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P32790

- SLA1_YEAST

UniProt

P32790 - SLA1_YEAST

Protein

Actin cytoskeleton-regulatory complex protein SLA1

Gene

SLA1

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 152 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization.15 Publications

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein binding Source: IntAct
    3. protein binding, bridging Source: SGD
    4. ubiquitin binding Source: SGD

    GO - Biological processi

    1. actin cortical patch assembly Source: SGD
    2. actin filament polymerization Source: SGD
    3. endocytosis Source: SGD
    4. fungal-type cell wall organization Source: SGD

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-28913-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Actin cytoskeleton-regulatory complex protein SLA1
    Gene namesi
    Name:SLA1
    Ordered Locus Names:YBL007C
    ORF Names:YBL0321
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBL007c.
    SGDiS000000103. SLA1.

    Subcellular locationi

    Nucleus. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeletonactin patch
    Note: Cytoplasmic and cortical actin patches. Is associated with cortical actin patches in its dephosphorylated form and dissociates upon phosphorylation by PRK1.

    GO - Cellular componenti

    1. actin cortical patch Source: SGD
    2. cell cortex Source: SGD
    3. endosome membrane Source: UniProtKB-SubCell
    4. nucleus Source: SGD
    5. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Endosome, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12441244Actin cytoskeleton-regulatory complex protein SLA1PRO_0000071943Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei447 – 4471Phosphoserine1 Publication
    Modified residuei449 – 4491Phosphoserine1 Publication
    Modified residuei454 – 4541Phosphoserine1 Publication
    Modified residuei799 – 7991Phosphoserine1 Publication
    Modified residuei831 – 8311Phosphothreonine1 Publication
    Modified residuei858 – 8581Phosphothreonine1 Publication
    Modified residuei887 – 8871Phosphothreonine2 Publications
    Modified residuei904 – 9041Phosphothreonine2 Publications
    Modified residuei984 – 9841Phosphothreonine2 Publications
    Modified residuei993 – 9931Phosphothreonine1 Publication
    Modified residuei996 – 9961Phosphoserine2 Publications
    Modified residuei1075 – 10751Phosphothreonine1 Publication

    Post-translational modificationi

    Phosphorylated by PRK1.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32790.
    PaxDbiP32790.
    PeptideAtlasiP32790.

    Expressioni

    Gene expression databases

    GenevestigatoriP32790.

    Interactioni

    Subunit structurei

    Component of the PAN1 actin cytoskeleton-regulatory complex. Interacts with ABP1, KRE6, LAS17, LSB5, RSP5, RVS167, VPS1 and YSC84.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself11EBI-17313,EBI-17313
    ABP1P158914EBI-17313,EBI-2036
    AIM21P405634EBI-17313,EBI-25376
    APP1P539334EBI-17313,EBI-28798
    BSP1Q066046EBI-17313,EBI-37047
    CHC1P221374EBI-17313,EBI-4766
    ECM25P325255EBI-17313,EBI-26215
    END3P390134EBI-17313,EBI-6460
    INP52P509423EBI-17313,EBI-28834
    KEX2P1313416EBI-17313,EBI-9658
    LAS17Q124466EBI-17313,EBI-10022
    LSB3P436038EBI-17313,EBI-22980
    LSB5P253695EBI-17313,EBI-10218
    MPS1P541992EBI-17313,EBI-11224
    PAN1P325215EBI-17313,EBI-12875
    RRP7P253683EBI-17313,EBI-16019
    STD1Q027943EBI-17313,EBI-18344
    SYP1P256233EBI-17313,EBI-21900
    VRP1P373703EBI-17313,EBI-20502
    YSC84P327938EBI-17313,EBI-24460
    ZDS2P547863EBI-17313,EBI-29637

    Protein-protein interaction databases

    BioGridi32692. 414 interactions.
    DIPiDIP-695N.
    IntActiP32790. 156 interactions.
    MINTiMINT-410065.
    STRINGi4932.YBL007C.

    Structurei

    Secondary structure

    1
    1244
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi357 – 3604
    Beta strandi379 – 3879
    Beta strandi389 – 3968
    Turni397 – 3993
    Beta strandi402 – 4065
    Helixi407 – 4093
    Beta strandi410 – 4123
    Turni413 – 4153
    Beta strandi497 – 5059
    Beta strandi508 – 51710
    Beta strandi520 – 5245
    Beta strandi530 – 5345
    Helixi540 – 55011
    Helixi555 – 5573
    Helixi657 – 6637
    Helixi668 – 68013
    Helixi685 – 6906
    Helixi693 – 6986
    Helixi703 – 71614

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SSHX-ray1.40B191-202[»]
    1Z9ZX-ray1.95A/B357-413[»]
    2HBPNMR-A495-560[»]
    2JT4NMR-A350-420[»]
    2V1QX-ray1.20A/B357-413[»]
    3IDWX-ray1.85A653-724[»]
    ProteinModelPortaliP32790.
    SMRiP32790. Positions 7-67, 76-129, 350-420, 495-560, 654-719.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32790.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 6962SH3 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini70 – 13263SH3 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini353 – 41563SH3 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati868 – 87471
    Repeati877 – 88372
    Repeati887 – 89373
    Repeati923 – 92974
    Repeati945 – 95175
    Repeati1003 – 100976
    Repeati1020 – 102677
    Repeati1031 – 103778
    Repeati1048 – 105479
    Repeati1065 – 1071710
    Repeati1084 – 1090711
    Repeati1129 – 1135712
    Repeati1155 – 1161713
    Repeati1170 – 1176714
    Repeati1185 – 1191715
    Repeati1200 – 1206716

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni868 – 120533816 X 7 AA approximate repeats of T-G-G-A-M-M-PAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SLA1 family.Curated
    Contains 3 SH3 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiNOG120160.
    GeneTreeiENSGT00730000114400.
    HOGENOMiHOG000157527.
    OMAiYIEEAPV.
    OrthoDBiEOG7VTDWK.

    Family and domain databases

    InterProiIPR001452. SH3_domain.
    IPR007131. SHD1.
    [Graphical view]
    PfamiPF00018. SH3_1. 2 hits.
    PF14604. SH3_9. 1 hit.
    PF03983. SHD1. 1 hit.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    SMARTiSM00326. SH3. 3 hits.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 3 hits.
    PROSITEiPS50002. SH3. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32790-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTVFLGIYRA VYAYEPQTPE ELAIQEDDLL YLLQKSDIDD WWTVKKRVIG     50
    SDSEEPVGLV PSTYIEEAPV LKKVRAIYDY EQVQNADEEL TFHENDVFDV 100
    FDDKDADWLL VKSTVSNEFG FIPGNYVEPE NGSTSKQEQA PAAAEAPAAT 150
    PAAAPASAAV LPTNFLPPPQ HNDRARMMQS KEDQAPDEDE EGPPPAMPAR 200
    PTATTETTDA TAAAVRSRTR LSYSDNDNDD EEDDYYYNSN SNNVGNHEYN 250
    TEYHSWNVTE IEGRKKKKAK LSIGNNKINF IPQKGTPHEW SIDKLVSYDN 300
    EKKHMFLEFV DPYRSLELHT GNTTTCEEIM NIIGEYKGAS RDPGLREVEM 350
    ASKSKKRGIV QYDFMAESQD ELTIKSGDKV YILDDKKSKD WWMCQLVDSG 400
    KSGLVPAQFI EPVRDKKHTE STASGIIKSI KKNFTKSPSR SRSRSRSKSN 450
    ANASWKDDEL QNDVVGSAAG KRSRKSSLSS HKKNSSATKD FPNPKKSRLW 500
    VDRSGTFKVD AEFIGCAKGK IHLHKANGVK IAVAADKLSN EDLAYVEKIT 550
    GFSLEKFKAN DGSSSRGTDS RDSERERRRR LKEQEEKERD RRLKERELYE 600
    LKKARELLDE ERSRLQEKEL PPIKPPRPTS TTSVPNTTSV PPAESSNNNN 650
    SSNKYDWFEF FLNCGVDVSN CQRYTINFDR EQLTEDMMPD INNSMLRTLG 700
    LREGDIVRVM KHLDKKFGRE NIASIPTNAT GNMFSQPDGS LNVATSPETS 750
    LPQQLLPQTT SPAQTAPSTS AETDDAWTVK PASKSESNLL SKKSEFTGSM 800
    QDLLDLQPLE PKKAAASTPE PNLKDLEPVK TGGTTVPAAP VSSAPVSSAP 850
    APLDPFKTGG NNILPLSTGF VMMPMITGGD MLPMQRTGGF VVPQTTFGMQ 900
    SQVTGGILPV QKTGNGLIPI SNTGGAMMPQ TTFGAAATVL PLQKTGGGLI 950
    PIATTGGAQF PQTSFNVQGQ QQLPTGSILP VQKTANGLIS ANTGVSMPTV 1000
    QRTGGTMIPQ TSFGVSQQLT GGAMMTQPQN TGSAMMPQTS FNAVPQITGG 1050
    AMMPQTSFNA LPQVTGGAMM PLQRTGGALN TFNTGGAMIP QTSFSSQAQN 1100
    TGGFRPQSQF GLTLQKTGGI APLNQNQFTG GAMNTLSTGG VLQQQQPQTM 1150
    NTFNTGGVMQ ELQMMTTFNT GGAMQQPQMM NTFNTDGIMQ QPQMMNTFNT 1200
    GGAMQQPQQQ ALQNQPTGFG FGNGPQQSRQ ANIFNATASN PFGF 1244
    Length:1,244
    Mass (Da):135,848
    Last modified:October 1, 1993 - v1
    Checksum:i7FD85AA776407624
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z22810 Genomic DNA. Translation: CAA80463.1.
    Z35768 Genomic DNA. Translation: CAA84826.1.
    S47695 Genomic DNA. Translation: AAB23985.1.
    BK006936 Genomic DNA. Translation: DAA07113.1.
    PIRiS25327.
    RefSeqiNP_009546.1. NM_001178247.1.

    Genome annotation databases

    EnsemblFungiiYBL007C; YBL007C; YBL007C.
    GeneIDi852276.
    KEGGisce:YBL007C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z22810 Genomic DNA. Translation: CAA80463.1 .
    Z35768 Genomic DNA. Translation: CAA84826.1 .
    S47695 Genomic DNA. Translation: AAB23985.1 .
    BK006936 Genomic DNA. Translation: DAA07113.1 .
    PIRi S25327.
    RefSeqi NP_009546.1. NM_001178247.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SSH X-ray 1.40 B 191-202 [» ]
    1Z9Z X-ray 1.95 A/B 357-413 [» ]
    2HBP NMR - A 495-560 [» ]
    2JT4 NMR - A 350-420 [» ]
    2V1Q X-ray 1.20 A/B 357-413 [» ]
    3IDW X-ray 1.85 A 653-724 [» ]
    ProteinModelPortali P32790.
    SMRi P32790. Positions 7-67, 76-129, 350-420, 495-560, 654-719.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32692. 414 interactions.
    DIPi DIP-695N.
    IntActi P32790. 156 interactions.
    MINTi MINT-410065.
    STRINGi 4932.YBL007C.

    Proteomic databases

    MaxQBi P32790.
    PaxDbi P32790.
    PeptideAtlasi P32790.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBL007C ; YBL007C ; YBL007C .
    GeneIDi 852276.
    KEGGi sce:YBL007C.

    Organism-specific databases

    CYGDi YBL007c.
    SGDi S000000103. SLA1.

    Phylogenomic databases

    eggNOGi NOG120160.
    GeneTreei ENSGT00730000114400.
    HOGENOMi HOG000157527.
    OMAi YIEEAPV.
    OrthoDBi EOG7VTDWK.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-28913-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P32790.
    NextBioi 970893.

    Gene expression databases

    Genevestigatori P32790.

    Family and domain databases

    InterProi IPR001452. SH3_domain.
    IPR007131. SHD1.
    [Graphical view ]
    Pfami PF00018. SH3_1. 2 hits.
    PF14604. SH3_9. 1 hit.
    PF03983. SHD1. 1 hit.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    SMARTi SM00326. SH3. 3 hits.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 3 hits.
    PROSITEi PS50002. SH3. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae."
      Holtzman D.A., Yang S., Drubin D.G.
      J. Cell Biol. 122:635-644(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: DDY 228.
    2. "Sequence of a 12.7 kb segment of yeast chromosome II identifies a PDR-like gene and several new open reading frames."
      Delaveau T., Jacq C., Perea J.
      Yeast 8:761-768(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "The EH-domain-containing protein Pan1 is required for normal organization of the actin cytoskeleton in Saccharomyces cerevisiae."
      Tang H.-Y., Cai M.
      Mol. Cell. Biol. 16:4897-4914(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "A role for the actin cytoskeleton of Saccharomyces cerevisiae in bipolar bud-site selection."
      Yang S., Ayscough K.R., Drubin D.G.
      J. Cell Biol. 136:111-123(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Bee1, a yeast protein with homology to Wiscott-Aldrich syndrome protein, is critical for the assembly of cortical actin cytoskeleton."
      Li R.
      J. Cell Biol. 136:649-658(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LAS17.
    8. "High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A."
      Ayscough K.R., Stryker J., Pokala N., Sanders M., Crews P., Drubin D.G.
      J. Cell Biol. 137:399-416(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Sla1p is a functionally modular component of the yeast cortical actin cytoskeleton required for correct localization of both Rho1p-GTPase and Sla2p, a protein with talin homology."
      Ayscough K.R., Eby J.J., Lila T., Dewar H., Kozminski K.G., Drubin D.G.
      Mol. Biol. Cell 10:1061-1075(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION.
    10. "Pan1p, End3p, and Sla1p, three yeast proteins required for normal cortical actin cytoskeleton organization, associate with each other and play essential roles in cell wall morphogenesis."
      Tang H.-Y., Xu J., Cai M.
      Mol. Cell. Biol. 20:12-25(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE PAN1 COMPLEX.
    11. "Regulation of yeast actin cytoskeleton-regulatory complex Pan1p/Sla1p/End3p by serine/threonine kinase Prk1p."
      Zeng G., Yu X., Cai M.
      Mol. Biol. Cell 12:3759-3772(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PAN1 COMPLEX, PHOSPHORYLATION BY PRK1, SUBCELLULAR LOCATION.
    12. "Sla1p serves as the targeting signal recognition factor for NPFX(1,2)D-mediated endocytosis."
      Howard J.P., Hutton J.L., Olson J.M., Payne G.S.
      J. Cell Biol. 157:315-326(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "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: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ABP1 AND LAS17.
    14. "Novel proteins linking the actin cytoskeleton to the endocytic machinery in Saccharomyces cerevisiae."
      Dewar H., Warren D.T., Gardiner F.C., Gourlay C.G., Satish N., Richardson M.R., Andrews P.D., Ayscough K.R.
      Mol. Biol. Cell 13:3646-3661(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LSB5 AND YSC84.
    15. "Actin patch assembly proteins Las17p and Sla1p restrict cell wall growth to daughter cells and interact with cis-Golgi protein Kre6p."
      Li H., Page N., Bussey H.
      Yeast 19:1097-1112(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KRE6.
    16. "Negative regulation of yeast WASp by two SH3 domain-containing proteins."
      Rodal A.A., Manning A.L., Goode B.L., Drubin D.G.
      Curr. Biol. 13:1000-1008(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "An interaction between Sla1p and Sla2p plays a role in regulating actin dynamics and endocytosis in budding yeast."
      Gourlay C.W., Dewar H., Warren D.T., Costa R., Satish N., Ayscough K.R.
      J. Cell Sci. 116:2551-2564(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SLA2.
    18. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    19. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    20. "The Rsp5 ubiquitin ligase binds to and ubiquitinates members of the yeast CIN85-endophilin complex, Sla1-Rvs167."
      Stamenova S.D., Dunn R., Adler A.S., Hicke L.
      J. Biol. Chem. 279:16017-16025(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RSP5 AND RVS167.
    21. "Lsb5p interacts with actin regulators Sla1p and Las17p, ubiquitin and Arf3p to couple actin dynamics to membrane trafficking processes."
      Costa R., Warren D.T., Ayscough K.R.
      Biochem. J. 387:649-658(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LSB5.
    22. "The yeast dynamin-related GTPase Vps1p functions in the organization of the actin cytoskeleton via interaction with Sla1p."
      Yu X., Cai M.
      J. Cell Sci. 117:3839-3853(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VPS1.
    23. "Actin and septin ultrastructures at the budding yeast cell cortex."
      Rodal A.A., Kozubowski L., Goode B.L., Drubin D.G., Hartwig J.H.
      Mol. Biol. Cell 16:372-384(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    25. "Nucleocytoplasmic trafficking is required for functioning of the adaptor protein Sla1p in endocytosis."
      Gardiner F.C., Costa R., Ayscough K.R.
      Traffic 8:347-358(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION.
    26. "A novel function of Arp2p in mediating Prk1p-specific regulation of actin and endocytosis in yeast."
      Jin M., Cai M.
      Mol. Biol. Cell 19:297-307(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY ARK1.
    27. "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-799; THR-831; THR-858; THR-887; THR-904; THR-984 AND SER-996, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "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 SER-447; SER-449; SER-454; THR-887; THR-904; THR-984; THR-993; SER-996 AND THR-1075, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "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].
    31. "Structure of Sla1p homology domain 1 and interaction with the NPFxD endocytic internalization motif."
      Mahadev R.K., Di Pietro S.M., Olson J.M., Piao H.L., Payne G.S., Overduin M.
      EMBO J. 26:1963-1971(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 495-560, DOMAIN.
    32. "Structural basis for ubiquitin recognition by SH3 domains."
      He Y., Hicke L., Radhakrishnan I.
      J. Mol. Biol. 373:190-196(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 350-420, DOMAIN.

    Entry informationi

    Entry nameiSLA1_YEAST
    AccessioniPrimary (citable) accession number: P32790
    Secondary accession number(s): D6VPZ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 152 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 952 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, 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 II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3