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Q15057

- ACAP2_HUMAN

UniProt

Q15057 - ACAP2_HUMAN

Protein

Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2

Gene

ACAP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 3 (15 Dec 2003)
      Previous versions | rss
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    Functioni

    GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6).1 Publication

    Enzyme regulationi

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri414 – 43724C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular response to nerve growth factor stimulus Source: UniProtKB
    2. protein localization to endosome Source: UniProtKB
    3. regulation of ARF GTPase activity Source: InterPro

    Keywords - Molecular functioni

    GTPase activation

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2
    Alternative name(s):
    Centaurin-beta-2
    Short name:
    Cnt-b2
    Gene namesi
    Name:ACAP2
    Synonyms:CENTB2, KIAA0041
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:16469. ACAP2.

    Subcellular locationi

    Endosome membrane By similarity; Peripheral membrane protein By similarity

    GO - Cellular componenti

    1. endosome membrane Source: UniProtKB
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi442 – 4421R → Q: Loss of GAP activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA26407.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 778778Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2PRO_0000074210Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei384 – 3841Phosphoserine1 Publication
    Modified residuei521 – 5211Phosphoserine1 Publication
    Modified residuei742 – 7421Phosphotyrosine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ15057.
    PaxDbiQ15057.
    PeptideAtlasiQ15057.
    PRIDEiQ15057.

    PTM databases

    PhosphoSiteiQ15057.

    Expressioni

    Tissue specificityi

    Widely expressed. Highest level in lung.1 Publication

    Gene expression databases

    ArrayExpressiQ15057.
    BgeeiQ15057.
    CleanExiHS_ACAP2.
    GenevestigatoriQ15057.

    Organism-specific databases

    HPAiHPA034807.
    HPA034808.

    Interactioni

    Subunit structurei

    Interacts with RAB35 (GTP-bound form); the interaction is direct and probably recruits ACAP2 to membranes. Interacts with MICALL1; the interaction is indirect through RAB35 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi117073. 4 interactions.
    IntActiQ15057. 1 interaction.
    STRINGi9606.ENSP00000324287.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15057.
    SMRiQ15057. Positions 7-360, 378-758.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 226226BARAdd
    BLAST
    Domaini266 – 36196PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini399 – 520122Arf-GAPPROSITE-ProRule annotationAdd
    BLAST
    Repeati640 – 66930ANK 1Add
    BLAST
    Repeati673 – 70230ANK 2Add
    BLAST
    Repeati706 – 73530ANK 3Add
    BLAST

    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 fingeri414 – 43724C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    ANK repeat, Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5347.
    HOGENOMiHOG000220815.
    HOVERGENiHBG050889.
    InParanoidiQ15057.
    KOiK12489.
    OMAiQHATDED.
    OrthoDBiEOG7PVWNT.
    PhylomeDBiQ15057.
    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.
    [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.

    Q15057-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKMTVDFEEC LKDSPRFRAA LEEVEGDVAE LELKLDKLVK LCIAMIDTGK    50
    AFCVANKQFM NGIRDLAQYS SNDAVVETSL TKFSDSLQEM INFHTILFDQ 100
    TQRSIKAQLQ NFVKEDLRKF KDAKKQFEKV SEEKENALVK NAQVQRNKQH 150
    EVEEATNILT ATRKCFRHIA LDYVLQINVL QSKRRSEILK SMLSFMYAHL 200
    AFFHQGYDLF SELGPYMKDL GAQLDRLVVD AAKEKREMEQ KHSTIQQKDF 250
    SSDDSKLEYN VDAANGIVME GYLFKRASNA FKTWNRRWFS IQNNQLVYQK 300
    KFKDNPTVVV EDLRLCTVKH CEDIERRFCF EVVSPTKSCM LQADSEKLRQ 350
    AWIKAVQTSI ATAYREKGDE SEKLDKKSSP STGSLDSGNE SKEKLLKGES 400
    ALQRVQCIPG NASCCDCGLA DPRWASINLG ITLCIECSGI HRSLGVHFSK 450
    VRSLTLDTWE PELLKLMCEL GNDVINRVYE ANVEKMGIKK PQPGQRQEKE 500
    AYIRAKYVER KFVDKYSISL SPPEQQKKFV SKSSEEKRLS ISKFGPGDQV 550
    RASAQSSVRS NDSGIQQSSD DGRESLPSTV SANSLYEPEG ERQDSSMFLD 600
    SKHLNPGLQL YRASYEKNLP KMAEALAHGA DVNWANSEEN KATPLIQAVL 650
    GGSLVTCEFL LQNGANVNQR DVQGRGPLHH ATVLGHTGQV CLFLKRGANQ 700
    HATDEEGKDP LSIAVEAANA DIVTLLRLAR MNEEMRESEG LYGQPGDETY 750
    QDIFRDFSQM ASNNPEKLNR FQQDSQKF 778
    Length:778
    Mass (Da):88,029
    Last modified:December 15, 2003 - v3
    Checksum:i64B620957FEE6195
    GO

    Sequence cautioni

    The sequence CAB41450.1 differs from that shown. Reason: Frameshift at positions 98, 106 and 111.
    The sequence BAA05064.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51V → G in CAB41450. (PubMed:11062263)Curated
    Sequence conflicti42 – 421C → G in CAB41450. (PubMed:11062263)Curated
    Sequence conflicti229 – 2291V → G in CAB41450. (PubMed:11062263)Curated
    Sequence conflicti252 – 2521S → R in CAB41450. (PubMed:11062263)Curated
    Sequence conflicti258 – 2581E → K in CAB41450. (PubMed:11062263)Curated
    Sequence conflicti296 – 2961L → V in CAB41450. (PubMed:11062263)Curated
    Sequence conflicti564 – 5641G → E in AAH60767. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ238248 mRNA. Translation: CAB41450.1. Frameshift.
    D26069 mRNA. Translation: BAA05064.2. Different initiation.
    AK290369 mRNA. Translation: BAF83058.1.
    CH471052 Genomic DNA. Translation: EAW78027.1.
    BC031005 mRNA. Translation: AAH31005.1.
    BC060767 mRNA. Translation: AAH60767.1.
    CCDSiCCDS33924.1.
    RefSeqiNP_036419.3. NM_012287.5.
    UniGeneiHs.593373.

    Genome annotation databases

    EnsembliENST00000326793; ENSP00000324287; ENSG00000114331.
    GeneIDi23527.
    KEGGihsa:23527.
    UCSCiuc003fun.4. human.

    Polymorphism databases

    DMDMi39932727.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ238248 mRNA. Translation: CAB41450.1 . Frameshift.
    D26069 mRNA. Translation: BAA05064.2 . Different initiation.
    AK290369 mRNA. Translation: BAF83058.1 .
    CH471052 Genomic DNA. Translation: EAW78027.1 .
    BC031005 mRNA. Translation: AAH31005.1 .
    BC060767 mRNA. Translation: AAH60767.1 .
    CCDSi CCDS33924.1.
    RefSeqi NP_036419.3. NM_012287.5.
    UniGenei Hs.593373.

    3D structure databases

    ProteinModelPortali Q15057.
    SMRi Q15057. Positions 7-360, 378-758.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117073. 4 interactions.
    IntActi Q15057. 1 interaction.
    STRINGi 9606.ENSP00000324287.

    PTM databases

    PhosphoSitei Q15057.

    Polymorphism databases

    DMDMi 39932727.

    Proteomic databases

    MaxQBi Q15057.
    PaxDbi Q15057.
    PeptideAtlasi Q15057.
    PRIDEi Q15057.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000326793 ; ENSP00000324287 ; ENSG00000114331 .
    GeneIDi 23527.
    KEGGi hsa:23527.
    UCSCi uc003fun.4. human.

    Organism-specific databases

    CTDi 23527.
    GeneCardsi GC03M194995.
    HGNCi HGNC:16469. ACAP2.
    HPAi HPA034807.
    HPA034808.
    MIMi 607766. gene.
    neXtProti NX_Q15057.
    PharmGKBi PA26407.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5347.
    HOGENOMi HOG000220815.
    HOVERGENi HBG050889.
    InParanoidi Q15057.
    KOi K12489.
    OMAi QHATDED.
    OrthoDBi EOG7PVWNT.
    PhylomeDBi Q15057.
    TreeFami TF318315.

    Miscellaneous databases

    ChiTaRSi ACAP2. human.
    GeneWikii CENTB2.
    GenomeRNAii 23527.
    NextBioi 45992.
    PROi Q15057.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15057.
    Bgeei Q15057.
    CleanExi HS_ACAP2.
    Genevestigatori Q15057.

    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.
    [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. "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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY, MUTAGENESIS OF ARG-442.
      Tissue: Leukocyte.
    2. "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.
    3. Ohara O., Nagase T., Kikuno R., Nomura N.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Tongue.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Brain and Placenta.
    7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-742, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiACAP2_HUMAN
    AccessioniPrimary (citable) accession number: Q15057
    Secondary accession number(s): A8K2V4, Q8N5Z8, Q9UQR3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 146 of the entry and version 3 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3