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Q9QWY8

- ASAP1_MOUSE

UniProt

Q9QWY8 - ASAP1_MOUSE

Protein

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

Gene

Asap1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (03 Oct 2012)
      Previous versions | rss
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    Functioni

    May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types. Plays a role in ciliogenesis By similarity. Posseses 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.By similarity

    Enzyme regulationi

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri469 – 49224C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ARF GTPase activator activity Source: FlyBase
    2. phosphatidylinositol-3,4,5-trisphosphate binding Source: FlyBase
    3. phosphatidylinositol-4,5-bisphosphate binding Source: FlyBase
    4. protein binding Source: IntAct
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cilium morphogenesis Source: UniProtKB
    2. positive regulation of GTPase activity Source: GOC
    3. 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, Shag1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:1342335. Asap1.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi811 – 8111R → A: Significant reduction in binding to SRC and CRK and loss of phosphorylation. Loss of binding and phosphorylation; when associated with A-910 and A-913. 1 Publication
    Mutagenesisi910 – 9101P → A: Significant reduction in binding to SRC and CRK and decrease in phosphorylation; when associated with A-913. Loss of binding and phosphorylation; when associated with A-811 and A-913. 1 Publication
    Mutagenesisi913 – 9131P → A: Significant reduction in binding to SRC and CRK and decrease in phosphorylation; when associated with A-910. Loss of binding and phosphorylation; when associated with A-811 and A-910. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11471147Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1PRO_0000074197Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei308 – 3081Phosphotyrosine; by FAK21 Publication
    Modified residuei732 – 7321Phosphoserine1 Publication
    Modified residuei858 – 8581Phosphoserine1 Publication
    Modified residuei1026 – 10261PhosphoserineBy similarity
    Modified residuei1045 – 10451PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated on tyrosine residues by SRC.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9QWY8.
    PaxDbiQ9QWY8.
    PRIDEiQ9QWY8.

    PTM databases

    PhosphoSiteiQ9QWY8.

    Miscellaneous databases

    PMAP-CutDBQ9QWY8.

    Expressioni

    Tissue specificityi

    Expressed in all tissues examined but a most abundant expression was found in the testis, brain, lung and spleen. A heightened expression was seen in the adipose tissue from obese (ob) and diabetic (db) animals.1 Publication

    Gene expression databases

    ArrayExpressiQ9QWY8.
    GenevestigatoriQ9QWY8.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with SRC and CRK. Interacts with RAB11FIP3. Interacts with PTK2B/PYK2.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SRCP005233EBI-698524,EBI-848039From a different organism.

    Protein-protein interaction databases

    IntActiQ9QWY8. 8 interactions.
    MINTiMINT-266354.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9QWY8.
    SMRiQ9QWY8. Positions 341-443, 452-724, 1087-1147.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini339 – 43193PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini454 – 577124Arf-GAPPROSITE-ProRule annotationAdd
    BLAST
    Repeati615 – 64733ANK 1Add
    BLAST
    Repeati651 – 68030ANK 2Add
    BLAST
    Domaini1085 – 114763SH3PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi798 – 1011214Pro-richAdd
    BLAST

    Domaini

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

    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 fingeri469 – 49224C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    ANK repeat, Repeat, SH3 domain, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5347.
    GeneTreeiENSGT00740000115306.
    HOGENOMiHOG000230570.
    HOVERGENiHBG051327.
    InParanoidiQ9QWY8.
    KOiK12488.
    OMAiDFLVQNC.
    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. 2 hits.
    PS50115. ARFGAP. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9QWY8-1) [UniParc]FASTAAdd to Basket

    Also known as: SHAG1a, ASAP1a

    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
    PKEVGGLYVA SRANSSRRDS QSRQGGYSMH QLQGNKEYGS EKKGFLLKKS 350
    DGIRKVWQRR KCAVKNGILT ISHATSNRQP AKLNLLTCQV KPNAEDKKSF 400
    DLISHNRTYH FQAEDEQDYI AWISVLTNSK EEALTMAFRG EQSTGENSLE 450
    DLTKAIIEDV QRLPGNDICC DCGSSEPTWL STNLGILTCI ECSGIHREMG 500
    VHISRIQSLE LDKLGTSELL LAKNVGNNSF NDIMEANLPS PSPKPTPSSD 550
    MTVRKEYITA KYVDHRFSRK TCASSSAKLN ELLEAIKSRD LLALIQVYAE 600
    GVELMEPLLE PGQELGETAL HLAVRTADQT SLHLVDFLVQ NCGNLDKQTS 650
    VGNTVLHYCS MYGKPECLKL LLRSKPTVDI VNQNGETALD IAKRLKATQC 700
    EDLLSQAKSG KFNPHVHVEY EWNLRQDEMD ESDDDLDDKP SPIKKERSPR 750
    PQSFCHSSSI SPQDKLALPG FSTPRDKQRL SYGAFTNQIF ASTSTDLPTS 800
    PTSEAPPLPP RNAGKGPTGP PSTLPLGTQT SSGSSTLSKK RPPPPPPGHK 850
    RTLSDPPSPL PHGPPNKGAI PWGNDVGPLS SSKTANKFEG LSQQASTSSA 900
    KTALGPRVLP KLPQKVALRK TETSHHLSLD RTNIPPETFQ KSSQLTELPQ 950
    KPPLGELPPK PVELAPKPQV GELPPKPGEL PPKPQLGDLP PKPQLSDLPP 1000
    KPQMKDLPPK PQLGDLLAKS QAGDVSAKVQ PPSEVTQRSH TGDLSPNVQS 1050
    RDAIQKQASE DSNDLTPTLP ETPVPLPRKI NTGKNKVRRV KTIYDCQADN 1100
    DDELTFIEGE VIIVTGEEDQ EWWIGHIEGQ PERKGVFPVS FVHILSD 1147
    Length:1,147
    Mass (Da):127,421
    Last modified:October 3, 2012 - v2
    Checksum:i12950D1C4F49A909
    GO
    Isoform 2 (identifier: Q9QWY8-2) [UniParc]FASTAAdd to Basket

    Also known as: SHAG1b, ASAP1b

    The sequence of this isoform differs from the canonical sequence as follows:
         816-872: Missing.

    Show »
    Length:1,090
    Mass (Da):121,675
    Checksum:i5C1F1D950B7B252A
    GO
    Isoform 3 (identifier: Q9QWY8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         304-315: Missing.

    Show »
    Length:1,135
    Mass (Da):126,246
    Checksum:i636A1D0E72FB8893
    GO
    Isoform 4 (identifier: Q9QWY8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         304-318: Missing.

    Show »
    Length:1,132
    Mass (Da):125,846
    Checksum:i32751FB034E7CD51
    GO

    Sequence cautioni

    The sequence AAH02201.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAH48818.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti654 – 6541T → S in AAB82338. (PubMed:9126384)Curated
    Sequence conflicti879 – 8791L → S in AAC98349. (PubMed:9819391)Curated
    Sequence conflicti879 – 8791L → S in AAC98350. (PubMed:9819391)Curated
    Sequence conflicti1051 – 10511R → I in AAB82338. (PubMed:9126384)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei304 – 31815Missing in isoform 4. 1 PublicationVSP_008367Add
    BLAST
    Alternative sequencei304 – 31512Missing in isoform 3. 1 PublicationVSP_008366Add
    BLAST
    Alternative sequencei816 – 87257Missing in isoform 2. 1 PublicationVSP_008368Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF075461 mRNA. Translation: AAC98349.1.
    AF075462 mRNA. Translation: AAC98350.1.
    AC098728 Genomic DNA. No translation available.
    AC131710 Genomic DNA. No translation available.
    AC156573 Genomic DNA. No translation available.
    BC002201 mRNA. Translation: AAH02201.1. Different initiation.
    BC048818 mRNA. Translation: AAH48818.1. Different initiation.
    BC094581 mRNA. Translation: AAH94581.1.
    AK122477 mRNA. Translation: BAC65759.1.
    U92478 mRNA. Translation: AAB82338.1.
    CCDSiCCDS56986.1. [Q9QWY8-1]
    CCDS70634.1. [Q9QWY8-2]
    PIRiT42627.
    RefSeqiNP_001263390.1. NM_001276461.1.
    NP_001263391.1. NM_001276462.1.
    NP_001263396.1. NM_001276467.1. [Q9QWY8-2]
    NP_034156.2. NM_010026.3. [Q9QWY8-1]
    UniGeneiMm.277236.
    Mm.491089.

    Genome annotation databases

    EnsembliENSMUST00000110115; ENSMUSP00000105742; ENSMUSG00000022377. [Q9QWY8-4]
    ENSMUST00000175793; ENSMUSP00000135718; ENSMUSG00000022377. [Q9QWY8-3]
    ENSMUST00000176384; ENSMUSP00000135190; ENSMUSG00000022377. [Q9QWY8-2]
    ENSMUST00000177374; ENSMUSP00000134825; ENSMUSG00000022377. [Q9QWY8-1]
    GeneIDi13196.
    KEGGimmu:13196.
    UCSCiuc007vzh.1. mouse. [Q9QWY8-3]
    uc007vzk.1. mouse.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF075461 mRNA. Translation: AAC98349.1 .
    AF075462 mRNA. Translation: AAC98350.1 .
    AC098728 Genomic DNA. No translation available.
    AC131710 Genomic DNA. No translation available.
    AC156573 Genomic DNA. No translation available.
    BC002201 mRNA. Translation: AAH02201.1 . Different initiation.
    BC048818 mRNA. Translation: AAH48818.1 . Different initiation.
    BC094581 mRNA. Translation: AAH94581.1 .
    AK122477 mRNA. Translation: BAC65759.1 .
    U92478 mRNA. Translation: AAB82338.1 .
    CCDSi CCDS56986.1. [Q9QWY8-1 ]
    CCDS70634.1. [Q9QWY8-2 ]
    PIRi T42627.
    RefSeqi NP_001263390.1. NM_001276461.1.
    NP_001263391.1. NM_001276462.1.
    NP_001263396.1. NM_001276467.1. [Q9QWY8-2 ]
    NP_034156.2. NM_010026.3. [Q9QWY8-1 ]
    UniGenei Mm.277236.
    Mm.491089.

    3D structure databases

    ProteinModelPortali Q9QWY8.
    SMRi Q9QWY8. Positions 341-443, 452-724, 1087-1147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9QWY8. 8 interactions.
    MINTi MINT-266354.

    PTM databases

    PhosphoSitei Q9QWY8.

    Proteomic databases

    MaxQBi Q9QWY8.
    PaxDbi Q9QWY8.
    PRIDEi Q9QWY8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000110115 ; ENSMUSP00000105742 ; ENSMUSG00000022377 . [Q9QWY8-4 ]
    ENSMUST00000175793 ; ENSMUSP00000135718 ; ENSMUSG00000022377 . [Q9QWY8-3 ]
    ENSMUST00000176384 ; ENSMUSP00000135190 ; ENSMUSG00000022377 . [Q9QWY8-2 ]
    ENSMUST00000177374 ; ENSMUSP00000134825 ; ENSMUSG00000022377 . [Q9QWY8-1 ]
    GeneIDi 13196.
    KEGGi mmu:13196.
    UCSCi uc007vzh.1. mouse. [Q9QWY8-3 ]
    uc007vzk.1. mouse.

    Organism-specific databases

    CTDi 50807.
    MGIi MGI:1342335. Asap1.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG5347.
    GeneTreei ENSGT00740000115306.
    HOGENOMi HOG000230570.
    HOVERGENi HBG051327.
    InParanoidi Q9QWY8.
    KOi K12488.
    OMAi DFLVQNC.
    TreeFami TF325156.

    Miscellaneous databases

    NextBioi 283328.
    PMAP-CutDB Q9QWY8.
    PROi Q9QWY8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9QWY8.
    Genevestigatori Q9QWY8.

    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. 2 hits.
    PS50115. ARFGAP. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CHARACTERIZATION, MUTAGENESIS OF ARG-811; PRO-910 AND PRO-913.
      Tissue: Brain and Embryo.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-1147 (ISOFORM 4).
      Strain: C57BL/6.
      Tissue: Eye and Mammary tumor.
    4. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
      DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-1147 (ISOFORM 3).
      Tissue: Brain.
    5. "Examining the specificity of Src homology 3 domain -- ligand interactions with alkaline phosphatase fusion proteins."
      Yamabhai M., Kay B.K.
      Anal. Biochem. 247:143-151(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 654-1147 (ISOFORM 1).
    6. "DEF-1, a novel src SH3 binding protein that promotes adipogenesis in fibroblastic cell lines."
      King F.J., Hu E., Harris D.F., Sarraf P., Spiegelman B.M., Roberts T.M.
      Mol. Cell. Biol. 19:2330-2337(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "The tyrosine kinase Pyk2 regulates Arf1 activity by phosphorylation and inhibition of the Arf-GTPase-activating protein ASAP1."
      Kruljac-Letunic A., Moelleken J., Kallin A., Wieland F., Blaukat A.
      J. Biol. Chem. 278:29560-29570(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-308, INTERACTION WITH PTK2B/PYK2.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732 AND SER-858, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. "Arf GTPase-activating protein ASAP1 interacts with Rab11 effector FIP3 and regulates pericentrosomal localization of transferrin receptor-positive recycling endosome."
      Inoue H., Ha V.L., Prekeris R., Randazzo P.A.
      Mol. Biol. Cell 19:4224-4237(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB11FIP3.

    Entry informationi

    Entry nameiASAP1_MOUSE
    AccessioniPrimary (citable) accession number: Q9QWY8
    Secondary accession number(s): O08612
    , Q505F0, Q80TG8, Q80UV6, Q99LV8, Q9Z2B6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 131 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3