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Ras-related protein RABF2b (AtRABF2b) (Ras-related protein Ara-7) (Ras-related protein Rab5B) (AtRab5B)

 RAF2B_ARATH             Reviewed;         200 AA.
Q9SN68;
05-APR-2011, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
20-JUN-2018, entry version 133.
RecName: Full=Ras-related protein RABF2b {ECO:0000303|PubMed:12644670};
Short=AtRABF2b {ECO:0000303|PubMed:12644670};
AltName: Full=Ras-related protein Ara-7 {ECO:0000303|PubMed:11532937};
AltName: Full=Ras-related protein Rab5B {ECO:0000305|PubMed:12644670};
Short=AtRab5B {ECO:0000305|PubMed:12644670};
Name=RABF2B {ECO:0000303|PubMed:12644670};
Synonyms=ARA-7 {ECO:0000303|PubMed:11532937},
RAB5B {ECO:0000305|PubMed:12644670};
OrderedLocusNames=At4g19640 {ECO:0000312|Araport:AT4G19640};
ORFNames=F24J7.190 {ECO:0000312|EMBL:CAA16940.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND MUTAGENESIS OF GLN-69.
PubMed=11532937; DOI=10.1093/emboj/20.17.4730;
Ueda T., Yamaguchi M., Uchimiya H., Nakano A.;
"Ara6, a plant-unique novel type Rab GTPase, functions in the
endocytic pathway of Arabidopsis thaliana.";
EMBO J. 20:4730-4741(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
GENE FAMILY, AND NOMENCLATURE.
PubMed=12644670; DOI=10.1104/pp.013052;
Vernoud V., Horton A.C., Yang Z., Nielsen E.;
"Analysis of the small GTPase gene superfamily of Arabidopsis.";
Plant Physiol. 131:1191-1208(2003).
[6]
SUBCELLULAR LOCATION.
PubMed=15509844; DOI=10.1093/pcp/pch142;
Lee G.J., Sohn E.J., Lee M.H., Hwang I.;
"The Arabidopsis rab5 homologs rha1 and ara7 localize to the
prevacuolar compartment.";
Plant Cell Physiol. 45:1211-1220(2004).
[7]
SUBCELLULAR LOCATION.
PubMed=15608333; DOI=10.1105/tpc.104.027821;
Haupt S., Cowan G.H., Ziegler A., Roberts A.G., Oparka K.J.,
Torrance L.;
"Two plant-viral movement proteins traffic in the endocytic recycling
pathway.";
Plant Cell 17:164-181(2005).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16103374; DOI=10.1073/pnas.0502060102;
Takano J., Miwa K., Yuan L., von Wiren N., Fujiwara T.;
"Endocytosis and degradation of BOR1, a boron transporter of
Arabidopsis thaliana, regulated by boron availability.";
Proc. Natl. Acad. Sci. U.S.A. 102:12276-12281(2005).
[9]
INTERACTION WITH VPS9A, AND INDUCTION.
PubMed=18055610; DOI=10.1105/tpc.107.053876;
Goh T., Uchida W., Arakawa S., Ito E., Dainobu T., Ebine K.,
Takeuchi M., Sato K., Ueda T., Nakano A.;
"VPS9a, the common activator for two distinct types of Rab5 GTPases,
is essential for the development of Arabidopsis thaliana.";
Plant Cell 19:3504-3515(2007).
[10]
DEVELOPMENTAL STAGE.
PubMed=18775970; DOI=10.1104/pp.108.126375;
Wang Y., Zhang W.Z., Song L.F., Zou J.J., Su Z., Wu W.H.;
"Transcriptome analyses show changes in gene expression to accompany
pollen germination and tube growth in Arabidopsis.";
Plant Physiol. 148:1201-1211(2008).
[11]
INTERACTION WITH TCTP1.
PubMed=20736351; DOI=10.1073/pnas.1007926107;
Brioudes F., Thierry A.M., Chambrier P., Mollereau B., Bendahmane M.;
"Translationally controlled tumor protein is a conserved mitotic
growth integrator in animals and plants.";
Proc. Natl. Acad. Sci. U.S.A. 107:16384-16389(2010).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23682115; DOI=10.1093/jxb/ert125;
Jia T., Gao C., Cui Y., Wang J., Ding Y., Cai Y., Ueda T., Nakano A.,
Jiang L.;
"ARA7(Q69L) expression in transgenic Arabidopsis cells induces the
formation of enlarged multivesicular bodies.";
J. Exp. Bot. 64:2817-2829(2013).
[13]
SUBCELLULAR LOCATION.
PubMed=23482856; DOI=10.1105/tpc.112.108829;
Zhou L.Z., Li S., Feng Q.N., Zhang Y.L., Zhao X., Zeng Y.L., Wang H.,
Jiang L., Zhang Y.;
"Protein S-acyl transferase10 is critical for development and salt
tolerance in Arabidopsis.";
Plant Cell 25:1093-1107(2013).
[14]
FUNCTION, INTERACTION WITH MON1, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF SER-24.
PubMed=24824487; DOI=10.1105/tpc.114.123141;
Cui Y., Zhao Q., Gao C., Ding Y., Zeng Y., Ueda T., Nakano A.,
Jiang L.;
"Activation of the Rab7 GTPase by the MON1-CCZ1 complex is essential
for PVC-to-vacuole trafficking and plant growth in Arabidopsis.";
Plant Cell 26:2080-2097(2014).
[15]
FUNCTION, INTERACTION WITH EREX, AND MUTAGENESIS OF SER-24.
PubMed=27288222; DOI=10.1105/tpc.16.00326;
Sakurai H.T., Inoue T., Nakano A., Ueda T.;
"ENDOSOMAL RAB EFFECTOR WITH PX-DOMAIN, an interacting partner of RAB5
GTPases, regulates membrane trafficking to protein storage vacuoles in
Arabidopsis.";
Plant Cell 28:1490-1503(2016).
[16]
SUBCELLULAR LOCATION, AND INTERACTION WITH VPS3.
PubMed=29463724; DOI=10.1073/pnas.1717839115;
Takemoto K., Ebine K., Askani J.C., Krueger F., Gonzalez Z.A., Ito E.,
Goh T., Schumacher K., Nakano A., Ueda T.;
"Distinct sets of tethering complexes, SNARE complexes, and Rab
GTPases mediate membrane fusion at the vacuole in Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 115:E2457-E2466(2018).
[17]
X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 1-179 IN COMPLEX WITH GDP,
INTERACTION WITH VPS9A, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
VAL-19; SER-24; VAL-36; THR-42; GLY-44; ALA-46; PHE-47; TRP-64;
ALA-67; GLN-69; SER-74; LEU-75; MET-78; TYR-79 AND ASN-123.
PubMed=20833725; DOI=10.1074/jbc.M110.152132;
Uejima T., Ihara K., Goh T., Ito E., Sunada M., Ueda T., Nakano A.,
Wakatsuki S.;
"GDP-bound and nucleotide-free intermediates of the guanine nucleotide
exchange in the Rab5.Vps9 system.";
J. Biol. Chem. 285:36689-36697(2010).
[18]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-179.
PubMed=23519409; DOI=10.1107/S0907444912047294;
Uejima T., Ihara K., Sunada M., Kawasaki M., Ueda T., Kato R.,
Nakano A., Wakatsuki S.;
"Direct metal recognition by guanine nucleotide-exchange factor in the
initial step of the exchange reaction.";
Acta Crystallogr. D 69:345-351(2013).
-!- FUNCTION: Endosomal protein that may be involved in endocytosis
(PubMed:16103374). Involved in the trafficking of proteins from
prevacuolar compartments (PVCs) to vacuoles (PubMed:23682115,
PubMed:24824487). May activate the MON1-CCZ1 complex which acts as
guanine nucleotide exchange factors (GEF) for Rab7 protein family,
and serves as a link between Rab5 and Rab7 families in PVCs, and
mediates PVC maturation (PubMed:24824487). Involved in vacuolar
transport of storage proteins with EREX as effector. Regulates
membrane trafficking to protein storage vacuoles (PSVs)
(PubMed:27288222). {ECO:0000269|PubMed:16103374,
ECO:0000269|PubMed:23682115, ECO:0000269|PubMed:24824487,
ECO:0000269|PubMed:27288222}.
-!- ENZYME REGULATION: Regulated by guanine nucleotide exchange
factors (GEFs) which promote the exchange of bound GDP for free
GTP. {ECO:0000305|PubMed:24824487}.
-!- SUBUNIT: Interacts with VPS9A homodimer (PubMed:18055610,
PubMed:20833725). Interacts with TCTP1 (PubMed:20736351).
Interacts with MON1 (PubMed:24824487). Interacts with EREX (via PX
domain) (PubMed:27288222). Binds to VPS3 (PubMed:29463724).
{ECO:0000269|PubMed:18055610, ECO:0000269|PubMed:20736351,
ECO:0000269|PubMed:20833725, ECO:0000269|PubMed:24824487,
ECO:0000269|PubMed:27288222, ECO:0000269|PubMed:29463724}.
-!- SUBCELLULAR LOCATION: Early endosome membrane
{ECO:0000269|PubMed:11532937, ECO:0000269|PubMed:23482856}; Lipid-
anchor {ECO:0000305}. Endosome membrane
{ECO:0000269|PubMed:15608333, ECO:0000269|PubMed:16103374,
ECO:0000269|PubMed:24824487}; Lipid-anchor {ECO:0000305}.
Prevacuolar compartment membrane {ECO:0000269|PubMed:15509844,
ECO:0000269|PubMed:24824487}; Lipid-anchor {ECO:0000305}.
Endosome, multivesicular body membrane
{ECO:0000269|PubMed:23682115}; Lipid-anchor {ECO:0000305}. Cell
membrane {ECO:0000305|PubMed:23519409}; Lipid-anchor
{ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:29463724}.
Note=Strong co-localization with VPS3 and VPS18 in cytoplasmic
puncta. {ECO:0000269|PubMed:29463724}.
-!- TISSUE SPECIFICITY: Expressed in roots and actively dividing
cells. {ECO:0000269|PubMed:11532937}.
-!- DEVELOPMENTAL STAGE: Expressed during pollen germination and
pollen tube growth. {ECO:0000269|PubMed:18775970}.
-!- INDUCTION: Activated by VPS9A. {ECO:0000269|PubMed:18055610}.
-!- MISCELLANEOUS: Over-expression of the constitutively active GTP-
bound mutant of Leu-69 induces the formation of large ring-like
structures of 1-2 micrometers in diameter.
{ECO:0000269|PubMed:23682115}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
{ECO:0000305}.
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EMBL; AB038491; BAB32669.1; -; mRNA.
EMBL; AL021768; CAA16940.1; -; Genomic_DNA.
EMBL; AL161551; CAB78966.1; -; Genomic_DNA.
EMBL; CP002687; AEE84207.1; -; Genomic_DNA.
EMBL; AF370309; AAK44124.1; -; mRNA.
EMBL; AY052670; AAK96574.1; -; mRNA.
EMBL; AY063095; AAL34269.1; -; mRNA.
PIR; T06157; T06157.
RefSeq; NP_193699.1; NM_118084.5.
UniGene; At.2030; -.
PDB; 2EFC; X-ray; 2.09 A; B/D=1-179.
PDB; 2EFD; X-ray; 3.00 A; B/D=1-179.
PDB; 2EFE; X-ray; 2.08 A; B/D=1-179.
PDB; 2EFH; X-ray; 2.10 A; B/D=1-179.
PDB; 4G01; X-ray; 2.20 A; B=1-179.
PDBsum; 2EFC; -.
PDBsum; 2EFD; -.
PDBsum; 2EFE; -.
PDBsum; 2EFH; -.
PDBsum; 4G01; -.
ProteinModelPortal; Q9SN68; -.
SMR; Q9SN68; -.
BioGrid; 12999; 1.
IntAct; Q9SN68; 2.
STRING; 3702.AT4G19640.1; -.
PaxDb; Q9SN68; -.
PRIDE; Q9SN68; -.
EnsemblPlants; AT4G19640.1; AT4G19640.1; AT4G19640.
GeneID; 827706; -.
Gramene; AT4G19640.1; AT4G19640.1; AT4G19640.
KEGG; ath:AT4G19640; -.
Araport; AT4G19640; -.
TAIR; locus:2123010; AT4G19640.
eggNOG; KOG0092; Eukaryota.
eggNOG; ENOG410YCCP; LUCA.
HOGENOM; HOG000233968; -.
InParanoid; Q9SN68; -.
OMA; LIKAKHW; -.
OrthoDB; EOG09360MTI; -.
PhylomeDB; Q9SN68; -.
Reactome; R-ATH-6798695; Neutrophil degranulation.
Reactome; R-ATH-8873719; RAB geranylgeranylation.
Reactome; R-ATH-8876198; RAB GEFs exchange GTP for GDP on RABs.
EvolutionaryTrace; Q9SN68; -.
PRO; PR:Q9SN68; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9SN68; baseline and differential.
Genevisible; Q9SN68; AT.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0005768; C:endosome; IDA:TAIR.
GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
GO; GO:0045324; P:late endosome to vacuole transport; IMP:UniProtKB.
GO; GO:0007033; P:vacuole organization; IMP:UniProtKB.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51419; RAB; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Cytoplasm; Endosome;
GTP-binding; Lipoprotein; Membrane; Nucleotide-binding; Prenylation;
Protein transport; Reference proteome; Transport.
CHAIN 1 200 Ras-related protein RABF2b.
/FTId=PRO_0000406605.
NP_BIND 17 25 GTP. {ECO:0000244|PDB:2EFC,
ECO:0000244|PDB:2EFH,
ECO:0000269|PubMed:20833725}.
NP_BIND 65 69 GTP. {ECO:0000244|PDB:2EFC,
ECO:0000244|PDB:2EFH,
ECO:0000269|PubMed:20833725}.
NP_BIND 123 126 GTP. {ECO:0000244|PDB:2EFC,
ECO:0000244|PDB:2EFH,
ECO:0000269|PubMed:20833725}.
NP_BIND 153 154 GTP. {ECO:0000244|PDB:2EFC,
ECO:0000244|PDB:2EFH,
ECO:0000269|PubMed:20833725}.
MOTIF 39 47 Effector region. {ECO:0000250}.
LIPID 198 198 S-geranylgeranyl cysteine. {ECO:0000250}.
LIPID 199 199 S-geranylgeranyl cysteine. {ECO:0000250}.
MUTAGEN 19 19 V->T: Loss of interaction with VPS9A.
Loss of interaction with MON1. Loss of
interaction with EREX.
{ECO:0000269|PubMed:20833725,
ECO:0000269|PubMed:24824487,
ECO:0000269|PubMed:27288222}.
MUTAGEN 24 24 S->N: Dominant negative (GDP-bound form);
no effect on the interaction with VPS9A.
{ECO:0000269|PubMed:20833725}.
MUTAGEN 36 36 V->P: No effect on the interaction with
VPS9A. {ECO:0000269|PubMed:20833725}.
MUTAGEN 42 42 T->A: No effect on the interaction with
VPS9A. {ECO:0000269|PubMed:20833725}.
MUTAGEN 44 44 G->P: No effect on the interaction with
VPS9A. {ECO:0000269|PubMed:20833725}.
MUTAGEN 46 46 A->D: Loss of interaction with VPS9A.
{ECO:0000269|PubMed:20833725}.
MUTAGEN 47 47 F->A: Loss of interaction with VPS9A.
{ECO:0000269|PubMed:20833725}.
MUTAGEN 64 64 W->A: Loss of interaction with VPS9A.
{ECO:0000269|PubMed:20833725}.
MUTAGEN 67 67 A->G: Loss of interaction with VPS9A.
{ECO:0000269|PubMed:20833725}.
MUTAGEN 69 69 Q->E: Loss of interaction with VPS9A.
{ECO:0000269|PubMed:11532937,
ECO:0000269|PubMed:20833725}.
MUTAGEN 69 69 Q->L: Constitutively active (GTP-bound
form); loss of targeting to plasma
membrane and interaction with VPS9A.
{ECO:0000269|PubMed:11532937,
ECO:0000269|PubMed:20833725}.
MUTAGEN 74 74 S->A: Loss of interaction with VPS9A.
{ECO:0000269|PubMed:20833725}.
MUTAGEN 75 75 L->A: Loss of interaction with VPS9A.
{ECO:0000269|PubMed:20833725}.
MUTAGEN 78 78 M->A: Loss of interaction with VPS9A.
{ECO:0000269|PubMed:20833725}.
MUTAGEN 79 79 Y->A: Loss of interaction with VPS9A.
{ECO:0000269|PubMed:20833725}.
MUTAGEN 123 123 N->I: Blocks nucleotide binding; no
effect on the interaction with VPS9A.
{ECO:0000269|PubMed:20833725}.
STRAND 9 16 {ECO:0000244|PDB:2EFE}.
HELIX 23 32 {ECO:0000244|PDB:2EFE}.
TURN 36 38 {ECO:0000244|PDB:2EFE}.
STRAND 41 43 {ECO:0000244|PDB:4G01}.
STRAND 46 54 {ECO:0000244|PDB:2EFE}.
STRAND 57 65 {ECO:0000244|PDB:2EFE}.
HELIX 70 76 {ECO:0000244|PDB:2EFE}.
HELIX 77 80 {ECO:0000244|PDB:2EFE}.
STRAND 84 91 {ECO:0000244|PDB:2EFE}.
HELIX 95 111 {ECO:0000244|PDB:2EFE}.
STRAND 117 123 {ECO:0000244|PDB:2EFE}.
TURN 128 130 {ECO:0000244|PDB:2EFE}.
HELIX 135 144 {ECO:0000244|PDB:2EFE}.
STRAND 148 151 {ECO:0000244|PDB:2EFE}.
STRAND 154 156 {ECO:0000244|PDB:2EFE}.
HELIX 160 169 {ECO:0000244|PDB:2EFE}.
SEQUENCE 200 AA; 21873 MW; 769F75CFC708C6D0 CRC64;
MAAAGNKSIN AKLVLLGDVG AGKSSLVLRF VKDQFVEFQE STIGAAFFSQ TLAVNDATVK
FEIWDTAGQE RYHSLAPMYY RGAAAAIIVF DVTNQASFER AKKWVQELQA QGNPNMVMAL
AGNKSDLLDA RKVTAEDAQT YAQENGLFFM ETSAKTATNV KEIFYEIARR LPRVQPTENP
TGMVLPDRAM DRAVSSSCCA


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18-003-43154 SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related - SMARCE1-related protein; HMG domain protein HMG20B; Structural DNA-binding protein BRAF35; BRCA2 0.05 mg Aff Pur
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EIAAB33504 Homo sapiens,Human,RAB34,RAB39,RAH,Ras-related protein Rab-34,Ras-related protein Rab-39,Ras-related protein Rah
EIAAB33569 Rab7,Rab7a,Ras-related protein BRL-RAS,Ras-related protein p23,Ras-related protein Rab-7a,Rat,Rattus norvegicus
EIAAB32961 Parathion hydrolase-related protein,Phosphotriesterase-related protein,Pter,Rat,Rattus norvegicus,Resiniferotoxin-binding phosphotriesterase-related protein,Rpr-1
EIAAB30632 Mouse,Mus musculus,Peroxin-5-related protein,Pex2,PEX2-related protein,Pex5l,PEX5-like protein,Pex5r,PEX5-related protein,Pex5Rp,Pxr2
20-272-191608 Tyrosinase Related Protein 75 - Mouse monoclonal [3F388] to Tyrosinase Related Protein 75; EC 1.14.18.-; DHICA oxidase; Tyrosinase-related protein 1; TRP-1; TRP1; TRP; Catalase B; Glycoprotein 75; Mel 0.05 ml
EIAAB38042 Frizzled-related protein 1b,FRP1B,FRP-1b,Homo sapiens,Human,SARP3,SARP-3,Secreted apoptosis-related protein 3,Secreted frizzled-related protein 5,SFRP5,sFRP-5
EIAAB46352 Homo sapiens,Human,PP10631,WAS_WASL-interacting protein family member 2,WASP-interacting protein-related protein,WICH,WIP- and CR16-homologous protein,WIPF2,WIP-related protein,WIRE
EIAAB12793 ELK3,ETS domain-containing protein Elk-3,ETS-related protein ERP,ETS-related protein NET,Homo sapiens,Human,NET,SAP2,SAP-2,Serum response factor accessory protein 2,SRF accessory protein 2
EIAAB08778 COX7A2L,COX7AR,COX7a-related protein,COX7RP,Cytochrome c oxidase subunit 7A-related protein, mitochondrial,Cytochrome c oxidase subunit VIIa-related protein,EB1,Homo sapiens,Human
EIAAB29234 Homo sapiens,Human,KIAA0772,ORP2,ORP-2,OSBPL2,OSBP-related protein 2,Oxysterol-binding protein-related protein 2
EIAAB29227 Homo sapiens,Human,ORP10,ORP-10,OSBP9,OSBPL10,OSBP-related protein 10,Oxysterol-binding protein-related protein 10
EIAAB33753 C21KG,G-22K,GTP-binding protein smg p21A,Homo sapiens,Human,KREV1,RAP1A,Ras-related protein Krev-1,Ras-related protein Rap-1A
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EIAAB29244 Homo sapiens,Human,ORP9,ORP-9,OSBP4,OSBPL9,OSBP-related protein 9,Oxysterol-binding protein-related protein 9
EIAAB29236 Homo sapiens,Human,KIAA0704,ORP3,ORP-3,OSBP3,OSBPL3,OSBP-related protein 3,Oxysterol-binding protein-related protein 3
EIAAB29242 Homo sapiens,Human,KIAA1451,ORP8,ORP-8,OSBP10,OSBPL8,OSBP-related protein 8,Oxysterol-binding protein-related protein 8
EIAAB29231 Homo sapiens,Human,ORP1,ORP-1,OSBP8,OSBPL1,OSBPL1A,OSBPL1B,OSBP-related protein 1,Oxysterol-binding protein-related protein 1
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18-003-42229 Hairy_enhancer-of-split related with YRPW motif 1 - Hairy and enhancer of split-related protein 1; HESR-1; Cardiovascular helix-loop-helix factor 2; HES-related repressor protein 2; HERP2 Polyclonal 0.1 mg Protein A
15-288-22161 Hairy_enhancer-of-split related with YRPW motif 1 - Hairy and enhancer of split-related protein 1; HESR-1; Cardiovascular helix-loop-helix factor 2; HES-related repressor protein 2; HERP2 Polyclonal 0.1 mg
EIAAB29230 Mouse,Mus musculus,Orp1,ORP-1,Orp1a,Osbpl1a,OSBP-related protein 1,Oxysterol-binding protein-related protein 1
EIAAB29240 Homo sapiens,Human,ORP6,ORP-6,OSBPL6,OSBP-related protein 6,Oxysterol-binding protein-related protein 6


 

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