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P15170

- ERF3A_HUMAN

UniProt

P15170 - ERF3A_HUMAN

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Protein

Eukaryotic peptide chain release factor GTP-binding subunit ERF3A

Gene

GSPT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in translation termination in response to the termination codons UAA, UAG and UGA. Stimulates the activity of ERF1. Involved in regulation of mammalian cell growth. 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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi81 – 888GTPBy similarity
Nucleotide bindingi158 – 1625GTPBy similarity
Nucleotide bindingi220 – 2234GTPBy similarity

GO - Molecular functioni

  1. GTPase activity Source: UniProtKB
  2. GTP binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: UniProtKB
  4. translation release factor activity Source: UniProtKB

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: UniProtKB
  2. GTP catabolic process Source: GOC
  3. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
  4. protein methylation Source: MGI
  5. translational termination Source: GOC
Complete GO annotation...

Keywords - Biological processi

Nonsense-mediated mRNA decay, Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic peptide chain release factor GTP-binding subunit ERF3A
Short name:
Eukaryotic peptide chain release factor subunit 3a
Short name:
eRF3a
Alternative name(s):
G1 to S phase transition protein 1 homolog
Gene namesi
Name:GSPT1
Synonyms:ERF3A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:4621. GSPT1.

Subcellular locationi

GO - Cellular componenti

  1. intracellular Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29012.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499Eukaryotic peptide chain release factor GTP-binding subunit ERF3APRO_0000091480Add
BLAST

Proteomic databases

MaxQBiP15170.
PaxDbiP15170.
PRIDEiP15170.

PTM databases

PhosphoSiteiP15170.

Miscellaneous databases

PMAP-CutDBP15170.

Expressioni

Gene expression databases

BgeeiP15170.
CleanExiHS_GSPT1.
ExpressionAtlasiP15170. baseline and differential.
GenevestigatoriP15170.

Organism-specific databases

HPAiHPA052488.

Interactioni

Subunit structurei

Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ETF1P624952EBI-948993,EBI-1047744
PABPC1P119402EBI-9094806,EBI-81531
UPF1Q929002EBI-948993,EBI-373471

Protein-protein interaction databases

BioGridi109190. 28 interactions.
IntActiP15170. 8 interactions.
MINTiMINT-2859376.
STRINGi9606.ENSP00000398131.

Structurei

Secondary structure

1
499
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi303 – 3053
Beta strandi308 – 3103
Beta strandi316 – 3183
Turni335 – 3373
Beta strandi340 – 3434
Beta strandi348 – 3514
Beta strandi354 – 3563
Beta strandi364 – 3674
Beta strandi379 – 3813
Beta strandi383 – 3853
Beta strandi392 – 3987
Beta strandi411 – 4188
Beta strandi420 – 4289
Beta strandi452 – 4598
Beta strandi478 – 4803
Beta strandi490 – 4945

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3E1YX-ray3.80E/F/G/H301-499[»]
3J5Yelectron microscopy9.70B69-496[»]
3KUIX-ray2.30B64-78[»]
ProteinModelPortaliP15170.
SMRiP15170. Positions 2-496.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96GF2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini72 – 298227tr-type GPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni81 – 888G1PROSITE-ProRule annotation
Regioni137 – 1415G2PROSITE-ProRule annotation
Regioni158 – 1614G3PROSITE-ProRule annotation
Regioni220 – 2234G4PROSITE-ProRule annotation
Regioni262 – 2643G5PROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. ERF3 subfamily.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5256.
GeneTreeiENSGT00620000087924.
HOGENOMiHOG000229291.
HOVERGENiHBG000179.
InParanoidiP15170.
KOiK03267.
OMAiLVVMPNK.
OrthoDBiEOG76X5ZT.
PhylomeDBiP15170.
TreeFamiTF300566.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamiPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P15170-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MELSEPIVEN GETEMSPEES WEHKEEISEA EPGGGSLGDG RPPEESAHEM
60 70 80 90 100
MEEEEEIPKP KSVVAPPGAP KKEHVNVVFI GHVDAGKSTI GGQIMYLTGM
110 120 130 140 150
VDKRTLEKYE REAKEKNRET WYLSWALDTN QEERDKGKTV EVGRAYFETE
160 170 180 190 200
KKHFTILDAP GHKSFVPNMI GGASQADLAV LVISARKGEF ETGFEKGGQT
210 220 230 240 250
REHAMLAKTA GVKHLIVLIN KMDDPTVNWS NERYEECKEK LVPFLKKVGF
260 270 280 290 300
NPKKDIHFMP CSGLTGANLK EQSDFCPWYI GLPFIPYLDN LPNFNRSVDG
310 320 330 340 350
PIRLPIVDKY KDMGTVVLGK LESGSICKGQ QLVMMPNKHN VEVLGILSDD
360 370 380 390 400
VETDTVAPGE NLKIRLKGIE EEEILPGFIL CDPNNLCHSG RTFDAQIVII
410 420 430 440 450
EHKSIICPGY NAVLHIHTCI EEVEITALIC LVDKKSGEKS KTRPRFVKQD
460 470 480 490
QVCIARLRTA GTICLETFKD FPQMGRFTLR DEGKTIAIGK VLKLVPEKD
Length:499
Mass (Da):55,756
Last modified:April 1, 1990 - v1
Checksum:iDE20482CCABC3576
GO
Isoform 2 (identifier: P15170-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDPGSGGGGG...CEGSNSAVSM
     8-8: Missing.

Show »
Length:636
Mass (Da):68,601
Checksum:i31E3FE3DEDF4BE5E
GO
Isoform 3 (identifier: P15170-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDPGSGGGGG...CEGSNSAVSM

Note: Gene prediction based on EST data.

Show »
Length:637
Mass (Da):68,700
Checksum:i7765D73A284F35C4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 2 (identifier: P15170-2)
Sequence conflicti6 – 94GGGG → G in AAH09503. (PubMed:15489334)Curated
Sequence conflicti92 – 921G → C in AAH09503. (PubMed:15489334)Curated
Sequence conflicti100 – 1001V → A in AAH09503. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MDPGSGGGGGGGGGGGSSSG SSSSDSAPDCWDQADMEAPG PGPCGGGGSLAAAAEAQREN LSAAFSRQLNVNAKPFVPNV HAAEFVPSFLRGPAAPPPPV GGAANNHGAGSGAGGRAAPV ESSQEEQSLCEGSNSAVSM in isoform 2 and isoform 3. 1 PublicationVSP_042198
Alternative sequencei8 – 81Missing in isoform 2. 1 PublicationVSP_042199

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X17644 mRNA. Translation: CAA35635.1.
U95742 Genomic DNA. Translation: AAB67250.1.
AC007216 Genomic DNA. No translation available.
BC009503 mRNA. Translation: AAH09503.2.
CCDSiCCDS45412.1. [P15170-3]
CCDS45413.1. [P15170-2]
CCDS45414.1. [P15170-1]
PIRiS06941.
RefSeqiNP_001123478.1. NM_001130006.1.
NP_001123479.1. NM_001130007.1. [P15170-1]
UniGeneiHs.528780.

Genome annotation databases

EnsembliENST00000420576; ENSP00000399539; ENSG00000103342. [P15170-1]
ENST00000434724; ENSP00000398131; ENSG00000103342. [P15170-3]
ENST00000439887; ENSP00000408399; ENSG00000103342. [P15170-2]
ENST00000563468; ENSP00000454351; ENSG00000103342. [P15170-1]
GeneIDi2935.
KEGGihsa:2935.
UCSCiuc002dbu.3. human. [P15170-2]
uc010bux.3. human. [P15170-1]

Polymorphism databases

DMDMi121688.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X17644 mRNA. Translation: CAA35635.1 .
U95742 Genomic DNA. Translation: AAB67250.1 .
AC007216 Genomic DNA. No translation available.
BC009503 mRNA. Translation: AAH09503.2 .
CCDSi CCDS45412.1. [P15170-3 ]
CCDS45413.1. [P15170-2 ]
CCDS45414.1. [P15170-1 ]
PIRi S06941.
RefSeqi NP_001123478.1. NM_001130006.1.
NP_001123479.1. NM_001130007.1. [P15170-1 ]
UniGenei Hs.528780.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3E1Y X-ray 3.80 E/F/G/H 301-499 [» ]
3J5Y electron microscopy 9.70 B 69-496 [» ]
3KUI X-ray 2.30 B 64-78 [» ]
ProteinModelPortali P15170.
SMRi P15170. Positions 2-496.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109190. 28 interactions.
IntActi P15170. 8 interactions.
MINTi MINT-2859376.
STRINGi 9606.ENSP00000398131.

PTM databases

PhosphoSitei P15170.

Polymorphism databases

DMDMi 121688.

Proteomic databases

MaxQBi P15170.
PaxDbi P15170.
PRIDEi P15170.

Protocols and materials databases

DNASUi 2935.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000420576 ; ENSP00000399539 ; ENSG00000103342 . [P15170-1 ]
ENST00000434724 ; ENSP00000398131 ; ENSG00000103342 . [P15170-3 ]
ENST00000439887 ; ENSP00000408399 ; ENSG00000103342 . [P15170-2 ]
ENST00000563468 ; ENSP00000454351 ; ENSG00000103342 . [P15170-1 ]
GeneIDi 2935.
KEGGi hsa:2935.
UCSCi uc002dbu.3. human. [P15170-2 ]
uc010bux.3. human. [P15170-1 ]

Organism-specific databases

CTDi 2935.
GeneCardsi GC16M011961.
HGNCi HGNC:4621. GSPT1.
HPAi HPA052488.
MIMi 139259. gene.
neXtProti NX_P15170.
PharmGKBi PA29012.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5256.
GeneTreei ENSGT00620000087924.
HOGENOMi HOG000229291.
HOVERGENi HBG000179.
InParanoidi P15170.
KOi K03267.
OMAi LVVMPNK.
OrthoDBi EOG76X5ZT.
PhylomeDBi P15170.
TreeFami TF300566.

Miscellaneous databases

ChiTaRSi GSPT1. human.
EvolutionaryTracei Q96GF2.
GeneWikii GSPT1.
GenomeRNAii 2935.
NextBioi 11631.
PMAP-CutDB P15170.
PROi P15170.
SOURCEi Search...

Gene expression databases

Bgeei P15170.
CleanExi HS_GSPT1.
ExpressionAtlasi P15170. baseline and differential.
Genevestigatori P15170.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view ]
Pfami PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 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. "A human homologue of the yeast GST1 gene codes for a GTP-binding protein and is expressed in a proliferation-dependent manner in mammalian cells."
    Hoshino S., Miyazawa H., Enomoto T., Hanaoka F., Kikuchi Y., Kikuchi A., Ui M.
    EMBO J. 8:3807-3814(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Lung.
  5. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SURF COMPLEX.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Molecular basis of eRF3 recognition by the MLLE domain of poly(A)-binding protein."
    Kozlov G., Gehring K.
    PLoS ONE 5:E10169-E10169(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 73-87 (ISOFORM 2).

Entry informationi

Entry nameiERF3A_HUMAN
AccessioniPrimary (citable) accession number: P15170
Secondary accession number(s): J3KQG6, Q96GF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 29, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3