Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1

Gene

ACAP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.5 Publications

Enzyme regulationi

GAP activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri420 – 44324C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ15027.

Names & Taxonomyi

Protein namesi
Recommended name:
Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1
Alternative name(s):
Centaurin-beta-1
Short name:
Cnt-b1
Gene namesi
Name:ACAP1
Synonyms:CENTB1, KIAA0050
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:16467. ACAP1.

Subcellular locationi

  • Recycling endosome membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

GO - Cellular componenti

  • membrane Source: UniProtKB
  • recycling endosome membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141S → A: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi29 – 291S → A: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi274 – 2741K → N: Loss of binding to PIP2 and PIP3. Loss of association with endosomal tubules when coexpressed with PIP5K1C. 1 Publication
Mutagenesisi277 – 2771S → A: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi280 – 2801F → A: Reduced membrane binding and ability to induce liposome tubulation. 1 Publication
Mutagenesisi280 – 2801F → E: Almost abolishes membrane binding. 1 Publication
Mutagenesisi280 – 2801F → W: Preserves membrane binding and ability to tubulate liposomes. 1 Publication
Mutagenesisi289 – 2891T → A: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi358 – 3581S → A: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi389 – 3891T → A: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi448 – 4481R → Q: Loss of GAP activity. No effect on GULP1 binding or association with endosomal tubules when coexpressed with PIP5K1C. 2 Publications
Mutagenesisi461 – 4611T → A: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi554 – 5541S → A: Loss of phosphorylation by PKB, interaction with ITGB1 and ITGB1-dependent cell migration. 2 Publications
Mutagenesisi554 – 5541S → D: Enhances interaction with ITGB1. 2 Publications
Mutagenesisi568 – 5681S → A: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi711 – 7111T → A: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi712 – 7121Y → F: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi724 – 7241S → A: Loss of phosphorylation at S-554, interaction with ITGB1 and ITGB1-dependent cell migration. 1 Publication
Mutagenesisi724 – 7241S → D: Enhances interaction with ITGB1. 1 Publication

Organism-specific databases

PharmGKBiPA26406.

Polymorphism and mutation databases

BioMutaiACAP1.
DMDMi3183210.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 740740Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1PRO_0000074209Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei485 – 4851Nitrated tyrosine1 Publication
Modified residuei554 – 5541Phosphoserine; by PKB1 Publication

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Nitration, Phosphoprotein

Proteomic databases

MaxQBiQ15027.
PaxDbiQ15027.
PRIDEiQ15027.

PTM databases

PhosphoSiteiQ15027.

Expressioni

Tissue specificityi

Highest level in lung and spleen. Low level in heart, kidney, liver and pancreas.1 Publication

Gene expression databases

BgeeiQ15027.
CleanExiHS_ACAP1.
ExpressionAtlasiQ15027. baseline and differential.
GenevestigatoriQ15027.

Organism-specific databases

HPAiHPA021127.

Interactioni

Subunit structurei

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GRB2P629933EBI-751746,EBI-401755

Protein-protein interaction databases

BioGridi115092. 5 interactions.
IntActiQ15027. 7 interactions.
MINTiMINT-1446333.
STRINGi9606.ENSP00000158762.

Structurei

Secondary structure

740
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 44Combined sources
Helixi7 – 126Combined sources
Helixi15 – 6854Combined sources
Beta strandi69 – 713Combined sources
Helixi74 – 11340Combined sources
Helixi115 – 1173Combined sources
Helixi118 – 14326Combined sources
Helixi149 – 21264Combined sources
Helixi214 – 24835Combined sources
Beta strandi258 – 2603Combined sources
Beta strandi263 – 2653Combined sources
Beta strandi267 – 2759Combined sources
Turni277 – 2793Combined sources
Beta strandi283 – 2919Combined sources
Beta strandi294 – 30310Combined sources
Beta strandi306 – 3105Combined sources
Helixi312 – 3143Combined sources
Beta strandi315 – 3195Combined sources
Beta strandi323 – 3253Combined sources
Beta strandi328 – 3358Combined sources
Beta strandi337 – 3415Combined sources
Helixi345 – 36117Combined sources
Helixi407 – 4126Combined sources
Turni415 – 4184Combined sources
Turni421 – 4233Combined sources
Beta strandi430 – 4323Combined sources
Turni433 – 4364Combined sources
Beta strandi437 – 4393Combined sources
Helixi441 – 45010Combined sources
Turni452 – 4543Combined sources
Beta strandi457 – 4593Combined sources
Turni460 – 4623Combined sources
Helixi467 – 4759Combined sources
Helixi478 – 4858Combined sources
Turni486 – 4938Combined sources
Helixi503 – 51412Combined sources
Helixi571 – 5788Combined sources
Beta strandi580 – 5823Combined sources
Helixi585 – 5939Combined sources
Turni603 – 6064Combined sources
Helixi610 – 6167Combined sources
Helixi620 – 6289Combined sources
Helixi643 – 6508Combined sources
Helixi653 – 6619Combined sources
Helixi676 – 6827Combined sources
Helixi686 – 69611Combined sources
Helixi713 – 7208Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JUEX-ray2.30A/B378-740[»]
3T9KX-ray2.30A/B378-740[»]
4CKGelectron microscopy12.00A/B/C/D1-377[»]
4CKHelectron microscopy14.00A/B/C/D1-377[»]
4F1PX-ray2.30A/B378-740[»]
4NSWX-ray2.20A/B1-377[»]
ProteinModelPortaliQ15027.
SMRiQ15027. Positions 1-364, 405-723.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15027.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 226226BARAdd
BLAST
Domaini265 – 36096PHPROSITE-ProRule annotationAdd
BLAST
Domaini405 – 527123Arf-GAPPROSITE-ProRule annotationAdd
BLAST
Repeati606 – 63530ANK 1Add
BLAST
Repeati639 – 66830ANK 2Add
BLAST
Repeati672 – 70231ANK 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 382382Required for formation of endosomal tubules when overexpressed with PIP5K1CAdd
BLAST
Regioni405 – 740336Required for interaction with GULP1Add
BLAST
Regioni525 – 56642Prevents interaction with ITGB1 when S-554 is not phosphorylatedAdd
BLAST

Domaini

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.1 Publication
The BAR domain mediates homodimerization, it can neither bind membrane nor impart curvature, but instead requires the neighboring PH domain to achieve these functions.1 Publication

Sequence similaritiesi

Contains 3 ANK repeats.PROSITE-ProRule annotation
Contains 1 Arf-GAP domain.PROSITE-ProRule annotation
Contains 1 BAR domain.Curated
Contains 1 PH domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri420 – 44324C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5347.
GeneTreeiENSGT00760000118874.
HOGENOMiHOG000220815.
HOVERGENiHBG050889.
InParanoidiQ15027.
KOiK12489.
OMAiCLDKFTQ.
OrthoDBiEOG7PVWNT.
PhylomeDBiQ15027.
TreeFamiTF318315.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
1.25.40.20. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000909. PLipase_C_PInositol-sp_X_dom.
[Graphical view]
PfamiPF00023. Ank. 2 hits.
PF01412. ArfGap. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSiPR00405. REVINTRACTNG.
SMARTiSM00248. ANK. 3 hits.
SM00105. ArfGap. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50115. ARFGAP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15027-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVKLDFEEC LKDSPRFRAS IELVEAEVSE LETRLEKLLK LGTGLLESGR
60 70 80 90 100
HYLAASRAFV VGICDLARLG PPEPMMAECL EKFTVSLNHK LDSHAELLDA
110 120 130 140 150
TQHTLQQQIQ TLVKEGLRGF REARRDFWRG AESLEAALTH NAEVPRRRAQ
160 170 180 190 200
EAEEAGAALR TARAGYRGRA LDYALQINVI EDKRKFDIME FVLRLVEAQA
210 220 230 240 250
THFQQGHEEL SRLSQYRKEL GAQLHQLVLN SAREKRDMEQ RHVLLKQKEL
260 270 280 290 300
GGEEPEPSLR EGPGGLVMEG HLFKRASNAF KTWSRRWFTI QSNQLVYQKK
310 320 330 340 350
YKDPVTVVVD DLRLCTVKLC PDSERRFCFE VVSTSKSCLL QADSERLLQL
360 370 380 390 400
WVSAVQSSIA SAFSQARLDD SPRGPGQGSG HLAIGSAATL GSGGMARGRE
410 420 430 440 450
PGGVGHVVAQ VQSVDGNAQC CDCREPAPEW ASINLGVTLC IQCSGIHRSL
460 470 480 490 500
GVHFSKVRSL TLDSWEPELV KLMCELGNVI INQIYEARVE AMAVKKPGPS
510 520 530 540 550
CSRQEKEAWI HAKYVEKKFL TKLPEIRGRR GGRGRPRGQP PVPPKPSIRP
560 570 580 590 600
RPGSLRSKPE PPSEDLGSLH PGALLFRASG HPPSLPTMAD ALAHGADVNW
610 620 630 640 650
VNGGQDNATP LIQATAANSL LACEFLLQNG ANVNQADSAG RGPLHHATIL
660 670 680 690 700
GHTGLACLFL KRGADLGARD SEGRDPLTIA METANADIVT LLRLAKMREA
710 720 730 740
EAAQGQAGDE TYLDIFRDFS LMASDDPEKL SRRSHDLHTL
Length:740
Mass (Da):81,536
Last modified:November 1, 1996 - v1
Checksum:i64891DA3CE00189C
GO

Sequence cautioni

The sequence BAA06418.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681R → C.
Corresponds to variant rs35933585 [ dbSNP | Ensembl ].
VAR_048328
Natural varianti114 – 1141K → R in a breast cancer sample; somatic mutation. 1 Publication
VAR_036178
Natural varianti129 – 1291R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036179
Natural varianti533 – 5331R → W.
Corresponds to variant rs35019942 [ dbSNP | Ensembl ].
VAR_048329

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30758 mRNA. Translation: BAA06418.2. Different initiation.
BT009788 mRNA. Translation: AAP88790.1.
BC018543 mRNA. Translation: AAH18543.1.
CCDSiCCDS11101.1.
RefSeqiNP_055531.1. NM_014716.3.
UniGeneiHs.337242.

Genome annotation databases

EnsembliENST00000158762; ENSP00000158762; ENSG00000072818.
GeneIDi9744.
KEGGihsa:9744.
UCSCiuc002ggd.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30758 mRNA. Translation: BAA06418.2. Different initiation.
BT009788 mRNA. Translation: AAP88790.1.
BC018543 mRNA. Translation: AAH18543.1.
CCDSiCCDS11101.1.
RefSeqiNP_055531.1. NM_014716.3.
UniGeneiHs.337242.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JUEX-ray2.30A/B378-740[»]
3T9KX-ray2.30A/B378-740[»]
4CKGelectron microscopy12.00A/B/C/D1-377[»]
4CKHelectron microscopy14.00A/B/C/D1-377[»]
4F1PX-ray2.30A/B378-740[»]
4NSWX-ray2.20A/B1-377[»]
ProteinModelPortaliQ15027.
SMRiQ15027. Positions 1-364, 405-723.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115092. 5 interactions.
IntActiQ15027. 7 interactions.
MINTiMINT-1446333.
STRINGi9606.ENSP00000158762.

PTM databases

PhosphoSiteiQ15027.

Polymorphism and mutation databases

BioMutaiACAP1.
DMDMi3183210.

Proteomic databases

MaxQBiQ15027.
PaxDbiQ15027.
PRIDEiQ15027.

Protocols and materials databases

DNASUi9744.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000158762; ENSP00000158762; ENSG00000072818.
GeneIDi9744.
KEGGihsa:9744.
UCSCiuc002ggd.2. human.

Organism-specific databases

CTDi9744.
GeneCardsiGC17P007239.
HGNCiHGNC:16467. ACAP1.
HPAiHPA021127.
MIMi607763. gene.
neXtProtiNX_Q15027.
PharmGKBiPA26406.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5347.
GeneTreeiENSGT00760000118874.
HOGENOMiHOG000220815.
HOVERGENiHBG050889.
InParanoidiQ15027.
KOiK12489.
OMAiCLDKFTQ.
OrthoDBiEOG7PVWNT.
PhylomeDBiQ15027.
TreeFamiTF318315.

Enzyme and pathway databases

SignaLinkiQ15027.

Miscellaneous databases

EvolutionaryTraceiQ15027.
GeneWikiiCENTB1.
GenomeRNAii9744.
NextBioi36666.
PROiQ15027.
SOURCEiSearch...

Gene expression databases

BgeeiQ15027.
CleanExiHS_ACAP1.
ExpressionAtlasiQ15027. baseline and differential.
GenevestigatoriQ15027.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
1.25.40.20. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000909. PLipase_C_PInositol-sp_X_dom.
[Graphical view]
PfamiPF00023. Ank. 2 hits.
PF01412. ArfGap. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSiPR00405. REVINTRACTNG.
SMARTiSM00248. ANK. 3 hits.
SM00105. ArfGap. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50115. ARFGAP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
    DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    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.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lymph.
  4. "ACAPs are arf6 GTPase-activating proteins that function in the cell periphery."
    Jackson T.R., Brown F.D., Nie Z., Miura K., Foroni L., Sun J., Hsu V.W., Donaldson J.G., Randazzo P.A.
    J. Cell Biol. 151:627-638(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY, MUTAGENESIS OF ARG-448.
  5. "Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent recycling of integrin beta1 to control cell migration."
    Li J., Ballif B.A., Powelka A.M., Dai J., Gygi S.P., Hsu V.W.
    Dev. Cell 9:663-673(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-554, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ITGB1, SUBCELLULAR LOCATION, 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.
  6. "Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry."
    Zhan X., Desiderio D.M.
    Anal. Biochem. 354:279-289(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-485, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pituitary adenoma.
  7. "Cooperation of phosphoinositides and BAR domain proteins in endosomal tubulation."
    Shinozaki-Narikawa N., Kodama T., Shibasaki Y.
    Traffic 7:1539-1550(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PHOSPHOLIPIDS, MUTAGENESIS OF LYS-274.
  8. "Regulation of Arf6 and ACAP1 signaling by the PTB-domain-containing adaptor protein GULP."
    Ma Z., Nie Z., Luo R., Casanova J.E., Ravichandran K.S.
    Curr. Biol. 17:722-727(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GULP AND ARF6, MUTAGENESIS OF ARG-448.
  9. "An ACAP1-containing clathrin coat complex for endocytic recycling."
    Li J., Peters P.J., Bai M., Dai J., Bos E., Kirchhausen T., Kandror K.V., Hsu V.W.
    J. Cell Biol. 178:453-464(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CLTC.
  10. "Mechanistic insights into regulated cargo binding by ACAP1 protein."
    Bai M., Pang X., Lou J., Zhou Q., Zhang K., Ma J., Li J., Sun F., Hsu V.W.
    J. Biol. Chem. 287:28675-28685(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, MUTAGENESIS OF SER-554.
  11. "A PH domain in ACAP1 possesses key features of the BAR domain in promoting membrane curvature."
    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.
    Dev. Cell 31:73-86(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-377, STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS) OF 1-377, SUBUNIT, BAR DOMAIN, PH DOMAIN, MUTAGENESIS OF PHE-280.
  12. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-114 AND GLN-129.

Entry informationi

Entry nameiACAP1_HUMAN
AccessioniPrimary (citable) accession number: Q15027
Secondary accession number(s): Q53XN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: May 27, 2015
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.