Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Ran-specific GTPase-activating protein (Ran-binding protein 1) (RanBP1)

 RANG_HUMAN              Reviewed;         201 AA.
P43487; Q53EY3;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
05-DEC-2018, entry version 175.
RecName: Full=Ran-specific GTPase-activating protein;
AltName: Full=Ran-binding protein 1;
Short=RanBP1;
Name=RANBP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE,
FUNCTION, INTERACTION WITH RAN, AND SUBUNIT.
PubMed=7882974;
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]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), IDENTIFICATION IN A COMPLEX
WITH RAN AND RCC1, AND FUNCTION.
TISSUE=Blood;
PubMed=7616957; DOI=10.1007/BF00290397;
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.";
Mol. Gen. Genet. 247:661-669(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Coronary arterial endothelium;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
INTERACTION WITH RAN.
PubMed=7891706; DOI=10.1128/MCB.15.4.2117;
Ren M., Villamarin A., Shih A., Coutavas E., Moore M.S., Locurcio M.,
Clarke V., Oppenheim J.D., D'Eustachio P., Rush M.G.;
"Separate domains of the Ran GTPase interact with different factors to
regulate nuclear protein import and RNA processing.";
Mol. Cell. Biol. 15:2117-2124(1995).
[7]
INTERACTION WITH RAN.
PubMed=8896452;
Goerlich D., Pante N., Kutay U., Aebi U., Bischoff F.R.;
"Identification of different roles for RanGDP and RanGTP in nuclear
protein import.";
EMBO J. 15:5584-5594(1996).
[8]
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A.,
Mann M.;
"Proteomic characterization of the human centrosome by protein
correlation profiling.";
Nature 426:570-574(2003).
[9]
IDENTIFICATION IN A COMPLEX WITH RAN AND RANGAP1.
PubMed=16428860;
Takeda E., Hieda M., Katahira J., Yoneda Y.;
"Phosphorylation of RanGAP1 stabilizes its interaction with Ran and
RanBP1.";
Cell Struct. Funct. 30:69-80(2005).
[10]
FUNCTION.
PubMed=17671426; DOI=10.4161/cc.6.15.4487;
Li H.Y., Ng W.P., Wong C.H., Iglesias P.A., Zheng Y.;
"Coordination of chromosome alignment and mitotic progression by the
chromosome-based Ran signal.";
Cell Cycle 6:1886-1895(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; THR-18 AND SER-21,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-150 AND LYS-183, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
FUNCTION.
PubMed=20485264; DOI=10.1038/emboj.2010.89;
Koyama M., Matsuura Y.;
"An allosteric mechanism to displace nuclear export cargo from CRM1
and RanGTP by RanBP1.";
EMBO J. 29:2002-2013(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-188, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-190, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-190, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-190, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[26] {ECO:0000244|PDB:1K5D, ECO:0000244|PDB:1K5G}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH RAN AND THE
FISSION YEAST ORTHOLOG OF RANGAP1.
PubMed=11832950; DOI=10.1038/415662a;
Seewald M.J., Korner C., Wittinghofer A., Vetter I.R.;
"RanGAP mediates GTP hydrolysis without an arginine finger.";
Nature 415:662-666(2002).
[27]
VARIANT [LARGE SCALE ANALYSIS] ASP-16.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Plays a role in RAN-dependent nucleocytoplasmic
transport. Alleviates the TNPO1-dependent inhibition of RAN GTPase
activity and mediates the dissociation of RAN from proteins
involved in transport into the nucleus (By similarity). Induces a
conformation change in the complex formed by XPO1 and RAN that
triggers the release of the nuclear export signal of cargo
proteins (PubMed:20485264). Promotes the disassembly of the
complex formed by RAN and importin beta. Promotes dissociation of
RAN from a complex with KPNA2 and CSE1L (By similarity). Required
for normal mitotic spindle assembly and normal progress through
mitosis via its effect on RAN (PubMed:17671426). Does not increase
the RAN GTPase activity by itself, but increases GTP hydrolysis
mediated by RANGAP1 (PubMed:7882974). Inhibits RCC1-dependent
exchange of RAN-bound GDP by GTP (PubMed:7882974, PubMed:7616957).
{ECO:0000250|UniProtKB:P34022, ECO:0000269|PubMed:17671426,
ECO:0000269|PubMed:20485264, ECO:0000269|PubMed:7616957,
ECO:0000269|PubMed:7882974}.
-!- SUBUNIT: Interacts with RAN (via C-terminus of GTP-bound form) but
not with GDP-bound RAN (PubMed:7882974, PubMed:7891706,
PubMed:8896452). Identified in a complex composed of RAN, RANGAP1
and RANBP1 (PubMed:16428860, PubMed:11832950). Identified in a
complex that contains TNPO1, RAN and RANBP1. Identified in a
complex that contains CSE1L, KPNA2, RAN and RANBP1 (By
similarity). Identified in a complex with nucleotide-free RAN and
RCC1 (PubMed:7882974, PubMed:7616957).
{ECO:0000250|UniProtKB:P34022, ECO:0000269|PubMed:11832950,
ECO:0000269|PubMed:16428860, ECO:0000269|PubMed:7616957,
ECO:0000269|PubMed:7882974, ECO:0000269|PubMed:7891706,
ECO:0000269|PubMed:8896452}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P43487-1; Sequence=Displayed;
Name=2;
IsoId=P43487-2; Sequence=VSP_055104;
-!- SIMILARITY: Belongs to the RANBP1 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X83617; CAA58592.1; -; mRNA.
EMBL; D38076; BAA07269.1; -; mRNA.
EMBL; CR456556; CAG30442.1; -; mRNA.
EMBL; AK223506; BAD97226.1; -; mRNA.
EMBL; AC006547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS13775.1; -. [P43487-1]
CCDS; CCDS63408.1; -. [P43487-2]
PIR; S54290; S54290.
RefSeq; NP_001265568.1; NM_001278639.1.
RefSeq; NP_001265569.1; NM_001278640.1. [P43487-2]
RefSeq; NP_002873.1; NM_002882.3. [P43487-1]
UniGene; Hs.24763; -.
PDB; 1K5D; X-ray; 2.70 A; B/E/H/K=1-201.
PDB; 1K5G; X-ray; 3.10 A; B/E/H/K=1-201.
PDBsum; 1K5D; -.
PDBsum; 1K5G; -.
ProteinModelPortal; P43487; -.
SMR; P43487; -.
BioGrid; 111838; 45.
CORUM; P43487; -.
DIP; DIP-35058N; -.
IntAct; P43487; 22.
MINT; P43487; -.
STRING; 9606.ENSP00000327583; -.
iPTMnet; P43487; -.
PhosphoSitePlus; P43487; -.
SwissPalm; P43487; -.
BioMuta; RANBP1; -.
DOSAC-COBS-2DPAGE; P43487; -.
OGP; P43487; -.
REPRODUCTION-2DPAGE; IPI00414127; -.
EPD; P43487; -.
MaxQB; P43487; -.
PaxDb; P43487; -.
PeptideAtlas; P43487; -.
PRIDE; P43487; -.
ProteomicsDB; 55636; -.
TopDownProteomics; P43487-1; -. [P43487-1]
DNASU; 5902; -.
Ensembl; ENST00000331821; ENSP00000327583; ENSG00000099901. [P43487-1]
Ensembl; ENST00000402752; ENSP00000384925; ENSG00000099901. [P43487-2]
GeneID; 5902; -.
KEGG; hsa:5902; -.
UCSC; uc002zro.3; human. [P43487-1]
CTD; 5902; -.
DisGeNET; 5902; -.
EuPathDB; HostDB:ENSG00000099901.16; -.
GeneCards; RANBP1; -.
HGNC; HGNC:9847; RANBP1.
HPA; HPA065868; -.
HPA; HPA065931; -.
MIM; 601180; gene.
neXtProt; NX_P43487; -.
OpenTargets; ENSG00000099901; -.
PharmGKB; PA34206; -.
eggNOG; KOG0864; Eukaryota.
eggNOG; COG5171; LUCA.
GeneTree; ENSGT00900000141073; -.
HOGENOM; HOG000176323; -.
HOVERGEN; HBG006958; -.
InParanoid; P43487; -.
KO; K15306; -.
PhylomeDB; P43487; -.
Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
ChiTaRS; RANBP1; human.
EvolutionaryTrace; P43487; -.
GeneWiki; RANBP1; -.
GenomeRNAi; 5902; -.
PRO; PR:P43487; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000099901; Expressed in 142 organ(s), highest expression level in right testis.
CleanEx; HS_RANBP1; -.
ExpressionAtlas; P43487; baseline and differential.
Genevisible; P43487; HS.
GO; GO:0005813; C:centrosome; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005635; C:nuclear envelope; TAS:Reactome.
GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0005092; F:GDP-dissociation inhibitor activity; IMP:GO_Central.
GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
GO; GO:0008536; F:Ran GTPase binding; IBA:GO_Central.
GO; GO:0046907; P:intracellular transport; IEA:InterPro.
GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
GO; GO:0016032; P:viral process; TAS:Reactome.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR000156; Ran_bind_dom.
Pfam; PF00638; Ran_BP1; 1.
SMART; SM00160; RanBD; 1.
PROSITE; PS50196; RANBD1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; GTPase activation; Isopeptide bond;
Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 201 Ran-specific GTPase-activating protein.
/FTId=PRO_0000213667.
DOMAIN 26 164 RanBD1. {ECO:0000255|PROSITE-
ProRule:PRU00164}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 13 13 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 18 18 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 150 150 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 150 150 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P34022}.
MOD_RES 183 183 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 190 190 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 169 169 Missing (in isoform 2).
{ECO:0000303|PubMed:7616957,
ECO:0000303|Ref.4}.
/FTId=VSP_055104.
VARIANT 16 16 E -> D (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036567.
VARIANT 145 145 A -> V (in dbSNP:rs5746863).
/FTId=VAR_053629.
CONFLICT 61 61 E -> V (in Ref. 5; BAD97226).
{ECO:0000305}.
STRAND 48 58 {ECO:0000244|PDB:1K5D}.
STRAND 67 79 {ECO:0000244|PDB:1K5D}.
STRAND 81 83 {ECO:0000244|PDB:1K5D}.
STRAND 86 92 {ECO:0000244|PDB:1K5D}.
TURN 93 95 {ECO:0000244|PDB:1K5D}.
STRAND 98 103 {ECO:0000244|PDB:1K5D}.
STRAND 117 127 {ECO:0000244|PDB:1K5D}.
STRAND 134 141 {ECO:0000244|PDB:1K5D}.
HELIX 145 165 {ECO:0000244|PDB:1K5D}.
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


Related products :

Catalog number Product name Quantity
EIAAB33748 HpaII tiny fragments locus 9a protein,Htf9a,Htf9-a,Mouse,Mus musculus,Ran-binding protein 1,RANBP1,Ranbp1,Ran-specific GTPase-activating protein
EIAAB33749 Homo sapiens,Human,Ran-binding protein 1,RanBP1,RANBP1,Ran-specific GTPase-activating protein
EIAAB33747 Bos taurus,Bovine,Ran-binding protein 1,RanBP1,RANBP1,Ran-specific GTPase-activating protein
CSB-EL019308MO Mouse Ran-specific GTPase-activating protein(RANBP1) ELISA kit 96T
G6251 Ran-specific GTPase-activating protein (RANBP1), Mouse, ELISA Kit 96T
CSB-EL019308BO Bovine Ran-specific GTPase-activating protein(RANBP1) ELISA kit 96T
G6249 Ran-specific GTPase-activating protein (RANBP1), Bovine, ELISA Kit 96T
G6250 Ran-specific GTPase-activating protein (RANBP1), Human, ELISA Kit 96T
CSB-EL019308HU Human Ran-specific GTPase-activating protein(RANBP1) ELISA kit 96T
EIAAB34717 Arhgap32,Brain-specific Rho GTPase-activating protein,GAB-associated Cdc42_Rac GTPase-activating protein,GC-GAP,Grit,Kiaa0712,Mouse,Mus musculus,p200RhoGAP,p250GAP,Rho GTPase-activating protein 32,Rho
CSB-EL019308MO Mouse Ran-specific GTPase-activating protein(RANBP1) ELISA kit SpeciesMouse 96T
CSB-EL019308HU Human Ran-specific GTPase-activating protein(RANBP1) ELISA kit SpeciesHuman 96T
CSB-EL019308BO Bovine Ran-specific GTPase-activating protein(RANBP1) ELISA kit SpeciesBovine 96T
RANG_HUMAN ELISA Kit FOR Ran-specific GTPase-activating protein; organism: Human; gene name: RANBP1 96T
RANG_MOUSE ELISA Kit FOR Ran-specific GTPase-activating protein; organism: Mouse; gene name: Ranbp1 96T
EIAAB34654 ARHGAP1,CDC42 GTPase-activating protein,CDC42GAP,GTPase-activating protein rhoOGAP,Homo sapiens,Human,p50-RhoGAP,Rho GTPase-activating protein 1,RHOGAP1,Rho-related small GTPase protein activator,Rho-
EIAAB34716 ARHGAP32,Brain-specific Rho GTPase-activating protein,GAB-associated Cdc42_Rac GTPase-activating protein,GC-GAP,GRIT,GTPase regulator interacting with TrkA,Homo sapiens,Human,KIAA0712,p200RhoGAP,p250G
EIAAB34719 ARHGAP33,Homo sapiens,Human,Rho GTPase-activating protein 33,Rho-type GTPase-activating protein 33,SNX26,Sorting nexin-26,Tc10_CDC42 GTPase-activating protein,TCGAP
EIAAB34718 Arhgap33,Mouse,Mus musculus,Rho GTPase-activating protein 33,Rho-type GTPase-activating protein 33,Snx26,Sorting nexin-26,Tc10_CDC42 GTPase-activating protein,Tcgap
EIAAB34703 Arhgap27,Camgap1,CIN85-associated multi-domain-containing Rho GTPase-activating protein 1,Mouse,Mus musculus,Rho GTPase-activating protein 27,Rho-type GTPase-activating protein 27
EIAAB34705 Arhgap27,Camgap1,CIN85-associated multi-domain-containing Rho GTPase-activating protein 1,Rat,Rattus norvegicus,Rho GTPase-activating protein 27,Rho-type GTPase-activating protein 27
EIAAB34690 ARHGAP10,ARHGAP21,Homo sapiens,Human,KIAA1424,Rho GTPase-activating protein 10,Rho GTPase-activating protein 21,Rho-type GTPase-activating protein 21
EIAAB34689 Arhgap10,Arhgap21,Kiaa1424,Mouse,Mus musculus,Rho GTPase-activating protein 10,Rho GTPase-activating protein 21,Rho-type GTPase-activating protein 21
EIAAB34704 ARHGAP27,CAMGAP1,CIN85-associated multi-domain-containing Rho GTPase-activating protein 1,Homo sapiens,Human,PP905,Rho GTPase-activating protein 27,Rho-type GTPase-activating protein 27,SH3 domain-con
EIAAB34669 ARHGAP10,GRAF2,Graf-related protein 2,GTPase regulator associated with focal adhesion kinase 2,Homo sapiens,Human,Rho GTPase-activating protein 10,Rho-type GTPase-activating protein 10


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur