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P32790

- SLA1_YEAST

UniProt

P32790 - SLA1_YEAST

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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

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, bridging Source: SGD
  3. 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
Complete GO annotation...

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 Source: UniProtKB-KW
  4. nucleus Source: SGD
  5. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

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. 415 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 – 3604Combined sources
Beta strandi379 – 3879Combined sources
Beta strandi389 – 3968Combined sources
Turni397 – 3993Combined sources
Beta strandi402 – 4065Combined sources
Helixi407 – 4093Combined sources
Beta strandi410 – 4123Combined sources
Turni413 – 4153Combined sources
Beta strandi497 – 5059Combined sources
Beta strandi508 – 51710Combined sources
Beta strandi520 – 5245Combined sources
Beta strandi530 – 5345Combined sources
Helixi540 – 55011Combined sources
Helixi555 – 5573Combined sources
Helixi657 – 6637Combined sources
Helixi668 – 68013Combined sources
Helixi685 – 6906Combined sources
Helixi693 – 6986Combined sources
Helixi703 – 71614Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP32790.
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

        10         20         30         40         50
MTVFLGIYRA VYAYEPQTPE ELAIQEDDLL YLLQKSDIDD WWTVKKRVIG
60 70 80 90 100
SDSEEPVGLV PSTYIEEAPV LKKVRAIYDY EQVQNADEEL TFHENDVFDV
110 120 130 140 150
FDDKDADWLL VKSTVSNEFG FIPGNYVEPE NGSTSKQEQA PAAAEAPAAT
160 170 180 190 200
PAAAPASAAV LPTNFLPPPQ HNDRARMMQS KEDQAPDEDE EGPPPAMPAR
210 220 230 240 250
PTATTETTDA TAAAVRSRTR LSYSDNDNDD EEDDYYYNSN SNNVGNHEYN
260 270 280 290 300
TEYHSWNVTE IEGRKKKKAK LSIGNNKINF IPQKGTPHEW SIDKLVSYDN
310 320 330 340 350
EKKHMFLEFV DPYRSLELHT GNTTTCEEIM NIIGEYKGAS RDPGLREVEM
360 370 380 390 400
ASKSKKRGIV QYDFMAESQD ELTIKSGDKV YILDDKKSKD WWMCQLVDSG
410 420 430 440 450
KSGLVPAQFI EPVRDKKHTE STASGIIKSI KKNFTKSPSR SRSRSRSKSN
460 470 480 490 500
ANASWKDDEL QNDVVGSAAG KRSRKSSLSS HKKNSSATKD FPNPKKSRLW
510 520 530 540 550
VDRSGTFKVD AEFIGCAKGK IHLHKANGVK IAVAADKLSN EDLAYVEKIT
560 570 580 590 600
GFSLEKFKAN DGSSSRGTDS RDSERERRRR LKEQEEKERD RRLKERELYE
610 620 630 640 650
LKKARELLDE ERSRLQEKEL PPIKPPRPTS TTSVPNTTSV PPAESSNNNN
660 670 680 690 700
SSNKYDWFEF FLNCGVDVSN CQRYTINFDR EQLTEDMMPD INNSMLRTLG
710 720 730 740 750
LREGDIVRVM KHLDKKFGRE NIASIPTNAT GNMFSQPDGS LNVATSPETS
760 770 780 790 800
LPQQLLPQTT SPAQTAPSTS AETDDAWTVK PASKSESNLL SKKSEFTGSM
810 820 830 840 850
QDLLDLQPLE PKKAAASTPE PNLKDLEPVK TGGTTVPAAP VSSAPVSSAP
860 870 880 890 900
APLDPFKTGG NNILPLSTGF VMMPMITGGD MLPMQRTGGF VVPQTTFGMQ
910 920 930 940 950
SQVTGGILPV QKTGNGLIPI SNTGGAMMPQ TTFGAAATVL PLQKTGGGLI
960 970 980 990 1000
PIATTGGAQF PQTSFNVQGQ QQLPTGSILP VQKTANGLIS ANTGVSMPTV
1010 1020 1030 1040 1050
QRTGGTMIPQ TSFGVSQQLT GGAMMTQPQN TGSAMMPQTS FNAVPQITGG
1060 1070 1080 1090 1100
AMMPQTSFNA LPQVTGGAMM PLQRTGGALN TFNTGGAMIP QTSFSSQAQN
1110 1120 1130 1140 1150
TGGFRPQSQF GLTLQKTGGI APLNQNQFTG GAMNTLSTGG VLQQQQPQTM
1160 1170 1180 1190 1200
NTFNTGGVMQ ELQMMTTFNT GGAMQQPQMM NTFNTDGIMQ QPQMMNTFNT
1210 1220 1230 1240
GGAMQQPQQQ ALQNQPTGFG FGNGPQQSRQ ANIFNATASN PFGF
Length:1,244
Mass (Da):135,848
Last modified:October 1, 1993 - v1
Checksum:i7FD85AA776407624
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 415 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.
InParanoidi P32790.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 154 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