Full text data of RANBP10
RANBP10
(KIAA1464)
[Confidence: low (only semi-automatic identification from reviews)]
Ran-binding protein 10; RanBP10
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ran-binding protein 10; RanBP10
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q6VN20
ID RBP10_HUMAN Reviewed; 620 AA.
AC Q6VN20; A4FTY2; Q9P264;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 80.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
RP 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].
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.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, HOMODIMERIZATION, INTERACTION WITH AR AND RANBP9, AND
RP SUBCELLULAR 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 [5]
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
RT modulates noncentrosomal microtubules.";
RL J. Biol. Chem. 283:14109-14119(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365 AND SER-369, AND
RP 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365 AND SER-369, AND
RP MASS 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369, 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) for
CC RAN GTPase (By similarity). May play an essential role in
CC hemostasis and in maintaining microtubule dynamics with respect to
CC both platelet shape and function (By similarity). May act as an
CC adapter protein to couple membrane receptors to intracellular
CC signaling pathways. Enhances dihydrotestosterone-induced
CC transactivation activity of AR, as well as dexamethasone-induced
CC transactivation activity of NR3C1, but does not affect estrogen-
CC induced transactivation. In contrast to RANBP9, does not interact
CC with Sos and does not activate the Ras pathway.
CC -!- SUBUNIT: May form homodimers. Interacts with RAN and RANBP9.
CC Interacts with the HGF receptor MET. Interacts with AR. Interacts
CC with TUBB1. May interact with TUBB5 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus.
CC Note=Predominantly cytoplasmic.
CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in
CC skeletal muscle.
CC -!- DOMAIN: The SPRY domain mediates the interaction with MET (By
CC similarity).
CC -!- SIMILARITY: Belongs to the RANBP9/10 family.
CC -!- SIMILARITY: Contains 1 B30.2/SPRY domain.
CC -!- SIMILARITY: Contains 1 CTLH domain.
CC -!- SIMILARITY: Contains 1 LisH domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95988.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AY337313; AAR01220.1; -; mRNA.
DR EMBL; AB040897; BAA95988.1; ALT_INIT; mRNA.
DR EMBL; BC099917; AAH99917.1; -; mRNA.
DR EMBL; BC121176; AAI21177.1; -; mRNA.
DR EMBL; BC121177; AAI21178.1; -; mRNA.
DR RefSeq; NP_065901.1; NM_020850.1.
DR UniGene; Hs.368569; -.
DR ProteinModelPortal; Q6VN20; -.
DR SMR; Q6VN20; 104-213.
DR IntAct; Q6VN20; 5.
DR STRING; 9606.ENSP00000316589; -.
DR PhosphoSite; Q6VN20; -.
DR DMDM; 74710336; -.
DR PaxDb; Q6VN20; -.
DR PRIDE; Q6VN20; -.
DR Ensembl; ENST00000317506; ENSP00000316589; ENSG00000141084.
DR GeneID; 57610; -.
DR KEGG; hsa:57610; -.
DR UCSC; uc002eud.3; human.
DR CTD; 57610; -.
DR GeneCards; GC16M067757; -.
DR H-InvDB; HIX0013157; -.
DR HGNC; HGNC:29285; RANBP10.
DR HPA; HPA045523; -.
DR MIM; 614031; gene.
DR neXtProt; NX_Q6VN20; -.
DR PharmGKB; PA134929520; -.
DR eggNOG; NOG316575; -.
DR HOGENOM; HOG000008133; -.
DR HOVERGEN; HBG053444; -.
DR InParanoid; Q6VN20; -.
DR OMA; YKGHGKN; -.
DR OrthoDB; EOG76MK7Z; -.
DR GenomeRNAi; 57610; -.
DR NextBio; 64259; -.
DR PRO; PR:Q6VN20; -.
DR ArrayExpress; Q6VN20; -.
DR Bgee; Q6VN20; -.
DR CleanEx; HS_RANBP10; -.
DR Genevestigator; Q6VN20; -.
DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005087; F:Ran guanyl-nucleotide exchange factor activity; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR006594; LisH_dimerisation.
DR InterPro; IPR013720; LisH_dimerisation_subgr.
DR InterPro; IPR027713; RANBP9/RANBP10/Ssh4.
DR InterPro; IPR018355; SPla/RYanodine_receptor_subgr.
DR InterPro; IPR003877; SPRY_rcpt.
DR PANTHER; PTHR12864:SF1; PTHR12864:SF1; 1.
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; SM00667; LisH; 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; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 620 Ran-binding protein 10.
FT /FTId=PRO_0000305237.
FT DOMAIN 35 222 B30.2/SPRY.
FT DOMAIN 253 285 LisH.
FT DOMAIN 291 348 CTLH.
FT COMPBIAS 346 453 Ser-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 365 365 Phosphoserine.
FT MOD_RES 369 369 Phosphoserine.
FT CONFLICT 223 223 L -> P (in Ref. 3; AAH99917).
FT CONFLICT 455 455 M -> V (in Ref. 3; AAH99917).
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
//
ID RBP10_HUMAN Reviewed; 620 AA.
AC Q6VN20; A4FTY2; Q9P264;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 80.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
RP 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].
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.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, HOMODIMERIZATION, INTERACTION WITH AR AND RANBP9, AND
RP SUBCELLULAR 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 [5]
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
RT modulates noncentrosomal microtubules.";
RL J. Biol. Chem. 283:14109-14119(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365 AND SER-369, AND
RP 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365 AND SER-369, AND
RP MASS 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369, 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) for
CC RAN GTPase (By similarity). May play an essential role in
CC hemostasis and in maintaining microtubule dynamics with respect to
CC both platelet shape and function (By similarity). May act as an
CC adapter protein to couple membrane receptors to intracellular
CC signaling pathways. Enhances dihydrotestosterone-induced
CC transactivation activity of AR, as well as dexamethasone-induced
CC transactivation activity of NR3C1, but does not affect estrogen-
CC induced transactivation. In contrast to RANBP9, does not interact
CC with Sos and does not activate the Ras pathway.
CC -!- SUBUNIT: May form homodimers. Interacts with RAN and RANBP9.
CC Interacts with the HGF receptor MET. Interacts with AR. Interacts
CC with TUBB1. May interact with TUBB5 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus.
CC Note=Predominantly cytoplasmic.
CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in
CC skeletal muscle.
CC -!- DOMAIN: The SPRY domain mediates the interaction with MET (By
CC similarity).
CC -!- SIMILARITY: Belongs to the RANBP9/10 family.
CC -!- SIMILARITY: Contains 1 B30.2/SPRY domain.
CC -!- SIMILARITY: Contains 1 CTLH domain.
CC -!- SIMILARITY: Contains 1 LisH domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95988.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AY337313; AAR01220.1; -; mRNA.
DR EMBL; AB040897; BAA95988.1; ALT_INIT; mRNA.
DR EMBL; BC099917; AAH99917.1; -; mRNA.
DR EMBL; BC121176; AAI21177.1; -; mRNA.
DR EMBL; BC121177; AAI21178.1; -; mRNA.
DR RefSeq; NP_065901.1; NM_020850.1.
DR UniGene; Hs.368569; -.
DR ProteinModelPortal; Q6VN20; -.
DR SMR; Q6VN20; 104-213.
DR IntAct; Q6VN20; 5.
DR STRING; 9606.ENSP00000316589; -.
DR PhosphoSite; Q6VN20; -.
DR DMDM; 74710336; -.
DR PaxDb; Q6VN20; -.
DR PRIDE; Q6VN20; -.
DR Ensembl; ENST00000317506; ENSP00000316589; ENSG00000141084.
DR GeneID; 57610; -.
DR KEGG; hsa:57610; -.
DR UCSC; uc002eud.3; human.
DR CTD; 57610; -.
DR GeneCards; GC16M067757; -.
DR H-InvDB; HIX0013157; -.
DR HGNC; HGNC:29285; RANBP10.
DR HPA; HPA045523; -.
DR MIM; 614031; gene.
DR neXtProt; NX_Q6VN20; -.
DR PharmGKB; PA134929520; -.
DR eggNOG; NOG316575; -.
DR HOGENOM; HOG000008133; -.
DR HOVERGEN; HBG053444; -.
DR InParanoid; Q6VN20; -.
DR OMA; YKGHGKN; -.
DR OrthoDB; EOG76MK7Z; -.
DR GenomeRNAi; 57610; -.
DR NextBio; 64259; -.
DR PRO; PR:Q6VN20; -.
DR ArrayExpress; Q6VN20; -.
DR Bgee; Q6VN20; -.
DR CleanEx; HS_RANBP10; -.
DR Genevestigator; Q6VN20; -.
DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005087; F:Ran guanyl-nucleotide exchange factor activity; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR006594; LisH_dimerisation.
DR InterPro; IPR013720; LisH_dimerisation_subgr.
DR InterPro; IPR027713; RANBP9/RANBP10/Ssh4.
DR InterPro; IPR018355; SPla/RYanodine_receptor_subgr.
DR InterPro; IPR003877; SPRY_rcpt.
DR PANTHER; PTHR12864:SF1; PTHR12864:SF1; 1.
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; SM00667; LisH; 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; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 620 Ran-binding protein 10.
FT /FTId=PRO_0000305237.
FT DOMAIN 35 222 B30.2/SPRY.
FT DOMAIN 253 285 LisH.
FT DOMAIN 291 348 CTLH.
FT COMPBIAS 346 453 Ser-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 365 365 Phosphoserine.
FT MOD_RES 369 369 Phosphoserine.
FT CONFLICT 223 223 L -> P (in Ref. 3; AAH99917).
FT CONFLICT 455 455 M -> V (in Ref. 3; AAH99917).
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
//
MIM
614031
*RECORD*
*FIELD* NO
614031
*FIELD* TI
*614031 RAN-BINDING PROTEIN 10; RANBP10
;;KIAA1464
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated fetal brain cDNA
read morelibrary, Nagase et al. (2000) cloned RANBP10, which they designated
KIAA1464. The deduced 621-amino acid protein shares significant
similarity with RANBPM (RANBP9; 603854). RT-PCR ELISA detected low
RANBP10 expression in all adult and fetal tissues and specific adult
brain regions examined.
By searching databases for sequences similar to RANBP9, followed by PCR
and RACE, Wang et al. (2004) cloned human RANBP10. The deduced 620-amino
acid protein has a calculated molecular mass of 67 kD. RANBP10 contains
a SPRY domain in its N-terminal half, but it lacks the proline- and
glutamine-rich region present in RANBP9. RANBP10 shares 68% amino acid
identity with RANBP9 and 95% identity with mouse Ranbp10. Northern blot
analysis detected a 5.3-kb RANBP10 transcript in several human tissues,
with highest expression in skeletal muscle. EST database analysis
revealed widespread RANBP10 expression.
Schulze et al. (2008) determined that mouse Ranbp10 contains a consensus
guanine nucleotide exchange factor (GEF) domain that is most similar to
the GEF domain of Sos2 (601247). Northern blot analysis detected Ranbp10
expression in adult mouse liver, spleen, and bone marrow, with lower
levels in other tissues examined. In fetal liver cultures, Ranbp10 was
highly expressed in mature megakaryocytes. Immunofluorescence analysis
showed that Ranbp10 localized to cytoplasmic microtubules in
megakaryocytes and platelets.
GENE FUNCTION
Using protein pull-down and coimmunoprecipitation analyses, Wang et al.
(2004) showed that, like RANBP9, RANBP10 interacted directly with RAN
(601179), a small nuclear GTPase, and MET (164860), a receptor protein
tyrosine kinase for hepatocyte growth factor (HGF; 142409). Pull-down
experiments revealed that RANBP9 and RANBP10 competed for MET binding.
RANBP9, but not RANBP10, induced ERK (MAPK3; 601795) phosphorylation and
expression from a serum response element (SRE) reporter gene. RANBP10
inhibited RANBP9-mediated reporter gene activation.
Megakaryocytes are large polyploid cells that conclude their maturation
by assembling nascent blood platelets within a complex reticular network
of microtubules. Using a yeast 2-hybrid assay, Schulze et al. (2008)
showed that mouse Ranbp10 bound beta-tubulins, including the platelet-
and megakaryocyte-specific beta-1 tubulin (TUBB1; 612901). The
N-terminal domain of Ranbp10 showed Ran-specific GEF activity. Depletion
of endogenous Ranbp10 from megakaryocytes via small interfering RNA
disrupted the reticular array of microtubule filaments, resulting in
scattered tubulin filaments, short fragments, and punctate foci.
Knockdown of Ranbp10 had no effect on intranuclear Ran localization.
Schulze et al. (2008) concluded that Ranbp10 regulates the microtubule
network of megakaryocytes and coordinates platelet assembly and release.
Kunert et al. (2009) found that overexpression of Ranbp10 in mouse
megakaryocytes resulted in exceptionally thick microtubules and
increased cytoplasmic Ran localization, likely due to elevated
Ran-specific GEF activity and accumulation of cytoplasmic Ran-GTP.
Harada et al. (2008) showed that both RANBP9 and RANBP10 enhanced
dihydrotestosterone (DHT)-induced transactivation activity of androgen
receptor (AR; 313700). Simultaneous overexpression of RANBP10 and RANBP9
had an additive effect on AR transactivation. Both RANBP10 and RANBP9
enhanced glucocorticoid receptor (GCCR; 138040) transactivation in the
presence of dexamethasone, but neither affected
17-beta-estradiol-induced transactivation of estrogen receptor (ESR1;
133430). Immunoprecipitation analysis revealed that RANBP10 complexed
with androgen receptor in the presence of DHT. Furthermore, RANBP10
dimerized with itself and with RANBP9.
MAPPING
Hartz (2011) mapped the RANBP10 gene to chromosome 16q22.1 based on an
alignment of the RANBP10 sequence (GenBank GENBANK AB040897) with the
genomic sequence (GRCh37).
ANIMAL MODEL
Kunert et al. (2009) found that Ranbp10 -/- mice were viable and had
normal platelet counts. However, Ranbp10 -/- mice showed prolonged
bleeding time, and Ranbp10 -/- fetal liver-derived megakaryocytes showed
slightly reduced proplatelet formation. Ultrastructural analysis
revealed significantly increased spherical shape in resting platelets,
and many platelets exhibited disorders in microtubule filament numbers
and localization. Ranbp10 -/- mice also showed a defect in granule
secretion. Kunert et al. (2009) concluded that Ranbp10 is dispensable
for platelet biogenesis, but is required for normal hemostasis.
*FIELD* RF
1. Harada, N.; Yokoyama, T.; Yamaji, R.; Nakano, Y.; Inui, H.: RanBP10
acts as a novel coactivator for the androgen receptor. Biochem. Biophys.
Res. Commun. 368: 121-125, 2008.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 4/27/2011.
3. Kunert, S.; Meyer, I.; Fleischhauer, S.; Wannack, M.; Fiedler,
J.; Shivdasani, R. A.; Schulze, H.: The microtubule modulator RanBP10
plays a critical role in regulation of platelet discoid shape and
degranulation. Blood 114: 5532-5540, 2009.
4. Nagase, T.; Kikuno, R.; Ishikawa, K.; Hirosawa, M.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XVII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 7: 143-150, 2000.
5. Schulze, H.; Dose, M.; Korpal, M.; Meyer, I.; Italino, J. E., Jr.;
Shivdasani, R. A.: RanBP10 is a cytoplasmic guanine nucleotide exchange
factor that modulates noncentrosomal microtubules. J. Biol. Chem. 283:
14109-14119, 2008.
6. Wang, D.; Li, Z.; Schoen, S. R.; Messing, E. M.; Wu, G.: A novel
MET-interacting protein shares high sequence similarity with RanBPM,
but fails to stimulate MET-induced Ras/Erk signaling. Biochem. Biophys.
Res. Commun. 313: 320-326, 2004.
*FIELD* CD
Patricia A. Hartz: 6/7/2011
*FIELD* ED
mgross: 06/07/2011
*RECORD*
*FIELD* NO
614031
*FIELD* TI
*614031 RAN-BINDING PROTEIN 10; RANBP10
;;KIAA1464
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated fetal brain cDNA
read morelibrary, Nagase et al. (2000) cloned RANBP10, which they designated
KIAA1464. The deduced 621-amino acid protein shares significant
similarity with RANBPM (RANBP9; 603854). RT-PCR ELISA detected low
RANBP10 expression in all adult and fetal tissues and specific adult
brain regions examined.
By searching databases for sequences similar to RANBP9, followed by PCR
and RACE, Wang et al. (2004) cloned human RANBP10. The deduced 620-amino
acid protein has a calculated molecular mass of 67 kD. RANBP10 contains
a SPRY domain in its N-terminal half, but it lacks the proline- and
glutamine-rich region present in RANBP9. RANBP10 shares 68% amino acid
identity with RANBP9 and 95% identity with mouse Ranbp10. Northern blot
analysis detected a 5.3-kb RANBP10 transcript in several human tissues,
with highest expression in skeletal muscle. EST database analysis
revealed widespread RANBP10 expression.
Schulze et al. (2008) determined that mouse Ranbp10 contains a consensus
guanine nucleotide exchange factor (GEF) domain that is most similar to
the GEF domain of Sos2 (601247). Northern blot analysis detected Ranbp10
expression in adult mouse liver, spleen, and bone marrow, with lower
levels in other tissues examined. In fetal liver cultures, Ranbp10 was
highly expressed in mature megakaryocytes. Immunofluorescence analysis
showed that Ranbp10 localized to cytoplasmic microtubules in
megakaryocytes and platelets.
GENE FUNCTION
Using protein pull-down and coimmunoprecipitation analyses, Wang et al.
(2004) showed that, like RANBP9, RANBP10 interacted directly with RAN
(601179), a small nuclear GTPase, and MET (164860), a receptor protein
tyrosine kinase for hepatocyte growth factor (HGF; 142409). Pull-down
experiments revealed that RANBP9 and RANBP10 competed for MET binding.
RANBP9, but not RANBP10, induced ERK (MAPK3; 601795) phosphorylation and
expression from a serum response element (SRE) reporter gene. RANBP10
inhibited RANBP9-mediated reporter gene activation.
Megakaryocytes are large polyploid cells that conclude their maturation
by assembling nascent blood platelets within a complex reticular network
of microtubules. Using a yeast 2-hybrid assay, Schulze et al. (2008)
showed that mouse Ranbp10 bound beta-tubulins, including the platelet-
and megakaryocyte-specific beta-1 tubulin (TUBB1; 612901). The
N-terminal domain of Ranbp10 showed Ran-specific GEF activity. Depletion
of endogenous Ranbp10 from megakaryocytes via small interfering RNA
disrupted the reticular array of microtubule filaments, resulting in
scattered tubulin filaments, short fragments, and punctate foci.
Knockdown of Ranbp10 had no effect on intranuclear Ran localization.
Schulze et al. (2008) concluded that Ranbp10 regulates the microtubule
network of megakaryocytes and coordinates platelet assembly and release.
Kunert et al. (2009) found that overexpression of Ranbp10 in mouse
megakaryocytes resulted in exceptionally thick microtubules and
increased cytoplasmic Ran localization, likely due to elevated
Ran-specific GEF activity and accumulation of cytoplasmic Ran-GTP.
Harada et al. (2008) showed that both RANBP9 and RANBP10 enhanced
dihydrotestosterone (DHT)-induced transactivation activity of androgen
receptor (AR; 313700). Simultaneous overexpression of RANBP10 and RANBP9
had an additive effect on AR transactivation. Both RANBP10 and RANBP9
enhanced glucocorticoid receptor (GCCR; 138040) transactivation in the
presence of dexamethasone, but neither affected
17-beta-estradiol-induced transactivation of estrogen receptor (ESR1;
133430). Immunoprecipitation analysis revealed that RANBP10 complexed
with androgen receptor in the presence of DHT. Furthermore, RANBP10
dimerized with itself and with RANBP9.
MAPPING
Hartz (2011) mapped the RANBP10 gene to chromosome 16q22.1 based on an
alignment of the RANBP10 sequence (GenBank GENBANK AB040897) with the
genomic sequence (GRCh37).
ANIMAL MODEL
Kunert et al. (2009) found that Ranbp10 -/- mice were viable and had
normal platelet counts. However, Ranbp10 -/- mice showed prolonged
bleeding time, and Ranbp10 -/- fetal liver-derived megakaryocytes showed
slightly reduced proplatelet formation. Ultrastructural analysis
revealed significantly increased spherical shape in resting platelets,
and many platelets exhibited disorders in microtubule filament numbers
and localization. Ranbp10 -/- mice also showed a defect in granule
secretion. Kunert et al. (2009) concluded that Ranbp10 is dispensable
for platelet biogenesis, but is required for normal hemostasis.
*FIELD* RF
1. Harada, N.; Yokoyama, T.; Yamaji, R.; Nakano, Y.; Inui, H.: RanBP10
acts as a novel coactivator for the androgen receptor. Biochem. Biophys.
Res. Commun. 368: 121-125, 2008.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 4/27/2011.
3. Kunert, S.; Meyer, I.; Fleischhauer, S.; Wannack, M.; Fiedler,
J.; Shivdasani, R. A.; Schulze, H.: The microtubule modulator RanBP10
plays a critical role in regulation of platelet discoid shape and
degranulation. Blood 114: 5532-5540, 2009.
4. Nagase, T.; Kikuno, R.; Ishikawa, K.; Hirosawa, M.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XVII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 7: 143-150, 2000.
5. Schulze, H.; Dose, M.; Korpal, M.; Meyer, I.; Italino, J. E., Jr.;
Shivdasani, R. A.: RanBP10 is a cytoplasmic guanine nucleotide exchange
factor that modulates noncentrosomal microtubules. J. Biol. Chem. 283:
14109-14119, 2008.
6. Wang, D.; Li, Z.; Schoen, S. R.; Messing, E. M.; Wu, G.: A novel
MET-interacting protein shares high sequence similarity with RanBPM,
but fails to stimulate MET-induced Ras/Erk signaling. Biochem. Biophys.
Res. Commun. 313: 320-326, 2004.
*FIELD* CD
Patricia A. Hartz: 6/7/2011
*FIELD* ED
mgross: 06/07/2011