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P32769

- HBS1_YEAST

UniProt

P32769 - HBS1_YEAST

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Protein

Elongation factor 1 alpha-like protein

Gene

HBS1

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

Functioni

Involved in protein translation. Together with DOM34, may function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi174 – 1818GTPBy similarity
Nucleotide bindingi251 – 2555GTPBy similarity
Nucleotide bindingi313 – 3164GTPBy similarity

GO - Molecular functioni

  1. GTPase activity Source: SGD
  2. GTP binding Source: UniProtKB-KW
  3. translation elongation factor activity Source: UniProtKB-KW

GO - Biological processi

  1. GTP catabolic process Source: GOC
  2. nonfunctional rRNA decay Source: SGD
  3. nuclear-transcribed mRNA catabolic process, no-go decay Source: SGD
  4. positive regulation of translation Source: SGD
  5. ribosome disassembly Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis, Translation regulation

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32047-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 1 alpha-like protein
Gene namesi
Name:HBS1
Ordered Locus Names:YKR084C
ORF Names:YKR404
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

CYGDiYKR084c.
SGDiS000001792. HBS1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi176 – 1761V → G: Loss of function. 1 Publication
Mutagenesisi255 – 2551H → E: Loss of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 611611Elongation factor 1 alpha-like proteinPRO_0000091490Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei124 – 1241Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32769.
PaxDbiP32769.
PeptideAtlasiP32769.

Expressioni

Gene expression databases

GenevestigatoriP32769.

Interactioni

Subunit structurei

Interacts with DOM34.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DOM34P333093EBI-8194,EBI-6012

Protein-protein interaction databases

BioGridi34215. 35 interactions.
DIPiDIP-762N.
IntActiP32769. 1 interaction.
MINTiMINT-4493888.
STRINGi4932.YKR084C.

Structurei

Secondary structure

1
611
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi157 – 1637
Beta strandi167 – 1748
Helixi176 – 1783
Helixi180 – 19011
Helixi196 – 2027
Helixi219 – 2224
Beta strandi237 – 2415
Beta strandi246 – 2505
Helixi256 – 2583
Helixi259 – 2668
Beta strandi270 – 2778
Helixi291 – 30212
Beta strandi308 – 3136
Helixi315 – 3184
Helixi322 – 33918
Helixi343 – 3453
Beta strandi346 – 3505
Beta strandi353 – 3553
Beta strandi359 – 3624
Helixi366 – 3716
Helixi377 – 39216
Beta strandi397 – 3993
Beta strandi402 – 4098
Beta strandi419 – 43012
Beta strandi435 – 4395
Turni440 – 4423
Beta strandi443 – 45210
Turni453 – 4553
Beta strandi464 – 4663
Beta strandi473 – 4808
Helixi483 – 4853
Beta strandi491 – 4933
Beta strandi504 – 5129
Beta strandi524 – 5296
Beta strandi532 – 54716
Beta strandi564 – 5718
Turni583 – 5853
Turni587 – 5904
Beta strandi591 – 5966
Beta strandi599 – 60911

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IZQelectron microscopy-11-611[»]
3P26X-ray2.50A/B135-611[»]
3P27X-ray2.95A/B135-611[»]
ProteinModelPortaliP32769.
SMRiP32769. Positions 20-86, 161-611.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini165 – 390226tr-type GPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni174 – 1818G1PROSITE-ProRule annotation
Regioni230 – 2345G2PROSITE-ProRule annotation
Regioni251 – 2544G3PROSITE-ProRule annotation
Regioni313 – 3164G4PROSITE-ProRule annotation
Regioni352 – 3543G5PROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5256.
GeneTreeiENSGT00600000085333.
HOGENOMiHOG000229291.
InParanoidiP32769.
KOiK14416.
OMAiICATDFE.
OrthoDBiEOG715QCW.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR000795. EF_GTP-bd_dom.
IPR015033. HBS1-like_N.
IPR027417. P-loop_NTPase.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamiPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF08938. HBS1_N. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32769-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAYSDYSDGA DDMPDFHDEG EFDDYLNDDE YDLMNEVFPT LKAQLQDYQG
60 70 80 90 100
WDNLSLKLAL FDNNFDLEST LAELKKTLKK KKTPKKPIAA ANGSANVTQK
110 120 130 140 150
LANISISQQR PNDRLPDWLD EEESEGERNG EEANDEKTVQ RYYKTTVPTK
160 170 180 190 200
PKKPHDISAF VKSALPHLSF VVLGHVDAGK STLMGRLLYD LNIVNQSQLR
210 220 230 240 250
KLQRESETMG KSSFKFAWIM DQTNEERERG VTVSICTSHF STHRANFTIV
260 270 280 290 300
DAPGHRDFVP NAIMGISQAD MAILCVDCST NAFESGFDLD GQTKEHMLLA
310 320 330 340 350
SSLGIHNLII AMNKMDNVDW SQQRFEEIKS KLLPYLVDIG FFEDNINWVP
360 370 380 390 400
ISGFSGEGVY KIEYTDEVRQ WYNGPNLMST LENAAFKISK ENEGINKDDP
410 420 430 440 450
FLFSVLEIIP SKKTSNDLAL VSGKLESGSI QPGESLTIYP SEQSCIVDKI
460 470 480 490 500
QVGSQQGQST NHEETDVAIK GDFVTLKLRK AYPEDIQNGD LAASVDYSSI
510 520 530 540 550
HSAQCFVLEL TTFDMNRPLL PGTPFILFIG VKEQPARIKR LISFIDKGNT
560 570 580 590 600
ASKKKIRHLG SKQRAFVEIE LIEVKRWIPL LTAHENDRLG RVVLRKDGRT
610
IAAGKISEIT Q
Length:611
Mass (Da):68,730
Last modified:June 1, 1994 - v2
Checksum:i11EC2CB6936396EE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 943NGS → MGV in M98437. (PubMed:1394434)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M98437 Genomic DNA. No translation available.
Z27116 Genomic DNA. Translation: CAA81635.1.
Z28309 Genomic DNA. Translation: CAA82163.1.
BK006944 Genomic DNA. Translation: DAA09234.1.
PIRiS38162.
RefSeqiNP_013010.3. NM_001179874.3.

Genome annotation databases

EnsemblFungiiYKR084C; YKR084C; YKR084C.
GeneIDi853959.
KEGGisce:YKR084C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M98437 Genomic DNA. No translation available.
Z27116 Genomic DNA. Translation: CAA81635.1 .
Z28309 Genomic DNA. Translation: CAA82163.1 .
BK006944 Genomic DNA. Translation: DAA09234.1 .
PIRi S38162.
RefSeqi NP_013010.3. NM_001179874.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3IZQ electron microscopy - 1 1-611 [» ]
3P26 X-ray 2.50 A/B 135-611 [» ]
3P27 X-ray 2.95 A/B 135-611 [» ]
ProteinModelPortali P32769.
SMRi P32769. Positions 20-86, 161-611.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34215. 35 interactions.
DIPi DIP-762N.
IntActi P32769. 1 interaction.
MINTi MINT-4493888.
STRINGi 4932.YKR084C.

Proteomic databases

MaxQBi P32769.
PaxDbi P32769.
PeptideAtlasi P32769.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YKR084C ; YKR084C ; YKR084C .
GeneIDi 853959.
KEGGi sce:YKR084C.

Organism-specific databases

CYGDi YKR084c.
SGDi S000001792. HBS1.

Phylogenomic databases

eggNOGi COG5256.
GeneTreei ENSGT00600000085333.
HOGENOMi HOG000229291.
InParanoidi P32769.
KOi K14416.
OMAi ICATDFE.
OrthoDBi EOG715QCW.

Enzyme and pathway databases

BioCyci YEAST:G3O-32047-MONOMER.

Miscellaneous databases

NextBioi 975380.

Gene expression databases

Genevestigatori P32769.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR000795. EF_GTP-bd_dom.
IPR015033. HBS1-like_N.
IPR027417. P-loop_NTPase.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view ]
Pfami PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF08938. HBS1_N. 1 hit.
[Graphical view ]
PRINTSi PR00315. ELONGATNFCT.
SUPFAMi SSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The complete sequence of an 18,002 bp segment of Saccharomyces cerevisiae chromosome XI contains the HBS1, MRP-L20 and PRP16 genes, and six new open reading frames."
    Garcia-Cantalejo J.M., Baladron V., Esteban P.F., Santos M.A., Bou G., Remacha M.A., Revuelta J.L., Ballesta J.P.G., Jimenez A., del Rey F.
    Yeast 10:231-245(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "The translation machinery and 70 kd heat shock protein cooperate in protein synthesis."
    Nelson R.J., Ziegelhoffer T., Nicolet C., Werner-Washburne M., Craig E.A.
    Cell 71:97-105(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 92-611.
  5. "Novel G-protein complex whose requirement is linked to the translational status of the cell."
    Carr-Schmid A., Pfund C., Craig E.A., Kinzy T.G.
    Mol. Cell. Biol. 22:2564-2574(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DOM34, MUTAGENESIS OF VAL-176 AND HIS-255.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation."
    Doma M.K., Parker R.
    Nature 440:561-564(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "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-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "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-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHBS1_YEAST
AccessioniPrimary (citable) accession number: P32769
Secondary accession number(s): D6VXE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: June 1, 1994
Last modified: October 29, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2750 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

External Data

Dasty 3