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Q04439 (MYO5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 140. 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:
Myosin-5
Alternative name(s):
Actin-dependent myosin-I MYO5
Class I unconventional myosin MYO5
Type I myosin MYO5
Gene names
Name:MYO5
Ordered Locus Names:YMR109W
ORF Names:YM9718.08
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1219 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

One of two redundant type-I myosins implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions redundantly with LAS17 as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Motor domain phosphorylation by PAK kinases CLA4 and STE20 promotes CDC42-regulated actin assembly. Functions together with the NPF PAN1 in late stages of endocytosis. Motor domain phosphorylation by PDK1 kinases PKH1 and PKH2, and by SGK kinases YPK1 and YPK2, promotes ligand-induced, but not constitutive endocytosis of the G protein-coupled receptor STE2. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.11 Ref.12 Ref.14

Subunit structure

Interacts (via myosin motor domain) with SHE4; this interaction is important for proper localization and may regulate the interaction of the motor domain with actin. Interacts (via SH3 domain) with VRP1; this interaction is required for localization to sites of polarized growth and may regulate the interaction of the tail domain with actin. Interacts (via SH3 domain) with PAN1; this interaction is important for late stages of endocytopsis. Interacts (via SH3 domain) with BBC1 and LAS17. Interacts (via C-terminal acidic tail) with ARC19 and ARC40; ARC19 and ARC40 are Arp2/3 complex subunits. Interacts with BZZ1, PKH1, PKH2, YPK1 and YPK2. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16

Subcellular location

Cytoplasmcytoskeletonactin patch. Note: Localizes to cortical patch-like protein structures that assemble actin patches. Enriched at sites of polarized growth. Ref.1 Ref.5 Ref.14 Ref.16

Domain

The myosin motor domain displays actin-stimulated ATPase activity and generates a mechanochemical force.

The tail domain participates in molecular interactions that specify the role of the motor domain. It is composed of several tail homology (TH) domains, namely a putative phospholipid-binding domain (TH1), an Ala- and Pro-rich domain (TH2), followed by an SH3 domain and a C-terminal acidic domain (TH3).

Post-translational modification

Phosphorylation of the TEDS site (Ser-357) is required for the polarization of the actin cytoskeleton and for ligand-induced, but not for constitutive internalization of STE2. Phosphorylation probably activates the myosin-I ATPase activity. Ser-357 is phosphorylated by YPK2 in vitro. Ref.14

Miscellaneous

Present with 2280 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.

Contains 2 IQ domains.

Contains 1 myosin motor domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   DomainRepeat
SH3 domain
   LigandActin-binding
ATP-binding
Nucleotide-binding
   Molecular functionHydrolase
Motor protein
Myosin
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cortical patch localization

Inferred from mutant phenotype PubMed 18177206. Source: SGD

bipolar cellular bud site selection

Traceable author statement PubMed 10652251. Source: SGD

endocytosis

Inferred from mutant phenotype PubMed 16824951. Source: SGD

exocytosis

Traceable author statement PubMed 10652251. Source: SGD

fungal-type cell wall organization

Traceable author statement PubMed 10652251. Source: SGD

metabolic process

Inferred from direct assay PubMed 16824951. Source: GOC

receptor-mediated endocytosis

Inferred from mutant phenotype Ref.4. Source: SGD

response to osmotic stress

Traceable author statement PubMed 10652251. Source: SGD

response to salt stress

Inferred from genetic interaction Ref.10. Source: SGD

   Cellular_componentactin cortical patch

Inferred from direct assay PubMed 16824951PubMed 20647997. Source: SGD

myosin complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

identical protein binding

Inferred from physical interaction PubMed 11743162PubMed 18467557PubMed 19841731PubMed 20647997Ref.5. Source: IntAct

microfilament motor activity

Inferred from direct assay PubMed 16824951. Source: SGD

protein binding

Inferred from physical interaction Ref.9. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12191219Myosin-5
PRO_0000123492

Regions

Domain36 – 715680Myosin motor
Domain719 – 73921IQ 1
Domain740 – 76526IQ 2
Domain1085 – 114763SH3
Nucleotide binding129 – 1368ATP Potential
Region404 – 48683Actin-binding By similarity
Region766 – 961196Basic, putative membrane-binding region
Compositional bias1000 – 108889Ala/Pro-rich
Compositional bias1011 – 10166Poly-Pro
Compositional bias1060 – 10634Poly-Ala
Compositional bias1073 – 10819Poly-Pro
Compositional bias1204 – 121815Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue3571Phosphoserine Ref.14 Ref.15 Ref.17 Ref.18
Modified residue3591Phosphotyrosine Ref.15
Modified residue7771Phosphoserine Ref.14
Modified residue9921Phosphoserine Ref.15
Modified residue12051Phosphoserine Ref.15 Ref.19

Experimental info

Mutagenesis1641V → I: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. Ref.12
Mutagenesis1681N → I: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. Ref.12
Mutagenesis2091N → S: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. Ref.12
Mutagenesis3571S → A: Leads to a depolarized actin cytoskeleton and a strong defect in the capacity to internalize STE2. Ref.14
Mutagenesis3571S → E: No growth defect, but leads to a partially depolarized actin cytoskeleton. Accelerates the constitutive internalization of STE2. Ref.14
Mutagenesis3771K → M: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. Ref.12
Mutagenesis4721E → K in MYO5-1; temperature sensitive loss of function. Ref.4
Mutagenesis11231W → S: Abolishes interaction with BBC1 and VRP1. Ref.6 Ref.9

Secondary structure

........... 1219
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q04439 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: DFFB9EC16B61CD29

FASTA1,219136,899
        10         20         30         40         50         60 
MAILKRGARK KVHQEPAKRS ANIKKATFDS SKKKEVGVSD LTLLSKISDE AINENLKKRF 

        70         80         90        100        110        120 
LNATIYTYIG HVLISVNPFR DLGIYTDAVM NEYKGKNRLE VPPHVFAIAE SMYYNMKSYN 

       130        140        150        160        170        180 
ENQCVIISGE SGAGKTEAAK RIMQYIAAAS STHTESIGKI KDMVLATNPL LESFGCAKTL 

       190        200        210        220        230        240 
RNNNSSRHGK YLEIKFNNQF EPCAGNITNY LLEKQRVVSQ IKNERNFHIF YQFTKGASDA 

       250        260        270        280        290        300 
YRQTFGVQKP EQYVYTAAAG CISAETIDDL QDYQETLKAM RVIGLGQEEQ DQIFRMLAAI 

       310        320        330        340        350        360 
LWIGNVSFIE NEEGNAQVRD TSVTDFVAYL LQIDSQLLIK SLVERIMETN HGMKRGSVYH 

       370        380        390        400        410        420 
VPLNIVQADA VRDALAKAIY NNLFDWIVSR VNKSLQAFPG AEKSIGILDI YGFEIFEHNS 

       430        440        450        460        470        480 
FEQICINYVN EKLQQIFIQL TLKSEQETYE REKIQWTPIK YFDNKVVCDL IEARRPPGIF 

       490        500        510        520        530        540 
AAMNDSVATA HADSNAADQA FAQRLNLFTT NPHFDLRSNK FVIKHYAGDV TYDIDGITDK 

       550        560        570        580        590        600 
NKDQLQKDLV ELIGTTTNTF LATIFPDTVD RESKRRPPTA GDKIIKSAND LVETLSKAQP 

       610        620        630        640        650        660 
SYIRTIKPNE TKSPNDYDDR QVLHQIKYLG LQENVRIRRA GFAYRQVFEK FVERFYLLSP 

       670        680        690        700        710        720 
HCSYAGDYTW QGDTLDAVKY ILQDSSIPQQ EYQLGVTSVF IKTPETLFAL EHMRDRYWHN 

       730        740        750        760        770        780 
MAARIQRAWR RFLQRRIDAA TKIQRTIRER KEGNKYEKLR DYGTKVLGGR KERRSMSLLG 

       790        800        810        820        830        840 
YRAFMGDYLS CNESKSKGAY IKRQVSIKEK VIFSIHGEAL HTKFGRSAQR LKKTFLLTPT 

       850        860        870        880        890        900 
TLYIVGQTLV QNAMTYTQDY KIDVRNIQAV SLTNLQDDWV AIKLASSGQP DPLINTYFKT 

       910        920        930        940        950        960 
ELITHLKRLN DKIQIKIGSA IEYQKKPGKL HSVKCQINES APKYGDIYKS STISVRRGNP 

       970        980        990       1000       1010       1020 
PNSQVHKKPR KKSSISSGYH ASSSQATRRP VSIAAAQHVP TAPASRHSKK PAPPPPGMQN 

      1030       1040       1050       1060       1070       1080 
KAATRRSVPN PASTLTASQS NARPSPPTAA TRATPAATPA AAAMGSGRQA NIPPPPPPPP 

      1090       1100       1110       1120       1130       1140 
PSSKPKEPMF EAAYDFPGSG SPSELPLKKG DVIYITREEP SGWSLGKLLD GSKEGWVPTA 

      1150       1160       1170       1180       1190       1200 
YMKPHSGNNN IPTPPQNRDV PKPVLNSVQH DNTSANVIPA AAQASLGDGL ANALAARANK 

      1210 
MRLESDDEEA NEDEEEDDW 

« Hide

References

« Hide 'large scale' references
[1]"Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton."
Goodson H.V., Anderson B.L., Warrick H.M., Pon L.A., Spudich J.A.
J. Cell Biol. 133:1277-1291(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"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.
[4]"Role of type I myosins in receptor-mediated endocytosis in yeast."
Geli M.I., Riezman H.
Science 272:533-535(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RECEPTOR ENDOCYTOSIS, MUTAGENESIS OF GLU-472.
[5]"The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization."
Anderson B.L., Boldogh I., Evangelista M., Boone C., Greene L.A., Pon L.A.
J. Cell Biol. 141:1357-1370(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VRP1, SUBCELLULAR LOCATION.
[6]"An intact SH3 domain is required for myosin I-induced actin polymerization."
Geli M.I., Lombardi R., Schmelzl B., Riezman H.
EMBO J. 19:4281-4291(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VRP1, MUTAGENESIS OF TRP-1123.
[7]"A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex."
Evangelista M., Klebl B.M., Tong A.H.Y., Webb B.A., Leeuw T., Leberer E., Whiteway M., Thomas D.Y., Boone C.
J. Cell Biol. 148:353-362(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ARC19 AND ARC40.
[8]"Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization."
Lechler T., Shevchenko A., Li R.
J. Cell Biol. 148:363-373(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LAS17.
[9]"The novel adaptor protein, Mti1p, and Vrp1p, a homolog of Wiskott-Aldrich syndrome protein-interacting protein (WIP), may antagonistically regulate type I myosins in Saccharomyces cerevisiae."
Mochida J., Yamamoto T., Fujimura-Kamada K., Tanaka K.
Genetics 160:923-934(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BBC1, MUTAGENESIS OF TRP-1123.
[10]"Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin patch polarization and is able to recruit actin-polymerizing machinery in vitro."
Soulard A., Lechler T., Spiridonov V., Shevchenko A., Shevchenko A., Li R., Winsor B.
Mol. Cell. Biol. 22:7889-7906(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BZZ1.
[11]"The UCS domain protein She4p binds to myosin motor domains and is essential for class I and class V myosin function."
Wesche S., Arnold M., Jansen R.-P.
Curr. Biol. 13:715-724(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SHE4.
[12]"She4p/Dim1p interacts with the motor domain of unconventional myosins in the budding yeast, Saccharomyces cerevisiae."
Toi H., Fujimura-Kamada K., Irie K., Takai Y., Todo S., Tanaka K.
Mol. Biol. Cell 14:2237-2249(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SHE4, MUTAGENESIS OF VAL-164; ASN-168; ASN-209 AND LYS-377.
[13]"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].
[14]"TEDS site phosphorylation of the yeast myosins I is required for ligand-induced but not for constitutive endocytosis of the G protein-coupled receptor Ste2p."
Grosshans B.L., Groetsch H., Mukhopadhyay D., Fernandez I.M., Pfannstiel J., Idrissi F.-Z., Lechner J., Riezman H., Geli M.I.
J. Biol. Chem. 281:11104-11114(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-357 AND SER-777, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-357, SUBCELLULAR LOCATION, INTERACTION WITH PKH1; PKH2; YPK1 AND YPK2.
[15]"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 SER-357; TYR-359; SER-992 AND SER-1205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[16]"Interaction of the endocytic scaffold protein Pan1 with the type I myosins contributes to the late stages of endocytosis."
Barker S.L., Lee L., Pierce B.D., Maldonado-Baez L., Drubin D.G., Wendland B.
Mol. Biol. Cell 18:2893-2903(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAN1, SUBCELLULAR LOCATION.
[17]"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-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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-1205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Yeast Myo5 SH3 domain, tetragonal crystal form."
Gonfloni S., Kursula P., Sacco R., Cesareni G., Wilmanns M.
Submitted (JAN-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 1088-1145.
[21]"High-resolution structure of yeast Myo5 SH3 domain."
Wilmanns M., Kursula P., Gonfloni S., Ferracuti S., Cesareni G.
Submitted (OCT-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.39 ANGSTROMS) OF 1088-1145.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49702 Genomic DNA. Translation: CAA89745.1.
BK006946 Genomic DNA. Translation: DAA10006.1.
PIRS54570.
RefSeqNP_013827.1. NM_001182609.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YP5X-ray1.68A1088-1145[»]
1ZUYX-ray1.39A/B1088-1145[»]
ProteinModelPortalQ04439.
SMRQ04439. Positions 37-715, 1088-1145.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35285. 116 interactions.
DIPDIP-2222N.
IntActQ04439. 99 interactions.
MINTMINT-593586.
STRING4932.YMR109W.

Proteomic databases

MaxQBQ04439.
PaxDbQ04439.
PeptideAtlasQ04439.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR109W; YMR109W; YMR109W.
GeneID855136.
KEGGsce:YMR109W.

Organism-specific databases

CYGDYMR109w.
SGDS000004715. MYO5.

Phylogenomic databases

eggNOGCOG5022.
GeneTreeENSGT00750000117868.
HOGENOMHOG000260265.
KOK10356.
OMALFRVINT.
OrthoDBEOG7VDXXK.

Enzyme and pathway databases

BioCycYEAST:G3O-32805-MONOMER.

Gene expression databases

GenevestigatorQ04439.

Family and domain databases

InterProIPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_tail_2.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00242. MYSc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS51456. MYOSIN_MOTOR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ04439.
NextBio978516.

Entry information

Entry nameMYO5_YEAST
AccessionPrimary (citable) accession number: Q04439
Secondary accession number(s): D6VZT2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 140 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 XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: 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