RBP10_HUMAN
ID RBP10_HUMAN Reviewed; 620 AA.
AC Q6VN20; A4FTY2; B4DID0; B4DQH9; E7EW27; Q9P264;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Ran-binding protein 10;
DE Short=RanBP10;
GN Name=RANBP10; Synonyms=KIAA1464;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND INTERACTION
RP WITH RAN AND MET.
RX PubMed=14684163; DOI=10.1016/j.bbrc.2003.11.124;
RA Wang D., Li Z., Schoen S.R., Messing E.M., Wu G.;
RT "A novel MET-interacting protein shares high sequence similarity with
RT RanBPM, but fails to stimulate MET-induced Ras/Erk signaling.";
RL Biochem. Biophys. Res. Commun. 313:320-326(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Hippocampus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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, HOMODIMERIZATION, INTERACTION WITH AR AND RANBP9, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18222118; DOI=10.1016/j.bbrc.2008.01.072;
RA Harada N., Yokoyama T., Yamaji R., Nakano Y., Inui H.;
RT "RanBP10 acts as a novel coactivator for the androgen receptor.";
RL Biochem. Biophys. Res. Commun. 368:121-125(2008).
RN [7]
RP INTERACTION WITH TUBB1.
RX PubMed=18347012; DOI=10.1074/jbc.m709397200;
RA Schulze H., Dose M., Korpal M., Meyer I., Italiano J.E. Jr.,
RA Shivdasani R.A.;
RT "RanBP10 is a cytoplasmic guanine nucleotide exchange factor that modulates
RT noncentrosomal microtubules.";
RL J. Biol. Chem. 283:14109-14119(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365 AND SER-369, AND
RP IDENTIFICATION BY MASS 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 [9]
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=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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365 AND SER-369, AND
RP IDENTIFICATION BY 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 [11]
RP INTERACTION WITH YPEL5.
RX PubMed=20580816; DOI=10.1016/j.ygeno.2010.05.003;
RA Hosono K., Noda S., Shimizu A., Nakanishi N., Ohtsubo M., Shimizu N.,
RA Minoshima S.;
RT "YPEL5 protein of the YPEL gene family is involved in the cell cycle
RT progression by interacting with two distinct proteins RanBPM and RanBP10.";
RL Genomics 96:102-111(2010).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369, 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 [14]
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=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361; SER-365; SER-369 AND
RP SER-422, AND IDENTIFICATION BY MASS SPECTROMETRY [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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369, AND IDENTIFICATION BY
RP 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 [17]
RP FUNCTION, IDENTIFICATION IN THE CTLH COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=29911972; DOI=10.7554/elife.35528;
RA Lampert F., Stafa D., Goga A., Soste M.V., Gilberto S., Olieric N.,
RA Picotti P., Stoffel M., Peter M.;
RT "The multi-subunit GID/CTLH E3 ligase promotes proliferation and targets
RT the transcription factor Hbp1 for degradation.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: May act as an adapter protein to couple membrane receptors to
CC intracellular signaling pathways (Probable). Core component of the CTLH
CC E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin
CC from UBE2H and mediates ubiquitination and subsequent proteasomal
CC degradation of the transcription factor HBP1 (PubMed:29911972).
CC Enhances dihydrotestosterone-induced transactivation activity of AR, as
CC well as dexamethasone-induced transactivation activity of NR3C1, but
CC does not affect estrogen-induced transactivation (PubMed:18222118).
CC Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May
CC play an essential role in hemostasis and in maintaining microtubule
CC dynamics with respect to both platelet shape and function (By
CC similarity). {ECO:0000250|UniProtKB:Q6VN19,
CC ECO:0000269|PubMed:18222118, ECO:0000269|PubMed:29911972, ECO:0000305}.
CC -!- SUBUNIT: May form homodimers (PubMed:18222118). Identified in the CTLH
CC complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A
CC (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5
CC (PubMed:29911972). Within this complex, MAEA, RMND5A (or alternatively
CC its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the
CC catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles
CC (PubMed:29911972). Interacts with RAN and RANBP9 (PubMed:14684163,
CC PubMed:18222118). Interacts with the HGF receptor MET
CC (PubMed:14684163). Interacts with AR (PubMed:18222118). Interacts with
CC TUBB1 (PubMed:18347012). Interacts with YPEL5 (PubMed:20580816). May
CC interact with TUBB5 (By similarity). Interacts with DDX4 (By
CC similarity). {ECO:0000250|UniProtKB:Q6VN19,
CC ECO:0000269|PubMed:14684163, ECO:0000269|PubMed:18222118,
CC ECO:0000269|PubMed:18347012, ECO:0000269|PubMed:20580816,
CC ECO:0000269|PubMed:29911972}.
CC -!- INTERACTION:
CC Q6VN20; P78358: CTAG1B; NbExp=3; IntAct=EBI-310569, EBI-1188472;
CC Q6VN20; P24592: IGFBP6; NbExp=3; IntAct=EBI-310569, EBI-947015;
CC Q6VN20; P43364: MAGEA11; NbExp=3; IntAct=EBI-310569, EBI-739552;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18222118}.
CC Nucleus {ECO:0000269|PubMed:18222118}. Note=Predominantly cytoplasmic.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6VN20-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6VN20-2; Sequence=VSP_055839, VSP_055841;
CC Name=3;
CC IsoId=Q6VN20-3; Sequence=VSP_055840, VSP_055841;
CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in skeletal
CC muscle. {ECO:0000269|PubMed:14684163}.
CC -!- DOMAIN: The SPRY domain mediates the interaction with MET.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RANBP9/10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95988.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY337313; AAR01220.1; -; mRNA.
DR EMBL; AB040897; BAA95988.1; ALT_INIT; mRNA.
DR EMBL; AK295530; BAG58442.1; -; mRNA.
DR EMBL; AK298806; BAG60941.1; -; mRNA.
DR EMBL; AC010530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC040162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC099917; AAH99917.1; -; mRNA.
DR EMBL; BC121176; AAI21177.1; -; mRNA.
DR EMBL; BC121177; AAI21178.1; -; mRNA.
DR CCDS; CCDS32469.1; -. [Q6VN20-1]
DR CCDS; CCDS81999.1; -. [Q6VN20-3]
DR RefSeq; NP_001307167.1; NM_001320238.1. [Q6VN20-2]
DR RefSeq; NP_001307168.1; NM_001320239.1. [Q6VN20-3]
DR RefSeq; NP_001307169.1; NM_001320240.1.
DR RefSeq; NP_065901.1; NM_020850.2. [Q6VN20-1]
DR AlphaFoldDB; Q6VN20; -.
DR SMR; Q6VN20; -.
DR BioGRID; 121657; 174.
DR IntAct; Q6VN20; 47.
DR MINT; Q6VN20; -.
DR STRING; 9606.ENSP00000316589; -.
DR GlyGen; Q6VN20; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6VN20; -.
DR PhosphoSitePlus; Q6VN20; -.
DR SwissPalm; Q6VN20; -.
DR BioMuta; RANBP10; -.
DR DMDM; 74710336; -.
DR CPTAC; CPTAC-1265; -.
DR CPTAC; CPTAC-1266; -.
DR EPD; Q6VN20; -.
DR jPOST; Q6VN20; -.
DR MassIVE; Q6VN20; -.
DR MaxQB; Q6VN20; -.
DR PaxDb; Q6VN20; -.
DR PeptideAtlas; Q6VN20; -.
DR PRIDE; Q6VN20; -.
DR ProteomicsDB; 4296; -.
DR ProteomicsDB; 4875; -.
DR ProteomicsDB; 67730; -. [Q6VN20-1]
DR Antibodypedia; 44334; 86 antibodies from 24 providers.
DR DNASU; 57610; -.
DR Ensembl; ENST00000317506.8; ENSP00000316589.3; ENSG00000141084.12. [Q6VN20-1]
DR Ensembl; ENST00000448631.6; ENSP00000392808.2; ENSG00000141084.12. [Q6VN20-3]
DR GeneID; 57610; -.
DR KEGG; hsa:57610; -.
DR MANE-Select; ENST00000317506.8; ENSP00000316589.3; NM_020850.3; NP_065901.1.
DR UCSC; uc002eud.4; human. [Q6VN20-1]
DR CTD; 57610; -.
DR DisGeNET; 57610; -.
DR GeneCards; RANBP10; -.
DR HGNC; HGNC:29285; RANBP10.
DR HPA; ENSG00000141084; Low tissue specificity.
DR MIM; 614031; gene.
DR neXtProt; NX_Q6VN20; -.
DR OpenTargets; ENSG00000141084; -.
DR PharmGKB; PA134929520; -.
DR VEuPathDB; HostDB:ENSG00000141084; -.
DR eggNOG; KOG1477; Eukaryota.
DR GeneTree; ENSGT00940000158257; -.
DR HOGENOM; CLU_009129_4_0_1; -.
DR InParanoid; Q6VN20; -.
DR PhylomeDB; Q6VN20; -.
DR TreeFam; TF331658; -.
DR PathwayCommons; Q6VN20; -.
DR Reactome; R-HSA-8851805; MET activates RAS signaling.
DR SignaLink; Q6VN20; -.
DR BioGRID-ORCS; 57610; 16 hits in 1075 CRISPR screens.
DR ChiTaRS; RANBP10; human.
DR GenomeRNAi; 57610; -.
DR Pharos; Q6VN20; Tbio.
DR PRO; PR:Q6VN20; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6VN20; protein.
DR Bgee; ENSG00000141084; Expressed in right uterine tube and 181 other tissues.
DR ExpressionAtlas; Q6VN20; baseline and differential.
DR Genevisible; Q6VN20; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR CDD; cd12909; SPRY_RanBP9_10; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035782; SPRY_RanBP9/10.
DR Pfam; PF10607; CLTH; 1.
DR Pfam; PF08513; LisH; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..620
FT /note="Ran-binding protein 10"
FT /id="PRO_0000305237"
FT DOMAIN 35..222
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT DOMAIN 253..285
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 291..348
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 362
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6VN19"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VN19"
FT MOD_RES 369
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 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VN19"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VN19"
FT VAR_SEQ 1..117
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055839"
FT VAR_SEQ 134..189
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055840"
FT VAR_SEQ 450
FT /note="T -> TSNPWLQLERRPNQAAPTTPPGPTPTSTPPH (in isoform 2
FT and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055841"
FT CONFLICT 223
FT /note="L -> P (in Ref. 5; AAH99917)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="M -> V (in Ref. 5; AAH99917)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 620 AA; 67257 MW; 66744ADBCB36D308 CRC64;
MAAATADPGA GNPQPGDSSG GGAGGGLPSP GEQELSRRLQ RLYPAVNQQE TPLPRSWSPK
DKYNYIGLSQ GNLRVHYKGH GKNHKDAASV RATHPIPAAC GIYYFEVKIV SKGRDGYMGI
GLSAQGVNMN RLPGWDKHSY GYHGDDGHSF CSSGTGQPYG PTFTTGDVIG CCVNLINGTC
FYTKNGHSLG IAFTDLPANL YPTVGLQTPG EIVDANFGQQ PFLFDIEDYM REWRAKVQGT
VHCFPISARL GEWQAVLQNM VSSYLVHHGY CATATAFARM TETPIQEEQA SIKNRQKIQK
LVLEGRVGEA IETTQRFYPG LLEHNPNLLF MLKCRQFVEM VNGTDSEVRS LSSRSPKSQD
SYPGSPSLSP RHGPSSSHMH NTGADSPSCS NGVASTKSKQ NHSKYPAPSS SSSSSSSSSS
SSPSSVNYSE SNSTDSTKSQ HHSSTSNQET SDSEMEMEAE HYPNGVLGSM STRIVNGAYK
HEDLQTDESS MDDRHPRRQL CGGNQAATER IILFGRELQA LSEQLGREYG KNLAHTEMLQ
DAFSLLAYSD PWSCPVGQQL DPIQREPVCA ALNSAILESQ NLPKQPPLML ALGQASECLR
LMARAGLGSC SFARVDDYLH
