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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.
02-JUN-2021, entry version 194.
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, ACTIVITY 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}.
-!- ACTIVITY 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:
Q15027; O94868-3: FCHSD2; NbExp=3; IntAct=EBI-751746, EBI-11958845;
Q15027; P62993: GRB2; NbExp=3; IntAct=EBI-751746, EBI-401755;
Q15027; Q92993: KAT5; NbExp=3; IntAct=EBI-751746, EBI-399080;
Q15027; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-751746, EBI-11742507;
Q15027; O76041: NEBL; NbExp=3; IntAct=EBI-751746, EBI-2880203;
Q15027; P17252: PRKCA; NbExp=3; IntAct=EBI-751746, EBI-1383528;
Q15027; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-751746, EBI-9090795;
Q15027; P14927: UQCRB; NbExp=3; IntAct=EBI-751746, EBI-743128;
Q15027; P22695: UQCRC2; NbExp=3; IntAct=EBI-751746, EBI-1051424;
Q15027; P61981: YWHAG; NbExp=3; IntAct=EBI-751746, EBI-359832;
-!- 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=Extended N-terminus.; 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.
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.
PDB; 5H3D; EM; 14.00 A; A/B/C/D=1-377.
PDBsum; 3JUE; -.
PDBsum; 3T9K; -.
PDBsum; 4CKG; -.
PDBsum; 4CKH; -.
PDBsum; 4F1P; -.
PDBsum; 4NSW; -.
PDBsum; 5H3D; -.
SMR; Q15027; -.
BioGRID; 115092; 13.
CORUM; Q15027; -.
IntAct; Q15027; 17.
STRING; 9606.ENSP00000158762; -.
GlyGen; Q15027; 2 sites, 1 O-linked glycan (2 sites).
iPTMnet; Q15027; -.
PhosphoSitePlus; Q15027; -.
BioMuta; ACAP1; -.
DMDM; 3183210; -.
EPD; Q15027; -.
jPOST; Q15027; -.
MassIVE; Q15027; -.
MaxQB; Q15027; -.
PaxDb; Q15027; -.
PeptideAtlas; Q15027; -.
PRIDE; Q15027; -.
ProteomicsDB; 60378; -.
Antibodypedia; 24069; 239 antibodies.
DNASU; 9744; -.
Ensembl; ENST00000158762; ENSP00000158762; ENSG00000072818.
Ensembl; ENST00000672212; ENSP00000499859; ENSG00000288169.
GeneID; 9744; -.
KEGG; hsa:9744; -.
UCSC; uc002ggd.3; human.
CTD; 9744; -.
DisGeNET; 9744; -.
GeneCards; ACAP1; -.
HGNC; HGNC:16467; ACAP1.
HPA; ENSG00000072818; Tissue enhanced (blood, bone marrow, lymphoid tissue).
MIM; 607763; gene.
neXtProt; NX_Q15027; -.
OpenTargets; ENSG00000072818; -.
PharmGKB; PA26406; -.
VEuPathDB; HostDB:ENSG00000072818.11; -.
eggNOG; KOG0521; Eukaryota.
GeneTree; ENSGT00940000160289; -.
HOGENOM; CLU_012513_0_0_1; -.
InParanoid; Q15027; -.
OMA; YALQVNV; -.
OrthoDB; 751525at2759; -.
PhylomeDB; Q15027; -.
TreeFam; TF318315; -.
PathwayCommons; Q15027; -.
SignaLink; Q15027; -.
SIGNOR; Q15027; -.
BioGRID-ORCS; 9744; 4 hits in 991 CRISPR screens.
ChiTaRS; ACAP1; human.
EvolutionaryTrace; Q15027; -.
GeneWiki; CENTB1; -.
GenomeRNAi; 9744; -.
Pharos; Q15027; Tbio.
PRO; PR:Q15027; -.
Proteomes; UP000005640; Chromosome 17.
RNAct; Q15027; protein.
Bgee; ENSG00000072818; Expressed in testis and 221 other tissues.
ExpressionAtlas; Q15027; baseline and differential.
Genevisible; Q15027; HS.
GO; GO:0016020; C:membrane; HDA: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:0043547; P:positive regulation of GTPase activity; IEA:GOC.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
Gene3D; 1.20.1270.60; -; 1.
Gene3D; 1.25.40.20; -; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.40.160; -; 1.
InterPro; IPR027267; AH/BAR_dom_sf.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR037278; ARFGAP/RecO.
InterPro; IPR001164; ArfGAP_dom.
InterPro; IPR038508; ArfGAP_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
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; SSF57863; SSF57863; 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; Endosome; GTPase activation; Membrane;
Metal-binding; Nitration; Phosphoprotein; Protein transport;
Reference proteome; Repeat; Transport; Zinc; Zinc-finger.
CHAIN 1..740
/note="Arf-GAP with coiled-coil, ANK repeat and PH domain-
containing protein 1"
/id="PRO_0000074209"
DOMAIN 1..226
/note="BAR"
DOMAIN 265..360
/note="PH"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
DOMAIN 405..527
/note="Arf-GAP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
REPEAT 606..635
/note="ANK 1"
REPEAT 639..668
/note="ANK 2"
REPEAT 672..702
/note="ANK 3"
ZN_FING 420..443
/note="C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
REGION 1..382
/note="Required for formation of endosomal tubules when
overexpressed with PIP5K1C"
REGION 405..740
/note="Required for interaction with GULP1"
REGION 525..581
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 525..566
/note="Prevents interaction with ITGB1 when S-554 is not
phosphorylated"
MOD_RES 485
/note="3'-nitrotyrosine"
/evidence="ECO:0007744|PubMed:16777052"
MOD_RES 554
/note="Phosphoserine; by PKB"
/evidence="ECO:0000269|PubMed:16256741"
VARIANT 68
/note="R -> C (in dbSNP:rs35933585)"
/id="VAR_048328"
VARIANT 114
/note="K -> R (in a breast cancer sample; somatic mutation;
dbSNP:rs759855054)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_036178"
VARIANT 129
/note="R -> Q (in a colorectal cancer sample; somatic
mutation; dbSNP:rs754740225)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_036179"
VARIANT 533
/note="R -> W (in dbSNP:rs35019942)"
/id="VAR_048329"
MUTAGEN 14
/note="S->A: No effect on interaction with ITGB1."
/evidence="ECO:0000269|PubMed:16256741"
MUTAGEN 29
/note="S->A: No effect on interaction with ITGB1."
/evidence="ECO:0000269|PubMed:16256741"
MUTAGEN 274
/note="K->N: Loss of binding to PIP2 and PIP3. Loss of
association with endosomal tubules when coexpressed with
PIP5K1C."
/evidence="ECO:0000269|PubMed:17010122"
MUTAGEN 277
/note="S->A: No effect on interaction with ITGB1."
/evidence="ECO:0000269|PubMed:16256741"
MUTAGEN 280
/note="F->A: Reduced membrane binding and ability to induce
liposome tubulation."
/evidence="ECO:0000269|PubMed:25284369"
MUTAGEN 280
/note="F->E: Almost abolishes membrane binding."
/evidence="ECO:0000269|PubMed:25284369"
MUTAGEN 280
/note="F->W: Preserves membrane binding and ability to
tubulate liposomes."
/evidence="ECO:0000269|PubMed:25284369"
MUTAGEN 289
/note="T->A: No effect on interaction with ITGB1."
/evidence="ECO:0000269|PubMed:16256741"
MUTAGEN 358
/note="S->A: No effect on interaction with ITGB1."
/evidence="ECO:0000269|PubMed:16256741"
MUTAGEN 389
/note="T->A: No effect on interaction with ITGB1."
/evidence="ECO:0000269|PubMed:16256741"
MUTAGEN 448
/note="R->Q: Loss of GAP activity. No effect on GULP1
binding or association with endosomal tubules when
coexpressed with PIP5K1C."
/evidence="ECO:0000269|PubMed:11062263,
ECO:0000269|PubMed:17398097"
MUTAGEN 461
/note="T->A: No effect on interaction with ITGB1."
/evidence="ECO:0000269|PubMed:16256741"
MUTAGEN 554
/note="S->A: Loss of phosphorylation by PKB, interaction
with ITGB1 and ITGB1-dependent cell migration."
/evidence="ECO:0000269|PubMed:16256741,
ECO:0000269|PubMed:22645133"
MUTAGEN 554
/note="S->D: Enhances interaction with ITGB1."
/evidence="ECO:0000269|PubMed:16256741,
ECO:0000269|PubMed:22645133"
MUTAGEN 568
/note="S->A: No effect on interaction with ITGB1."
/evidence="ECO:0000269|PubMed:16256741"
MUTAGEN 711
/note="T->A: No effect on interaction with ITGB1."
/evidence="ECO:0000269|PubMed:16256741"
MUTAGEN 712
/note="Y->F: No effect on interaction with ITGB1."
/evidence="ECO:0000269|PubMed:16256741"
MUTAGEN 724
/note="S->A: Loss of phosphorylation at S-554, interaction
with ITGB1 and ITGB1-dependent cell migration."
/evidence="ECO:0000269|PubMed:16256741"
MUTAGEN 724
/note="S->D: Enhances interaction with ITGB1."
/evidence="ECO:0000269|PubMed:16256741"
STRAND 1..4
/evidence="ECO:0007829|PDB:4NSW"
HELIX 7..12
/evidence="ECO:0007829|PDB:4NSW"
HELIX 15..68
/evidence="ECO:0007829|PDB:4NSW"
STRAND 69..71
/evidence="ECO:0007829|PDB:4NSW"
HELIX 74..113
/evidence="ECO:0007829|PDB:4NSW"
HELIX 115..117
/evidence="ECO:0007829|PDB:4NSW"
HELIX 118..143
/evidence="ECO:0007829|PDB:4NSW"
HELIX 149..212
/evidence="ECO:0007829|PDB:4NSW"
HELIX 214..248
/evidence="ECO:0007829|PDB:4NSW"
STRAND 258..260
/evidence="ECO:0007829|PDB:4NSW"
STRAND 263..265
/evidence="ECO:0007829|PDB:4NSW"
STRAND 267..275
/evidence="ECO:0007829|PDB:4NSW"
TURN 277..279
/evidence="ECO:0007829|PDB:4NSW"
STRAND 283..291
/evidence="ECO:0007829|PDB:4NSW"
STRAND 294..303
/evidence="ECO:0007829|PDB:4NSW"
STRAND 306..310
/evidence="ECO:0007829|PDB:4NSW"
HELIX 312..314
/evidence="ECO:0007829|PDB:4NSW"
STRAND 315..319
/evidence="ECO:0007829|PDB:4NSW"
STRAND 323..325
/evidence="ECO:0007829|PDB:4NSW"
STRAND 328..335
/evidence="ECO:0007829|PDB:4NSW"
STRAND 337..341
/evidence="ECO:0007829|PDB:4NSW"
HELIX 345..361
/evidence="ECO:0007829|PDB:4NSW"
HELIX 407..412
/evidence="ECO:0007829|PDB:3JUE"
TURN 415..418
/evidence="ECO:0007829|PDB:3JUE"
TURN 421..423
/evidence="ECO:0007829|PDB:3JUE"
STRAND 430..432
/evidence="ECO:0007829|PDB:3JUE"
TURN 433..436
/evidence="ECO:0007829|PDB:3JUE"
STRAND 437..439
/evidence="ECO:0007829|PDB:3JUE"
HELIX 441..450
/evidence="ECO:0007829|PDB:3JUE"
TURN 452..454
/evidence="ECO:0007829|PDB:3JUE"
STRAND 457..459
/evidence="ECO:0007829|PDB:3JUE"
TURN 460..462
/evidence="ECO:0007829|PDB:3JUE"
HELIX 467..475
/evidence="ECO:0007829|PDB:3JUE"
HELIX 478..485
/evidence="ECO:0007829|PDB:3JUE"
TURN 486..493
/evidence="ECO:0007829|PDB:3JUE"
HELIX 503..514
/evidence="ECO:0007829|PDB:3JUE"
HELIX 571..578
/evidence="ECO:0007829|PDB:3JUE"
STRAND 580..582
/evidence="ECO:0007829|PDB:3JUE"
HELIX 585..593
/evidence="ECO:0007829|PDB:3JUE"
TURN 603..606
/evidence="ECO:0007829|PDB:3JUE"
HELIX 610..616
/evidence="ECO:0007829|PDB:3JUE"
HELIX 620..628
/evidence="ECO:0007829|PDB:3JUE"
HELIX 643..650
/evidence="ECO:0007829|PDB:3JUE"
HELIX 653..661
/evidence="ECO:0007829|PDB:3JUE"
HELIX 676..682
/evidence="ECO:0007829|PDB:3JUE"
HELIX 686..696
/evidence="ECO:0007829|PDB:3JUE"
HELIX 713..720
/evidence="ECO:0007829|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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EIAAB07128 C9orf49,CHCHD2P9,CHCHD9,Coiled-coil-helix-coiled-coil-helix domain-containing 2 pseudogene 9,Homo sapiens,Human,Putative coiled-coil-helix-coiled-coil-helix domain-containing protein CHCHD2P9, mitocho
EIAAB46890 CCDC131,Coiled-coil domain-containing protein 131,Homo sapiens,Human,KIAA0546,Proline_serine-rich coiled-coil protein 2,PSRC2,ZFC3H1,Zinc finger C3H1 domain-containing protein
EIAAB06031 Ccdc86,Coiled-coil domain-containing protein 86,Cyclon,Cytokine-induced protein with coiled-coil domain,D19Ertd678e,mCyclon,MNCb-4327,Mouse,Mus musculus
EIAAB05828 C6orf184,C6orf185,CCDC162,CCDC162P,Coiled-coil domain-containing protein 162,Coiled-coil domain-containing protein 162 pseudogene,Homo sapiens,Human
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
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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
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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
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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
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Pathways :
WP1689: Porphyrin and chlorophyll metabolism
WP1566: Citrate cycle (TCA cycle)
WP210: Cytoplasmic Ribosomal Proteins
WP2218: sGC
WP1045: TGF-beta Receptor Signaling Pathway
WP1571: EBV LMP1 signaling
WP1835: Interferon alpha/beta signaling
WP258: TGF-beta Receptor Signaling Pathway
WP668: Octadecanoid Pathway
WP1226: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1672: Mismatch repair
WP211: BMP signaling pathway
WP433: tRNA Synthetases
WP763: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1269: Fatty Acid Beta Oxidation
WP1676: Non-homologous end-joining
WP2199: Seed Development
WP471: Beta Oxidation of Unsaturated Fatty Acids
WP105: Fatty Acid Beta Oxidation 2
WP1616: ABC transporters
WP1892: Protein folding
WP305: Glucocorticoid Metabolism
WP1106: Keap1-Nrf2
WP1628: beta-Alanine metabolism
WP1909: Signal regulatory protein (SIRP) family interactions

Related Genes :
[ACAP1 CENTB1 KIAA0050] Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 (Centaurin-beta-1) (Cnt-b1)
[AGAP3 CENTG3] Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 3 (AGAP-3) (CRAM-associated GTPase) (CRAG) (Centaurin-gamma-3) (Cnt-g3) (MR1-interacting protein) (MRIP-1)
[Acap1 Centb1 Kiaa0050] Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 (Centaurin-beta-1) (Cnt-b1)
[Asap1 Ddef1 Kiaa1249 Shag1] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
[ASAP1 DDEF1 KIAA1249 PAG2] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
[ACAP1 CENTB1] Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 (Centaurin-beta-1) (Cnt-b1)
[Asap1 Ddef1] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
[ASAP1 DDEF1] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
[HUWE1 KIAA0312 KIAA1578 UREB1 HSPC272] E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26) (ARF-binding protein 1) (ARF-BP1) (HECT, UBA and WWE domain-containing protein 1) (HECT-type E3 ubiquitin transferase HUWE1) (Homologous to E6AP carboxyl terminus homologous protein 9) (HectH9) (Large structure of UREB1) (LASU1) (Mcl-1 ubiquitin ligase E3) (Mule) (Upstream regulatory element-binding protein 1) (URE-B1) (URE-binding protein 1)
[AGD3 FKD2 SFC VAN3 At5g13300 T31B5.120] ADP-ribosylation factor GTPase-activating protein AGD3 (ARF GAP AGD3) (Protein ARF-GAP DOMAIN 3) (AtAGD3) (Protein FORKED 2) (Protein SCARFACE) (Protein VASCULAR NETWORK 3)
[AGD1 At5g61980 K22G18.9] ADP-ribosylation factor GTPase-activating protein AGD1 (ARF GAP AGD1) (Protein ARF-GAP DOMAIN 1) (AtAGD1)
[Sh2b1 Sh2bpsm1] SH2B adapter protein 1 (Pro-rich, PH and SH2 domain-containing signaling mediator) (PSM) (SH2 domain-containing protein 1B) (SH2-B PH domain-containing signaling mediator 1)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[AGFG1 HRB RAB RIP] Arf-GAP domain and FG repeat-containing protein 1 (HIV-1 Rev-binding protein) (Nucleoporin-like protein RIP) (Rev-interacting protein) (Rev/Rex activation domain-binding protein)
[] Capsid protein VP0 (EC 2.7.7.48) (EC 3.4.22.28) (EC 3.4.22.46) (EC 3.6.1.15) (Capsid protein VP1) (Capsid protein VP3) (Capsid protein VP4) (Genome polyprotein) (Genome-linked protein VPg1) (Genome-linked protein VPg2) (Genome-linked protein VPg3) (Leader protease) (P1A) (P1B) (P1C) (P1D) (P52) (P56A) (Picornain 3C) (Protease 3C) (Protease P20B) (Protein 2A) (Protein 2C) (Protein 3A) (Protein 3B-1) (Protein 3B-2) (Protein 3B-3) (RNA-directed RNA polymerase 3D-POL) (VP4-VP2) (Virion protein 1) (Virion protein 2) (Virion protein 3) (Virion protein 4) (protein 2B)
[SH2B1 KIAA1299 SH2B] SH2B adapter protein 1 (Pro-rich, PH and SH2 domain-containing signaling mediator) (PSM) (SH2 domain-containing protein 1B)
[Pafah1b1 Lis-1 Lis1 Pafaha] Platelet-activating factor acetylhydrolase IB subunit beta (Lissencephaly-1 protein) (LIS-1) (PAF acetylhydrolase 45 kDa subunit) (PAF-AH 45 kDa subunit) (PAF-AH alpha) (PAFAH alpha)
[Sh2b1 Sh2-b Sh2bpsm1] SH2B adapter protein 1 (FceRI gamma-chain-interacting protein SH2-B) (SH2 domain-containing protein 1B) (SH2-B PH domain-containing signaling mediator 1)
[Pre C,C C core E PC pre-C pre-C/C PreC preC PreC/C preC/C precore-core HBVgp4] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)
[LAMB1] Laminin subunit beta-1 (Laminin B1 chain) (Laminin-1 subunit beta) (Laminin-10 subunit beta) (Laminin-12 subunit beta) (Laminin-2 subunit beta) (Laminin-6 subunit beta) (Laminin-8 subunit beta)
[Agfg1 Hrb Rip] Arf-GAP domain and FG repeat-containing protein 1 (HIV-1 Rev-binding protein homolog) (Nucleoporin-like protein RIP)
[Lamb1 Lamb-1 Lamb1-1] Laminin subunit beta-1 (Laminin B1 chain) (Laminin-1 subunit beta) (Laminin-10 subunit beta) (Laminin-12 subunit beta) (Laminin-2 subunit beta) (Laminin-6 subunit beta) (Laminin-8 subunit beta)
[LAMB3 LAMNB1] Laminin subunit beta-3 (Epiligrin subunit bata) (Kalinin B1 chain) (Kalinin subunit beta) (Laminin B1k chain) (Laminin-5 subunit beta) (Nicein subunit beta)
[S 2] Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Host translation inhibitor nsp1 (Leader protein) (Non-structural protein 1) (nsp1); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL2-PRO) (Papain-like protease) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.69) (Main protease) (Mpro) (Non-structural protein 5) (nsp5) (SARS coronavirus main proteinase); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Non-structural protein 12) (nsp12); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Non-structural protein 13) (nsp13); Proofreading exoribonuclease (ExoN) (EC 3.1.13.-) (Guanine-N7 methyltransferase) (Non-structural protein 14) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (Non-structural protein 15) (nsp15); 2'-O-methyltransferase (EC 2.1.1.-) (Non-structural protein 16) (nsp16)]
[AP2B1 ADTB2 CLAPB1] AP-2 complex subunit beta (AP105B) (Adaptor protein complex AP-2 subunit beta) (Adaptor-related protein complex 2 subunit beta) (Beta-2-adaptin) (Beta-adaptin) (Clathrin assembly protein complex 2 beta large chain) (Plasma membrane adaptor HA2/AP2 adaptin beta subunit)
[GTF2IRD1 CREAM1 GTF3 MUSTRD1 RBAP2 WBSCR11 WBSCR12] General transcription factor II-I repeat domain-containing protein 1 (GTF2I repeat domain-containing protein 1) (General transcription factor III) (MusTRD1/BEN) (Muscle TFII-I repeat domain-containing protein 1) (Slow-muscle-fiber enhancer-binding protein) (USE B1-binding protein) (Williams-Beuren syndrome chromosomal region 11 protein) (Williams-Beuren syndrome chromosomal region 12 protein)
[Rock1 Ac2-154] Rho-associated protein kinase 1 (EC 2.7.11.1) (Liver regeneration-related protein LRRG199) (Rho-associated, coiled-coil-containing protein kinase 1) (Rho-associated, coiled-coil-containing protein kinase I) (ROCK-I) (p150 RhoA-binding kinase ROK beta) (p160 ROCK-1) (p160ROCK)
[Lamb3] Laminin subunit beta-3 (Epiligrin subunit bata) (Kalinin B1 chain) (Kalinin subunit beta) (Laminin-5 subunit beta) (Nicein subunit beta)
[Ap2b1 Clapb1] AP-2 complex subunit beta (AP105B) (Adaptor protein complex AP-2 subunit beta) (Adaptor-related protein complex 2 subunit beta) (Beta-2-adaptin) (Beta-adaptin) (Clathrin assembly protein complex 2 beta large chain) (Plasma membrane adaptor HA2/AP2 adaptin beta subunit)

Bibliography :
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