Full text data of RANBP1
RANBP1
[Confidence: low (only semi-automatic identification from reviews)]
Ran-specific GTPase-activating protein (Ran-binding protein 1; RanBP1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ran-specific GTPase-activating protein (Ran-binding protein 1; RanBP1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P43487
ID RANG_HUMAN Reviewed; 201 AA.
AC P43487;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1995, sequence version 1.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Ran-specific GTPase-activating protein;
DE AltName: Full=Ran-binding protein 1;
DE Short=RanBP1;
GN Name=RANBP1;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7882974;
RA Bischoff F.R., Krebber H., Smirnova E., Dong W., Ponstingl H.;
RT "Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-
RT GTP binding protein RanBP1.";
RL EMBO J. 14:705-715(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=7616957; DOI=10.1007/BF00290397;
RA Hayashi N., Yokoyama N., Seki T., Azuma Y., Ohba T., Nishimoto T.;
RT "RanBP1, a Ras-like nuclear G protein binding to Ran/TC4, inhibits
RT RCC1 via Ran/TC4.";
RL Mol. Gen. Genet. 247:661-669(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; THR-18 AND SER-21,
RP AND 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 [5]
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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-150 AND LYS-183, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [8]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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-60, 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 VARIANT [LARGE SCALE ANALYSIS] ASP-16.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1
CC trimeric complex. Increase GTP hydrolysis induced by the Ran
CC GTPase activating protein RANGAP1. May act in an intracellular
CC signaling pathway which may control the progression through the
CC cell cycle by regulating the transport of protein and nucleic
CC acids across the nuclear membrane.
CC -!- INTERACTION:
CC P29372:MPG; NbExp=1; IntAct=EBI-1032909, EBI-1043398;
CC -!- SIMILARITY: Belongs to the RANBP1 family.
CC -!- SIMILARITY: Contains 1 RanBD1 domain.
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; X83617; CAA58592.1; -; mRNA.
DR EMBL; D38076; BAA07269.1; -; mRNA.
DR EMBL; CR456556; CAG30442.1; -; mRNA.
DR PIR; S54290; S54290.
DR RefSeq; NP_001265568.1; NM_001278639.1.
DR RefSeq; NP_001265569.1; NM_001278640.1.
DR RefSeq; NP_002873.1; NM_002882.3.
DR UniGene; Hs.24763; -.
DR PDB; 1K5D; X-ray; 2.70 A; B/E/H/K=1-201.
DR PDB; 1K5G; X-ray; 3.10 A; B/E/H/K=1-201.
DR PDBsum; 1K5D; -.
DR PDBsum; 1K5G; -.
DR ProteinModelPortal; P43487; -.
DR SMR; P43487; 22-167.
DR IntAct; P43487; 7.
DR MINT; MINT-1584597; -.
DR STRING; 9606.ENSP00000327583; -.
DR PhosphoSite; P43487; -.
DR DMDM; 1172837; -.
DR DOSAC-COBS-2DPAGE; P43487; -.
DR OGP; P43487; -.
DR REPRODUCTION-2DPAGE; IPI00414127; -.
DR PaxDb; P43487; -.
DR PeptideAtlas; P43487; -.
DR PRIDE; P43487; -.
DR DNASU; 5902; -.
DR Ensembl; ENST00000331821; ENSP00000327583; ENSG00000099901.
DR Ensembl; ENST00000402752; ENSP00000384925; ENSG00000099901.
DR GeneID; 5902; -.
DR KEGG; hsa:5902; -.
DR UCSC; uc002zro.1; human.
DR CTD; 5902; -.
DR GeneCards; GC22P020103; -.
DR HGNC; HGNC:9847; RANBP1.
DR HPA; CAB046463; -.
DR MIM; 601180; gene.
DR neXtProt; NX_P43487; -.
DR PharmGKB; PA34206; -.
DR eggNOG; COG5171; -.
DR HOGENOM; HOG000176323; -.
DR HOVERGEN; HBG006958; -.
DR InParanoid; P43487; -.
DR KO; K15306; -.
DR OMA; ENELPEW; -.
DR PhylomeDB; P43487; -.
DR Reactome; REACT_116125; Disease.
DR ChiTaRS; RANBP1; human.
DR EvolutionaryTrace; P43487; -.
DR GeneWiki; RANBP1; -.
DR GenomeRNAi; 5902; -.
DR NextBio; 22960; -.
DR PRO; PR:P43487; -.
DR ArrayExpress; P43487; -.
DR Bgee; P43487; -.
DR CleanEx; HS_RANBP1; -.
DR Genevestigator; P43487; -.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; TAS:Reactome.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; TAS:ProtInc.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0008536; F:Ran GTPase binding; TAS:ProtInc.
DR GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
DR GO; GO:0046604; P:positive regulation of mitotic centrosome separation; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR GO; GO:0007051; P:spindle organization; IEA:Ensembl.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR000156; Ran_bind_dom.
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; Complete proteome;
KW Direct protein sequencing; GTPase activation; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 201 Ran-specific GTPase-activating protein.
FT /FTId=PRO_0000213667.
FT DOMAIN 26 164 RanBD1.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 13 13 Phosphothreonine.
FT MOD_RES 18 18 Phosphothreonine.
FT MOD_RES 21 21 Phosphoserine.
FT MOD_RES 60 60 Phosphoserine.
FT MOD_RES 150 150 N6-acetyllysine.
FT MOD_RES 183 183 N6-acetyllysine.
FT VARIANT 16 16 E -> D (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036567.
FT VARIANT 145 145 A -> V (in dbSNP:rs5746863).
FT /FTId=VAR_053629.
FT CONFLICT 169 169 Missing (in Ref. 2; BAA07269).
FT STRAND 48 58
FT STRAND 67 79
FT STRAND 81 83
FT STRAND 86 92
FT TURN 93 95
FT STRAND 98 103
FT STRAND 117 127
FT STRAND 134 141
FT HELIX 145 165
SQ SEQUENCE 201 AA; 23310 MW; 05FC9B35DADA48C9 CRC64;
MAAAKDTHED HDTSTENTDE SNHDPQFEPI VSLPEQEIKT LEEDEEELFK MRAKLFRFAS
ENDLPEWKER GTGDVKLLKH KEKGAIRLLM RRDKTLKICA NHYITPMMEL KPNAGSDRAW
VWNTHADFAD ECPKPELLAI RFLNAENAQK FKTKFEECRK EIEEREKKAG SGKNDHAEKV
AEKLEALSVK EETKEDAEEK Q
//
ID RANG_HUMAN Reviewed; 201 AA.
AC P43487;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1995, sequence version 1.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Ran-specific GTPase-activating protein;
DE AltName: Full=Ran-binding protein 1;
DE Short=RanBP1;
GN Name=RANBP1;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7882974;
RA Bischoff F.R., Krebber H., Smirnova E., Dong W., Ponstingl H.;
RT "Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-
RT GTP binding protein RanBP1.";
RL EMBO J. 14:705-715(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=7616957; DOI=10.1007/BF00290397;
RA Hayashi N., Yokoyama N., Seki T., Azuma Y., Ohba T., Nishimoto T.;
RT "RanBP1, a Ras-like nuclear G protein binding to Ran/TC4, inhibits
RT RCC1 via Ran/TC4.";
RL Mol. Gen. Genet. 247:661-669(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; THR-18 AND SER-21,
RP AND 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 [5]
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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-150 AND LYS-183, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [8]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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-60, 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 VARIANT [LARGE SCALE ANALYSIS] ASP-16.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1
CC trimeric complex. Increase GTP hydrolysis induced by the Ran
CC GTPase activating protein RANGAP1. May act in an intracellular
CC signaling pathway which may control the progression through the
CC cell cycle by regulating the transport of protein and nucleic
CC acids across the nuclear membrane.
CC -!- INTERACTION:
CC P29372:MPG; NbExp=1; IntAct=EBI-1032909, EBI-1043398;
CC -!- SIMILARITY: Belongs to the RANBP1 family.
CC -!- SIMILARITY: Contains 1 RanBD1 domain.
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; X83617; CAA58592.1; -; mRNA.
DR EMBL; D38076; BAA07269.1; -; mRNA.
DR EMBL; CR456556; CAG30442.1; -; mRNA.
DR PIR; S54290; S54290.
DR RefSeq; NP_001265568.1; NM_001278639.1.
DR RefSeq; NP_001265569.1; NM_001278640.1.
DR RefSeq; NP_002873.1; NM_002882.3.
DR UniGene; Hs.24763; -.
DR PDB; 1K5D; X-ray; 2.70 A; B/E/H/K=1-201.
DR PDB; 1K5G; X-ray; 3.10 A; B/E/H/K=1-201.
DR PDBsum; 1K5D; -.
DR PDBsum; 1K5G; -.
DR ProteinModelPortal; P43487; -.
DR SMR; P43487; 22-167.
DR IntAct; P43487; 7.
DR MINT; MINT-1584597; -.
DR STRING; 9606.ENSP00000327583; -.
DR PhosphoSite; P43487; -.
DR DMDM; 1172837; -.
DR DOSAC-COBS-2DPAGE; P43487; -.
DR OGP; P43487; -.
DR REPRODUCTION-2DPAGE; IPI00414127; -.
DR PaxDb; P43487; -.
DR PeptideAtlas; P43487; -.
DR PRIDE; P43487; -.
DR DNASU; 5902; -.
DR Ensembl; ENST00000331821; ENSP00000327583; ENSG00000099901.
DR Ensembl; ENST00000402752; ENSP00000384925; ENSG00000099901.
DR GeneID; 5902; -.
DR KEGG; hsa:5902; -.
DR UCSC; uc002zro.1; human.
DR CTD; 5902; -.
DR GeneCards; GC22P020103; -.
DR HGNC; HGNC:9847; RANBP1.
DR HPA; CAB046463; -.
DR MIM; 601180; gene.
DR neXtProt; NX_P43487; -.
DR PharmGKB; PA34206; -.
DR eggNOG; COG5171; -.
DR HOGENOM; HOG000176323; -.
DR HOVERGEN; HBG006958; -.
DR InParanoid; P43487; -.
DR KO; K15306; -.
DR OMA; ENELPEW; -.
DR PhylomeDB; P43487; -.
DR Reactome; REACT_116125; Disease.
DR ChiTaRS; RANBP1; human.
DR EvolutionaryTrace; P43487; -.
DR GeneWiki; RANBP1; -.
DR GenomeRNAi; 5902; -.
DR NextBio; 22960; -.
DR PRO; PR:P43487; -.
DR ArrayExpress; P43487; -.
DR Bgee; P43487; -.
DR CleanEx; HS_RANBP1; -.
DR Genevestigator; P43487; -.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; TAS:Reactome.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; TAS:ProtInc.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0008536; F:Ran GTPase binding; TAS:ProtInc.
DR GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
DR GO; GO:0046604; P:positive regulation of mitotic centrosome separation; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR GO; GO:0007051; P:spindle organization; IEA:Ensembl.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR000156; Ran_bind_dom.
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; Complete proteome;
KW Direct protein sequencing; GTPase activation; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 201 Ran-specific GTPase-activating protein.
FT /FTId=PRO_0000213667.
FT DOMAIN 26 164 RanBD1.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 13 13 Phosphothreonine.
FT MOD_RES 18 18 Phosphothreonine.
FT MOD_RES 21 21 Phosphoserine.
FT MOD_RES 60 60 Phosphoserine.
FT MOD_RES 150 150 N6-acetyllysine.
FT MOD_RES 183 183 N6-acetyllysine.
FT VARIANT 16 16 E -> D (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036567.
FT VARIANT 145 145 A -> V (in dbSNP:rs5746863).
FT /FTId=VAR_053629.
FT CONFLICT 169 169 Missing (in Ref. 2; BAA07269).
FT STRAND 48 58
FT STRAND 67 79
FT STRAND 81 83
FT STRAND 86 92
FT TURN 93 95
FT STRAND 98 103
FT STRAND 117 127
FT STRAND 134 141
FT HELIX 145 165
SQ SEQUENCE 201 AA; 23310 MW; 05FC9B35DADA48C9 CRC64;
MAAAKDTHED HDTSTENTDE SNHDPQFEPI VSLPEQEIKT LEEDEEELFK MRAKLFRFAS
ENDLPEWKER GTGDVKLLKH KEKGAIRLLM RRDKTLKICA NHYITPMMEL KPNAGSDRAW
VWNTHADFAD ECPKPELLAI RFLNAENAQK FKTKFEECRK EIEEREKKAG SGKNDHAEKV
AEKLEALSVK EETKEDAEEK Q
//
MIM
601180
*RECORD*
*FIELD* NO
601180
*FIELD* TI
*601180 RAN-BINDING PROTEIN 1; RANBP1
;;HPAII TINY FRAGMENTS LOCUS 9A; HTF9A
*FIELD* TX
read more
CLONING
Coutavas et al. (1993) isolated a Ran/TC4-binding protein, RanBP1, that
interacts specifically with GTP-charged RAN (601179). The authors cloned
the mouse RanBP1 cDNA by screening an expression library containing
cDNAs from 16-day mouse embryos.
Bischoff et al. (1995) identified a 23-kD protein, RANBP1, that binds to
RAN complexed with GTP but not GDP. Based on partial peptide sequence of
the purified protein, primers were designed to amplify a cDNA encoding
the protein. They also showed that RANBP1 does not activate GTPase
activity of RAN but does markedly increase GTP hydrolysis by the
RanGTPase-activating protein (RanGAP1).
Hayashi et al. (1995) isolated human RANBP1 using the 2-hybrid method
with either RAN or RCC1 (179710) as targets. The RANBP1 cDNA encodes a
201-amino acid protein that is 92% identical to its mouse homolog.
Hayashi et al. (1995) showed that, in both mammalian cells and in yeast,
RANBP1 acts as a negative regulator of RCC1 by inhibiting
RCC1-stimulated guanine nucleotide release from RAN. See also 601181.
BIOCHEMICAL FEATURES
- Crystal Structure
Seewald et al. (2002) presented the 3-dimensional structure of a
Ran-RanBP1-RanGAP ternary complex in the ground state and in a
transition-state mimic. The structure and biochemical experiments showed
that RanGAP does not act through an arginine finger, that the basic
machinery for fast GTP hydrolysis is provided exclusively by Ran, and
that correct positioning of the catalytic glutamine is essential for
catalysis.
GENE FUNCTION
Guarguaglini et al. (1997) found that mouse Htf9c (611151) and Ranbp1
were divergently transcribed from a bidirectional promoter. Expression
of both genes was activated upon entry into the cell cycle, peaked in S
phase, and was downregulated during completion of the cell cycle. The
bidirectional promoter was downregulated in both orientations in
arrested cells. Activation of the promoter was specific, resulting in
more restricted Htf9c expression and a sharper peak of Htf9c expression
in S phase compared with Ranbp1 expression. A region containing an E2f
(189971) site was important for cell cycle control of Htf9c, and a
common region containing sites for Sp1 (189906) and E2f contributed to
activation in both orientations.
*FIELD* RF
1. Bischoff, F. R.; Krebber, H.; Smirnova, E.; Dong, W.; Ponstingl,
H.: Co-activation of RanGTPase and inhibition of GTP dissociation
by Ran-GTP binding protein RanBP1. EMBO J. 14: 705-715, 1995.
2. Coutavas, E.; Ren, M.; Oppenheim, J. D.; D'Eustachio, P.; Rush,
M. G.: Characterization of proteins that interact with the cell-cycle
regulatory protein Ran/TC4. Nature 366: 585-587, 1993.
3. Guarguaglini, G.; Battistoni, A.; Pittoggi, C.; Di Matteo, G.;
Di Fiore, B.; Lavia, P.: Expression of the murine RanBP1 and Htf9-c
genes is regulated from a shared bidirectional promoter during cell
cycle progression. Biochem. J. 325: 277-286, 1997.
4. Hayashi, N.; Yokoyama, N.; Seki, T.; Azuma, Y.; Ohba, T.; Nishimoto,
T.: RanBP1, a Ras-like nuclear G protein binding to Ran/TC4, inhibits
RCC1 via Ran/TC4. Molec. Gen. Genet. 247: 661-669, 1995.
5. Seewald, M. J.; Korner, C.; Wittinghofer, A.; Vetter, I. R.: RanGAP
mediates GTP hydrolysis without an arginine finger. Nature 415:
662-666, 2002.
*FIELD* CN
Patricia A. Hartz - updated: 06/28/2007
Ada Hamosh - updated: 2/4/2002
Joanna S. Amberger - updated: 2/6/1998
*FIELD* CD
Alan F. Scott: 4/4/1996
*FIELD* ED
mgross: 06/28/2007
alopez: 2/7/2002
terry: 2/4/2002
alopez: 6/24/1998
alopez: 2/6/1998
joanna: 2/6/1998
mark: 4/5/1996
terry: 4/4/1996
mark: 4/4/1996
*RECORD*
*FIELD* NO
601180
*FIELD* TI
*601180 RAN-BINDING PROTEIN 1; RANBP1
;;HPAII TINY FRAGMENTS LOCUS 9A; HTF9A
*FIELD* TX
read more
CLONING
Coutavas et al. (1993) isolated a Ran/TC4-binding protein, RanBP1, that
interacts specifically with GTP-charged RAN (601179). The authors cloned
the mouse RanBP1 cDNA by screening an expression library containing
cDNAs from 16-day mouse embryos.
Bischoff et al. (1995) identified a 23-kD protein, RANBP1, that binds to
RAN complexed with GTP but not GDP. Based on partial peptide sequence of
the purified protein, primers were designed to amplify a cDNA encoding
the protein. They also showed that RANBP1 does not activate GTPase
activity of RAN but does markedly increase GTP hydrolysis by the
RanGTPase-activating protein (RanGAP1).
Hayashi et al. (1995) isolated human RANBP1 using the 2-hybrid method
with either RAN or RCC1 (179710) as targets. The RANBP1 cDNA encodes a
201-amino acid protein that is 92% identical to its mouse homolog.
Hayashi et al. (1995) showed that, in both mammalian cells and in yeast,
RANBP1 acts as a negative regulator of RCC1 by inhibiting
RCC1-stimulated guanine nucleotide release from RAN. See also 601181.
BIOCHEMICAL FEATURES
- Crystal Structure
Seewald et al. (2002) presented the 3-dimensional structure of a
Ran-RanBP1-RanGAP ternary complex in the ground state and in a
transition-state mimic. The structure and biochemical experiments showed
that RanGAP does not act through an arginine finger, that the basic
machinery for fast GTP hydrolysis is provided exclusively by Ran, and
that correct positioning of the catalytic glutamine is essential for
catalysis.
GENE FUNCTION
Guarguaglini et al. (1997) found that mouse Htf9c (611151) and Ranbp1
were divergently transcribed from a bidirectional promoter. Expression
of both genes was activated upon entry into the cell cycle, peaked in S
phase, and was downregulated during completion of the cell cycle. The
bidirectional promoter was downregulated in both orientations in
arrested cells. Activation of the promoter was specific, resulting in
more restricted Htf9c expression and a sharper peak of Htf9c expression
in S phase compared with Ranbp1 expression. A region containing an E2f
(189971) site was important for cell cycle control of Htf9c, and a
common region containing sites for Sp1 (189906) and E2f contributed to
activation in both orientations.
*FIELD* RF
1. Bischoff, F. R.; Krebber, H.; Smirnova, E.; Dong, W.; Ponstingl,
H.: Co-activation of RanGTPase and inhibition of GTP dissociation
by Ran-GTP binding protein RanBP1. EMBO J. 14: 705-715, 1995.
2. Coutavas, E.; Ren, M.; Oppenheim, J. D.; D'Eustachio, P.; Rush,
M. G.: Characterization of proteins that interact with the cell-cycle
regulatory protein Ran/TC4. Nature 366: 585-587, 1993.
3. Guarguaglini, G.; Battistoni, A.; Pittoggi, C.; Di Matteo, G.;
Di Fiore, B.; Lavia, P.: Expression of the murine RanBP1 and Htf9-c
genes is regulated from a shared bidirectional promoter during cell
cycle progression. Biochem. J. 325: 277-286, 1997.
4. Hayashi, N.; Yokoyama, N.; Seki, T.; Azuma, Y.; Ohba, T.; Nishimoto,
T.: RanBP1, a Ras-like nuclear G protein binding to Ran/TC4, inhibits
RCC1 via Ran/TC4. Molec. Gen. Genet. 247: 661-669, 1995.
5. Seewald, M. J.; Korner, C.; Wittinghofer, A.; Vetter, I. R.: RanGAP
mediates GTP hydrolysis without an arginine finger. Nature 415:
662-666, 2002.
*FIELD* CN
Patricia A. Hartz - updated: 06/28/2007
Ada Hamosh - updated: 2/4/2002
Joanna S. Amberger - updated: 2/6/1998
*FIELD* CD
Alan F. Scott: 4/4/1996
*FIELD* ED
mgross: 06/28/2007
alopez: 2/7/2002
terry: 2/4/2002
alopez: 6/24/1998
alopez: 2/6/1998
joanna: 2/6/1998
mark: 4/5/1996
terry: 4/4/1996
mark: 4/4/1996