RNB3L_HUMAN
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 03-AUG-2022, entry version 146.
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;
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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 PeptideAtlas; Q86VV4; -.
DR PRIDE; Q86VV4; -.
DR ProteomicsDB; 20364; -.
DR ProteomicsDB; 70072; -. [Q86VV4-1]
DR ProteomicsDB; 70073; -. [Q86VV4-2]
DR Antibodypedia; 43549; 101 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 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; NSTEQGP; -.
DR OrthoDB; 918488at2759; -.
DR PhylomeDB; Q86VV4; -.
DR TreeFam; TF313181; -.
DR PathwayCommons; Q86VV4; -.
DR SignaLink; Q86VV4; -.
DR BioGRID-ORCS; 202151; 7 hits in 1064 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 95 other tissues.
DR ExpressionAtlas; Q86VV4; baseline and differential.
DR Genevisible; Q86VV4; HS.
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 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; 2.
DR Pfam; PF00638; Ran_BP1; 1.
DR SMART; SM00160; RanBD; 1.
DR PROSITE; PS50196; RANBD1; 1.
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
