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Q80YS6

- AFAP1_MOUSE

UniProt

Q80YS6 - AFAP1_MOUSE

Protein

Actin filament-associated protein 1

Gene

Afap1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Can cross-link actin filaments into both network and bundle structures. May modulate changes in actin filament integrity and induce lamellipodia formation. May function as an adapter molecule that links other proteins, such as SRC and PKC to the actin cytoskeleton By similarity.By similarity

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Actin filament-associated protein 1
    Alternative name(s):
    110 kDa actin filament-associated protein
    Short name:
    AFAP-110
    Gene namesi
    Name:Afap1
    Synonyms:Kiaa3018
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1917542. Afap1.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity
    Note: Localizes with stress fibers in quiescent cells, concentrated in cell motility structures such as lamellipodia, filopodia and membrane ruffles.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: Ensembl
    2. cytoplasm Source: UniProtKB-KW
    3. focal adhesion Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 731731Actin filament-associated protein 1PRO_0000317659Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei283 – 2831PhosphoserineBy similarity
    Modified residuei284 – 2841PhosphoserineBy similarity
    Modified residuei549 – 5491PhosphoserineBy similarity
    Modified residuei665 – 6651PhosphoserineBy similarity
    Modified residuei666 – 6661PhosphoserineBy similarity
    Modified residuei669 – 6691Phosphoserine1 Publication
    Modified residuei680 – 6801PhosphoserineBy similarity
    Modified residuei688 – 6881PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated on tyrosine residues by SRC.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ80YS6.
    PRIDEiQ80YS6.

    PTM databases

    PhosphoSiteiQ80YS6.

    Expressioni

    Gene expression databases

    BgeeiQ80YS6.
    CleanExiMM_AFAP1.
    GenevestigatoriQ80YS6.

    Interactioni

    Subunit structurei

    Monomer and homomultimer. Interacts via its C-terminus with F-actin; probably involving AFAP1 multimers. Interacts with activated SRC SH3-SH2 domains. Interacts via its PH 1 domain with PRKCA, PRKCB and PRKCI By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ80YS6. 1 interaction.
    MINTiMINT-7300872.
    STRINGi10090.ENSMUSP00000067779.

    Structurei

    3D structure databases

    ProteinModelPortaliQ80YS6.
    SMRiQ80YS6. Positions 343-438.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini152 – 24897PH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini348 – 44295PH 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni595 – 63844Interaction with F-actinBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili558 – 64992Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi70 – 734SH3-bindingBy similarity
    Motifi93 – 964SH2-binding 1By similarity
    Motifi452 – 4576SH2-binding 2By similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi59 – 10547Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 2 PH domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, SH3-binding

    Phylogenomic databases

    eggNOGiNOG48103.
    GeneTreeiENSGT00390000003998.
    HOGENOMiHOG000033832.
    HOVERGENiHBG106875.
    InParanoidiQ80YS6.
    OMAiAGRKTQV.
    OrthoDBiEOG7KQ217.
    PhylomeDBiQ80YS6.
    TreeFamiTF332622.

    Family and domain databases

    Gene3Di2.30.29.30. 2 hits.
    InterProiIPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PfamiPF00169. PH. 2 hits.
    [Graphical view]
    SMARTiSM00233. PH. 2 hits.
    [Graphical view]
    PROSITEiPS50003. PH_DOMAIN. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q80YS6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEELIVELRL FLELLDHEYL TSTVREKKAV LTNILLRLQS SKGFEVKDHA    50
    QKAEANNLPA PPQMPLPEIP QPWLPPDSGP PPLPTSSLPE GYYEEAVPLS 100
    PGKAPEYITS NYDSDAMSSS YESYDEEEED GKGKKTRHQW PSEEASMDLV 150
    KDAKICAFLL RKKRFGQWTK LLCVIKDTKL LCYKSSKDQQ PQMELPLQGC 200
    SITYIPRDSK KKKHELKITQ QGTDPLVLAV QSKEQAEQWL KVIKEAYSGC 250
    SGPVDPECSP PPSTSAPVNK AELEKKLSSE RPSSDGEGGV ENGVTTCNGK 300
    EQAKRKKPSK SEAKGTVSKV TGKKITKIIG LGKKKPSTDE QTSSAEEDVP 350
    TCGYLNVLSN SRWRERWCRV KDSKLILHKD RADLKTHLVS IPLRGCEVIP 400
    GLDSKHPLTF RLLRNGQEVA VLEASSSEDM GRWIGILLAE TGSSTDPGAL 450
    HYDYIDVEMS ANVIQTAKQT FCFMNRRAVS TSPYLGSLSN GYAHPSGTAL 500
    HYDDVPCVNG SLKNKKPPAS SNGVPVKGKA PSSQQKKVET AGGVKRTASN 550
    AEQYKYGKNR VEADAKRLQS KEEELLKRKE ALRNRLAQLR KERKDLRAAI 600
    EVNAGRKTQA ALEDKLKRLE EECKQREAER VSLELELTEV KESLKKALAG 650
    GVTLGLAIEP RSGTSSPQSP VFRHRTLENS PISSCDTSDA EGPLPVNSAA 700
    VLKKSQPSSG SSPCRGHVLQ KAKEWELKNG T 731
    Length:731
    Mass (Da):80,615
    Last modified:June 1, 2003 - v1
    Checksum:i58D3D31BED5C2FCD
    GO

    Sequence cautioni

    The sequence BAC98293.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti43 – 431G → R in BAE28086. (PubMed:16141072)Curated
    Sequence conflicti52 – 521K → R in BAE28086. (PubMed:16141072)Curated
    Sequence conflicti232 – 2321S → G in BAC98293. (PubMed:14621295)Curated
    Sequence conflicti249 – 2491G → D in BAC98293. (PubMed:14621295)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK129483 mRNA. Translation: BAC98293.1. Different initiation.
    AK147706 mRNA. Translation: BAE28086.1.
    AK148000 mRNA. Translation: BAE28280.1.
    AK161385 mRNA. Translation: BAE36364.1.
    BC050814 mRNA. Translation: AAH50814.1.
    CCDSiCCDS19236.1.
    RefSeqiNP_081649.1. NM_027373.2.
    UniGeneiMm.125167.

    Genome annotation databases

    EnsembliENSMUST00000064571; ENSMUSP00000067779; ENSMUSG00000029094.
    GeneIDi70292.
    KEGGimmu:70292.
    UCSCiuc008xej.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK129483 mRNA. Translation: BAC98293.1 . Different initiation.
    AK147706 mRNA. Translation: BAE28086.1 .
    AK148000 mRNA. Translation: BAE28280.1 .
    AK161385 mRNA. Translation: BAE36364.1 .
    BC050814 mRNA. Translation: AAH50814.1 .
    CCDSi CCDS19236.1.
    RefSeqi NP_081649.1. NM_027373.2.
    UniGenei Mm.125167.

    3D structure databases

    ProteinModelPortali Q80YS6.
    SMRi Q80YS6. Positions 343-438.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q80YS6. 1 interaction.
    MINTi MINT-7300872.
    STRINGi 10090.ENSMUSP00000067779.

    PTM databases

    PhosphoSitei Q80YS6.

    Proteomic databases

    PaxDbi Q80YS6.
    PRIDEi Q80YS6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000064571 ; ENSMUSP00000067779 ; ENSMUSG00000029094 .
    GeneIDi 70292.
    KEGGi mmu:70292.
    UCSCi uc008xej.1. mouse.

    Organism-specific databases

    CTDi 60312.
    MGIi MGI:1917542. Afap1.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG48103.
    GeneTreei ENSGT00390000003998.
    HOGENOMi HOG000033832.
    HOVERGENi HBG106875.
    InParanoidi Q80YS6.
    OMAi AGRKTQV.
    OrthoDBi EOG7KQ217.
    PhylomeDBi Q80YS6.
    TreeFami TF332622.

    Miscellaneous databases

    ChiTaRSi AFAP1. mouse.
    NextBioi 331322.
    PROi Q80YS6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q80YS6.
    CleanExi MM_AFAP1.
    Genevestigatori Q80YS6.

    Family and domain databases

    Gene3Di 2.30.29.30. 2 hits.
    InterProi IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    Pfami PF00169. PH. 2 hits.
    [Graphical view ]
    SMARTi SM00233. PH. 2 hits.
    [Graphical view ]
    PROSITEi PS50003. PH_DOMAIN. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 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., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
      DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Melanocyte, Placenta and Testis.
    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: Testis.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-669, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiAFAP1_MOUSE
    AccessioniPrimary (citable) accession number: Q80YS6
    Secondary accession number(s): Q3UGX1, Q6ZPE4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 91 of the entry and version 1 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