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P15891

- ABP1_YEAST

UniProt

P15891 - ABP1_YEAST

Protein

Actin-binding protein

Gene

ABP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Regulates ARP2/3 complex-mediated actin assembly. Recruits ARP2/3 complex to sides of preexisting actin filaments, which may promote nucleation or stabilization of filament branches. Binds to actin filaments, but not actin monomers. Actin binding is required for ARP2/3 complex activation. May also have a role in linking the actin cytoskeleton to endocytosis. recruits components of the endocytotic machinery to cortical actin patches, known sites of endocytosis.1 Publication

    GO - Molecular functioni

    1. actin filament binding Source: SGD
    2. protein binding Source: IntAct

    GO - Biological processi

    1. actin cortical patch assembly Source: SGD
    2. barbed-end actin filament capping Source: SGD
    3. protein localization Source: SGD

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29382-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Actin-binding protein
    Gene namesi
    Name:ABP1
    Ordered Locus Names:YCR088W
    ORF Names:YCR88W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome III

    Organism-specific databases

    SGDiS000000684. ABP1.

    Subcellular locationi

    Cytoplasmcytoskeletonactin patch 3 Publications
    Note: Cortical actin patches.

    GO - Cellular componenti

    1. actin cortical patch Source: SGD
    2. cell cortex Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi21 – 211K → A in ABP1-1; moderately reduces actin binding and partially reduces ARP2/3 complex activation; when associated with A-24. 2 Publications
    Mutagenesisi24 – 241R → A in ABP1-1; moderately reduces actin binding and partially reduces ARP2/3 complex activation; when associated with A-21. 2 Publications
    Mutagenesisi80 – 801K → A in ABP1-2; strongly reduces actin binding and abolishes ARP2/3 complex activation. 2 Publications
    Mutagenesisi94 – 941K → A in ABP1-3; reduces actin binding and abolishes ARP2/3 complex activation; when associated with A-96. 2 Publications
    Mutagenesisi96 – 961R → A in ABP1-3; reduces actin binding and abolishes ARP2/3 complex activation; when associated with A-94. 2 Publications
    Mutagenesisi122 – 1221D → A in ABP1-4; no effect; when associated with A-125. 2 Publications
    Mutagenesisi125 – 1251D → A in ABP1-4; no effect; when associated with A-122. 2 Publications
    Mutagenesisi134 – 1341K → A in ABP1-5; moderately reduces actin binding and abolishes ARP2/3 complex activation. 2 Publications
    Mutagenesisi201 – 2033DDW → AAA: Abolishes ARP2/3 complex activation, but not actin binding. 1 Publication
    Mutagenesisi437 – 4393DDW → AAA: Abolishes ARP2/3 complex activation, but not actin binding. 1 Publication
    Mutagenesisi569 – 5691W → A: Abolishes protein binding. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 592591Actin-binding proteinPRO_0000064429Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei165 – 1651Phosphothreonine1 Publication
    Modified residuei167 – 1671Phosphoserine1 Publication
    Modified residuei169 – 1691Phosphoserine3 Publications
    Modified residuei181 – 1811Phosphothreonine4 Publications
    Modified residuei183 – 1831Phosphoserine3 Publications
    Modified residuei313 – 3131Phosphoserine2 Publications
    Modified residuei365 – 3651Phosphoserine3 Publications
    Modified residuei389 – 3891Phosphoserine2 Publications
    Modified residuei458 – 4581Phosphoserine1 Publication
    Modified residuei481 – 4811Phosphoserine2 Publications

    Post-translational modificationi

    The actin depolymerizing factor homology (ADF) domain mediates actin filament binding.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP15891.
    PaxDbiP15891.
    PeptideAtlasiP15891.

    Expressioni

    Gene expression databases

    GenevestigatoriP15891.

    Interactioni

    Subunit structurei

    Binds F-actin, but not G-actin. Interacts with the ARP2/3 complex. Interacts with APP1, ARK1, PRK1, SCP1, SRV2 and YIR003W via its SH3 domain. Interacts with the SH3 domain of RVS167 and with SLA1.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AIM21P4056310EBI-2036,EBI-25376
    APP1P539339EBI-2036,EBI-28798
    ARK1P5397411EBI-2036,EBI-9817
    BSP1Q066042EBI-2036,EBI-37047
    HUA2Q121343EBI-2036,EBI-37262
    INP52P509422EBI-2036,EBI-28834
    LSB3P436036EBI-2036,EBI-22980
    PRK1P4049410EBI-2036,EBI-9703
    RVS167P397436EBI-2036,EBI-14500
    SCP1Q088736EBI-2036,EBI-33137
    SLA1P327904EBI-2036,EBI-17313
    SRV2P175559EBI-2036,EBI-4024
    YSC84P327933EBI-2036,EBI-24460

    Protein-protein interaction databases

    BioGridi31060. 87 interactions.
    DIPiDIP-534N.
    IntActiP15891. 35 interactions.
    MINTiMINT-370108.
    STRINGi4932.YCR088W.

    Structurei

    Secondary structure

    1
    592
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi12 – 2413
    Beta strandi32 – 376
    Beta strandi43 – 508
    Helixi52 – 565
    Beta strandi65 – 717
    Beta strandi80 – 867
    Helixi93 – 10917
    Beta strandi115 – 1228
    Helixi123 – 1264
    Helixi128 – 1369
    Beta strandi537 – 5415
    Beta strandi546 – 5505
    Beta strandi558 – 5636
    Beta strandi566 – 5749
    Turni575 – 5773
    Beta strandi580 – 5845
    Helixi585 – 5873
    Beta strandi588 – 5903

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HQZX-ray2.101/2/3/4/5/6/7/8/91-141[»]
    1JO8X-ray1.30A535-592[»]
    2K3BNMR-A535-592[»]
    2RPNNMR-A535-592[»]
    DisProtiDP00634.
    ProteinModelPortaliP15891.
    SMRiP15891. Positions 3-141, 535-592.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15891.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 136130ADF-HPROSITE-ProRule annotationAdd
    BLAST
    Repeati200 – 209101
    Repeati436 – 445102
    Domaini532 – 59261SH3PROSITE-ProRule annotationAdd
    BLAST
    Repeati566 – 575103

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni200 – 5753763 X 10 AA approximate repeats (acidic)Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi518 – 5225Poly-Pro

    Sequence similaritiesi

    Belongs to the ABP1 family.Curated
    Contains 1 ADF-H domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiNOG265859.
    HOGENOMiHOG000246671.
    OMAiIINIEFV.
    OrthoDBiEOG7B05P0.

    Family and domain databases

    Gene3Di3.40.20.10. 1 hit.
    InterProiIPR002108. ADF-H.
    IPR029006. ADF-H/Gelsolin-like_dom.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00241. Cofilin_ADF. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    SMARTiSM00102. ADF. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS51263. ADF_H. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P15891-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALEPIDYTT HSREIDAEYL KIVRGSDPDT TWLIISPNAK KEYEPESTGS    50
    SFHDFLQLFD ETKVQYGLAR VSPPGSDVEK IIIIGWCPDS APLKTRASFA 100
    ANFAAVANNL FKGYHVQVTA RDEDDLDENE LLMKISNAAG ARYSIQTSSK 150
    QQGKASTPPV KKSFTPSKSP APVSKKEPVK TPSPAPAAKI SSRVNDNNDD 200
    DDWNEPELKE RDFDQAPLKP NQSSYKPIGK IDLQKVIAEE KAKEDPRLVQ 250
    KPTAAGSKID PSSDIANLKN ESKLKRDSEF NSFLGTTKPP SMTESSLKND 300
    DDKVIKGFRN EKSPAQLWAE RKAKQNSGNA ETKAEAPKPE VPEDEPEGEP 350
    DVKDLKSKFE GLAASEKEEE EMENKFAPPP KKSEPTIISP KPFSKPQEPV 400
    KAEEAEQPKT DYKKIGNPLP GMHIEADNEE EPEENDDDWD DDEDEAAQPP 450
    LPSRNVASGA PVQKEEPEQE EIAPSLPSRN SIPAPKQEEA PEQAPEEEIE 500
    EEAEEAAPQL PSRSSAAPPP PPRRATPEKK PKENPWATAE YDYDAAEDNE 550
    LTFVENDKII NIEFVDDDWW LGELEKDGSK GLFPSNYVSL GN 592
    Length:592
    Mass (Da):65,576
    Last modified:January 23, 2007 - v4
    Checksum:i39523510704D94AA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti58 – 581L → S in CAA36075. (PubMed:2405279)Curated
    Sequence conflicti312 – 3121K → I in CAA36075. (PubMed:2405279)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51780 Genomic DNA. Translation: CAA36075.1.
    X59720 Genomic DNA. Translation: CAA42253.1.
    BK006937 Genomic DNA. Translation: DAA07557.1.
    PIRiS19503. LLBY.
    RefSeqiNP_010012.1. NM_001178794.1.

    Genome annotation databases

    EnsemblFungiiYCR088W; YCR088W; YCR088W.
    GeneIDi850450.
    KEGGisce:YCR088W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51780 Genomic DNA. Translation: CAA36075.1 .
    X59720 Genomic DNA. Translation: CAA42253.1 .
    BK006937 Genomic DNA. Translation: DAA07557.1 .
    PIRi S19503. LLBY.
    RefSeqi NP_010012.1. NM_001178794.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HQZ X-ray 2.10 1/2/3/4/5/6/7/8/9 1-141 [» ]
    1JO8 X-ray 1.30 A 535-592 [» ]
    2K3B NMR - A 535-592 [» ]
    2RPN NMR - A 535-592 [» ]
    DisProti DP00634.
    ProteinModelPortali P15891.
    SMRi P15891. Positions 3-141, 535-592.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31060. 87 interactions.
    DIPi DIP-534N.
    IntActi P15891. 35 interactions.
    MINTi MINT-370108.
    STRINGi 4932.YCR088W.

    Proteomic databases

    MaxQBi P15891.
    PaxDbi P15891.
    PeptideAtlasi P15891.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YCR088W ; YCR088W ; YCR088W .
    GeneIDi 850450.
    KEGGi sce:YCR088W.

    Organism-specific databases

    SGDi S000000684. ABP1.

    Phylogenomic databases

    eggNOGi NOG265859.
    HOGENOMi HOG000246671.
    OMAi IINIEFV.
    OrthoDBi EOG7B05P0.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29382-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P15891.
    NextBioi 966066.
    PROi P15891.

    Gene expression databases

    Genevestigatori P15891.

    Family and domain databases

    Gene3Di 3.40.20.10. 1 hit.
    InterProi IPR002108. ADF-H.
    IPR029006. ADF-H/Gelsolin-like_dom.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00241. Cofilin_ADF. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    SMARTi SM00102. ADF. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS51263. ADF_H. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I."
      Drubin D.G., Mulholland J., Zhu Z., Botstein D.
      Nature 343:288-290(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The complete DNA sequence of yeast chromosome III."
      Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
      , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
      Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Bienvenut W.V., Peters C.
      Submitted (JUN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-13 AND 97-112, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    5. "A conserved proline-rich region of the Saccharomyces cerevisiae cyclase-associated protein binds SH3 domains and modulates cytoskeletal localization."
      Freeman N.L., Lila T., Mintzer K.A., Chen Z., Pahk A.J., Ren R., Drubin D.G., Field J.
      Mol. Cell. Biol. 16:548-556(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRV2.
    6. "In vivo analysis of the domains of yeast Rvs167p suggests Rvs167p function is mediated through multiple protein interactions."
      Colwill K., Field D., Moore L., Friesen J., Andrews B.
      Genetics 152:881-893(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RVS167.
    7. "Activation of the Arp2/3 complex by the actin filament binding protein Abp1p."
      Goode B.L., Rodal A.A., Barnes G., Drubin D.G.
      J. Cell Biol. 153:627-634(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ACTIN AND ARP2/3 COMPLEX, MUTAGENESIS OF 201-ASP--TRP-203 AND 437-ASP--TRP-439.
    8. "Sla1p couples the yeast endocytic machinery to proteins regulating actin dynamics."
      Warren D.T., Andrews P.D., Gourlay C.W., Ayscough K.R.
      J. Cell Sci. 115:1703-1715(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLA1, SUBCELLULAR LOCATION.
    9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    11. Cited for: INTERACTION WITH APP1; PRK1; SCP1 AND YIR003W.
    12. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-181; SER-183; SER-365 AND SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    13. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; THR-181; SER-183 AND SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; THR-181; SER-183; SER-313; SER-365; SER-389; SER-458 AND SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-165; SER-167; SER-169; THR-181; SER-313 AND SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis."
      Fazi B., Cope M.J.T.V., Douangamath A., Ferracuti S., Schirwitz K., Zucconi A., Drubin D.G., Wilmanns M., Cesareni G., Castagnoli L.
      J. Biol. Chem. 277:5290-5298(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF SH3 DOMAIN, MUTAGENESIS OF TRP-569, INTERACTION WITH ARK1 AND PRK1.
    19. "Structural and functional dissection of the Abp1 ADFH actin-binding domain reveals versatile in vivo adapter functions."
      Quintero-Monzon O., Rodal A.A., Strokopytov B., Almo S.C., Goode B.L.
      Mol. Biol. Cell 16:3128-3139(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF ADF DOMAIN, MUTAGENESIS OF LYS-21; ARG-24; LYS-80; LYS-94; ARG-96; ASP-122; ASP-125 AND LYS-134, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiABP1_YEAST
    AccessioniPrimary (citable) accession number: P15891
    Secondary accession number(s): D6VR88
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 150 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 606 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome III
      Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

    External Data

    Dasty 3