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

Beta-chimaerin (Beta-chimerin) (Rho GTPase-activating protein 3)

 CHIO_HUMAN              Reviewed;         468 AA.
P52757; A4D1A2; B3VCF1; B3VCF2; B3VCF3; B3VCF7; B3VCG1; C9J7B0;
E9PGE0; F8QPL9; Q2M203; Q75MM2;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
18-JUL-2018, entry version 183.
RecName: Full=Beta-chimaerin;
AltName: Full=Beta-chimerin;
AltName: Full=Rho GTPase-activating protein 3;
Name=CHN2; Synonyms=ARHGAP3, BCH;
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 BETA-2).
TISSUE=Cerebellum;
PubMed=8175705;
Leung T., How B.-E., Manser E., Lim L.;
"Cerebellar beta 2-chimaerin, a GTPase-activating protein for p21 ras-
related rac is specifically expressed in granule cells and has a
unique N-terminal SH2 domain.";
J. Biol. Chem. 269:12888-12892(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2).
TISSUE=Fetal brain;
PubMed=7614486;
Yuan S., Miller D.W., Barnett G.H., Hahn J.F., Williams B.R.G.;
"Identification and characterization of human beta 2-chimaerin:
association with malignant transformation in astrocytoma.";
Cancer Res. 55:3456-3461(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5; 6; 7 AND 8).
Barrio-Real L., Caloca M.J., Gonzalez-Sarmiento R.;
"Identification of new alternative splicing isoforms of beta
chimaerin.";
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-3).
Zubeldia-Brenner L., Leskow F.C.;
"beta3-chimaerin, a novel Rac-GAP.";
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS BETA-2; 3 AND 4), AND
VARIANT ARG-204.
TISSUE=Caudate nucleus, Cerebellum, and Ileal mucosa;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 7-466 IN COMPLEX WITH
PHORBOL-ESTER, AND ENZYME REGULATION.
PubMed=15507211; DOI=10.1016/j.cell.2004.10.012;
Canagarajah B., Leskow F.C., Ho J.Y., Mischak H., Saidi L.F.,
Kazanietz M.G., Hurley J.H.;
"Structural mechanism for lipid activation of the Rac-specific GAP,
beta2-chimaerin.";
Cell 119:407-418(2004).
-!- FUNCTION: GTPase-activating protein for p21-rac. Insufficient
expression of beta-2 chimaerin is expected to lead to higher Rac
activity and could therefore play a role in the progression from
low-grade to high-grade tumors.
-!- ENZYME REGULATION: In the inactive state, the N terminus protrudes
into the active site of the Rho-GAP domain, sterically blocking
Rac binding. Phospholipid binding to the Phorbol-ester/DAG-type
zinc-finger/C1 domain triggers the cooperative dissociation of
these interactions, allowing the N-terminus to move out of the
active site and thereby activating the enzyme.
{ECO:0000269|PubMed:15507211}.
-!- INTERACTION:
O43639:NCK2; NbExp=4; IntAct=EBI-714925, EBI-713635;
P63000:RAC1; NbExp=4; IntAct=EBI-714925, EBI-413628;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane
protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Name=Beta-2;
IsoId=P52757-1; Sequence=Displayed;
Name=Beta-1;
IsoId=P52757-2; Sequence=Not described;
Name=3;
IsoId=P52757-3; Sequence=VSP_046271, VSP_046272;
Note=No experimental confirmation available.;
Name=4; Synonyms=B1-CHNdel ex7p;
IsoId=P52757-4; Sequence=VSP_047600, VSP_047601;
Name=5; Synonyms=B1-CHNdel ex9;
IsoId=P52757-5; Sequence=VSP_046271, VSP_046272, VSP_047602;
Name=6; Synonyms=B1-CHNdel ex7p,11;
IsoId=P52757-6; Sequence=VSP_047600, VSP_047601, VSP_047603;
Name=7;
IsoId=P52757-7; Sequence=VSP_046271, VSP_046272, VSP_047603;
Name=8;
IsoId=P52757-8; Sequence=VSP_053323;
Name=Beta-3;
IsoId=P52757-9; Sequence=VSP_053679;
-!- TISSUE SPECIFICITY: Highest levels in the brain and pancreas. Also
expressed in the heart, placenta, and weakly in the kidney and
liver. Expression is much reduced in the malignant gliomas,
compared to normal brain or low-grade astrocytomas.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; L29126; AAA19191.1; -; mRNA.
EMBL; U07223; AAA16836.1; -; mRNA.
EMBL; U28926; AAA86528.1; -; mRNA.
EMBL; EU732752; ACF04989.1; -; mRNA.
EMBL; EU732753; ACF04990.1; -; mRNA.
EMBL; EU732754; ACF04991.1; -; mRNA.
EMBL; EU732758; ACF04995.1; -; mRNA.
EMBL; EU732762; ACF04999.1; -; mRNA.
EMBL; GQ924106; ADK47390.1; -; mRNA.
EMBL; AK026415; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK313021; BAG35856.1; -; mRNA.
EMBL; AK316030; BAH14401.1; -; mRNA.
EMBL; AC004417; AAC06177.1; -; Genomic_DNA.
EMBL; AC004593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC007096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC007255; AAS07498.1; -; Genomic_DNA.
EMBL; CH236948; EAL24205.1; -; Genomic_DNA.
EMBL; CH471073; EAW93919.1; -; Genomic_DNA.
EMBL; BC112155; AAI12156.1; -; mRNA.
CCDS; CCDS47566.1; -. [P52757-3]
CCDS; CCDS5420.1; -. [P52757-1]
CCDS; CCDS78219.1; -. [P52757-5]
PIR; A53764; A53764.
RefSeq; NP_001035025.1; NM_001039936.2. [P52757-3]
RefSeq; NP_001279998.1; NM_001293069.1. [P52757-9]
RefSeq; NP_001279999.1; NM_001293070.1.
RefSeq; NP_001280000.1; NM_001293071.1.
RefSeq; NP_001280002.1; NM_001293073.1. [P52757-4]
RefSeq; NP_001280004.1; NM_001293075.1. [P52757-6]
RefSeq; NP_001280005.1; NM_001293076.1. [P52757-5]
RefSeq; NP_001280006.1; NM_001293077.1.
RefSeq; NP_001280007.1; NM_001293078.1.
RefSeq; NP_001280008.1; NM_001293079.1.
RefSeq; NP_001280009.1; NM_001293080.1. [P52757-7]
RefSeq; NP_004058.1; NM_004067.3. [P52757-1]
UniGene; Hs.654611; -.
UniGene; Hs.710429; -.
UniGene; Hs.734596; -.
PDB; 1XA6; X-ray; 3.20 A; A=7-468.
PDBsum; 1XA6; -.
ProteinModelPortal; P52757; -.
SMR; P52757; -.
BioGrid; 107548; 9.
IntAct; P52757; 14.
MINT; P52757; -.
STRING; 9606.ENSP00000222792; -.
BindingDB; P52757; -.
ChEMBL; CHEMBL4504; -.
iPTMnet; P52757; -.
PhosphoSitePlus; P52757; -.
BioMuta; CHN2; -.
DMDM; 2506455; -.
PaxDb; P52757; -.
PeptideAtlas; P52757; -.
PRIDE; P52757; -.
ProteomicsDB; 56529; -.
Ensembl; ENST00000222792; ENSP00000222792; ENSG00000106069. [P52757-1]
Ensembl; ENST00000412711; ENSP00000486515; ENSG00000106069. [P52757-3]
Ensembl; ENST00000421775; ENSP00000394284; ENSG00000106069. [P52757-5]
GeneID; 1124; -.
KEGG; hsa:1124; -.
UCSC; uc003szz.4; human. [P52757-1]
CTD; 1124; -.
DisGeNET; 1124; -.
EuPathDB; HostDB:ENSG00000106069.20; -.
GeneCards; CHN2; -.
HGNC; HGNC:1944; CHN2.
HPA; HPA018989; -.
MIM; 602857; gene.
neXtProt; NX_P52757; -.
OpenTargets; ENSG00000106069; -.
PharmGKB; PA26474; -.
eggNOG; KOG1453; Eukaryota.
eggNOG; ENOG410YM3I; LUCA.
GeneTree; ENSGT00920000148945; -.
HOGENOM; HOG000231926; -.
HOVERGEN; HBG080489; -.
InParanoid; P52757; -.
KO; K20630; -.
OMA; KCEDCGF; -.
OrthoDB; EOG091G0834; -.
PhylomeDB; P52757; -.
TreeFam; TF342052; -.
Reactome; R-HSA-194840; Rho GTPase cycle.
SignaLink; P52757; -.
SIGNOR; P52757; -.
ChiTaRS; CHN2; human.
EvolutionaryTrace; P52757; -.
GeneWiki; Chimerin_2; -.
GenomeRNAi; 1124; -.
PRO; PR:P52757; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000106069; -.
CleanEx; HS_CHN2; -.
ExpressionAtlas; P52757; baseline and differential.
Genevisible; P52757; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005096; F:GTPase activator activity; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
CDD; cd00029; C1; 1.
CDD; cd04372; RhoGAP_chimaerin; 1.
CDD; cd10352; SH2_a2chimerin_b2chimerin; 1.
Gene3D; 1.10.555.10; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR035840; Chimaerin_SH2.
InterPro; IPR017356; CHN1/CHN2.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR037860; RhoGAP_chimaerin.
InterPro; IPR000198; RhoGAP_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
Pfam; PF00130; C1_1; 1.
Pfam; PF00620; RhoGAP; 1.
Pfam; PF00017; SH2; 1.
PIRSF; PIRSF038015; N-chimaerin; 1.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 1.
SMART; SM00324; RhoGAP; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF48350; SSF48350; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50238; RHOGAP; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
GTPase activation; Membrane; Metal-binding; Polymorphism;
Reference proteome; SH2 domain; Zinc; Zinc-finger.
CHAIN 1 468 Beta-chimaerin.
/FTId=PRO_0000056697.
DOMAIN 59 127 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 277 468 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
ZN_FING 214 264 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
VAR_SEQ 1 56 MAASSNSSLSGSSVSSDAEEYQPPIWKSYLYQLQQEAPRPK
RIICPREVENRPKYY -> MFSEELWLENEKKCAVVRKSKQ
GRKRQELLAVAFGVKVGVKGGFLWPPLKLFACSQ (in
isoform 3, isoform 5 and isoform 7).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.3}.
/FTId=VSP_046271.
VAR_SEQ 1 36 MAASSNSSLSGSSVSSDAEEYQPPIWKSYLYQLQQE -> M
FSEELWLENEKKCAVVRKSKQGRKRQELLAVAFGV (in
isoform 4 and isoform 6).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.3}.
/FTId=VSP_047600.
VAR_SEQ 1 15 MAASSNSSLSGSSVS -> MTQTHRAKSASSCPNLLVPETW
PHQVSASHAGRSKQPQGGILKINEEHRRGAIQDLLASPGFT
FGKRVVFDSHCLKRQHTFADGLHSSCT (in isoform
Beta-3). {ECO:0000303|Ref.4}.
/FTId=VSP_053679.
VAR_SEQ 37 217 Missing (in isoform 4 and isoform 6).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.3}.
/FTId=VSP_047601.
VAR_SEQ 49 192 Missing (in isoform 8).
{ECO:0000303|Ref.3}.
/FTId=VSP_053323.
VAR_SEQ 57 192 Missing (in isoform 3, isoform 5 and
isoform 7). {ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.3}.
/FTId=VSP_046272.
VAR_SEQ 247 304 Missing (in isoform 5).
{ECO:0000303|Ref.3}.
/FTId=VSP_047602.
VAR_SEQ 331 377 DGEKADISANVYPDINIITGALKLYFRDLPIPVITYDTYSK
FIDAAK -> E (in isoform 6 and isoform 7).
{ECO:0000303|Ref.3}.
/FTId=VSP_047603.
VARIANT 204 204 H -> R (in dbSNP:rs3750103).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_022118.
VARIANT 438 438 P -> S (in dbSNP:rs34971642).
/FTId=VAR_049136.
CONFLICT 1 6 MAASSN -> MRLL (in Ref. 1; AAA16836/
AAA19191). {ECO:0000305}.
HELIX 29 36 {ECO:0000244|PDB:1XA6}.
STRAND 58 63 {ECO:0000244|PDB:1XA6}.
HELIX 66 73 {ECO:0000244|PDB:1XA6}.
STRAND 79 84 {ECO:0000244|PDB:1XA6}.
STRAND 86 88 {ECO:0000244|PDB:1XA6}.
STRAND 92 98 {ECO:0000244|PDB:1XA6}.
STRAND 101 104 {ECO:0000244|PDB:1XA6}.
STRAND 108 114 {ECO:0000244|PDB:1XA6}.
STRAND 116 118 {ECO:0000244|PDB:1XA6}.
HELIX 125 138 {ECO:0000244|PDB:1XA6}.
HELIX 141 146 {ECO:0000244|PDB:1XA6}.
HELIX 153 155 {ECO:0000244|PDB:1XA6}.
STRAND 156 161 {ECO:0000244|PDB:1XA6}.
TURN 229 231 {ECO:0000244|PDB:1XA6}.
TURN 237 240 {ECO:0000244|PDB:1XA6}.
STRAND 246 248 {ECO:0000244|PDB:1XA6}.
HELIX 255 257 {ECO:0000244|PDB:1XA6}.
TURN 266 269 {ECO:0000244|PDB:1XA6}.
HELIX 279 286 {ECO:0000244|PDB:1XA6}.
HELIX 292 303 {ECO:0000244|PDB:1XA6}.
STRAND 306 308 {ECO:0000244|PDB:1XA6}.
TURN 309 313 {ECO:0000244|PDB:1XA6}.
HELIX 318 328 {ECO:0000244|PDB:1XA6}.
TURN 331 334 {ECO:0000244|PDB:1XA6}.
STRAND 339 342 {ECO:0000244|PDB:1XA6}.
HELIX 346 358 {ECO:0000244|PDB:1XA6}.
HELIX 369 373 {ECO:0000244|PDB:1XA6}.
TURN 374 377 {ECO:0000244|PDB:1XA6}.
HELIX 381 392 {ECO:0000244|PDB:1XA6}.
HELIX 397 405 {ECO:0000244|PDB:1XA6}.
TURN 406 410 {ECO:0000244|PDB:1XA6}.
HELIX 411 414 {ECO:0000244|PDB:1XA6}.
TURN 415 419 {ECO:0000244|PDB:1XA6}.
HELIX 424 431 {ECO:0000244|PDB:1XA6}.
TURN 432 434 {ECO:0000244|PDB:1XA6}.
HELIX 445 448 {ECO:0000244|PDB:1XA6}.
HELIX 450 462 {ECO:0000244|PDB:1XA6}.
HELIX 464 467 {ECO:0000244|PDB:1XA6}.
SEQUENCE 468 AA; 53924 MW; 63254958E0B5804C CRC64;
MAASSNSSLS GSSVSSDAEE YQPPIWKSYL YQLQQEAPRP KRIICPREVE NRPKYYGREF
HGIISREQAD ELLGGVEGAY ILRESQRQPG CYTLALRFGN QTLNYRLFHD GKHFVGEKRF
ESIHDLVTDG LITLYIETKA AEYISKMTTN PIYEHIGYAT LLREKVSRRL SRSKNEPRKT
NVTHEEHTAV EKISSLVRRA ALTHNDNHFN YEKTHNFKVH TFRGPHWCEY CANFMWGLIA
QGVRCSDCGL NVHKQCSKHV PNDCQPDLKR IKKVYCCDLT TLVKAHNTQR PMVVDICIRE
IEARGLKSEG LYRVSGFTEH IEDVKMAFDR DGEKADISAN VYPDINIITG ALKLYFRDLP
IPVITYDTYS KFIDAAKISN ADERLEAVHE VLMLLPPAHY ETLRYLMIHL KKVTMNEKDN
FMNAENLGIV FGPTLMRPPE DSTLTTLHDM RYQKLIVQIL IENEDVLF


Related products :

Catalog number Product name Quantity
EIAAB07171 Arhgap3,Bch,Beta-chimaerin,Beta-chimerin,Chn2,Rat,Rattus norvegicus,Rho GTPase-activating protein 3
EIAAB07173 Arhgap3,Bch,Beta-chimaerin,Beta-chimerin,Chn2,Mouse,Mus musculus,Rho GTPase-activating protein 3
EIAAB07172 ARHGAP3,BCH,Beta-chimaerin,Beta-chimerin,CHN2,Homo sapiens,Human,Rho GTPase-activating protein 3
EIAAB07169 A-chimaerin,Alpha-chimerin,Arhgap2,Chn1,Mouse,Mus musculus,NC,N-chimaerin,N-chimerin,Rho GTPase-activating protein 2
EIAAB07167 A-chimaerin,Alpha-chimerin,Arhgap2,Chn,Chn1,NC,N-chimaerin,N-chimerin,Rat,Rattus norvegicus,Rho GTPase-activating protein 2
EIAAB07168 A-chimaerin,Alpha-chimerin,ARHGAP2,Bos taurus,Bovine,CHN,CHN1,NC,N-chimaerin,N-chimerin,Rho GTPase-activating protein 2
EIAAB07170 A-chimaerin,Alpha-chimerin,ARHGAP2,CHN,CHN1,Homo sapiens,Human,NC,N-chimaerin,N-chimerin,Rho GTPase-activating protein 2
FP-0016 Fusion proteins: Beta-chimaerin (Beta-chimerin), CHN2 10ug
FP-0016 Beta-chimaerin (Beta-chimerin); SH2-Domain: CHN2 10ug
FP-0016 Beta-chimaerin (Beta-chimerin) 10ug
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-
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
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
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
E7606h Human Ral GTPase Activating Protein Beta ELISA Kit 96T
EIAAB34731 ARHGAP42,Homo sapiens,Human,Rho GTPase-activating protein 10-like,Rho GTPase-activating protein 42,Rho-type GTPase-activating protein 42
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
EIAAB34700 ARHGAP26,GRAF,GTPase regulator associated with focal adhesion kinase,Homo sapiens,Human,KIAA0621,Oligophrenin-1-like protein,OPHN1L,Rho GTPase-activating protein 26,Rho-type GTPase-activating protein
RLGPB_MOUSE Mouse ELISA Kit FOR Ral GTPase-activating protein subunit beta 96T
CSB-EL012240HU Human Ral GTPase-activating protein subunit beta(KIAA1219) ELISA kit 96T


 

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 Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | 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

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
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 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
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | 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
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

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