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Protein

Coatomer subunit beta'

Gene

SEC27

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.1 Publication

GO - Molecular functioni

  1. structural molecule activity Source: InterPro
  2. ubiquitin binding Source: SGD

GO - Biological processi

  1. ER to Golgi vesicle-mediated transport Source: SGD
  2. intracellular protein transport Source: InterPro
  3. late endosome to vacuole transport via multivesicular body sorting pathway Source: SGD
  4. retrograde vesicle-mediated transport, Golgi to ER Source: SGD
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-30632-MONOMER.
ReactomeiREACT_314440. COPI Mediated Transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Coatomer subunit beta'
Alternative name(s):
Beta'-coat protein
Short name:
Beta'-COP
Gene namesi
Name:SEC27
Ordered Locus Names:YGL137W
ORF Names:G2827
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGL137w.
SGDiS000003105. SEC27.

Subcellular locationi

Cytoplasm By similarity. Golgi apparatus membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmic vesicleCOPI-coated vesicle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Note: The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it.By similarity

GO - Cellular componenti

  1. COPI vesicle coat Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 889889Coatomer subunit beta'PRO_0000050918Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei326 – 3261Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP41811.
PaxDbiP41811.
PeptideAtlasiP41811.

Expressioni

Gene expression databases

GenevestigatoriP41811.

Interactioni

Subunit structurei

Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Interacts with the ESCRT-0 subunit VPS27.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
COP1P5362217EBI-4898,EBI-4860
RET3P536003EBI-4898,EBI-4905
SEC28P405094EBI-4898,EBI-4884

Protein-protein interaction databases

BioGridi33115. 249 interactions.
DIPiDIP-6468N.
IntActiP41811. 71 interactions.
MINTiMINT-428887.
STRINGi4932.YGL137W.

Structurei

Secondary structure

1
889
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127Combined sources
Beta strandi16 – 216Combined sources
Beta strandi23 – 3210Combined sources
Beta strandi35 – 417Combined sources
Turni42 – 454Combined sources
Beta strandi46 – 527Combined sources
Beta strandi58 – 647Combined sources
Helixi65 – 673Combined sources
Beta strandi69 – 746Combined sources
Beta strandi77 – 837Combined sources
Turni84 – 863Combined sources
Beta strandi89 – 946Combined sources
Beta strandi100 – 1056Combined sources
Beta strandi107 – 11610Combined sources
Beta strandi121 – 1255Combined sources
Turni126 – 1305Combined sources
Beta strandi132 – 1365Combined sources
Beta strandi143 – 1486Combined sources
Beta strandi155 – 1606Combined sources
Beta strandi163 – 1697Combined sources
Beta strandi176 – 1805Combined sources
Beta strandi189 – 1924Combined sources
Beta strandi200 – 2045Combined sources
Beta strandi208 – 2147Combined sources
Turni215 – 2173Combined sources
Beta strandi220 – 2256Combined sources
Beta strandi231 – 2366Combined sources
Beta strandi238 – 24710Combined sources
Beta strandi252 – 2565Combined sources
Turni257 – 2593Combined sources
Beta strandi262 – 2665Combined sources
Beta strandi269 – 27810Combined sources
Helixi283 – 2853Combined sources
Beta strandi287 – 2915Combined sources
Beta strandi294 – 2996Combined sources
Beta strandi313 – 3186Combined sources
Beta strandi321 – 3233Combined sources
Beta strandi327 – 3326Combined sources
Beta strandi341 – 3433Combined sources
Beta strandi350 – 3545Combined sources
Beta strandi360 – 3645Combined sources
Beta strandi368 – 3758Combined sources
Beta strandi378 – 3836Combined sources
Turni384 – 3863Combined sources
Beta strandi389 – 3946Combined sources
Beta strandi396 – 4005Combined sources
Beta strandi404 – 4107Combined sources
Beta strandi416 – 4205Combined sources
Beta strandi423 – 4275Combined sources
Beta strandi438 – 4403Combined sources
Beta strandi442 – 4487Combined sources
Beta strandi453 – 4564Combined sources
Turni458 – 4603Combined sources
Beta strandi463 – 4675Combined sources
Beta strandi471 – 4766Combined sources
Beta strandi480 – 4878Combined sources
Turni490 – 4934Combined sources
Beta strandi496 – 5027Combined sources
Helixi504 – 5129Combined sources
Beta strandi518 – 5203Combined sources
Helixi523 – 5253Combined sources
Beta strandi526 – 5327Combined sources
Beta strandi537 – 5426Combined sources
Beta strandi545 – 5495Combined sources
Beta strandi554 – 5585Combined sources
Beta strandi563 – 5686Combined sources
Beta strandi573 – 5797Combined sources
Turni580 – 5834Combined sources
Beta strandi584 – 5896Combined sources
Beta strandi594 – 5985Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YNNX-ray1.78A1-304[»]
2YNOX-ray1.80A/B1-304[»]
2YNPX-ray2.96A1-604[»]
4J73X-ray1.44A1-301[»]
4J77X-ray1.76A/B1-301[»]
4J78X-ray1.48A1-301[»]
4J79X-ray1.56A1-300[»]
4J81X-ray1.74A/B1-301[»]
4J82X-ray1.46A/B1-301[»]
4J84X-ray1.47A/B1-301[»]
4J86X-ray1.48A/B1-301[»]
ProteinModelPortaliP41811.
SMRiP41811. Positions 1-812.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati11 – 4131WD 1Add
BLAST
Repeati53 – 8331WD 2Add
BLAST
Repeati95 – 12531WD 3Add
BLAST
Repeati138 – 16932WD 4Add
BLAST
Repeati182 – 21433WD 5Add
BLAST
Repeati226 – 25631WD 6Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat COPB2 family.Curated
Contains 6 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00780000122009.
HOGENOMiHOG000163444.
KOiK17302.
OMAiIAHNPNG.
OrthoDBiEOG7TN016.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR006692. Coatomer_WD-assoc_reg.
IPR016453. COPB2.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF04053. Coatomer_WDAD. 1 hit.
PF00400. WD40. 4 hits.
[Graphical view]
PIRSFiPIRSF005567. Coatomer_beta'_subunit. 1 hit.
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 4 hits.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41811-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLDIKKTFS NRSDRVKGID FHPTEPWVLT TLYSGRVELW NYETQVEVRS
60 70 80 90 100
IQVTETPVRA GKFIARKNWI IVGSDDFRIR VFNYNTGEKV VDFEAHPDYI
110 120 130 140 150
RSIAVHPTKP YVLSGSDDLT VKLWNWENNW ALEQTFEGHE HFVMCVAFNP
160 170 180 190 200
KDPSTFASGC LDRTVKVWSL GQSTPNFTLT TGQERGVNYV DYYPLPDKPY
210 220 230 240 250
MITASDDLTI KIWDYQTKSC VATLEGHMSN VSFAVFHPTL PIIISGSEDG
260 270 280 290 300
TLKIWNSSTY KVEKTLNVGL ERSWCIATHP TGRKNYIASG FDNGFTVLSL
310 320 330 340 350
GNDEPTLSLD PVGKLVWSGG KNAAASDIFT AVIRGNEEVE QDEPLSLQTK
360 370 380 390 400
ELGSVDVFPQ SLAHSPNGRF VTVVGDGEYV IYTALAWRNK AFGKCQDFVW
410 420 430 440 450
GPDSNSYALI DETGQIKYYK NFKEVTSWSV PMHSAIDRLF SGALLGVKSD
460 470 480 490 500
GFVYFFDWDN GTLVRRIDVN AKDVIWSDNG ELVMIVNTNS NGDEASGYTL
510 520 530 540 550
LFNKDAYLEA ANNGNIDDSE GVDEAFDVLY ELSESITSGK WVGDVFIFTT
560 570 580 590 600
ATNRLNYFVG GKTYNLAHYT KEMYLLGYLA RDNKVYLADR EVHVYGYEIS
610 620 630 640 650
LEVLEFQTLT LRGEIEEAIE NVLPNVEGKD SLTKIARFLE GQEYYEEALN
660 670 680 690 700
ISPDQDQKFE LALKVGQLTL ARDLLTDESA EMKWRALGDA SLQRFNFKLA
710 720 730 740 750
VEAFTNAHDL ESLFLLHSSF NNKEGLVTLA KDAERAGKFN LAFNAYWIAG
760 770 780 790 800
DIQGAKDLLI KSQRFSEAAF LGSTYGLGDD AVNDIVTKWK ENLILNGKNT
810 820 830 840 850
VSERVCGAEG LPGSSSSGDA QPLIDLDSTP APEQADENKE AEVEDSEFKE
860 870 880
SNSEAVEAEK KEEEAPQQQQ SEQQPEQGEA VPEPVEEES
Length:889
Mass (Da):99,445
Last modified:November 1, 1995 - v1
Checksum:i6A5E50BBEB02CB58
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11237 Genomic DNA. Translation: AAA61711.1.
X92670 Genomic DNA. Translation: CAA63359.1.
Z72659 Genomic DNA. Translation: CAA96848.1.
BK006941 Genomic DNA. Translation: DAA07973.1.
PIRiB55123.
RefSeqiNP_011378.1. NM_001181002.1.

Genome annotation databases

EnsemblFungiiYGL137W; YGL137W; YGL137W.
GeneIDi852740.
KEGGisce:YGL137W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11237 Genomic DNA. Translation: AAA61711.1.
X92670 Genomic DNA. Translation: CAA63359.1.
Z72659 Genomic DNA. Translation: CAA96848.1.
BK006941 Genomic DNA. Translation: DAA07973.1.
PIRiB55123.
RefSeqiNP_011378.1. NM_001181002.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YNNX-ray1.78A1-304[»]
2YNOX-ray1.80A/B1-304[»]
2YNPX-ray2.96A1-604[»]
4J73X-ray1.44A1-301[»]
4J77X-ray1.76A/B1-301[»]
4J78X-ray1.48A1-301[»]
4J79X-ray1.56A1-300[»]
4J81X-ray1.74A/B1-301[»]
4J82X-ray1.46A/B1-301[»]
4J84X-ray1.47A/B1-301[»]
4J86X-ray1.48A/B1-301[»]
ProteinModelPortaliP41811.
SMRiP41811. Positions 1-812.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33115. 249 interactions.
DIPiDIP-6468N.
IntActiP41811. 71 interactions.
MINTiMINT-428887.
STRINGi4932.YGL137W.

Proteomic databases

MaxQBiP41811.
PaxDbiP41811.
PeptideAtlasiP41811.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL137W; YGL137W; YGL137W.
GeneIDi852740.
KEGGisce:YGL137W.

Organism-specific databases

CYGDiYGL137w.
SGDiS000003105. SEC27.

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00780000122009.
HOGENOMiHOG000163444.
KOiK17302.
OMAiIAHNPNG.
OrthoDBiEOG7TN016.

Enzyme and pathway databases

BioCyciYEAST:G3O-30632-MONOMER.
ReactomeiREACT_314440. COPI Mediated Transport.

Miscellaneous databases

NextBioi972153.
PROiP41811.

Gene expression databases

GenevestigatoriP41811.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR006692. Coatomer_WD-assoc_reg.
IPR016453. COPB2.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF04053. Coatomer_WDAD. 1 hit.
PF00400. WD40. 4 hits.
[Graphical view]
PIRSFiPIRSF005567. Coatomer_beta'_subunit. 1 hit.
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 4 hits.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast beta- and beta'-coat proteins (COP). Two coatomer subunits essential for endoplasmic reticulum-to-Golgi protein traffic."
    Duden R., Hosobuchi M., Hamamoto S., Winey M., Byers B., Schekman R.
    J. Biol. Chem. 269:24486-24495(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11.
    Strain: RSY255.
  2. "Sequence analysis of a 14.6 kb DNA fragment of Saccharomyces cerevisiae chromosome VII reveals SEC27, SSM1b, a putative S-adenosylmethionine-dependent enzyme and six new open reading frames."
    Escribano V., Eraso P., Portillo F., Mazon M.J.
    Yeast 12:887-892(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Yeast coatomer contains a subunit homologous to mammalian beta'-COP."
    Harter C., Draken E., Lottspeich F., Wieland F.T.
    FEBS Lett. 332:71-73(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-27.
    Strain: ATCC 208279 / BJ926.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Involvement of specific COPI subunits in protein sorting from the late endosome to the vacuole in yeast."
    Gabriely G., Kama R., Gerst J.E.
    Mol. Cell. Biol. 27:526-540(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPS27.
  9. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCOPB2_YEAST
AccessioniPrimary (citable) accession number: P41811
Secondary accession number(s): D6VU12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 1, 2015
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 129000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.