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Q15027

- ACAP1_HUMAN

UniProt

Q15027 - ACAP1_HUMAN

Protein

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

Gene

ACAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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

    1. ARF GTPase activator activity Source: InterPro
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. protein transport Source: UniProtKB-KW
    2. regulation of ARF GTPase activity Source: InterPro

    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: 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

    1. membrane Source: UniProtKB
    2. recycling endosome membrane Source: UniProtKB-SubCell

    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
    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.

    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

    ArrayExpressiQ15027.
    BgeeiQ15027.
    CleanExiHS_ACAP1.
    GenevestigatoriQ15027.

    Organism-specific databases

    HPAiHPA021127.

    Interactioni

    Subunit structurei

    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.5 Publications

    Protein-protein interaction databases

    BioGridi115092. 3 interactions.
    IntActiQ15027. 6 interactions.
    MINTiMINT-1446333.
    STRINGi9606.ENSP00000158762.

    Structurei

    Secondary structure

    1
    740
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi407 – 4126
    Turni415 – 4184
    Turni421 – 4233
    Beta strandi430 – 4323
    Turni433 – 4364
    Beta strandi437 – 4393
    Helixi441 – 45010
    Turni452 – 4543
    Beta strandi457 – 4593
    Turni460 – 4623
    Helixi467 – 4759
    Helixi478 – 4858
    Turni486 – 4938
    Helixi503 – 51412
    Helixi571 – 5788
    Beta strandi580 – 5823
    Helixi585 – 5939
    Turni603 – 6064
    Helixi610 – 6167
    Helixi620 – 6289
    Helixi643 – 6508
    Helixi653 – 6619
    Helixi676 – 6827
    Helixi686 – 69611
    Helixi713 – 7208

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3JUEX-ray2.30A/B378-740[»]
    3T9KX-ray2.30A/B378-740[»]
    4F1PX-ray2.30A/B378-740[»]
    ProteinModelPortaliQ15027.
    SMRiQ15027. Positions 4-357, 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.

    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.
    HOGENOMiHOG000220815.
    HOVERGENiHBG050889.
    InParanoidiQ15027.
    KOiK12489.
    OMAiFSQAHLD.
    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

    MTVKLDFEEC LKDSPRFRAS IELVEAEVSE LETRLEKLLK LGTGLLESGR    50
    HYLAASRAFV VGICDLARLG PPEPMMAECL EKFTVSLNHK LDSHAELLDA 100
    TQHTLQQQIQ TLVKEGLRGF REARRDFWRG AESLEAALTH NAEVPRRRAQ 150
    EAEEAGAALR TARAGYRGRA LDYALQINVI EDKRKFDIME FVLRLVEAQA 200
    THFQQGHEEL SRLSQYRKEL GAQLHQLVLN SAREKRDMEQ RHVLLKQKEL 250
    GGEEPEPSLR EGPGGLVMEG HLFKRASNAF KTWSRRWFTI QSNQLVYQKK 300
    YKDPVTVVVD DLRLCTVKLC PDSERRFCFE VVSTSKSCLL QADSERLLQL 350
    WVSAVQSSIA SAFSQARLDD SPRGPGQGSG HLAIGSAATL GSGGMARGRE 400
    PGGVGHVVAQ VQSVDGNAQC CDCREPAPEW ASINLGVTLC IQCSGIHRSL 450
    GVHFSKVRSL TLDSWEPELV KLMCELGNVI INQIYEARVE AMAVKKPGPS 500
    CSRQEKEAWI HAKYVEKKFL TKLPEIRGRR GGRGRPRGQP PVPPKPSIRP 550
    RPGSLRSKPE PPSEDLGSLH PGALLFRASG HPPSLPTMAD ALAHGADVNW 600
    VNGGQDNATP LIQATAANSL LACEFLLQNG ANVNQADSAG RGPLHHATIL 650
    GHTGLACLFL KRGADLGARD SEGRDPLTIA METANADIVT LLRLAKMREA 700
    EAAQGQAGDE TYLDIFRDFS LMASDDPEKL SRRSHDLHTL 740
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi3183210.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D30758 mRNA. Translation: BAA06418.2 . Different initiation.
    BT009788 mRNA. Translation: AAP88790.1 .
    BC018543 mRNA. Translation: AAH18543.1 .
    CCDSi CCDS11101.1.
    RefSeqi NP_055531.1. NM_014716.3.
    UniGenei Hs.337242.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3JUE X-ray 2.30 A/B 378-740 [» ]
    3T9K X-ray 2.30 A/B 378-740 [» ]
    4F1P X-ray 2.30 A/B 378-740 [» ]
    ProteinModelPortali Q15027.
    SMRi Q15027. Positions 4-357, 405-723.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115092. 3 interactions.
    IntActi Q15027. 6 interactions.
    MINTi MINT-1446333.
    STRINGi 9606.ENSP00000158762.

    PTM databases

    PhosphoSitei Q15027.

    Polymorphism databases

    DMDMi 3183210.

    Proteomic databases

    MaxQBi Q15027.
    PaxDbi Q15027.
    PRIDEi Q15027.

    Protocols and materials databases

    DNASUi 9744.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000158762 ; ENSP00000158762 ; ENSG00000072818 .
    GeneIDi 9744.
    KEGGi hsa:9744.
    UCSCi uc002ggd.2. human.

    Organism-specific databases

    CTDi 9744.
    GeneCardsi GC17P007239.
    HGNCi HGNC:16467. ACAP1.
    HPAi HPA021127.
    MIMi 607763. gene.
    neXtProti NX_Q15027.
    PharmGKBi PA26406.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5347.
    HOGENOMi HOG000220815.
    HOVERGENi HBG050889.
    InParanoidi Q15027.
    KOi K12489.
    OMAi FSQAHLD.
    OrthoDBi EOG7PVWNT.
    PhylomeDBi Q15027.
    TreeFami TF318315.

    Enzyme and pathway databases

    SignaLinki Q15027.

    Miscellaneous databases

    EvolutionaryTracei Q15027.
    GeneWikii CENTB1.
    GenomeRNAii 9744.
    NextBioi 36666.
    PROi Q15027.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15027.
    Bgeei Q15027.
    CleanExi HS_ACAP1.
    Genevestigatori Q15027.

    Family and domain databases

    Gene3Di 1.20.1270.60. 1 hit.
    1.25.40.20. 1 hit.
    2.30.29.30. 1 hit.
    InterProi IPR027267. 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 ]
    Pfami PF00023. Ank. 2 hits.
    PF01412. ArfGap. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view ]
    PRINTSi PR00405. REVINTRACTNG.
    SMARTi SM00248. ANK. 3 hits.
    SM00105. ArfGap. 1 hit.
    SM00233. PH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 2 hits.
    PS50115. ARFGAP. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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: October 1, 2014
    This is version 140 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