P32790 (SLA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Actin cytoskeleton-regulatory complex protein SLA1

Gene names

Name:	SLA1
Ordered Locus Names:	YBL007C
ORF Names:	YBL0321

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1244 AA.
Sequence status	Complete.
Protein existence	Evidence 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.26
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. Cytoplasm › cytoskeleton › actin 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.26
Post-translational modification	Phosphorylated by PRK1. Ref.11 Ref.27
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 process	Endocytosis
Cellular component	Cell membrane Cytoplasm Cytoskeleton Endosome Membrane Nucleus
Domain	Repeat SH3 domain
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cortical patch assembly Traceable author statement PubMed 10652251. Source: SGD endocytosis Inferred from physical interaction Ref.12. Source: SGD fungal-type cell wall organization Traceable author statement PubMed 10652251. Source: SGD
Cellular_component	actin cortical patch Inferred from direct assay Ref.9. Source: SGD endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mating projection tip Inferred from direct assay PubMed 19053807. Source: SGD nucleus Inferred from mutant phenotype Ref.26. Source: SGD plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ubiquitin binding Inferred from direct assay PubMed 17244534. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABP1	P15891	4	EBI-17313,EBI-2036
BSP1	Q06604	5	EBI-17313,EBI-37047
ECM25	P32525	3	EBI-17313,EBI-26215
END3	P39013	4	EBI-17313,EBI-6460
LSB3	P43603	6	EBI-17313,EBI-22980
LSB5	P25369	5	EBI-17313,EBI-10218
PAN1	P32521	5	EBI-17313,EBI-12875
VRP1	P37370	3	EBI-17313,EBI-20502
YSC84	P32793	6	EBI-17313,EBI-24460

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1244

1244

Actin cytoskeleton-regulatory complex protein SLA1

PRO_0000071943

Regions

Domain

8 – 69

62

SH3 1

Domain

70 – 132

63

SH3 2

Domain

353 – 415

63

SH3 3

Repeat

868 – 874

7

1

Repeat

877 – 883

7

2

Repeat

887 – 893

7

3

Repeat

923 – 929

7

4

Repeat

945 – 951

7

5

Repeat

1003 – 1009

7

6

Repeat

1020 – 1026

7

7

Repeat

1031 – 1037

7

8

Repeat

1048 – 1054

7

9

Repeat

1065 – 1071

7

10

Repeat

1084 – 1090

7

11

Repeat

1129 – 1135

7

12

Repeat

1155 – 1161

7

13

Repeat

1170 – 1176

7

14

Repeat

1185 – 1191

7

15

Repeat

1200 – 1206

7

16

Region

868 – 1205

338

16 X 7 AA approximate repeats of T-G-G-A-M-M-P

Amino acid modifications

Modified residue

202

1

Phosphothreonine Ref.25

Modified residue

437

1

Phosphoserine Ref.25 Ref.28

Modified residue

449

1

Phosphoserine Ref.28

Modified residue

454

1

Phosphoserine Ref.28

Modified residue

486

1

Phosphoserine Ref.24

Modified residue

785

1

Phosphoserine Ref.28

Modified residue

797

1

Phosphothreonine Ref.25 Ref.28

Modified residue

799

1

Phosphoserine Ref.25 Ref.28

Modified residue

818

1

Phosphothreonine Ref.28

Modified residue

831

1

Phosphothreonine Ref.24 Ref.28

Modified residue

858

1

Phosphothreonine Ref.28

Modified residue

877

1

Phosphothreonine Ref.28

Modified residue

887

1

Phosphothreonine Ref.28

Modified residue

904

1

Phosphothreonine Ref.28

Modified residue

921

1

Phosphoserine Ref.28

Modified residue

923

1

Phosphothreonine Ref.28

Modified residue

955

1

Phosphothreonine Ref.28

Modified residue

984

1

Phosphothreonine Ref.28

Modified residue

996

1

Phosphoserine Ref.28

Modified residue

1065

1

Phosphothreonine Ref.28

Secondary structure

1

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1244

Helix Strand Turn

Details...

Beta strand

357 – 360

4

Beta strand

379 – 387

9

Beta strand

389 – 396

8

Turn

397 – 399

3

Beta strand

402 – 406

5

Helix

407 – 409

3

Beta strand

410 – 412

3

Turn

413 – 415

3

Beta strand

497 – 505

9

Beta strand

508 – 517

10

Beta strand

520 – 524

5

Beta strand

530 – 534

5

Helix

540 – 550

11

Helix

555 – 557

3

Helix

657 – 663

7

Helix

668 – 680

13

Helix

685 – 690

6

Helix

693 – 698

6

Helix

703 – 716

14

Sequences

	Sequence		Length	Mass (Da)
	P32790 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 7FD85AA776407624	FASTA	1,244	135,848
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486 AND THR-831, MASS SPECTROMETRY. Strain: YAL6B.
[25]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202; SER-437; THR-797 AND SER-799, MASS SPECTROMETRY.
[26]	"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.
[27]	"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.
[28]	"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-437; SER-449; SER-454; SER-785; THR-797; SER-799; THR-818; THR-831; THR-858; THR-877; THR-887; THR-904; SER-921; THR-923; THR-955; THR-984; SER-996 AND THR-1065, MASS SPECTROMETRY.
[29]	"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.
[30]	"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.

PIR

S25327.

RefSeq

NP_009546.1. NM_001178247.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P32790.

SMR

P32790. Positions 7-67, 76-129, 350-420, 495-560, 654-719.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-695N.

IntAct

P32790. 64 interactions.

MINT

MINT-410065.

STRING

4932.YBL007C.

Proteomic databases

PaxDb

P32790.

PeptideAtlas

P32790.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YBL007C; YBL007C; YBL007C.

GeneID

852276.

KEGG

sce:YBL007C.

Organism-specific databases

CYGD

YBL007c.

SGD

S000000103. SLA1.

Phylogenomic databases

eggNOG

NOG120160.

GeneTree

ENSGT00680000101300.

HOGENOM

HOG000157527.

OMA

FGAQMTG.

OrthoDB

EOG4N33X1.

Gene expression databases

Genevestigator

P32790.

GermOnline

YBL007C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001452. SH3_domain.
IPR007131. SHD1.
[Graphical view]

Pfam

PF00018. SH3_1. 3 hits.
PF03983. SHD1. 1 hit.
[Graphical view]

PRINTS

PR00452. SH3DOMAIN.

SMART

SM00326. SH3. 3 hits.
[Graphical view]

SUPFAM

SSF50044. SH3. 3 hits.

PROSITE

PS50002. SH3. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P32790.

NextBio

970893.

Entry information

Entry name

SLA1_YEAST

Accession

Primary (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:	May 1, 2013
This is version 138 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program