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SFB3/YHR098C Single Page Format

This page provides an alternative format to the SGD Locus Summary Page. Note that additional information may be available on or linked from the standard format SGD Locus Summary page.

Contents

Names and Identifiers GO Annotations Pathways Summary Paragraph Mutant Phenotypes Interactions Homologs Protein Info (physical properties, transcript info) PDB Homologs (protein structure info) Motifs Genome-wide Expression (and other large-scale analyses) Locus History (misc. notes) Sequence Retrieval and Analysis Map and Displays Localization Community Annotation Literature Guide

Sequence Coordinates   ChrVIII: 301937 to 299148 CDS: 301937 - 299148 Click on map for expanded view SGD ORF map GBrowse

SGD Locus Page

Names and Identifiers [TOP] [NEXT]
Standard Name	Systematic Name	Alias	Feature Type	SGDID
SFB3	YHR098C	LST1	ORF, Verified	S000001140
Description
Component of the Sec23p-Sfb3p heterodimer of the COPII vesicle coat, required for cargo selection during vesicle formation in ER to Golgi transport; homologous to Sec24p and Sfb2p

GO Annotations [TOP] [NEXT]
Molecular Function Annotation(s) Reference(s) Evidence Assigned By signal sequence binding Miller EA, et al. (2003) Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114(4):497-509      ISS : Inferred from Sequence or structural Similarity with SGD:SEC24 Assigned on 2010-01-05 SGD zinc ion binding DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR006895 Assigned on 2007-05-23 UniProtKB
Biological Process Annotation(s) Reference(s) Evidence Assigned By ER to Golgi vesicle-mediated transport DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR006895 , EBI:IPR006896 , EBI:IPR006900 Assigned on 2008-02-13 UniProtKB cargo loading into COPII-coated vesicle Miller E, et al. (2002) Cargo selection into COPII vesicles is driven by the Sec24p subunit. EMBO J 21(22):6105-13          IDA : Inferred from Direct Assay Assigned on 2010-01-05 SGD Miller EA, et al. (2003) Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114(4):497-509      IMP : Inferred from Mutant Phenotype IDA : Inferred from Direct Assay Assigned on 2010-01-05 SGD intracellular protein transport DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR006895 , EBI:IPR006896 , EBI:IPR006900 Assigned on 2007-05-23 UniProtKB protein transport GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0653 Assigned on 2007-05-23 UniProtKB transport GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0813 Assigned on 2007-05-23 UniProtKB vesicle-mediated transport GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0931 Assigned on 2008-02-14 UniProtKB
Cellular Component Annotation(s) Reference(s) Evidence Assigned By COPII vesicle coat Shimoni Y, et al. (2000) Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. J Cell Biol 151(5):973-84        IDA : Inferred from Direct Assay Assigned on 2010-01-05 SGD Miller E, et al. (2002) Cargo selection into COPII vesicles is driven by the Sec24p subunit. EMBO J 21(22):6105-13          IDA : Inferred from Direct Assay Assigned on 2010-01-05 SGD DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR006895 , EBI:IPR006896 , EBI:IPR006900 Assigned on 2007-05-23 UniProtKB Golgi apparatus GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0333 Assigned on 2008-02-14 UniProtKB Golgi membrane GOA curators and UniProt curators (2007) Gene Ontology annotation based on Swiss-Prot Subcellular Location vocabulary mapping.      IEA : Inferred from Electronic Annotation with EBI:SL-0134 Assigned on 2008-07-02 UniProtKB cytoplasm GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0963 Assigned on 2008-02-14 UniProtKB GOA curators and UniProt curators (2007) Gene Ontology annotation based on Swiss-Prot Subcellular Location vocabulary mapping.      IEA : Inferred from Electronic Annotation with EBI:SL-0086 Assigned on 2008-02-13 UniProtKB endoplasmic reticulum GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0256 Assigned on 2007-05-23 UniProtKB endoplasmic reticulum membrane GOA curators and UniProt curators (2007) Gene Ontology annotation based on Swiss-Prot Subcellular Location vocabulary mapping.      IEA : Inferred from Electronic Annotation with EBI:SL-0097 Assigned on 2008-07-02 UniProtKB mating projection tip Narayanaswamy R, et al. (2009) Systematic Definition of Protein Constituents along the Major Polarization Axis Reveals an Adaptive Reuse of the Polarization Machinery in Pheromone-Treated Budding Yeast. J Proteome Res 8(1):6-19        IDA : Inferred from Direct Assay Assigned on 2008-12-19 SGD membrane GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0472 Assigned on 2008-06-16 UniProtKB

Pathways [TOP] [NEXT]
No pathways available

Summary Paragraph [TOP] [NEXT]

SUMMARY PARAGRAPH for SFB3/YHR098C for SFB3 Transport of proteins from the endoplasmic reticulum (ER) to the Golgi is mediated by COPII vesicles (1). The COPII vesicle coat is minimally comprised of 5 subunits: the GTPase Sar1p, the Sec23p-Sec24p heterodimer, and the Sec13p-Sec31p complex (2, 3, 4, 5). COPII vesicle coats can also contain heterodimers of Sec23p complexed with either of the Sec24p homologs, Sfb2p or Sfb3p (6, 7, 8). In S. cerevisiae, COPII vesicle formation occurs throughout the ER (9). In most other eukaryotes, COPII vesicle-mediated protein export is localized to specialized regions termed transitional ER (tER) or ER exit sites (ERES) (3). COPII vesicle formation requires the assembly of the COPII vesicle coat and cargo selection and is regulated by cycles of GTP hydrolysis. The GTP exchange factor (GEF) Sec12p, an ER membrane protein, activates Sar1p by exchanging GDP for GTP. Sar1p-GTP recruits the Sec23p-Sec24p heterodimer. Sec23p is a GTPase activating protein (GAP) for the Sar1p GTPase activity (10, 11, and reviewed in 3). Sec24p, Sfb2p, and Sfb3p, are involved in cargo selection (12, 8, 7). Sar1p, the Sec23p-Sec24p heterodimer, and cargo form the prebudding complex. Improper cargo selection results in GTP hydrolysis and diassembly of the prebudding complex (13). However, once the pre-budding complex is assembled, Sec13p and Sec31p polymerize to form the outer layer or scaffold of the COPII vesicle coat. The Sec13p-Sec31p complex further stimulates the GTPase activity of Sar1p (reviewed in 3). Although Sar1p, Sec23p, Sec24p, Sec13p, and Sec31p are necessary and sufficient for vesicle formation, additional factors such as Sec16p and Sed4p are also involved in this process. Through interactions with other COPII proteins, Sec16p is thought to facilitate the assembly of the vesicle coat by stabilizing the pre-budding complex (14) while Sed4p may regulate the vesicle budding process by inhibiting the GAP activity of Sec23p (15). Mutations in genes involved in COPII vesicle formation are also impaired in other processes such as ERAD (ER-associated degradation) and autophagy, suggesting that ER to the Golgi transport is a prerequisite for these processes to occur (16, 17, 18, 19). Mutations in the human homolog of SEC23, Sec23A, cause the autosomal recessive disorder Cranio-lenticulo sutural dysplasia (CLSD), while mutation of Sar1B, one of the two human isoforms of S. cerevisiae Sar1p, cause defects in lipoprotein metabolism including the diseases that are known as the chylomicron retention diseases (CMRDs) (reviewed in 3). Last Updated: 2010-01-07

Basic References [TOP]

BASIC INFORMATION REFERENCES forSFB3/YHR098C for SFB3 1) Bonifacino JS and Glick BS (2004) The mechanisms of vesicle budding and fusion. Cell 116(2):153-66        2) Lee MC and Miller EA (2007) Molecular mechanisms of COPII vesicle formation. Semin Cell Dev Biol 18(4):424-34        3) Hughes H and Stephens DJ (2008) Assembly, organization, and function of the COPII coat. Histochem Cell Biol 129(2):129-51        4) Barlowe C, et al. (1994) COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 77(6):895-907        5) Fath S, et al. (2007) Structure and organization of coat proteins in the COPII cage. Cell 129(7):1325-36          6) Peng R, et al. (2000) Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p family members. J Biol Chem 275(15):11521-8        7) Miller E, et al. (2002) Cargo selection into COPII vesicles is driven by the Sec24p subunit. EMBO J 21(22):6105-13          8) Miller EA, et al. (2003) Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114(4):497-509      9) Rossanese OW, et al. (1999) Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae. J Cell Biol 145(1):69-81        10) Barlowe C, et al. (1993) Purification and characterization of SAR1p, a small GTP-binding protein required for transport vesicle formation from the endoplasmic reticulum. J Biol Chem 268(2):873-9      11) Yoshihisa T, et al. (1993) Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum. Science 259(5100):1466-8      12) Shimoni Y, et al. (2000) Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. J Cell Biol 151(5):973-84        13) Sato K and Nakano A (2005) Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis. Nat Struct Mol Biol 12(2):167-74        14) Supek F, et al. (2002) Sec16p potentiates the action of COPII proteins to bud transport vesicles. J Cell Biol 158(6):1029-38        15) Saito-Nakano Y and Nakano A (2000) Sed4p functions as a positive regulator of Sar1p probably through inhibition of the GTPase activation by Sec23p. Genes Cells 5(12):1039-48        16) Taxis C, et al. (2002) ER-golgi traffic is a prerequisite for efficient ER degradation. Mol Biol Cell 13(6):1806-18        17) Hamasaki M, et al. (2003) The early secretory pathway contributes to autophagy in yeast. Cell Struct Funct 28(1):49-54        18) Fu L and Sztul E (2003) Traffic-independent function of the Sar1p/COPII machinery in proteasomal sorting of the cystic fibrosis transmembrane conductance regulator. J Cell Biol 160(2):157-63        19) Ishihara N, et al. (2001) Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion. Mol Biol Cell 12(11):3690-702        20) Roberg KJ, et al. (1999) LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum. J Cell Biol 145(4):659-72

Mutant Phenotypes [TOP] [NEXT]
Phenotype page for SFB3/YHR098C

Interactions: genetic, physical, and other gene-gene links. [TOP] [NEXT]
Interaction page for SFB3/YHR098C

Homologs [TOP] [NEXT]
Comparison Resources PSI-BLAST Results Ashbya Homologs (AGD) BLASTN vs. fungi BLASTP at NCBI BLASTP vs. fungi Candida Homologs (CGD) Candida Homologs (CandidaDB) Fungal Alignment Fungal Orthogroups Repository Ortholog Search (P-POD) PhylomeDB Synteny Viewer Yeast Gene Order Browser (YGOB) eukarYotic OrtholoGY (YOGY)

Physical Properties and Transcript Information: predicted from sequence [TOP] [NEXT]

Protein Sequence Calculations from Predicted Full length Translation N-term MSQQNIL C-term HQKFVQF Length(aa) 929 MW(Da) 103,949 pI 6.24 Amino Acid Composition (full length) GCG tools: PepPlot, Helical Wheel, PepStruct Transcript Translation Calculations Codon Bias 0.134   Codon Adaptation Index 0.176   Frequency of Optimal Codons 0.489   Hydropathicity of Protein -0.229   Aromaticity Score 0.088

10 20 30 40 50 | | | | | MSQQNILAASVSALSLDESTVHTGGASSKKSRRPHRAYHNFSSGTVPTLG NSPYTTPQLNQQDGFQQPQAFTPKQFGGFNNGSGSVMSTPVMVSQERFGA SEASSPYGQSMLDMTAPQPTSHIVPTQRFEDQAQYLQRSFETCRDSVPPL PTTQFYCVDQGSCDPHLMSLSMYNIPESEHLRAATKLPLGLTIQPFSTLT PNDAEVPTIPLPMDGTPLRCRRCRAYANPKFQFTYDSSVICNICRVKMQV PGEHFAPMGPNGQRSDLNEKSELLHGTVDFLVPSIYNAIQEKELLPLHYV FLIDVSLLANENGSSLAMVEGVRSCIEYISDFQPNCEVAIIVYDNKLRFF NLRPDLDNAQEYIVSELDDVFLPFYNGLFVKPGNSMKIINDTLIKISGYI STDKYSHVPQVCYGSALQAAKLALDTVTGGQGGKIICSLNSLPTIGNGNL SLKRDNAHIAHVKCDNGFYKKLASDFLKSYISLDLYVTNAGFIDMATVGH PVEMTSGILKYYPHFQQETDAFTLVNDMVTNVSNIVGYQALLKVRCSTGL SVEQYYCDSSDNTDHDPIIPVLTRDTTLDVLLKYDSKIKTGTDVHFQTAL LYTDIDGVRKVRSINTSGAVSNNIREIFKFINQNPVMRIMIKDVIKTLGD CDFVKIRRLIDDKMVEILTQYRGLVSSNSSTQLILPDSIKTLPAYMLAFE KSELMKPNAQSTRGNERIYDLLKYDSLNSAQLCYKLYPQIVPFHVLLEET DLTFYDANDKLLQINSSSINNLSVRASHSNFINGGCYLIFQGDTIYLWFN ENTNRMLLQDLLSVDESLPVSQISLFSGTLPETGTSINQKASNVIKNWQQ VVNKSSLPLVLLRPNVDQYYSNVMSQLLCEDKTVNRIESYDNYLVIMHKK IQEKLQKDDFIKVSTAATHENIHQKFVQF*

Protein Structures from PDB: proteins of known structure with sequence similarity to SFB3/YHR098C, based on Smith-Waterman analysis. [TOP] [NEXT]

PDB protein structure(s) homologous to SFB3 Homolog Source (per PDB) Protein Alignment: SFB3 vs. Homolog External Links P-Value %Identical %Similar Alignment 3eg9 ( Chain: B, A) Crystal structure of the mammalian copii-coat protein sec23/24 bound to the transport signal sequence of membrin PDB_Info PDB_Structure Homo sapiens Chain B = 5.5e-57 26 34 View alignment SCOP MMDB CATH Chain A = 9.6e-05 19 29 View alignment 3efo ( Chain: B, A) Crystal structure of the mammalian copii-coat protein sec23/24 bound to the transport signal sequence of syntaxin 5 PDB_Info PDB_Structure Homo sapiens Chain B = 5.5e-57 26 34 View alignment SCOP MMDB CATH Chain A = 0.000110 19 29 View alignment 3eh2 ( Chain: C, B, A) Crystal structure of the human copii-coat protein sec24c PDB_Info PDB_Structure Homo sapiens Chain C = 1.1e-56 27 32 View alignment SCOP MMDB CATH Chain B = 1.1e-56 27 32 View alignment Chain A = 1.1e-56 27 32 View alignment 3eh1 ( Chain: A) Crystal structure of the human copii-coat protein sec24b PDB_Info PDB_Structure Homo sapiens 4.4e-49 26 33 View alignment SCOP MMDB CATH 3egd ( Chain: B, A) Crystal structure of the mammalian copii-coat protein sec23a/24a complexed with the snare protein sec22 and bound to the transport signal sequence of vesicular stomatitis virus glycoprotein PDB_Info PDB_Structure Homo sapiens Chain B = 1.0e-48 24 35 View alignment SCOP MMDB CATH Chain A = 9.6e-05 19 29 View alignment 3egx ( Chain: B, A) Crystal structure of the mammalian copii-coat protein sec23a/24a complexed with the snare protein sec22b and bound to the transport signal sequence of the snare protein bet1 PDB_Info PDB_Structure Homo sapiens Chain B = 1.0e-48 24 35 View alignment SCOP MMDB CATH Chain A = 9.6e-05 19 29 View alignment 2nut ( Chain: B, A) Crystal structure of the human sec23a/24a heterodimer, complexed with the snare protein sec22b PDB_Info PDB_Structure Homo sapiens Chain B = 1.6e-48 24 35 View alignment SCOP MMDB CATH Chain A = 0.000160 19 29 View alignment 2nup ( Chain: B, A) Crystal structure of the human sec23a/24a heterodimer, complexed with the snare protein sec22b PDB_Info PDB_Structure Homo sapiens Chain B = 1.6e-48 24 35 View alignment SCOP MMDB CATH Chain A = 0.000160 19 29 View alignment 1m2v ( Chain: B) Crystal structure of the yeast sec23/24 heterodimer PDB_Info PDB_Structure Saccharomyces cerevisiae 4.8e-46 24 32 View alignment SCOP MMDB CATH 1pcx ( Chain: A) Crystal structure of the copii coat subunit, sec24, complexed with a peptide from the snare protein bet1 PDB_Info PDB_Structure Saccharomyces cerevisiae 9.1e-44 24 32 View alignment SCOP MMDB CATH 1pd0 ( Chain: A) Crystal structure of the copii coat subunit, sec24, complexed with a peptide from the snare protein sed5 (yeast syntaxin-5) PDB_Info PDB_Structure Saccharomyces cerevisiae 9.1e-44 24 32 View alignment SCOP MMDB CATH 1pd1 ( Chain: A) Crystal structure of the copii coat subunit, sec24, complexed with a peptide containing the dxe cargo sorting signal of yeast sys1 protein PDB_Info PDB_Structure Saccharomyces cerevisiae 9.1e-44 24 32 View alignment SCOP MMDB CATH 2np0 ( Chain: A) Crystal structure of the botulinum neurotoxin type b complexed with synaptotagamin-ii ectodomain PDB_Info PDB_Structure Clostridium botulinum | Mus musculus 0.001200 21 31 View alignment SCOP MMDB CATH 1g9a ( Chain: A) Crystal structure of clostridium botulinum neurotoxin b complexed with an inhibitor (experiment 3) PDB_Info PDB_Structure Clostridium botulinum 0.001200 21 31 View alignment SCOP MMDB CATH 1s0e ( Chain: A) Crystal structure of botulinum neurotoxin type b at ph 6.0 PDB_Info PDB_Structure Clostridium botulinum 0.001200 21 31 View alignment SCOP MMDB CATH 1epw ( Chain: A) Crystal structure of clostridium neurotoxin type b PDB_Info PDB_Structure Clostridium botulinum 0.001200 21 31 View alignment SCOP MMDB CATH 1g9d ( Chain: A) Crystal structure of clostridium botulinum neurotoxin b complexed with an inhibitor (experiment 2) PDB_Info PDB_Structure Clostridium botulinum 0.001200 21 31 View alignment SCOP MMDB CATH 1s0b ( Chain: A) Crystal structure of botulinum neurotoxin type b at ph 4.0 PDB_Info PDB_Structure Clostridium botulinum 0.001200 21 31 View alignment SCOP MMDB CATH 1s0d ( Chain: A) Crystal structure of botulinum neurotoxin type b at ph 5.5 PDB_Info PDB_Structure Clostridium botulinum 0.001200 21 31 View alignment SCOP MMDB CATH 1s0g ( Chain: A) Crystal structure of botulinum neurotoxin type b apo form PDB_Info PDB_Structure Clostridium botulinum 0.001200 21 31 View alignment SCOP MMDB CATH 1f31 ( Chain: A) Crystal structure of clostridium botulinum neurotoxin b complexed with a trisaccharide PDB_Info PDB_Structure Clostridium botulinum 0.001200 21 31 View alignment SCOP MMDB CATH 1i1e ( Chain: A) Crystal structure of clostridium botulinum neurotoxin b complexed with doxorubicin PDB_Info PDB_Structure Clostridium botulinum 0.001200 21 31 View alignment SCOP MMDB CATH 1s0c ( Chain: A) Crystal structure of botulinum neurotoxin type b at ph 5.0 PDB_Info PDB_Structure Clostridium botulinum 0.001200 21 31 View alignment SCOP MMDB CATH 1s0f ( Chain: A) Crystal structure of botulinum neurotoxin type b at ph 7.0 PDB_Info PDB_Structure Clostridium botulinum 0.001200 21 31 View alignment SCOP MMDB CATH 1g9c ( Chain: A) Crystal structure of clostridium botulinum neurotoxin b complexed with an inhibitor (experiment 4) PDB_Info PDB_Structure Clostridium botulinum 0.001200 21 31 View alignment SCOP MMDB CATH 1g9b ( Chain: A) Crystal structure of clostridium botulinum neurotoxin b complexed with an inhibitor (experiment 1) PDB_Info PDB_Structure Clostridium botulinum 0.001200 21 31 View alignment SCOP MMDB CATH 1z0h ( Chain: A, B) N-terminal helix reorients in recombinant c-fragment of clostridium botulinum type b PDB_Info PDB_Structure Clostridium botulinum Chain A = 0.001999 23 29 View alignment SCOP MMDB CATH Chain B = 0.001999 23 29 View alignment 2nm1 ( Chain: A) Structure of bont/b in complex with its protein receptor PDB_Info PDB_Structure Clostridium botulinum | Rattus norvegicus 0.003701 22 31 View alignment SCOP MMDB CATH

Genome-wide Expression and Other Large-Scale Analyses [TOP] [NEXT]
Functional Analysis Expression Connection Summary Cell cycle and metabolic oscillation Cell cycle transcript profile Cyclebase Genevestigator GermOnline SPELL Microarray Search YGAC Triples Yeast Microarray Global Viewer YeastFunc	You can also search multiple datasets simultaneously using Expression Connection for expression studies or Function Junction for other large scale analyses.

Locus History (misc. notes) [TOP] [NEXT]

Nomenclature History

Standard Name	Reference
SFB3	Peng R, et al. (2000) Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p family members. J Biol Chem 275(15):11521-8

Alias Name(s)	Reference
LST1	Roberg KJ, et al. (1999) LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum. J Cell Biol 145(4):659-72

Sequence Retrieval [TOP] [NEXT]
Sequence Type	Output Format
Genomic DNA	GCG | FASTA | NoHeader
Genomic DNA with 1 kb up and downstream	GCG | FASTA | NoHeader
DNA coding sequence (without introns, without flanking regions)	GCG | FASTA | NoHeader
Protein Translation of ORF	GCG | FASTA | NoHeader
6-Frame Translation(with Restriction Map)	GCG
Restriction Fragment Sizes	GCG
Sequence Analysis Tools BLASTP BLASTN Design Primers FASTA aa FASTA nt Restriction Fragment Map Restriction Fragment Sizes Six-Frame Translation

Sequence from other databases
Sequence ID	Source
YHR098C	SGD Systematic Sequence
856498	NCBI: Gene ID
NP_011966.1	NCBI: RefSeq protein version ID
NP_011966.1	NCBI: RefSeq protein version ID
6321890	NCBI: NCBI protein GI

Map and Displays [TOP] [NEXT]
Physical, Genetic Maps:	Chromosomal Feature Map	GBrowse	Combined Physical and Genetic Map	Genetic Distance vs. Physical Distance Ratios
Similarity Viewers:	Synteny Viewer	Genomic Stripe View	SAGE Results Map

Localization [TOP] [NEXT]
Localization Resources YeastRC Localization (Seattle) YGAC Triples YeastGFP DB (UCSF) at SGD

Community Annotation [TOP] [NEXT]
Protein Details Topic Research Highlight Reference Contributor Protein Modification Description: Identified as an efficient substrate of Clb2-Cdk1-as1 in a screen of a proteomic GST-fusion library. Modification Type: Phosphorylation Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64          Jeff Ubersax 2004-01-27

Literature Guide: papers categorized by topic. [TOP]
Topics	Reference	Other Genes Addressed
24 curated references; 0 references not yet curated
Protein Sequence Features	Ma L, et al. (2010) Proteins deleterious on overexpression are associated with high intrinsic disorder, specific interaction domains and low abundance. J Proteome Res	|ENA1 |ENA2 |ENA5 |PHM7 |PMA1 |PMA2 |PMC1 |PMR1 |RIM15 |RSN1 |SEC23 |SEC24 |SFB2 |SKN7 |MORE
Function/Process Mutants/Phenotypes	Brown JC and Lindquist S (2009) A heritable switch in carbon source utilization driven by an unusual yeast prion. Genes Dev 23(19):2320-32	|HXT3 |MTH1 |PMA1 |RGT1 |SSA1 |SSA2 |STD1 |SUR4
Reviews	Fonzi WA (2009) The protein secretory pathway of Candida albicans. Mycoses	|BTT1 |EGD1 |EGD2 |GEA1 |GEA2 |GSG1 |NCE101 |NCE102 |SCR1 |SEC14 |SEC3 |SEC4 |SEC61 |SEC65 |MORE
Cellular Location	Narayanaswamy R, et al. (2009) Systematic Definition of Protein Constituents along the Major Polarization Axis Reveals an Adaptive Reuse of the Polarization Machinery in Pheromone-Treated Budding Yeast. J Proteome Res 8(1):6-19	|ABP1 |ABP140 |AIM21 |AIP1 |ARK1 |BCK1 |BEM1 |BEM3 |BNI1 |BOI1 |BSP1 |BUD6 |BZZ1 |CAP1 |MORE
Reviews	Papanikou E and Glick BS (2009) The yeast Golgi apparatus: insights and mysteries. FEBS Lett 583(23):3746-51	|BSC6 |COP1 |GLO3 |GRH1 |MTC1 |MYO2 |NEO1 |PMA1 |RBD2 |RER1 |RET2 |RET3 |SAR1 |SEC13 |MORE
Reviews	Baines AC and Zhang B (2007) Receptor-mediated protein transport in the early secretory pathway. Trends Biochem Sci 32(8):381-8	|EMP24 |EMP46 |EMP47 |ERV14 |ERV25 |ERV29 |ERV41 |ERV46 |SAR1 |SEC13 |SEC23 |SEC24 |SEC31 |SFB2 |MORE
Reviews	Toulmay A and Schneiter R (2007) Lipid-dependent surface transport of the proton pumping ATPase: A model to study plasma membrane biogenesis in yeast. Biochimie 89(2):249-54	|AST1 |AUR1 |BUL1 |BUL2 |PMA1 |RSP5 |SOP4 |SUR4
Fungal Related Genes/Proteins	Esaki M, et al. (2006) The budding yeast Pichia pastoris has a novel Sec23p homolog. FEBS Lett 580(22):5215-21	|SEC23 |SEC24
Fungal Related Genes/Proteins Non-Fungal Related Genes/Proteins	Jiang SY and Ramachandran S (2006) Comparative and evolutionary analysis of genes encoding small GTPases and their activating proteins in eukaryotic genomes. Physiol Genomics 24(3):235-51	|AGE1 |AGE2 |ARF1 |ARF2 |ARF3 |ARL1 |BAG7 |BEM2 |BEM3 |BUB2 |BUD2 |CIN4 |GCS1 |GLO3 |MORE
Protein Processing/Modification/Regulation Regulation of Techniques and Reagents	Dephoure N, et al. (2005) Combining chemical genetics and proteomics to identify protein kinase substrates. Proc Natl Acad Sci U S A 102(50):17940-5	|AME1 |BCP1 |CDC19 |DMA1 |FPK1 |GLC8 |GTS1 |ISR1 |KCC4 |KSP1 |NPL3 |PAH1 |PAM1 |PAN3 |MORE
Function/Process Genetic Interactions Mutants/Phenotypes Strains/Constructs	Karhinen L, et al. (2005) Endoplasmic reticulum exit of a secretory glycoprotein in the absence of sec24p family proteins in yeast. Traffic 6(7):562-74	|HSP150 |SAR1 |SEC13 |SEC16 |SEC23 |SEC24 |SEC31 |SFB2
Protein/Nucleic Acid Structure Reviews	Bickford LC, et al. (2004) A structural view of the COPII vesicle coat. Curr Opin Struct Biol 14(2):147-53	|SAR1 |SEC13 |SEC16 |SEC23 |SEC24 |SEC31 |SFB2
Reviews	Bonifacino JS and Glick BS (2004) The mechanisms of vesicle budding and fusion. Cell 116(2):153-66	|BET1 |EMP24 |EMP46 |EMP47 |ERV25 |ERV41 |GAP1 |SAR1 |SEC12 |SEC13 |SEC16 |SEC17 |SEC18 |SEC23 |MORE
Genetic Interactions Mutants/Phenotypes Strains/Constructs	Cohen M, et al. (2003) Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23. Nat Cell Biol 5(7):661-7	|BRE5 |SEC23 |UBP3
Alias Function/Process Genetic Interactions Mutants/Phenotypes Protein Sequence Features Protein-protein Interactions Strains/Constructs	Miller EA, et al. (2003) Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114(4):497-509	|BET1 |BOS1 |EMP24 |EMP47 |ERP1 |ERP2 |GAP1 |PRM8 |SEC13 |SEC22 |SEC23 |SEC24 |SEC31 |SED5 |MORE
Protein Processing/Modification/Regulation Regulation of	Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64	|ACE2 |ACF4 |ACM1 |ADY3 |ALY2 |ARG1 |ASE1 |ASH1 |ATG20 |AXL2 |BBP1 |BCK2 |BEM1 |BEM3 |MORE
Cellular Location Function/Process Fungal Related Genes/Proteins	Lee MC, et al. (2002) Ceramide biosynthesis is required for the formation of the oligomeric H+-ATPase Pma1p in the yeast endoplasmic reticulum. J Biol Chem 277(25):22395-401	|PMA1 |SEC24
Cellular Location Function/Process Protein-protein Interactions	Miller E, et al. (2002) Cargo selection into COPII vesicles is driven by the Sec24p subunit. EMBO J 21(22):6105-13	|BET1 |BOS1 |SAR1 |SEC22 |SEC24
Non-Fungal Related Genes/Proteins	Belles-Boix E, et al. (2000) CEF, a sec24 homologue of Arabidopsis thaliana, enhances the survival of yeast under oxidative stress conditions. J Exp Bot 51(351):1761-2	|SEC24
Strains/Constructs	De Antoni A and Gallwitz D (2000) A novel multi-purpose cassette for repeated integrative epitope tagging of genes in Saccharomyces cerevisiae. Gene 246(1-2):179-85	|SEC23 |SEC24 |SFB2
Cellular Location Function/Process Fungal Related Genes/Proteins Genetic Interactions Mutants/Phenotypes Protein Processing/Modification/Regulation Protein-protein Interactions	Peng R, et al. (2000) Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p family members. J Biol Chem 275(15):11521-8	|GAS1 |SAR1 |SEC13 |SEC23 |SEC24 |SEC31 |SED5 |SFB2
Function/Process Mutants/Phenotypes Protein-protein Interactions Strains/Constructs	Shimoni Y, et al. (2000) Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. J Cell Biol 151(5):973-84	|PMA1 |SEC23 |SEC24
Function/Process Mutants/Phenotypes Non-Fungal Related Genes/Proteins Strains/Constructs	Pagano A, et al. (1999) Sec24 proteins and sorting at the endoplasmic reticulum. J Biol Chem 274(12):7833-40	|SEC23 |SEC24 |SFB2
Cellular Location Function/Process Fungal Related Genes/Proteins Genetic Interactions Mutants/Phenotypes Protein Sequence Features Regulatory Role Strains/Constructs	Roberg KJ, et al. (1999) LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum. J Cell Biol 145(4):659-72	|PMA1 |SEC23 |SEC24 |YHR035W

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