037559" FT CONFLICT 181 FT /note="Q -> R (in Ref. 1; BAH13852)" FT /evidence="ECO:0000305" SQ SEQUENCE 465 AA; 52211 MW; 3A47BE51C1D34A64 CRC64; MTTIPRKGSS HLPGSLHTCK LKLQEDRRQQ EKSVIAQPIF VFEKGEQTFK RPAEDTLYEA AEPECNGFPT KRVRSSSFTF HITDSQSQGV RKNNVFMTSA LVQSSVDIKS AEQGPVKHSK HVIRPAILQL PQARSCAKVR KTFGHKALES CKTKEKTNNK ISEGNSYLLS ENLSRARISV QLSTNQDFLG ATSVGCQPNE DKCSFKSCSS NFVFGENMVE RVLGTQKLTQ PQLENDSYAK EKPFKSIPKF PVNFLSSRTD SIKNTSLIES AAAFSSQPSR KCLLEKIDVI TGEETEHNVL KINCKLFIFN KTTQSWIERG RGTLRLNDTA STDCGTLQSR LIMRNQGSLR LILNSKLWAQ MKIQRANHKN VRITATDLED YSIKIFLIQA SAQDTAYLYA AIHHRLVALQ SFNKQRDVNQ AESLSETAQQ LNCESCDENE DDFIQVTKNG SDPSSWTHRQ SVACS //