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P16649 (TUP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. 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:
General transcriptional corepressor TUP1
Alternative name(s):
Flocculation suppressor protein
Glucose repression regulatory protein TUP1
Repressor AER2
Gene names
Name:TUP1
Synonyms:AAR1, AER2, AMM1, CYC9, FLK1, SFL2, UMR7
Ordered Locus Names:YCR084C
ORF Names:YCR84C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length713 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as component of the CYC8-TUP1 corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. May also be involved in the derepression of at least some target genes. The complex is recruited to target genes by interaction with DNA-bound transcriptional repressors, like MATALPHA2, MIG1, RFX1 and SKO1. The complex recruits histone deacetylases to produce a repressive chromatin structure, interacts with hypoacetylated N-terminal tails of histones H3 and H4 that have been programmed for repression by the action of histone deacetylases and interferes directly with the transcriptional machinery by associating with the RNA polymerase II mediator complex. Ref.1 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17

Subunit structure

Associates with CYC8/SSN6 to form the CYC8-TUP1 (or TUP1-SSN6) corepressor complex that is composed of 4 copies of TUP1 and one copy of CYC8. Interacts with histone H3, histone H4, MATALPHA2, RFX1, SKO1, PGD1, HDA1, HDA2, HOS1, HOS2 AND RPD3. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.18

Subcellular location

Nucleus Ref.19.

Miscellaneous

Present with 5840 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the WD repeat TUP1 family.

Contains 7 WD repeats.

Sequence caution

The sequence CAA34411.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
WD repeat
   Molecular functionRepressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistone exchange

Inferred from mutant phenotype PubMed 17387147. Source: SGD

negative regulation of dipeptide transport by negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 18708352. Source: SGD

negative regulation of mating-type specific transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 1312982. Source: SGD

negative regulation of transcription from RNA polymerase II promoter by glucose

Inferred from mutant phenotype PubMed 9461460. Source: SGD

negative regulation of transcription from RNA polymerase II promoter during mitosis

Inferred from mutant phenotype PubMed 9560430. Source: SGD

nucleosome positioning

Inferred from direct assay PubMed 15116071. Source: SGD

regulation of fatty acid biosynthetic process by regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 9280286. Source: SGD

regulation of response to DNA damage stimulus

Inferred from mutant phenotype Ref.10. Source: SGD

regulation of transcription from RNA polymerase II promoter in response to hypoxia

Inferred from mutant phenotype Ref.2. Source: SGD

regulation of transcription from RNA polymerase II promoter in response to osmotic stress

Inferred from mutant phenotype PubMed 9858577. Source: SGD

   Cellular_componentnucleus

Inferred from direct assay PubMed 1739976. Source: SGD

transcriptional repressor complex

Inferred from direct assay PubMed 9111019. Source: SGD

   Molecular_functionRNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription

Inferred from direct assay Ref.10. Source: SGD

histone binding

Inferred from direct assay Ref.8. Source: SGD

histone deacetylase binding

Inferred from direct assay Ref.18. Source: SGD

mediator complex binding

Inferred from direct assay PubMed 11226276. Source: SGD

phosphatidylinositol-3,5-bisphosphate binding

Inferred from direct assay PubMed 21536737. Source: SGD

protein binding

Inferred from physical interaction Ref.12Ref.11Ref.18PubMed 16429126PubMed 18467557Ref.10. Source: IntAct

ubiquitin binding

Inferred from direct assay PubMed 21070969. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 713713General transcriptional corepressor TUP1
PRO_0000051312

Regions

Repeat342 – 37130WD 1
Repeat441 – 47131WD 2
Repeat483 – 51331WD 3
Repeat524 – 55532WD 4
Repeat574 – 60431WD 5
Repeat628 – 65831WD 6
Repeat670 – 70637WD 7
Compositional bias97 – 11822Gln-rich
Compositional bias181 – 19818Poly-Gln
Compositional bias399 – 40911Thr-rich

Amino acid modifications

Modified residue4391Phosphoserine Ref.23

Experimental info

Sequence conflict751E → A in AAA35182. Ref.1
Sequence conflict1001R → Q in AAA35182. Ref.1
Sequence conflict6851P → S in AAA35182. Ref.1
Sequence conflict6851P → S in AAA34413. Ref.2

Secondary structure

........................................................................... 713
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16649 [UniParc].

Last modified May 1, 1991. Version 2.
Checksum: 444104AAD63CB944

FASTA71378,308
        10         20         30         40         50         60 
MTASVSNTQN KLNELLDAIR QEFLQVSQEA NTYRLQNQKD YDFKMNQQLA EMQQIRNTVY 

        70         80         90        100        110        120 
ELELTHRKMK DAYEEEIKHL KLGLEQRDHQ IASLTVQQQR QQQQQQQVQQ HLQQQQQQLA 

       130        140        150        160        170        180 
AASASVPVAQ QPPATTSATA TPAANTTTGS PSAFPVQASR PNLVGSQLPT TTLPVVSSNA 

       190        200        210        220        230        240 
QQQLPQQQLQ QQQLQQQQPP PQVSVAPLSN TAINGSPTSK ETTTLPSVKA PESTLKETEP 

       250        260        270        280        290        300 
ENNNTSKIND TGSATTATTT TATETEIKPK EEDATPASLH QDHYLVPYNQ RANHSKPIPP 

       310        320        330        340        350        360 
FLLDLDSQSV PDALKKQTND YYILYNPALP REIDVELHKS LDHTSVVCCV KFSNDGEYLA 

       370        380        390        400        410        420 
TGCNKTTQVY RVSDGSLVAR LSDDSAANNH RNSITENNTT TSTDNNTMTT TTTTTITTTA 

       430        440        450        460        470        480 
MTSAAELAKD VENLNTSSSP SSDLYIRSVC FSPDGKFLAT GAEDRLIRIW DIENRKIVMI 

       490        500        510        520        530        540 
LQGHEQDIYS LDYFPSGDKL VSGSGDRTVR IWDLRTGQCS LTLSIEDGVT TVAVSPGDGK 

       550        560        570        580        590        600 
YIAAGSLDRA VRVWDSETGF LVERLDSENE SGTGHKDSVY SVVFTRDGQS VVSGSLDRSV 

       610        620        630        640        650        660 
KLWNLQNANN KSDSKTPNSG TCEVTYIGHK DFVLSVATTQ NDEYILSGSK DRGVLFWDKK 

       670        680        690        700        710 
SGNPLLMLQG HRNSVISVAV ANGSPLGPEY NVFATGSGDC KARIWKYKKI APN 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of TUP1, a mediator of glucose repression in Saccharomyces cerevisiae."
Williams F.E., Trumbly R.J.
Mol. Cell. Biol. 10:6500-6511(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"A yeast protein with homology to the beta-subunit of G proteins is involved in control of heme-regulated and catabolite-repressed genes."
Zhang M., Rosenblum-Vos L.S., Lowry C.V., Boakye K., Zitomer R.S.
Gene 97:153-161(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of the yeast SFL2 gene: its disruption results in pleiotropic phenotypes characteristic for tup1 mutants."
Fujita A., Matsumoto S., Kuhara S., Misumi Y., Kobayashi H.
Gene 89:93-99(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 44774 / DBY747.
[4]"The complete DNA sequence of yeast chromosome III."
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. expand/collapse author list , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"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.
[6]"The SFL2 (TUP1?) protein of Saccharomyces cerevisiae contains a repeating motif homologous to beta subunits of G proteins."
Kearsley S.
Gene 98:147-148(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SIMILARITY TO BETA SUBUNIT OF G-PROTEINS.
[7]"The WD repeats of Tup1 interact with the homeo domain protein alpha 2."
Komachi K., Redd M.J., Johnson A.D.
Genes Dev. 8:2857-2867(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MATALPHA2.
[8]"Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4."
Edmondson D.G., Smith M.M., Roth S.Y.
Genes Dev. 10:1247-1259(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HISTONE H3 AND HISTONE H4.
[9]"The Cyc8 (Ssn6)-Tup1 corepressor complex is composed of one Cyc8 and four Tup1 subunits."
Varanasi U.S., Klis M., Mikesell P.B., Trumbly R.J.
Mol. Cell. Biol. 16:6707-6714(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[10]"The DNA replication and damage checkpoint pathways induce transcription by inhibition of the Crt1 repressor."
Huang M., Zhou Z., Elledge S.J.
Cell 94:595-605(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RFX1.
[11]"Ssn6-Tup1 interacts with class I histone deacetylases required for repression."
Watson A.D., Edmondson D.G., Bone J.R., Mukai Y., Yu Y., Du W., Stillman D.J., Roth S.Y.
Genes Dev. 14:2737-2744(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CYC8 AND RPD3, FUNCTION OF THE CYC8-TUP1 COMPLEX.
[12]"Hrs1/Med3 is a Cyc8-Tup1 corepressor target in the RNA polymerase II holoenzyme."
Papamichos-Chronakis M., Conlan R.S., Gounalaki N., Copf T., Tzamarias D.
J. Biol. Chem. 275:8397-8403(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PGD1, FUNCTION OF THE CYC8-TUP1 COMPLEX.
[13]"Regulation of the Sko1 transcriptional repressor by the Hog1 MAP kinase in response to osmotic stress."
Proft M., Pascual-Ahuir A., de Nadal E., Arino J., Serrano R., Posas F.
EMBO J. 20:1123-1133(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE CYC8-TUP1 COMPLEX.
[14]"Multiple levels of control regulate the yeast cAMP-response element-binding protein repressor Sko1p in response to stress."
Pascual-Ahuir A., Posas F., Serrano R., Proft M.
J. Biol. Chem. 276:37373-37378(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKO1.
[15]"TUP1 utilizes histone H3/H2B-specific HDA1 deacetylase to repress gene activity in yeast."
Wu J., Suka N., Carlson M., Grunstein M.
Mol. Cell 7:117-126(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HDA1 AND HDA2, FUNCTION OF THE CYC8-TUP1 COMPLEX.
[16]"Histone-dependent association of Tup1-Ssn6 with repressed genes in vivo."
Davie J.K., Trumbly R.J., Dent S.Y.
Mol. Cell. Biol. 22:693-703(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE CYC8-TUP1 COMPLEX.
[17]"Recruitment of Tup1-Ssn6 by yeast hypoxic genes and chromatin-independent exclusion of TATA binding protein."
Mennella T.A., Klinkenberg L.G., Zitomer R.S.
Eukaryot. Cell 2:1288-1303(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE CYC8-TUP1 COMPLEX.
[18]"Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo."
Davie J.K., Edmondson D.G., Coco C.B., Dent S.Y.
J. Biol. Chem. 278:50158-50162(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HOS1; HOS2 AND RPD3.
[19]"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].
[20]"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].
[21]"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.
[22]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"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-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"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].
[25]"Structure of the C-terminal domain of Tup1, a corepressor of transcription in yeast."
Sprague E.R., Redd M.J., Johnson A.D., Wolberger C.
EMBO J. 19:3016-3027(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 282-713.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31733 Genomic DNA. Translation: AAA35182.1.
M35861 Genomic DNA. Translation: AAA34413.1.
X16365 Genomic DNA. Translation: CAA34411.1. Different initiation.
X59720 Genomic DNA. Translation: CAA42259.1.
BK006937 Genomic DNA. Translation: DAA07554.1.
PIRJN0133.
RefSeqNP_010007.1. NM_001178790.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ERJX-ray2.30A/B/C282-388[»]
A/B/C432-713[»]
3VP8X-ray1.91A/B/C/D1-92[»]
3VP9X-ray1.80A/B1-92[»]
ProteinModelPortalP16649.
SMRP16649. Positions 2-81, 283-710.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31057. 92 interactions.
DIPDIP-512N.
IntActP16649. 16 interactions.
MINTMINT-648551.

Proteomic databases

MaxQBP16649.
PaxDbP16649.
PeptideAtlasP16649.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCR084C; YCR084C; YCR084C.
GeneID850445.
KEGGsce:YCR084C.

Organism-specific databases

CYGDYCR084c.
SGDS000000680. TUP1.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00750000117788.
HOGENOMHOG000200558.
KOK06666.
OMAINEMALM.
OrthoDBEOG7TN01P.

Enzyme and pathway databases

BioCycYEAST:G3O-29380-MONOMER.

Gene expression databases

GenevestigatorP16649.

Family and domain databases

Gene3D2.130.10.10. 2 hits.
InterProIPR020472. G-protein_beta_WD-40_rep.
IPR013890. Tscrpt_rep_Tup1_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF08581. Tup_N. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
ProDomPD010558. Transcrip_repressor_Tup1_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 2 hits.
PROSITEPS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16649.
NextBio966057.

Entry information

Entry nameTUP1_YEAST
AccessionPrimary (citable) accession number: P16649
Secondary accession number(s): D6VR85, P17995, P18323
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: May 1, 1991
Last modified: July 9, 2014
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: 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