P32769 (HBS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongation factor 1 alpha-like protein

Gene names

Name:	HBS1
Ordered Locus Names:	YKR084C
ORF Names:	YKR404

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	611 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8
Subunit structure	Interacts with DOM34. Ref.5
Subcellular location	Cytoplasm Ref.6.
Miscellaneous	Present with 2750 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the GTP-binding elongation factor family.

Ontologies

Keywords
Biological process	Protein biosynthesis Translation regulation
Cellular component	Cytoplasm
Ligand	GTP-binding Nucleotide-binding
Molecular function	Elongation factor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nonfunctional rRNA decay Inferred from mutant phenotype PubMed 19481524. Source: SGD nuclear-transcribed mRNA catabolic process, no-go decay Inferred from genetic interaction Ref.8. Source: SGD regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW ribosome disassembly Inferred from direct assay PubMed 20947765. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay Ref.6. Source: SGD
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from direct assay PubMed 20947765. Source: SGD translation elongation factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DOM34	P33309	3	EBI-8194,EBI-6012

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 611

611

Elongation factor 1 alpha-like protein

PRO_0000091490

Regions

Nucleotide binding

174 – 181

8

GTP By similarity

Nucleotide binding

251 – 255

5

GTP By similarity

Nucleotide binding

313 – 316

4

GTP By similarity

Amino acid modifications

Modified residue

124

1

Phosphoserine Ref.9 Ref.10

Experimental info

Mutagenesis

176

1

V → G: Loss of function. Ref.5

Mutagenesis

255

1

H → E: Loss of function. Ref.5

Sequence conflict

92 – 94

3

NGS → MGV in M98437. Ref.4

Secondary structure

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611

Helix Strand Turn

Details...

Helix

157 – 163

7

Beta strand

167 – 174

8

Helix

176 – 178

3

Helix

180 – 190

11

Helix

196 – 202

7

Helix

219 – 222

4

Beta strand

237 – 241

5

Beta strand

246 – 250

5

Helix

256 – 258

3

Helix

259 – 266

8

Beta strand

270 – 277

8

Helix

291 – 302

12

Beta strand

308 – 313

6

Helix

315 – 318

4

Helix

322 – 339

18

Helix

343 – 345

3

Beta strand

346 – 350

5

Beta strand

353 – 355

3

Beta strand

359 – 362

4

Helix

366 – 371

6

Helix

377 – 392

16

Beta strand

397 – 399

3

Beta strand

402 – 409

8

Beta strand

419 – 430

12

Beta strand

435 – 439

5

Turn

440 – 442

3

Beta strand

443 – 452

10

Turn

453 – 455

3

Beta strand

464 – 466

3

Beta strand

473 – 480

8

Helix

483 – 485

3

Beta strand

491 – 493

3

Beta strand

504 – 512

9

Beta strand

524 – 529

6

Beta strand

532 – 547

16

Beta strand

564 – 571

8

Turn

583 – 585

3

Turn

587 – 590

4

Beta strand

591 – 596

6

Beta strand

599 – 609

11

Sequences

	Sequence		Length	Mass (Da)
	P32769 [UniParc]. Last modified June 1, 1994. Version 2. Checksum: 11EC2CB6936396EE	FASTA	611	68,730
	10 20 30 40 50 60 MAYSDYSDGA DDMPDFHDEG EFDDYLNDDE YDLMNEVFPT LKAQLQDYQG WDNLSLKLAL 70 80 90 100 110 120 FDNNFDLEST LAELKKTLKK KKTPKKPIAA ANGSANVTQK LANISISQQR PNDRLPDWLD 130 140 150 160 170 180 EEESEGERNG EEANDEKTVQ RYYKTTVPTK PKKPHDISAF VKSALPHLSF VVLGHVDAGK 190 200 210 220 230 240 STLMGRLLYD LNIVNQSQLR KLQRESETMG KSSFKFAWIM DQTNEERERG VTVSICTSHF 250 260 270 280 290 300 STHRANFTIV DAPGHRDFVP NAIMGISQAD MAILCVDCST NAFESGFDLD GQTKEHMLLA 310 320 330 340 350 360 SSLGIHNLII AMNKMDNVDW SQQRFEEIKS KLLPYLVDIG FFEDNINWVP ISGFSGEGVY 370 380 390 400 410 420 KIEYTDEVRQ WYNGPNLMST LENAAFKISK ENEGINKDDP FLFSVLEIIP SKKTSNDLAL 430 440 450 460 470 480 VSGKLESGSI QPGESLTIYP SEQSCIVDKI QVGSQQGQST NHEETDVAIK GDFVTLKLRK 490 500 510 520 530 540 AYPEDIQNGD LAASVDYSSI HSAQCFVLEL TTFDMNRPLL PGTPFILFIG VKEQPARIKR 550 560 570 580 590 600 LISFIDKGNT ASKKKIRHLG SKQRAFVEIE LIEVKRWIPL LTAHENDRLG RVVLRKDGRT 610 IAAGKISEIT Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"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].
[7]	"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].
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M98437 Genomic DNA. No translation available.
Z27116 Genomic DNA. Translation: CAA81635.1.
Z28309 Genomic DNA. Translation: CAA82163.1.
BK006944 Genomic DNA. Translation: DAA09234.1.

PIR

S38162.

RefSeq

NP_013010.3. NM_001179874.3.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P32769.

SMR

P32769. Positions 20-86, 161-611.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-762N.

IntAct

P32769. 1 interaction.

MINT

MINT-4493888.

STRING

4932.YKR084C.

Proteomic databases

PaxDb

P32769.

PeptideAtlas

P32769.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YKR084C; YKR084C; YKR084C.

GeneID

853959.

KEGG

sce:YKR084C.

Organism-specific databases

CYGD

YKR084c.

SGD

S000001792. HBS1.

Phylogenomic databases

eggNOG

COG5256.

GeneTree

ENSGT00600000085333.

HOGENOM

HOG000229291.

KO

K14416.

OMA

EYDLMNE.

OrthoDB

EOG470XS1.

Enzyme and pathway databases

BioCyc

YEAST:G3O-32047-MONOMER.

Gene expression databases

Genevestigator

P32769.

GermOnline

YKR084C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]

Pfam

PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]

PRINTS

PR00315. ELONGATNFCT.

SUPFAM

SSF50465. Elong_init_C. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF50447. Translat_factor. 1 hit.

PROSITE

PS00301. EFACTOR_GTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

975380.

Entry information

Entry name

HBS1_YEAST

Accession

Primary (citable) accession number: P32769
Secondary accession number(s): D6VXE4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	June 1, 1994
Last modified:	May 29, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program