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Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 (Centaurin-beta-1) (Cnt-b1)

 ACAP1_HUMAN             Reviewed;         740 AA.
Q15027; Q53XN9;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 168.
RecName: Full=Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1;
AltName: Full=Centaurin-beta-1;
Short=Cnt-b1;
Name=ACAP1; Synonyms=CENTB1, KIAA0050;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow;
PubMed=7584044; DOI=10.1093/dnares/1.5.223;
Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S.,
Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
"Prediction of the coding sequences of unidentified human genes. II.
The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 1:223-229(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph;
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).
[4]
FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
ARG-448.
PubMed=11062263; DOI=10.1083/jcb.151.3.627;
Jackson T.R., Brown F.D., Nie Z., Miura K., Foroni L., Sun J.,
Hsu V.W., Donaldson J.G., Randazzo P.A.;
"ACAPs are arf6 GTPase-activating proteins that function in the cell
periphery.";
J. Cell Biol. 151:627-638(2000).
[5]
FUNCTION, PHOSPHORYLATION AT SER-554, IDENTIFICATION BY MASS
SPECTROMETRY, INTERACTION WITH ITGB1, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF SER-14; SER-29; SER-277; THR-289; SER-358; THR-389;
THR-461; SER-554; SER-568; THR-711; TYR-712 AND SER-724.
PubMed=16256741; DOI=10.1016/j.devcel.2005.09.012;
Li J., Ballif B.A., Powelka A.M., Dai J., Gygi S.P., Hsu V.W.;
"Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent
recycling of integrin beta1 to control cell migration.";
Dev. Cell 9:663-673(2005).
[6]
NITRATION [LARGE SCALE ANALYSIS] AT TYR-485, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pituitary adenoma;
PubMed=16777052; DOI=10.1016/j.ab.2006.05.024;
Zhan X., Desiderio D.M.;
"Nitroproteins from a human pituitary adenoma tissue discovered with a
nitrotyrosine affinity column and tandem mass spectrometry.";
Anal. Biochem. 354:279-289(2006).
[7]
INTERACTION WITH PHOSPHOLIPIDS, AND MUTAGENESIS OF LYS-274.
PubMed=17010122; DOI=10.1111/j.1600-0854.2006.00480.x;
Shinozaki-Narikawa N., Kodama T., Shibasaki Y.;
"Cooperation of phosphoinositides and BAR domain proteins in endosomal
tubulation.";
Traffic 7:1539-1550(2006).
[8]
FUNCTION, INTERACTION WITH GULP AND ARF6, AND MUTAGENESIS OF ARG-448.
PubMed=17398097; DOI=10.1016/j.cub.2007.03.014;
Ma Z., Nie Z., Luo R., Casanova J.E., Ravichandran K.S.;
"Regulation of Arf6 and ACAP1 signaling by the PTB-domain-containing
adaptor protein GULP.";
Curr. Biol. 17:722-727(2007).
[9]
FUNCTION, AND INTERACTION WITH CLTC.
PubMed=17664335; DOI=10.1083/jcb.200608033;
Li J., Peters P.J., Bai M., Dai J., Bos E., Kirchhausen T.,
Kandror K.V., Hsu V.W.;
"An ACAP1-containing clathrin coat complex for endocytic recycling.";
J. Cell Biol. 178:453-464(2007).
[10]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 378-740 WILD TYPE AND MUTANT
ASP-554 IN COMPLEX WITH ITGB1 PEPTIDE AND ZINC IONS, FUNCTION,
INTERACTION WITH ITGB1, AND MUTAGENESIS OF SER-554.
PubMed=22645133; DOI=10.1074/jbc.M112.378810;
Bai M., Pang X., Lou J., Zhou Q., Zhang K., Ma J., Li J., Sun F.,
Hsu V.W.;
"Mechanistic insights into regulated cargo binding by ACAP1 protein.";
J. Biol. Chem. 287:28675-28685(2012).
[11]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-377, STRUCTURE BY ELECTRON
MICROSCOPY (12.0 ANGSTROMS) OF 1-377, SUBUNIT, BAR DOMAIN, PH DOMAIN,
AND MUTAGENESIS OF PHE-280.
PubMed=25284369; DOI=10.1016/j.devcel.2014.08.020;
Pang X., Fan J., Zhang Y., Zhang K., Gao B., Ma J., Li J., Deng Y.,
Zhou Q., Egelman E.H., Hsu V.W., Sun F.;
"A PH domain in ACAP1 possesses key features of the BAR domain in
promoting membrane curvature.";
Dev. Cell 31:73-86(2014).
[12]
VARIANTS [LARGE SCALE ANALYSIS] ARG-114 AND GLN-129.
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: GTPase-activating protein (GAP) for ADP ribosylation
factor 6 (ARF6) required for clathrin-dependent export of proteins
from recycling endosomes to trans-Golgi network and cell surface.
Required for regulated export of ITGB1 from recycling endosomes to
the cell surface and ITGB1-dependent cell migration.
{ECO:0000269|PubMed:11062263, ECO:0000269|PubMed:16256741,
ECO:0000269|PubMed:17398097, ECO:0000269|PubMed:17664335,
ECO:0000269|PubMed:22645133}.
-!- ENZYME REGULATION: GAP activity stimulated by phosphatidylinositol
4,5-bisphosphate (PIP2) and phosphatidic acid.
{ECO:0000269|PubMed:11062263}.
-!- SUBUNIT: Banana-shaped homodimer laterally assembling into
tetramers, the tetramers further pack helically onto the membrane.
Interacts with GTP-bound ARF6. Interacts with third cytoplasmic
loop of SLC2A4/GLUT4. Interacts with CLTC. Interacts with GULP1.
Forms a complex with GDP-bound ARF6 and GULP1. Interacts with
ITGB1; required for ITGB1 recycling. {ECO:0000269|PubMed:16256741,
ECO:0000269|PubMed:17010122, ECO:0000269|PubMed:17398097,
ECO:0000269|PubMed:17664335, ECO:0000269|PubMed:22645133,
ECO:0000269|PubMed:25284369}.
-!- INTERACTION:
P62993:GRB2; NbExp=3; IntAct=EBI-751746, EBI-401755;
-!- SUBCELLULAR LOCATION: Recycling endosome membrane
{ECO:0000269|PubMed:16256741}; Peripheral membrane protein
{ECO:0000269|PubMed:16256741}; Cytoplasmic side
{ECO:0000269|PubMed:16256741}.
-!- TISSUE SPECIFICITY: Highest level in lung and spleen. Low level in
heart, kidney, liver and pancreas. {ECO:0000269|PubMed:11062263}.
-!- DOMAIN: PH domain binds phospholipids including phosphatidic acid,
phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-
bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate
(PIP3). May mediate ACAP1-binding to PIP2 or PIP3 containing
membranes. Only one PH domain of one ACAP1 dimer inserts into the
membrane, while the other PH domain acts primaryly to interact
with adjacent ACAP1 dimers. {ECO:0000269|PubMed:25284369}.
-!- DOMAIN: The BAR domain mediates homodimerization, it can neither
bind membrane nor impart curvature, but instead requires the
neighboring PH domain to achieve these functions.
{ECO:0000269|PubMed:25284369}.
-!- PTM: Phosphorylation at Ser-554 by PKB is required for interaction
with ITGB1, export of ITGB1 from recycling endosomes to the cell
surface and ITGB1-dependent cell migration.
{ECO:0000269|PubMed:16256741}.
-!- MISCELLANEOUS: Cells overexpressing ACAP1 show an accumulation of
ITGB1 in recycling endosomes and inhibition of stimulation-
dependent cell migration. Cells with reduced levels of ACAP1 or
AKT1 and AKT2 show inhibition of stimulation-dependent cell
migration. Cells overexpressing ACAP1 and PIP5K1C show formation
of tubular structures derived from endosomal membranes.
-!- SEQUENCE CAUTION:
Sequence=BAA06418.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; D30758; BAA06418.2; ALT_INIT; mRNA.
EMBL; BT009788; AAP88790.1; -; mRNA.
EMBL; BC018543; AAH18543.1; -; mRNA.
CCDS; CCDS11101.1; -.
RefSeq; NP_055531.1; NM_014716.3.
UniGene; Hs.337242; -.
PDB; 3JUE; X-ray; 2.30 A; A/B=378-740.
PDB; 3T9K; X-ray; 2.30 A; A/B=378-740.
PDB; 4CKG; EM; 12.00 A; A/B/C/D=1-377.
PDB; 4CKH; EM; 14.00 A; A/B/C/D=1-377.
PDB; 4F1P; X-ray; 2.30 A; A/B=378-740.
PDB; 4NSW; X-ray; 2.20 A; A/B=1-377.
PDBsum; 3JUE; -.
PDBsum; 3T9K; -.
PDBsum; 4CKG; -.
PDBsum; 4CKH; -.
PDBsum; 4F1P; -.
PDBsum; 4NSW; -.
ProteinModelPortal; Q15027; -.
SMR; Q15027; -.
BioGrid; 115092; 7.
CORUM; Q15027; -.
IntAct; Q15027; 8.
MINT; MINT-1446333; -.
STRING; 9606.ENSP00000158762; -.
iPTMnet; Q15027; -.
PhosphoSitePlus; Q15027; -.
BioMuta; ACAP1; -.
DMDM; 3183210; -.
EPD; Q15027; -.
MaxQB; Q15027; -.
PaxDb; Q15027; -.
PeptideAtlas; Q15027; -.
PRIDE; Q15027; -.
DNASU; 9744; -.
Ensembl; ENST00000158762; ENSP00000158762; ENSG00000072818.
GeneID; 9744; -.
KEGG; hsa:9744; -.
UCSC; uc002ggd.3; human.
CTD; 9744; -.
DisGeNET; 9744; -.
EuPathDB; HostDB:ENSG00000072818.11; -.
GeneCards; ACAP1; -.
HGNC; HGNC:16467; ACAP1.
HPA; HPA062130; -.
MIM; 607763; gene.
neXtProt; NX_Q15027; -.
OpenTargets; ENSG00000072818; -.
PharmGKB; PA26406; -.
eggNOG; KOG0521; Eukaryota.
eggNOG; COG5347; LUCA.
GeneTree; ENSGT00760000118874; -.
HOGENOM; HOG000220815; -.
HOVERGEN; HBG050889; -.
InParanoid; Q15027; -.
KO; K12489; -.
OMA; GPPEPMM; -.
OrthoDB; EOG091G029F; -.
PhylomeDB; Q15027; -.
TreeFam; TF318315; -.
SignaLink; Q15027; -.
SIGNOR; Q15027; -.
EvolutionaryTrace; Q15027; -.
GeneWiki; CENTB1; -.
GenomeRNAi; 9744; -.
PRO; PR:Q15027; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000072818; -.
CleanEx; HS_ACAP1; -.
ExpressionAtlas; Q15027; baseline and differential.
Genevisible; Q15027; HS.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
CDD; cd00204; ANK; 1.
Gene3D; 1.20.1270.60; -; 1.
Gene3D; 1.25.40.20; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR027267; AH/BAR-dom.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR001164; ArfGAP.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
Pfam; PF12796; Ank_2; 1.
Pfam; PF01412; ArfGap; 1.
Pfam; PF00169; PH; 1.
PRINTS; PR00405; REVINTRACTNG.
SMART; SM00248; ANK; 3.
SMART; SM00105; ArfGap; 1.
SMART; SM00233; PH; 1.
SUPFAM; SSF103657; SSF103657; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF50729; SSF50729; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 2.
PROSITE; PS50115; ARFGAP; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; ANK repeat; Complete proteome; Endosome;
GTPase activation; Membrane; Metal-binding; Nitration; Phosphoprotein;
Polymorphism; Protein transport; Reference proteome; Repeat;
Transport; Zinc; Zinc-finger.
CHAIN 1 740 Arf-GAP with coiled-coil, ANK repeat and
PH domain-containing protein 1.
/FTId=PRO_0000074209.
DOMAIN 1 226 BAR.
DOMAIN 265 360 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 405 527 Arf-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00288}.
REPEAT 606 635 ANK 1.
REPEAT 639 668 ANK 2.
REPEAT 672 702 ANK 3.
ZN_FING 420 443 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00288}.
REGION 1 382 Required for formation of endosomal
tubules when overexpressed with PIP5K1C.
REGION 405 740 Required for interaction with GULP1.
REGION 525 566 Prevents interaction with ITGB1 when S-
554 is not phosphorylated.
MOD_RES 485 485 Nitrated tyrosine.
{ECO:0000244|PubMed:16777052}.
MOD_RES 554 554 Phosphoserine; by PKB.
{ECO:0000269|PubMed:16256741}.
VARIANT 68 68 R -> C (in dbSNP:rs35933585).
/FTId=VAR_048328.
VARIANT 114 114 K -> R (in a breast cancer sample;
somatic mutation; dbSNP:rs759855054).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036178.
VARIANT 129 129 R -> Q (in a colorectal cancer sample;
somatic mutation; dbSNP:rs754740225).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036179.
VARIANT 533 533 R -> W (in dbSNP:rs35019942).
/FTId=VAR_048329.
MUTAGEN 14 14 S->A: No effect on interaction with
ITGB1. {ECO:0000269|PubMed:16256741}.
MUTAGEN 29 29 S->A: No effect on interaction with
ITGB1. {ECO:0000269|PubMed:16256741}.
MUTAGEN 274 274 K->N: Loss of binding to PIP2 and PIP3.
Loss of association with endosomal
tubules when coexpressed with PIP5K1C.
{ECO:0000269|PubMed:17010122}.
MUTAGEN 277 277 S->A: No effect on interaction with
ITGB1. {ECO:0000269|PubMed:16256741}.
MUTAGEN 280 280 F->A: Reduced membrane binding and
ability to induce liposome tubulation.
{ECO:0000269|PubMed:25284369}.
MUTAGEN 280 280 F->E: Almost abolishes membrane binding.
{ECO:0000269|PubMed:25284369}.
MUTAGEN 280 280 F->W: Preserves membrane binding and
ability to tubulate liposomes.
{ECO:0000269|PubMed:25284369}.
MUTAGEN 289 289 T->A: No effect on interaction with
ITGB1. {ECO:0000269|PubMed:16256741}.
MUTAGEN 358 358 S->A: No effect on interaction with
ITGB1. {ECO:0000269|PubMed:16256741}.
MUTAGEN 389 389 T->A: No effect on interaction with
ITGB1. {ECO:0000269|PubMed:16256741}.
MUTAGEN 448 448 R->Q: Loss of GAP activity. No effect on
GULP1 binding or association with
endosomal tubules when coexpressed with
PIP5K1C. {ECO:0000269|PubMed:11062263,
ECO:0000269|PubMed:17398097}.
MUTAGEN 461 461 T->A: No effect on interaction with
ITGB1. {ECO:0000269|PubMed:16256741}.
MUTAGEN 554 554 S->A: Loss of phosphorylation by PKB,
interaction with ITGB1 and ITGB1-
dependent cell migration.
{ECO:0000269|PubMed:16256741,
ECO:0000269|PubMed:22645133}.
MUTAGEN 554 554 S->D: Enhances interaction with ITGB1.
{ECO:0000269|PubMed:16256741,
ECO:0000269|PubMed:22645133}.
MUTAGEN 568 568 S->A: No effect on interaction with
ITGB1. {ECO:0000269|PubMed:16256741}.
MUTAGEN 711 711 T->A: No effect on interaction with
ITGB1. {ECO:0000269|PubMed:16256741}.
MUTAGEN 712 712 Y->F: No effect on interaction with
ITGB1. {ECO:0000269|PubMed:16256741}.
MUTAGEN 724 724 S->A: Loss of phosphorylation at S-554,
interaction with ITGB1 and ITGB1-
dependent cell migration.
{ECO:0000269|PubMed:16256741}.
MUTAGEN 724 724 S->D: Enhances interaction with ITGB1.
{ECO:0000269|PubMed:16256741}.
STRAND 1 4 {ECO:0000244|PDB:4NSW}.
HELIX 7 12 {ECO:0000244|PDB:4NSW}.
HELIX 15 68 {ECO:0000244|PDB:4NSW}.
STRAND 69 71 {ECO:0000244|PDB:4NSW}.
HELIX 74 113 {ECO:0000244|PDB:4NSW}.
HELIX 115 117 {ECO:0000244|PDB:4NSW}.
HELIX 118 143 {ECO:0000244|PDB:4NSW}.
HELIX 149 212 {ECO:0000244|PDB:4NSW}.
HELIX 214 248 {ECO:0000244|PDB:4NSW}.
STRAND 258 260 {ECO:0000244|PDB:4NSW}.
STRAND 263 265 {ECO:0000244|PDB:4NSW}.
STRAND 267 275 {ECO:0000244|PDB:4NSW}.
TURN 277 279 {ECO:0000244|PDB:4NSW}.
STRAND 283 291 {ECO:0000244|PDB:4NSW}.
STRAND 294 303 {ECO:0000244|PDB:4NSW}.
STRAND 306 310 {ECO:0000244|PDB:4NSW}.
HELIX 312 314 {ECO:0000244|PDB:4NSW}.
STRAND 315 319 {ECO:0000244|PDB:4NSW}.
STRAND 323 325 {ECO:0000244|PDB:4NSW}.
STRAND 328 335 {ECO:0000244|PDB:4NSW}.
STRAND 337 341 {ECO:0000244|PDB:4NSW}.
HELIX 345 361 {ECO:0000244|PDB:4NSW}.
HELIX 407 412 {ECO:0000244|PDB:3JUE}.
TURN 415 418 {ECO:0000244|PDB:3JUE}.
TURN 421 423 {ECO:0000244|PDB:3JUE}.
STRAND 430 432 {ECO:0000244|PDB:3JUE}.
TURN 433 436 {ECO:0000244|PDB:3JUE}.
STRAND 437 439 {ECO:0000244|PDB:3JUE}.
HELIX 441 450 {ECO:0000244|PDB:3JUE}.
TURN 452 454 {ECO:0000244|PDB:3JUE}.
STRAND 457 459 {ECO:0000244|PDB:3JUE}.
TURN 460 462 {ECO:0000244|PDB:3JUE}.
HELIX 467 475 {ECO:0000244|PDB:3JUE}.
HELIX 478 485 {ECO:0000244|PDB:3JUE}.
TURN 486 493 {ECO:0000244|PDB:3JUE}.
HELIX 503 514 {ECO:0000244|PDB:3JUE}.
HELIX 571 578 {ECO:0000244|PDB:3JUE}.
STRAND 580 582 {ECO:0000244|PDB:3JUE}.
HELIX 585 593 {ECO:0000244|PDB:3JUE}.
TURN 603 606 {ECO:0000244|PDB:3JUE}.
HELIX 610 616 {ECO:0000244|PDB:3JUE}.
HELIX 620 628 {ECO:0000244|PDB:3JUE}.
HELIX 643 650 {ECO:0000244|PDB:3JUE}.
HELIX 653 661 {ECO:0000244|PDB:3JUE}.
HELIX 676 682 {ECO:0000244|PDB:3JUE}.
HELIX 686 696 {ECO:0000244|PDB:3JUE}.
HELIX 713 720 {ECO:0000244|PDB:3T9K}.
SEQUENCE 740 AA; 81536 MW; 64891DA3CE00189C CRC64;
MTVKLDFEEC LKDSPRFRAS IELVEAEVSE LETRLEKLLK LGTGLLESGR HYLAASRAFV
VGICDLARLG PPEPMMAECL EKFTVSLNHK LDSHAELLDA TQHTLQQQIQ TLVKEGLRGF
REARRDFWRG AESLEAALTH NAEVPRRRAQ EAEEAGAALR TARAGYRGRA LDYALQINVI
EDKRKFDIME FVLRLVEAQA THFQQGHEEL SRLSQYRKEL GAQLHQLVLN SAREKRDMEQ
RHVLLKQKEL GGEEPEPSLR EGPGGLVMEG HLFKRASNAF KTWSRRWFTI QSNQLVYQKK
YKDPVTVVVD DLRLCTVKLC PDSERRFCFE VVSTSKSCLL QADSERLLQL WVSAVQSSIA
SAFSQARLDD SPRGPGQGSG HLAIGSAATL GSGGMARGRE PGGVGHVVAQ VQSVDGNAQC
CDCREPAPEW ASINLGVTLC IQCSGIHRSL GVHFSKVRSL TLDSWEPELV KLMCELGNVI
INQIYEARVE AMAVKKPGPS CSRQEKEAWI HAKYVEKKFL TKLPEIRGRR GGRGRPRGQP
PVPPKPSIRP RPGSLRSKPE PPSEDLGSLH PGALLFRASG HPPSLPTMAD ALAHGADVNW
VNGGQDNATP LIQATAANSL LACEFLLQNG ANVNQADSAG RGPLHHATIL GHTGLACLFL
KRGADLGARD SEGRDPLTIA METANADIVT LLRLAKMREA EAAQGQAGDE TYLDIFRDFS
LMASDDPEKL SRRSHDLHTL


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EIAAB06030 CCDC86,Coiled-coil domain-containing protein 86,CYCLON,Cytokine-induced protein with coiled-coil domain,Homo sapiens,Human
EIAAB06029 Ccdc86,Coiled-coil domain-containing protein 86,Cyclon,Cytokine-induced protein with coiled-coil domain,Rat,Rattus norvegicus
CSB-EL001132RA Rat Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2(ACAP2) ELISA kit 96T
ACAP1_MOUSE Mouse ELISA Kit FOR Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 96T
EIAAB41359 Homo sapiens,Human,KIAA1728,Protein TANC1,TANC1,Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1
EIAAB41360 Homo sapiens,Human,KIAA1148,KIAA1636,Protein TANC2,TANC2,Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 2
EIAAB41361 Kiaa1148,Mouse,Mus musculus,Protein TANC2,Tanc2,Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 2
EIAAB41358 Mouse,Mus musculus,Protein TANC1,Tanc1,Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1
CSB-EL001131BO Bovine Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1(ACAP1) ELISA kit 96T
CSB-EL001132MO Mouse Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2(ACAP2) ELISA kit 96T
CSB-EL001131MO Mouse Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1(ACAP1) ELISA kit 96T
CSB-EL001133HU Human Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 3(ACAP3) ELISA kit 96T
CSB-EL001132HU Human Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2(ACAP2) ELISA kit 96T
CSB-EL001131HU Human Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1(ACAP1) ELISA kit 96T
CSB-EL001132RA Rat Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2(ACAP2) ELISA kit SpeciesRat 96T
CSB-EL001132CH Chicken Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2(ACAP2) ELISA kit 96T
CSB-EL001132RB Rabbit Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2(ACAP2) ELISA kit SpeciesRabbit 96T
CSB-EL001132MO Mouse Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2(ACAP2) ELISA kit SpeciesMouse 96T
CSB-EL001131MO Mouse Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1(ACAP1) ELISA kit SpeciesMouse 96T
CSB-EL001131HU Human Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1(ACAP1) ELISA kit SpeciesHuman 96T
CSB-EL001133HU Human Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 3(ACAP3) ELISA kit SpeciesHuman 96T


 

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