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P32790 (SLA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actin cytoskeleton-regulatory complex protein SLA1
Gene names
Name:SLA1
Ordered Locus Names:YBL007C
ORF Names:YBL0321
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1244 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5 Ref.6 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.20 Ref.23 Ref.25

Subunit structure

Component of the PAN1 actin cytoskeleton-regulatory complex. Interacts with ABP1, KRE6, LAS17, LSB5, RSP5, RVS167, VPS1 and YSC84. Ref.7 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17 Ref.20 Ref.21 Ref.22

Subcellular location

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. Ref.9 Ref.11 Ref.13 Ref.17 Ref.18 Ref.25

Post-translational modification

Phosphorylated by PRK1. Ref.11 Ref.26

Miscellaneous

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

Sequence similarities

Belongs to the SLA1 family.

Contains 3 SH3 domains.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Endosome
Membrane
Nucleus
   DomainRepeat
SH3 domain
   LigandActin-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cortical patch assembly

Traceable author statement PubMed 10652251. Source: SGD

actin filament polymerization

Inferred from direct assay PubMed 22973053. Source: SGD

endocytosis

Inferred from mutant phenotype Ref.12. Source: SGD

fungal-type cell wall organization

Traceable author statement PubMed 10652251. Source: SGD

   Cellular_componentactin cortical patch

Inferred from direct assay Ref.9. Source: SGD

cell cortex

Inferred from direct assay Ref.13. Source: SGD

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.25. Source: SGD

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 11805826Ref.14PubMed 18467557PubMed 20150898. Source: IntAct

protein binding

Inferred from physical interaction Ref.10PubMed 10688190PubMed 11743162PubMed 11805826Ref.13Ref.14PubMed 14737190Ref.21PubMed 16429126Ref.31PubMed 18467557PubMed 19841731PubMed 20150898. Source: IntAct

protein binding, bridging

Inferred from physical interaction Ref.13. Source: SGD

ubiquitin binding

Inferred from direct assay PubMed 17244534. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12441244Actin cytoskeleton-regulatory complex protein SLA1
PRO_0000071943

Regions

Domain8 – 6962SH3 1
Domain70 – 13263SH3 2
Domain353 – 41563SH3 3
Repeat868 – 87471
Repeat877 – 88372
Repeat887 – 89373
Repeat923 – 92974
Repeat945 – 95175
Repeat1003 – 100976
Repeat1020 – 102677
Repeat1031 – 103778
Repeat1048 – 105479
Repeat1065 – 1071710
Repeat1084 – 1090711
Repeat1129 – 1135712
Repeat1155 – 1161713
Repeat1170 – 1176714
Repeat1185 – 1191715
Repeat1200 – 1206716
Region868 – 120533816 X 7 AA approximate repeats of T-G-G-A-M-M-P

Amino acid modifications

Modified residue4471Phosphoserine Ref.28
Modified residue4491Phosphoserine Ref.28
Modified residue4541Phosphoserine Ref.28
Modified residue7991Phosphoserine Ref.27
Modified residue8311Phosphothreonine Ref.27
Modified residue8581Phosphothreonine Ref.27
Modified residue8871Phosphothreonine Ref.27 Ref.28
Modified residue9041Phosphothreonine Ref.27 Ref.28
Modified residue9841Phosphothreonine Ref.27 Ref.28
Modified residue9931Phosphothreonine Ref.28
Modified residue9961Phosphoserine Ref.27 Ref.28
Modified residue10751Phosphothreonine Ref.28

Secondary structure

................................... 1244
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32790 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 7FD85AA776407624

FASTA1,244135,848
        10         20         30         40         50         60 
MTVFLGIYRA VYAYEPQTPE ELAIQEDDLL YLLQKSDIDD WWTVKKRVIG SDSEEPVGLV 

        70         80         90        100        110        120 
PSTYIEEAPV LKKVRAIYDY EQVQNADEEL TFHENDVFDV FDDKDADWLL VKSTVSNEFG 

       130        140        150        160        170        180 
FIPGNYVEPE NGSTSKQEQA PAAAEAPAAT PAAAPASAAV LPTNFLPPPQ HNDRARMMQS 

       190        200        210        220        230        240 
KEDQAPDEDE EGPPPAMPAR PTATTETTDA TAAAVRSRTR LSYSDNDNDD EEDDYYYNSN 

       250        260        270        280        290        300 
SNNVGNHEYN TEYHSWNVTE IEGRKKKKAK LSIGNNKINF IPQKGTPHEW SIDKLVSYDN 

       310        320        330        340        350        360 
EKKHMFLEFV DPYRSLELHT GNTTTCEEIM NIIGEYKGAS RDPGLREVEM ASKSKKRGIV 

       370        380        390        400        410        420 
QYDFMAESQD ELTIKSGDKV YILDDKKSKD WWMCQLVDSG KSGLVPAQFI EPVRDKKHTE 

       430        440        450        460        470        480 
STASGIIKSI KKNFTKSPSR SRSRSRSKSN ANASWKDDEL QNDVVGSAAG KRSRKSSLSS 

       490        500        510        520        530        540 
HKKNSSATKD FPNPKKSRLW VDRSGTFKVD AEFIGCAKGK IHLHKANGVK IAVAADKLSN 

       550        560        570        580        590        600 
EDLAYVEKIT GFSLEKFKAN DGSSSRGTDS RDSERERRRR LKEQEEKERD RRLKERELYE 

       610        620        630        640        650        660 
LKKARELLDE ERSRLQEKEL PPIKPPRPTS TTSVPNTTSV PPAESSNNNN SSNKYDWFEF 

       670        680        690        700        710        720 
FLNCGVDVSN CQRYTINFDR EQLTEDMMPD INNSMLRTLG LREGDIVRVM KHLDKKFGRE 

       730        740        750        760        770        780 
NIASIPTNAT GNMFSQPDGS LNVATSPETS LPQQLLPQTT SPAQTAPSTS AETDDAWTVK 

       790        800        810        820        830        840 
PASKSESNLL SKKSEFTGSM QDLLDLQPLE PKKAAASTPE PNLKDLEPVK TGGTTVPAAP 

       850        860        870        880        890        900 
VSSAPVSSAP APLDPFKTGG NNILPLSTGF VMMPMITGGD MLPMQRTGGF VVPQTTFGMQ 

       910        920        930        940        950        960 
SQVTGGILPV QKTGNGLIPI SNTGGAMMPQ TTFGAAATVL PLQKTGGGLI PIATTGGAQF 

       970        980        990       1000       1010       1020 
PQTSFNVQGQ QQLPTGSILP VQKTANGLIS ANTGVSMPTV QRTGGTMIPQ TSFGVSQQLT 

      1030       1040       1050       1060       1070       1080 
GGAMMTQPQN TGSAMMPQTS FNAVPQITGG AMMPQTSFNA LPQVTGGAMM PLQRTGGALN 

      1090       1100       1110       1120       1130       1140 
TFNTGGAMIP QTSFSSQAQN TGGFRPQSQF GLTLQKTGGI APLNQNQFTG GAMNTLSTGG 

      1150       1160       1170       1180       1190       1200 
VLQQQQPQTM NTFNTGGVMQ ELQMMTTFNT GGAMQQPQMM NTFNTDGIMQ QPQMMNTFNT 

      1210       1220       1230       1240 
GGAMQQPQQQ ALQNQPTGFG FGNGPQQSRQ ANIFNATASN PFGF 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[19]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z22810 Genomic DNA. Translation: CAA80463.1.
Z35768 Genomic DNA. Translation: CAA84826.1.
S47695 Genomic DNA. Translation: AAB23985.1.
BK006936 Genomic DNA. Translation: DAA07113.1.
PIRS25327.
RefSeqNP_009546.1. NM_001178247.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP32790.
SMRP32790. Positions 7-67, 76-129, 350-420, 495-560, 654-719.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32692. 412 interactions.
DIPDIP-695N.
IntActP32790. 156 interactions.
MINTMINT-410065.
STRING4932.YBL007C.

Proteomic databases

MaxQBP32790.
PaxDbP32790.
PeptideAtlasP32790.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBL007C; YBL007C; YBL007C.
GeneID852276.
KEGGsce:YBL007C.

Organism-specific databases

CYGDYBL007c.
SGDS000000103. SLA1.

Phylogenomic databases

eggNOGNOG120160.
GeneTreeENSGT00730000114400.
HOGENOMHOG000157527.
OMAYIEEAPV.
OrthoDBEOG7VTDWK.

Enzyme and pathway databases

BioCycYEAST:G3O-28913-MONOMER.

Gene expression databases

GenevestigatorP32790.

Family and domain databases

InterProIPR001452. SH3_domain.
IPR007131. SHD1.
[Graphical view]
PfamPF00018. SH3_1. 2 hits.
PF14604. SH3_9. 1 hit.
PF03983. SHD1. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00326. SH3. 3 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 3 hits.
PROSITEPS50002. SH3. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32790.
NextBio970893.

Entry information

Entry nameSLA1_YEAST
AccessionPrimary (citable) accession number: P32790
Secondary accession number(s): D6VPZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 11, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references