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P40482 (SEC24_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 136. 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:
Protein transport protein SEC24
Alternative name(s):
Abnormal nuclear morphology 1
Gene names
Name:SEC24
Synonyms:ANU1
Ordered Locus Names:YIL109C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length926 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SEC24 specifically recruits cargo proteins like BET1 or SYS1 to the COPII vesicles. The SEC23/24 complex is also involved in internalisation of plasma membrane proteins like the maltose transporter. Ref.5 Ref.8 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.28 Ref.29 Ref.32 Ref.33

Subunit structure

The COPII coat is composed of at least 7 proteins: the SEC23/24 complex, the SEC13/31 complex, SFB2, SFB3 and the protein SAR1. Interacts with BET1, EMP24, GRH1, SEC22, SED5 and SYS1. Ref.4 Ref.6 Ref.7 Ref.9 Ref.11 Ref.13 Ref.16 Ref.19 Ref.20 Ref.21 Ref.28 Ref.31 Ref.33 Ref.34 Ref.36

Subcellular location

Cytoplasm. Cytoplasmic vesicleCOPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Potential Ref.5 Ref.9 Ref.14 Ref.16 Ref.17 Ref.18 Ref.26 Ref.30.

Sequence similarities

Belongs to the SEC23/SEC24 family. SEC24 subfamily.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 926926Protein transport protein SEC24
PRO_0000205150

Regions

Region231 – 25626Zinc finger-like
Compositional bias110 – 1145Poly-Gln
Compositional bias157 – 1604Poly-Pro

Sites

Metal binding2311Zinc
Metal binding2341Zinc
Metal binding2531Zinc
Metal binding2561Zinc

Amino acid modifications

Modified residue1781Phosphoserine Ref.22

Experimental info

Mutagenesis2301R → A: Abolishes binding to and packaging of cargo protein BET1. Ref.28
Mutagenesis2311C → S: Lethal. Ref.4
Mutagenesis2351R → A: Abolishes binding to and packaging of cargo protein BET1. Ref.28
Mutagenesis5591R → M: Abolishes binding to and packaging of cargo protein BET1. Ref.28
Mutagenesis5611R → M: Abolishes binding to and packaging of cargo protein BET1. Ref.28
Mutagenesis6161L → W: Abolishes binding to and packaging of cargo protein BET1. Ref.28

Secondary structure

.................................................................................................................................... 926
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P40482 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 35E2BDD24CC75899

FASTA926103,636
        10         20         30         40         50         60 
MSHHKKRVYP QAQLQYGQNA TPLQQPAQFM PPQDPAAAGM SYGQMGMPPQ GAVPSMGQQQ 

        70         80         90        100        110        120 
FLTPAQEQLH QQIDQATTSM NDMHLHNVPL VDPNAYMQPQ VPVQMGTPLQ QQQQPMAAPA 

       130        140        150        160        170        180 
YGQPSAAMGQ NMRPMNQLYP IDLLTELPPP ITDLTLPPPP LVIPPERMLV PSELSNASPD 

       190        200        210        220        230        240 
YIRSTLNAVP KNSSLLKKSK LPFGLVIRPY QHLYDDIDPP PLNEDGLIVR CRRCRSYMNP 

       250        260        270        280        290        300 
FVTFIEQGRR WRCNFCRLAN DVPMQMDQSD PNDPKSRYDR NEIKCAVMEY MAPKEYTLRQ 

       310        320        330        340        350        360 
PPPATYCFLI DVSQSSIKSG LLATTINTLL QNLDSIPNHD ERTRISILCV DNAIHYFKIP 

       370        380        390        400        410        420 
LDSENNEESA DQINMMDIAD LEEPFLPRPN SMVVSLKACR QNIETLLTKI PQIFQSNLIT 

       430        440        450        460        470        480 
NFALGPALKS AYHLIGGVGG KIIVVSGTLP NLGIGKLQRR NESGVVNTSK ETAQLLSCQD 

       490        500        510        520        530        540 
SFYKNFTIDC SKVQITVDLF LASEDYMDVA SLSNLSRFTA GQTHFYPGFS GKNPNDIVKF 

       550        560        570        580        590        600 
STEFAKHISM DFCMETVMRA RGSTGLRMSR FYGHFFNRSS DLCAFSTMPR DQSYLFEVNV 

       610        620        630        640        650        660 
DESIMADYCY VQVAVLLSLN NSQRRIRIIT LAMPTTESLA EVYASADQLA IASFYNSKAV 

       670        680        690        700        710        720 
EKALNSSLDD ARVLINKSVQ DILATYKKEI VVSNTAGGAP LRLCANLRMF PLLMHSLTKH 

       730        740        750        760        770        780 
MAFRSGIVPS DHRASALNNL ESLPLKYLIK NIYPDVYSLH DMADEAGLPV QTEDGEATGT 

       790        800        810        820        830        840 
IVLPQPINAT SSLFERYGLY LIDNGNELFL WMGGDAVPAL VFDVFGTQDI FDIPIGKQEI 

       850        860        870        880        890        900 
PVVENSEFNQ RVRNIINQLR NHDDVITYQS LYIVRGASLS EPVNHASARE VATLRLWASS 

       910        920 
TLVEDKILNN ESYREFLQIM KARISK 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"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.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"Specific interaction of the yeast cis-Golgi syntaxin Sed5p and the coat protein complex II component Sec24p of endoplasmic reticulum-derived transport vesicles."
Peng R., Grabowski R., De Antoni A., Gallwitz D.
Proc. Natl. Acad. Sci. U.S.A. 96:3751-3756(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 731-740 AND 774-793, INTERACTION WITH SED5, MUTAGENESIS OF CYS-231.
[5]"COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast."
Bednarek S.Y., Ravazzola M., Hosobuchi M., Amherdt M., Perrelet A., Schekman R.W., Orci L.
Cell 83:1183-1196(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"COPII coat subunit interactions: Sec24p and Sec23p bind to adjacent regions of Sec16p."
Gimeno R.E., Espenshade P.J., Kaiser C.A.
Mol. Biol. Cell 7:1815-1823(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SEC16.
[7]"COPII subunit interactions in the assembly of the vesicle coat."
Shaywitz D.A., Espenshade P.J., Gimeno R.E., Kaiser C.A.
J. Biol. Chem. 272:25413-25416(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE COPII COAT, INTERACTION WITH SEC16.
[8]"Selective packaging of cargo molecules into endoplasmic reticulum-derived COPII vesicles."
Campbell J.L., Schekman R.W.
Proc. Natl. Acad. Sci. U.S.A. 94:837-842(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes."
Matsuoka K., Orci L., Amherdt M., Bednarek S.Y., Hamamoto S., Schekman R.W., Yeung T.
Cell 93:263-275(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[10]"COPII-cargo interactions direct protein sorting into ER-derived transport vesicles."
Kuehn M.J., Herrmann J.M., Schekman R.W.
Nature 391:187-190(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE SEC23/24 COMPLEX.
[11]"Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs."
Springer S., Schekman R.W.
Science 281:698-700(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BET1; BOS1; SAR1 AND SEC23.
[12]"Clathrin and two components of the COPII complex, Sec23p and Sec24p, could be involved in endocytosis of the Saccharomyces cerevisiae maltose transporter."
Penalver E., Lucero P., Moreno E., Lagunas R.
J. Bacteriol. 181:2555-2563(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE SEC23/24 COMPLEX.
[13]"Shr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesicles."
Gilstring C.F., Melin-Larsson M., Ljungdahl P.O.
Mol. Biol. Cell 10:3549-3565(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHR3.
[14]"Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p family members."
Peng R., De Antoni A., Gallwitz D.
J. Biol. Chem. 275:11521-11528(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[15]"Sfb2p, a yeast protein related to Sec24p, can function as a constituent of COPII coats required for vesicle budding from the endoplasmic reticulum."
Higashio H., Kimata Y., Kiriyama T., Hirata A., Kohno K.
J. Biol. Chem. 275:17900-17908(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae."
Shimoni Y., Kurihara T., Ravazzola M., Amherdt M., Orci L., Schekman R.W.
J. Cell Biol. 151:973-984(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PMA1.
[17]"The use of liposomes to study COPII- and COPI-coated vesicle formation and membrane protein sorting."
Matsuoka K., Schekman R.W.
Methods 20:417-428(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[18]"Sec24p and Iss1p function interchangeably in transport vesicle formation from the endoplasmic reticulum in Saccharomyces cerevisiae."
Kurihara T., Hamamoto S., Gimeno R.E., Kaiser C.A., Schekman R.W., Yoshihisa T.
Mol. Biol. Cell 11:983-998(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[19]"An acidic sequence of a putative yeast Golgi membrane protein binds COPII and facilitates ER export."
Votsmeier C., Gallwitz D.
EMBO J. 20:6742-6750(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYS1.
[20]"Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in transport between the endoplasmic reticulum and Golgi complex."
Belden W.J., Barlowe C.
J. Biol. Chem. 276:43040-43048(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EMP24 AND ERV25.
[21]"Dynamics of the COPII coat with GTP and stable analogues."
Antonny B., Madden D.T., Hamamoto S., Orci L., Schekman R.W.
Nat. Cell Biol. 3:531-537(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE COPII COAT.
[22]"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-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[23]"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].
[24]"Structure of the Sec23p/24p and Sec13p/31p complexes of COPII."
Lederkremer G.Z., Cheng Y., Petre B.M., Vogan E., Springer S., Schekman R.W., Walz T., Kirchhausen T.
Proc. Natl. Acad. Sci. U.S.A. 98:10704-10709(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ELECTRON MICROSCOPY OF THE SEC23/24 COMPLEX.
[25]"Surface structure of the COPII-coated vesicle."
Matsuoka K., Schekman R.W., Orci L., Heuser J.E.
Proc. Natl. Acad. Sci. U.S.A. 98:13705-13709(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ELECTRON MICROSCOPY OF THE SEC23/24 COMPLEX.
[26]"Sec16p potentiates the action of COPII proteins to bud transport vesicles."
Supek F., Madden D.T., Hamamoto S., Orci L., Schekman R.W.
J. Cell Biol. 158:1029-1038(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[27]"Self-assembly of minimal COPII cages."
Antonny B., Gounon P., Schekman R.W., Orci L.
EMBO Rep. 4:419-424(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF THE COPII COMPLEX.
[28]"Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles."
Miller E.A., Beilharz T.H., Malkus P.N., Lee M.C.S., Hamamoto S., Orci L., Schekman R.W.
Cell 114:497-509(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BET1 AND SYS1, MUTAGENESIS OF ARG-230; ARG-235; ARG-559; ARG-561 AND LEU-616.
[29]"The early secretory pathway contributes to autophagy in yeast."
Hamasaki M., Noda T., Ohsumi Y.
Cell Struct. Funct. 28:49-54(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[30]"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].
[31]"Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23."
Cohen M., Stutz F., Belgareh N., Haguenauer-Tsapis R., Dargemont C.
Nat. Cell Biol. 5:661-667(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SEC23.
[32]"Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting."
Sato K., Nakano A.
J. Biol. Chem. 279:1330-1335(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: COPII COMPLEX ASSEMBLY, FUNCTION OF THE COPII COMPLEX.
[33]"Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile."
Schuldiner M., Collins S.R., Thompson N.J., Denic V., Bhamidipati A., Punna T., Ihmels J., Andrews B., Boone C., Greenblatt J.F., Weissman J.S., Krogan N.J.
Cell 123:507-519(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GRH1.
[34]"The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein that contributes to ER to Golgi traffic."
Behnia R., Barr F.A., Flanagan J.J., Barlowe C., Munro S.
J. Cell Biol. 176:255-261(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GHR1.
[35]"Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat."
Bi X., Corpina R.A., Goldberg J.
Nature 419:271-277(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SEC23 AND ZINC.
[36]"SNARE selectivity of the COPII coat."
Mossessova E., Bickford L.C., Goldberg J.
Cell 114:483-495(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 117-926 IN COMPLEX WITH SED5; SYS1; BET1 AND ZINC, INTERACTION WITH SEC22.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z38125 Genomic DNA. Translation: CAA86271.1.
AY692888 Genomic DNA. Translation: AAT92907.1.
BK006942 Genomic DNA. Translation: DAA08444.1.
PIRS48463.
RefSeqNP_012157.3. NM_001179457.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M2VX-ray2.75B1-926[»]
1PCXX-ray2.50A117-926[»]
1PD0X-ray2.60A117-926[»]
1PD1X-ray2.60A117-926[»]
4BZIelectron microscopy23.00E/F/L/M/N/O1-926[»]
ProteinModelPortalP40482.
SMRP40482. Positions 133-926.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34882. 71 interactions.
DIPDIP-2233N.
IntActP40482. 22 interactions.
MINTMINT-476513.
STRING4932.YIL109C.

Proteomic databases

MaxQBP40482.
PaxDbP40482.
PeptideAtlasP40482.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIL109C; YIL109C; YIL109C.
GeneID854697.
KEGGsce:YIL109C.

Organism-specific databases

CYGDYIL109c.
SGDS000001371. SEC24.

Phylogenomic databases

eggNOGCOG5028.
GeneTreeENSGT00590000082962.
HOGENOMHOG000196365.
KOK14007.
OMAIDETIND.
OrthoDBEOG71K6BX.

Enzyme and pathway databases

BioCycYEAST:G3O-31364-MONOMER.

Gene expression databases

GenevestigatorP40482.

Family and domain databases

Gene3D3.40.20.10. 1 hit.
3.40.50.410. 1 hit.
InterProIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR006900. Sec23/24_helical_dom.
IPR006896. Sec23/24_trunk_dom.
IPR012990. Sec23_24_beta_S.
IPR002035. VWF_A.
IPR006895. Znf_Sec23_Sec24.
[Graphical view]
PfamPF00626. Gelsolin. 1 hit.
PF08033. Sec23_BS. 1 hit.
PF04815. Sec23_helical. 1 hit.
PF04811. Sec23_trunk. 1 hit.
PF04810. zf-Sec23_Sec24. 1 hit.
[Graphical view]
SUPFAMSSF53300. SSF53300. 1 hit.
SSF81811. SSF81811. 1 hit.
SSF82919. SSF82919. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP40482.
NextBio977337.

Entry information

Entry nameSEC24_YEAST
AccessionPrimary (citable) accession number: P40482
Secondary accession number(s): D6VVH8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 136 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 IX

Yeast (Saccharomyces cerevisiae) chromosome IX: 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