P62495 (ERF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Eukaryotic peptide chain release factor subunit 1
Short name=Eukaryotic release factor 1
Short name=eRF1

Alternative name(s):
Protein Cl1
TB3-1

Gene names

Name:	ETF1
Synonyms:	ERF1, RF1, SUP45L1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Ref.2
Subunit structure	Heterodimer of two subunits, one of which binds GTP. Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the eukaryotic release factor 1 family.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay Protein biosynthesis
Cellular component	Cytoplasm
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from electronic annotation. Source: UniProtKB-KW protein methylation Inferred from direct assay. Source: MGI regulation of translational termination Traceable author statement. Source: ProtInc
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	protein binding Inferred from physical interaction. Source: UniProtKB ribosome binding Traceable author statement. Source: UniProtKB translation release factor activity, codon specific Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 437

436

Eukaryotic peptide chain release factor subunit 1

PRO_0000143138

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.8 Ref.9

Secondary structure

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437

Helix Strand Turn

Details...

Turn

7 – 9

3

Helix

10 – 25

16

Beta strand

30 – 32

3

Beta strand

34 – 39

6

Beta strand

41 – 43

3

Helix

45 – 59

15

Helix

66 – 82

17

Beta strand

93 – 101

9

Helix

103 – 105

3

Beta strand

107 – 114

8

Beta strand

124 – 130

7

Helix

134 – 139

6

Beta strand

145 – 150

6

Beta strand

158 – 162

5

Beta strand

165 – 170

6

Helix

188 – 197

10

Turn

198 – 203

6

Helix

204 – 208

5

Turn

209 – 212

4

Beta strand

216 – 218

3

Beta strand

220 – 222

3

Beta strand

225 – 229

5

Turn

230 – 233

4

Helix

234 – 237

4

Beta strand

240 – 242

3

Turn

244 – 249

6

Beta strand

253 – 255

3

Helix

262 – 271

10

Turn

274 – 276

3

Helix

278 – 295

18

Beta strand

296 – 298

3

Beta strand

301 – 304

4

Helix

305 – 313

9

Beta strand

318 – 324

7

Helix

374 – 380

7

Turn

383 – 386

4

Beta strand

389 – 392

4

Beta strand

394 – 396

3

Helix

397 – 404

8

Turn

405 – 408

4

Beta strand

409 – 412

4

Sequences

	Sequence		Length	Mass (Da)
	P62495 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: CECC50D100E59D19	FASTA	437	49,031
	10 20 30 40 50 60 MADDPSAADR NVEIWKIKKL IKSLEAARGN GTSMISLIIP PKDQISRVAK MLADEFGTAS 70 80 90 100 110 120 NIKSRVNRLS VLGAITSVQQ RLKLYNKVPP NGLVVYCGTI VTEEGKEKKV NIDFEPFKPI 130 140 150 160 170 180 NTSLYLCDNK FHTEALTALL SDDSKFGFIV IDGSGALFGT LQGNTREVLH KFTVDLPKKH 190 200 210 220 230 240 GRGGQSALRF ARLRMEKRHN YVRKVAETAV QLFISGDKVN VAGLVLAGSA DFKTELSQSD 250 260 270 280 290 300 MFDQRLQSKV LKLVDISYGG ENGFNQAIEL STEVLSNVKF IQEKKLIGRY FDEISQDTGK 310 320 330 340 350 360 YCFGVEDTLK ALEMGAVEIL IVYENLDIMR YVLHCQGTEE EKILYLTPEQ EKDKSHFTDK 370 380 390 400 410 420 ETGQEHELIE SMPLLEWFAN NYKKFGATLE IVTDKSQEGS QFVKGFGGIG GILRYRVDFQ 430 GMEYQGGDDE FFDLDDY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a human cDNA with high homology to yeast omnipotent suppressor 45." Grenett H.E., Fuller G.M., Bounelis P. Gene 110:239-243(1992) [PubMed: 1537561] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor." Frolova L., Le Goff X., Rasmussen H.H., Cheprergin S., Drugeon G., Haenni A.-L., Celis J.E., Philippe M., Justesen J., Kisselev L. Nature 372:701-703(1994) [PubMed: 7990965] [Abstract] Cited for: SEQUENCE REVISION, FUNCTION.
[3]	"The catalytic subunit of protein phosphatase 2A associates with the translation termination factor eRF1." Andjelkovic N., Zolnierowicz S., van Hoof C., Goris J., Hemmings B.A. EMBO J. 15:7156-7167(1996) [PubMed: 9003791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[4]	"Human release factor eRF1: structural organisation of the unique functional gene on chromosome 5 and of the three processed pseudogenes." Guenet L., Toutain B., Guilleret I., Chauvel B., Deaven L.L., Longmire J.L., Le Gall L.Y., David V., Le Treut A. FEBS Lett. 454:131-136(1999) [PubMed: 10413110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thalamus.
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[8]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-10, ACETYLATION AT ALA-2. Tissue: Platelet.
[9]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate remodeling of the mRNA surveillance complex during nonsense-mediated mRNA decay." Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B., Katsuhata Y., Muramatsu R., Morita T., Iwamatsu A., Hachiya T., Kurata R., Hirano H., Anderson P., Ohno S. Genes Dev. 23:1091-1105(2009) [PubMed: 19417104] [Abstract] Cited for: IDENTIFICATION IN THE SURF COMPLEX.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"The crystal structure of human eukaryotic release factor eRF1 --mechanism of stop codon recognition and peptidyl-tRNA hydrolysis." Song H., Mugnier P., Das A.K., Webb H.M., Evans D.R., Tuite M.F., Hemmings B.A., Barford D. Cell 100:311-321(2000) [PubMed: 10676813] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[13]	"Eukaryotic class 1 translation termination factor eRF1 -- the NMR structure and dynamics of the middle domain involved in triggering ribosome-dependent peptidyl-tRNA hydrolysis." Ivanova E.V., Kolosov P.M., Birdsall B., Kelly G., Pastore A., Kisselev L.L., Polshakov V.I. FEBS J. 274:4223-4237(2007) [PubMed: 17651434] [Abstract] Cited for: STRUCTURE BY NMR OF 140-277.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M75715 mRNA. Translation: AAA36665.1. Sequence problems.
X81625 mRNA. Translation: CAA57281.1.
U90176 mRNA. Translation: AAB49726.1.
AF095901 Genomic DNA. Translation: AAD43966.1.
AK312510 mRNA. Translation: BAG35411.1.
CH471062 Genomic DNA. Translation: EAW62130.1.
CH471062 Genomic DNA. Translation: EAW62131.1.
BC088358 mRNA. Translation: AAH88358.1.

IPI

IPI00429191.

PIR

S50853.

RefSeq

NP_004721.1. NM_004730.2.

UniGene

Hs.483494.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DT9	X-ray	2.70	A	1-437	[»]
2HST	NMR	-	A	140-275	[»]
2KTU	NMR	-	A	276-437	[»]
2KTV	NMR	-	A	276-437	[»]
3E1Y	X-ray	3.80	A/B/C/D	1-437	[»]

ProteinModelPortal

P62495.

SMR

P62495. Positions 5-437.

DisProt

DP00310.

ModBase

Search...

Protein-protein interaction databases

IntAct

P62495. 6 interactions.

MINT

MINT-5004401.

STRING

P62495.

PTM databases

PhosphoSite

P62495.

Polymorphism databases

DMDM

50402099.

Proteomic databases

PeptideAtlas

P62495.

PRIDE

P62495.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000360541; ENSP00000353741; ENSG00000120705.

GeneID

2107.

KEGG

hsa:2107.

UCSC

uc003ldc.2. human.

Organism-specific databases

CTD

2107.

GeneCards

GC05M137869.

H-InvDB

HIX0200761.

HGNC

HGNC:3477. ETF1.

HPA

CAB011686.

MIM

600285. gene.

neXtProt

NX_P62495.

PharmGKB

PA27893.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG07956.

HOGENOM

HBG497188.

HOVERGEN

HBG005602.

InParanoid

P62495.

OMA

GDYLHHE.

PhylomeDB

P62495.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P62495.

Bgee

P62495.

CleanEx

HS_ETF1.

Genevestigator

P62495.

GermOnline

ENSG00000120705. Homo sapiens.

Family and domain databases

InterPro

IPR005140. eRF1_1_Pelota.
IPR005141. eRF1_2.
IPR005142. eRF1_3.
IPR004403. Peptide_chain-rel_eRF1/aRF1.
IPR024049. Release_factor_eRF1/aRF1_N.
[Graphical view]

Gene3D

G3DSA:3.30.960.10. G3DSA:3.30.960.10. 1 hit.

KO

K03265.

PANTHER

PTHR10113. eRF1. 1 hit.

Pfam

PF03463. eRF1_1. 1 hit.
PF03464. eRF1_2. 1 hit.
PF03465. eRF1_3. 1 hit.
[Graphical view]

SUPFAM

SSF55481. SSF55481. 1 hit.

TIGRFAMs

TIGR03676. ARF1/eRF1. 1 hit.

ProtoNet

Search...

Other

NextBio

8519.

SOURCE

Search...

Entry information

Entry name

ERF1_HUMAN

Accession

Primary (citable) accession number: P62495
Secondary accession number(s): B2R6B4 , D3DQC1, P46055, Q5M7Z7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 84 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.