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Q9ULH1

- ASAP1_HUMAN

UniProt

Q9ULH1 - ASAP1_HUMAN

Protein

Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1

Gene

ASAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 4 (18 May 2010)
      Previous versions | rss
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    Functioni

    Possesses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types By similarity. Plays a role in ciliogenesis.By similarity1 Publication

    Enzyme regulationi

    Activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2).By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri454 – 47724C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. cilium morphogenesis Source: UniProtKB
    2. regulation of ARF GTPase activity Source: InterPro

    Keywords - Molecular functioni

    GTPase activation

    Keywords - Biological processi

    Cilium biogenesis/degradation

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1
    Alternative name(s):
    130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein
    ADP-ribosylation factor-directed GTPase-activating protein 1
    Short name:
    ARF GTPase-activating protein 1
    Development and differentiation-enhancing factor 1
    Short name:
    DEF-1
    Short name:
    Differentiation-enhancing factor 1
    PIP2-dependent ARF1 GAP
    Gene namesi
    Name:ASAP1
    Synonyms:DDEF1, KIAA1249
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:2720. ASAP1.

    Subcellular locationi

    Cytoplasm By similarity. Membrane By similarity
    Note: Predominantly cytoplasmic. Partially membrane-associated.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164716055.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11291129Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1PRO_0000074196Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei717 – 7171PhosphoserineBy similarity
    Modified residuei843 – 8431Phosphoserine2 Publications
    Modified residuei1008 – 10081Phosphoserine1 Publication
    Modified residuei1027 – 10271Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated on tyrosine residues by SRC.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9ULH1.
    PaxDbiQ9ULH1.
    PRIDEiQ9ULH1.

    PTM databases

    PhosphoSiteiQ9ULH1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9ULH1.
    BgeeiQ9ULH1.
    CleanExiHS_ASAP1.
    GenevestigatoriQ9ULH1.

    Organism-specific databases

    HPAiCAB037292.
    HPA048565.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with SRC and CRK. Interacts with RAB11FIP3. Interacts with PTK2B/PYK2 By similarity. Interacts with CTTN. Interacts (via SH3 domain) with APC.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    apcP700395EBI-346622,EBI-8069633From a different organism.
    CBLBQ131912EBI-346622,EBI-744027
    CRKP461082EBI-346622,EBI-886
    CTTNQ142477EBI-346622,EBI-351886
    FYNP062413EBI-346622,EBI-515315
    GRB2P629937EBI-346622,EBI-401755
    HCKP086312EBI-346622,EBI-346340
    NCK1P163336EBI-346622,EBI-389883
    PLCG1P191743EBI-346622,EBI-79387
    SH3KBP1Q96B978EBI-346622,EBI-346595
    SRCP129313EBI-346622,EBI-621482
    UBCP0CG482EBI-346622,EBI-3390054

    Protein-protein interaction databases

    BioGridi119126. 24 interactions.
    IntActiQ9ULH1. 29 interactions.
    MINTiMINT-243352.
    STRINGi9606.ENSP00000350297.

    Structurei

    Secondary structure

    1
    1129
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi327 – 3348
    Beta strandi336 – 3383
    Beta strandi342 – 3509
    Beta strandi353 – 3564
    Beta strandi366 – 3694
    Turni370 – 3723
    Beta strandi373 – 3775
    Beta strandi379 – 3835
    Beta strandi385 – 3895
    Beta strandi392 – 3976
    Helixi401 – 41919
    Beta strandi1070 – 10767
    Beta strandi1081 – 10855
    Beta strandi1093 – 10986
    Beta strandi1101 – 11099
    Beta strandi1116 – 11205
    Helixi1121 – 11233
    Beta strandi1124 – 11263

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D1XX-ray1.90P/Q823-837[»]
    2DA0NMR-A323-423[»]
    2ED1NMR-A1067-1129[»]
    2RQTNMR-A1069-1129[»]
    2RQUNMR-A1069-1129[»]
    ProteinModelPortaliQ9ULH1.
    SMRiQ9ULH1. Positions 31-429, 437-709, 1069-1129.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9ULH1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini324 – 41693PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini439 – 560122Arf-GAPPROSITE-ProRule annotationAdd
    BLAST
    Repeati600 – 63233ANK 1Add
    BLAST
    Repeati636 – 66530ANK 2Add
    BLAST
    Domaini1067 – 112963SH3PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi783 – 993211Pro-richAdd
    BLAST

    Domaini

    The PH domain most probably contributes to the phosphoinositide-dependent regulation of ADP ribosylation factors.By similarity

    Sequence similaritiesi

    Contains 2 ANK repeats.PROSITE-ProRule annotation
    Contains 1 Arf-GAP domain.PROSITE-ProRule annotation
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri454 – 47724C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    ANK repeat, Repeat, SH3 domain, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5347.
    HOGENOMiHOG000230570.
    HOVERGENiHBG051327.
    KOiK12488.
    OMAiDFLVQNC.
    PhylomeDBiQ9ULH1.
    TreeFamiTF325156.

    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.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF12796. Ank_2. 1 hit.
    PF01412. ArfGap. 1 hit.
    PF00169. PH. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00405. REVINTRACTNG.
    SMARTiSM00248. ANK. 2 hits.
    SM00105. ArfGap. 1 hit.
    SM00233. PH. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    SSF50044. SSF50044. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 1 hit.
    PS50115. ARFGAP. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: Q9ULH1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MRSSASRLSS FSSRDSLWNR MPDQISVSEF IAETTEDYNS PTTSSFTTRL     50
    HNCRNTVTLL EEALDQDRTA LQKVKKSVKA IYNSGQDHVQ NEENYAQVLD 100
    KFGSNFLSRD NPDLGTAFVK FSTLTKELST LLKNLLQGLS HNVIFTLDSL 150
    LKGDLKGVKG DLKKPFDKAW KDYETKFTKI EKEKREHAKQ HGMIRTEITG 200
    AEIAEEMEKE RRLFQLQMCE YLIKVNEIKT KKGVDLLQNL IKYYHAQCNF 250
    FQDGLKTADK LKQYIEKLAA DLYNIKQTQD EEKKQLTALR DLIKSSLQLD 300
    QKEDSQSRQG GYSMHQLQGN KEYGSEKKGY LLKKSDGIRK VWQRRKCSVK 350
    NGILTISHAT SNRQPAKLNL LTCQVKPNAE DKKSFDLISH NRTYHFQAED 400
    EQDYVAWISV LTNSKEEALT MAFRGEQSAG ENSLEDLTKA IIEDVQRLPG 450
    NDICCDCGSS EPTWLSTNLG ILTCIECSGI HREMGVHISR IQSLELDKLG 500
    TSELLLAKNV GNNSFNDIME ANLPSPSPKP TPSSDMTVRK EYITAKYVDH 550
    RFSRKTCSTS SAKLNELLEA IKSRDLLALI QVYAEGVELM EPLLEPGQEL 600
    GETALHLAVR TADQTSLHLV DFLVQNCGNL DKQTALGNTV LHYCSMYSKP 650
    ECLKLLLRSK PTVDIVNQAG ETALDIAKRL KATQCEDLLS QAKSGKFNPH 700
    VHVEYEWNLR QEEIDESDDD LDDKPSPIKK ERSPRPQSFC HSSSISPQDK 750
    LALPGFSTPR DKQRLSYGAF TNQIFVSTST DSPTSPTTEA PPLPPRNAGK 800
    GPTGPPSTLP LSTQTSSGSS TLSKKRPPPP PPGHKRTLSD PPSPLPHGPP 850
    NKGAVPWGND GGPSSSSKTT NKFEGLSQQS STSSAKTALG PRVLPKLPQK 900
    VALRKTDHLS LDKATIPPEI FQKSSQLAEL PQKPPPGDLP PKPTELAPKP 950
    QIGDLPPKPG ELPPKPQLGD LPPKPQLSDL PPKPQMKDLP PKPQLGDLLA 1000
    KSQTGDVSPK AQQPSEVTLK SHPLDLSPNV QSRDAIQKQA SEDSNDLTPT 1050
    LPETPVPLPR KINTGKNKVR RVKTIYDCQA DNDDELTFIE GEVIIVTGEE 1100
    DQEWWIGHIE GQPERKGVFP VSFVHILSD 1129
    Length:1,129
    Mass (Da):125,498
    Last modified:May 18, 2010 - v4
    Checksum:i7F54B22015638D55
    GO
    Isoform 1 (identifier: Q9ULH1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         303-303: E → ESRR

    Show »
    Length:1,132
    Mass (Da):125,897
    Checksum:iA0440C36242D033C
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti728 – 7281I → V.
    Corresponds to variant rs966185 [ dbSNP | Ensembl ].
    VAR_055528

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei303 – 3031E → ESRR in isoform 1. 1 PublicationVSP_008365

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC009682 Genomic DNA. No translation available.
    AC103725 Genomic DNA. No translation available.
    AC131568 Genomic DNA. No translation available.
    AC139019 Genomic DNA. No translation available.
    CH471060 Genomic DNA. Translation: EAW92130.1.
    BC137135 mRNA. Translation: AAI37136.1.
    BX537768 mRNA. Translation: CAD97831.1.
    AB033075 mRNA. Translation: BAA86563.1.
    CCDSiCCDS6362.1. [Q9ULH1-1]
    RefSeqiNP_001234925.1. NM_001247996.1.
    NP_060952.2. NM_018482.3. [Q9ULH1-1]
    XP_005250982.1. XM_005250925.1. [Q9ULH1-2]
    XP_006716626.1. XM_006716563.1. [Q9ULH1-2]
    UniGeneiHs.655552.

    Genome annotation databases

    EnsembliENST00000357668; ENSP00000350297; ENSG00000153317. [Q9ULH1-1]
    ENST00000518721; ENSP00000429900; ENSG00000153317. [Q9ULH1-1]
    GeneIDi50807.
    KEGGihsa:50807.
    UCSCiuc003yta.2. human. [Q9ULH1-1]

    Polymorphism databases

    DMDMi296439459.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC009682 Genomic DNA. No translation available.
    AC103725 Genomic DNA. No translation available.
    AC131568 Genomic DNA. No translation available.
    AC139019 Genomic DNA. No translation available.
    CH471060 Genomic DNA. Translation: EAW92130.1 .
    BC137135 mRNA. Translation: AAI37136.1 .
    BX537768 mRNA. Translation: CAD97831.1 .
    AB033075 mRNA. Translation: BAA86563.1 .
    CCDSi CCDS6362.1. [Q9ULH1-1 ]
    RefSeqi NP_001234925.1. NM_001247996.1.
    NP_060952.2. NM_018482.3. [Q9ULH1-1 ]
    XP_005250982.1. XM_005250925.1. [Q9ULH1-2 ]
    XP_006716626.1. XM_006716563.1. [Q9ULH1-2 ]
    UniGenei Hs.655552.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D1X X-ray 1.90 P/Q 823-837 [» ]
    2DA0 NMR - A 323-423 [» ]
    2ED1 NMR - A 1067-1129 [» ]
    2RQT NMR - A 1069-1129 [» ]
    2RQU NMR - A 1069-1129 [» ]
    ProteinModelPortali Q9ULH1.
    SMRi Q9ULH1. Positions 31-429, 437-709, 1069-1129.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119126. 24 interactions.
    IntActi Q9ULH1. 29 interactions.
    MINTi MINT-243352.
    STRINGi 9606.ENSP00000350297.

    Chemistry

    ChEMBLi CHEMBL2146311.

    PTM databases

    PhosphoSitei Q9ULH1.

    Polymorphism databases

    DMDMi 296439459.

    Proteomic databases

    MaxQBi Q9ULH1.
    PaxDbi Q9ULH1.
    PRIDEi Q9ULH1.

    Protocols and materials databases

    DNASUi 50807.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357668 ; ENSP00000350297 ; ENSG00000153317 . [Q9ULH1-1 ]
    ENST00000518721 ; ENSP00000429900 ; ENSG00000153317 . [Q9ULH1-1 ]
    GeneIDi 50807.
    KEGGi hsa:50807.
    UCSCi uc003yta.2. human. [Q9ULH1-1 ]

    Organism-specific databases

    CTDi 50807.
    GeneCardsi GC08M131064.
    H-InvDB HIX0007806.
    HGNCi HGNC:2720. ASAP1.
    HPAi CAB037292.
    HPA048565.
    MIMi 605953. gene.
    neXtProti NX_Q9ULH1.
    PharmGKBi PA164716055.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5347.
    HOGENOMi HOG000230570.
    HOVERGENi HBG051327.
    KOi K12488.
    OMAi DFLVQNC.
    PhylomeDBi Q9ULH1.
    TreeFami TF325156.

    Miscellaneous databases

    ChiTaRSi ASAP1. human.
    EvolutionaryTracei Q9ULH1.
    GeneWikii DDEF1.
    GenomeRNAii 50807.
    NextBioi 53242.
    PROi Q9ULH1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9ULH1.
    Bgeei Q9ULH1.
    CleanExi HS_ASAP1.
    Genevestigatori Q9ULH1.

    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.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF12796. Ank_2. 1 hit.
    PF01412. ArfGap. 1 hit.
    PF00169. PH. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00405. REVINTRACTNG.
    SMARTi SM00248. ANK. 2 hits.
    SM00105. ArfGap. 1 hit.
    SM00233. PH. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    SSF50044. SSF50044. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 1 hit.
    PS50115. ARFGAP. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 174-1129 (ISOFORM 2).
      Tissue: Bone marrow.
    5. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
      DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-1129 (ISOFORM 1).
      Tissue: Brain.
    6. "ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src."
      Brown M.T., Andrade J., Radhakrishna H., Donaldson J.G., Cooper J.A., Randazzo P.A.
      Mol. Cell. Biol. 18:7038-7051(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
    7. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1027, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-843 AND SER-1008, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-843 AND SER-1027, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Functional genomic screen for modulators of ciliogenesis and cilium length."
      Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T., Aza-Blanc P., Gleeson J.G.
      Nature 464:1048-1051(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    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-1027, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Targeting AMAP1 and cortactin binding bearing an atypical src homology 3/proline interface for prevention of breast cancer invasion and metastasis."
      Hashimoto S., Hirose M., Hashimoto A., Morishige M., Yamada A., Hosaka H., Akagi K., Ogawa E., Oneyama C., Agatsuma T., Okada M., Kobayashi H., Wada H., Nakano H., Ikegami T., Nakagawa A., Sabe H.
      Proc. Natl. Acad. Sci. U.S.A. 103:7036-7041(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 823-837 IN COMPLEX WITH CTTN.
    13. "Solution structure of the PH domain of PIP2-dependent ARF1 GTPase-activating protein from human."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 319-428.
    14. "Solution structure of the SH3 domain of 130 kDA phosphatidylinositol 4,5-biphosphate-dependent ARF1 GTPase-activating protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1067-1129.
    15. "Structural basis of the recognition of the SAMP motif of adenomatous polyposis coli by the Src-homology 3 domain."
      Kaieda S., Matsui C., Mimori-Kiyosue Y., Ikegami T.
      Biochemistry 49:5143-5153(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1069-1129 IN COMPLEX WITH APC, INTERACTION WITH APC.

    Entry informationi

    Entry nameiASAP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9ULH1
    Secondary accession number(s): B2RNV3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 137 of the entry and version 4 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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