116 kDa U5 small nuclear ribonucleoprotein component

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Q15029 (U5S1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 136. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
116 kDa U5 small nuclear ribonucleoprotein component

Alternative name(s):
Elongation factor Tu GTP-binding domain-containing protein 2
SNU114 homolog
Short name=hSNU114
U5 snRNP-specific protein, 116 kDa
Short name=U5-116 kDa

Gene names

Name:	EFTUD2
Synonyms:	KIAA0031, SNRP116

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	972 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the U5 snRNP complex required for pre-mRNA splicing. Binds GTP.
Subunit structure	Identified in the spliceosome C complex. Interacts with ERBB4 and PRPF8. Ref.5 Ref.12
Subcellular location	Nucleus Ref.12.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
Sequence similarities	Belongs to the GTP-binding elongation factor family. EF-G/EF-2 subfamily.
Sequence caution	The sequence BAA04699.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Coding sequence diversity	Polymorphism
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	nuclear mRNA splicing, via spliceosome Inferred by curator Ref.6. Source: UniProtKB
Cellular component	Cajal body Inferred from direct assay. Source: BHF-UCL catalytic step 2 spliceosome Inferred from direct assay Ref.6. Source: UniProtKB cytoplasm Inferred from direct assay. Source: HPA nuclear speck Inferred from direct assay. Source: BHF-UCL
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction Ref.12. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MYC	P01106	5	EBI-357897,EBI-447544
PRPF8	Q6P2Q9	2	EBI-357897,EBI-538479

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 972

972

116 kDa U5 small nuclear ribonucleoprotein component

PRO_0000091563

Regions

Nucleotide binding

136 – 143

GTP Potential

Nucleotide binding

204 – 208

GTP Potential

Nucleotide binding

258 – 261

GTP Potential

Amino acid modifications

Modified residue

N-acetylmethionine Ref.10

Modified residue

Phosphoserine Ref.8 Ref.10

Modified residue

Phosphothreonine Ref.10

Modified residue

Phosphothreonine Ref.7 Ref.9

Modified residue

944

Phosphoserine Ref.11

Natural variations

Natural variant

773

G → V.
Corresponds to variant rs1056505 [ dbSNP | Ensembl ].

VAR_014931

Experimental info

Sequence conflict

321

G → V in AAH02360. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q15029 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 862BD6CA7993F118
Show »

FASTA

972

109,436

        10         20         30         40         50         60 
MDTDLYDEFG NYIGPELDSD EDDDELGRET KDLDEMDDDD DDDDVGDHDD DHPGMEVVLH 

        70         80         90        100        110        120 
EDKKYYPTAE EVYGPEVETI VQEEDTQPLT EPIIKPVKTK KFTLMEQTLP VTVYEMDFLA 

       130        140        150        160        170        180 
DLMDNSELIR NVTLCGHLHH GKTCFVDCLI EQTHPEIRKR YDQDLCYTDI LFTEQERGVG 

       190        200        210        220        230        240 
IKSTPVTVVL PDTKGKSYLF NIMDTPGHVN FSDEVTAGLR ISDGVVLFID AAEGVMLNTE 

       250        260        270        280        290        300 
RLIKHAVQER LAVTVCINKI DRLILELKLP PTDAYYKLRH IVDEVNGLIS MYSTDENLIL 

       310        320        330        340        350        360 
SPLLGNVCFS SSQYSICFTL GSFAKIYADT FGDINYQEFA KRLWGDIYFN PKTRKFTKKA 

       370        380        390        400        410        420 
PTSSSQRSFV EFILEPLYKI LAQVVGDVDT SLPRTLDELG IHLTKEELKL NIRPLLRLVC 

       430        440        450        460        470        480 
KKFFGEFTGF VDMCVQHIPS PKVGAKPKIE HTYTGGVDSD LGEAMSDCDP DGPLMCHTTK 

       490        500        510        520        530        540 
MYSTDDGVQF HAFGRVLSGT IHAGQPVKVL GENYTLEDEE DSQICTVGRL WISVARYHIE 

       550        560        570        580        590        600 
VNRVPAGNWV LIEGVDQPIV KTATITEPRG NEEAQIFRPL KFNTTSVIKI AVEPVNPSEL 

       610        620        630        640        650        660 
PKMLDGLRKV NKSYPSLTTK VEESGEHVIL GTGELYLDCV MHDLRKMYSE IDIKVADPVV 

       670        680        690        700        710        720 
TFCETVVETS SLKCFAETPN KKNKITMIAE PLEKGLAEDI ENEVVQITWN RKKLGEFFQT 

       730        740        750        760        770        780 
KYDWDLLAAR SIWAFGPDAT GPNILVDDTL PSEVDKALLG SVKDSIVQGF QWGTREGPLC 

       790        800        810        820        830        840 
DELIRNVKFK ILDAVVAQEP LHRGGGQIIP TARRVVYSAF LMATPRLMEP YYFVEVQAPA 

       850        860        870        880        890        900 
DCVSAVYTVL ARRRGHVTQD APIPGSPLYT IKAFIPAIDS FGFETDLRTH TQGQAFSLSV 

       910        920        930        940        950        960 
FHHWQIVPGD PLDKSIVIRP LEPQPAPHLA REFMIKTRRR KGLSEDVSIS KFFDDPMLLE 

       970 
LAKQDVVLNY PM

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1." Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S. DNA Res. 1:27-35(1994) [PubMed: 7584026] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow.
[2]	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. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: Muscle.
[4]	"An evolutionarily conserved U5 snRNP-specific protein is a GTP-binding factor closely related to the ribosomal translocase EF-2." Fabrizio P., Laggerbauer B., Lauber J., Lane W.S., Luehrmann R. EMBO J. 16:4092-4106(1997) [PubMed: 9233818] [Abstract] Cited for: CHARACTERIZATION.
[5]	"The human U5-220kD protein (hPrp8) forms a stable RNA-free complex with several U5-specific proteins, including an RNA unwindase, a homologue of ribosomal elongation factor EF-2, and a novel WD-40 protein." Achsel T., Ahrens K., Brahms H., Teigelkamp S., Luehrmann R. Mol. Cell. Biol. 18:6756-6766(1998) [PubMed: 9774689] [Abstract] Cited for: INTERACTION WITH PRPF8.
[6]	"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis." Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J. RNA 8:426-439(2002) [PubMed: 11991638] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[7]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"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 MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND THR-30, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-944, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways." Gilmore-Hebert M., Ramabhadran R., Stern D.F. Mol. Cancer Res. 8:1388-1398(2010) [PubMed: 20858735] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, SUBCELLULAR LOCATION.
[13]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D21163 mRNA. Translation: BAA04699.2. Different initiation. CH471178 Genomic DNA. Translation: EAW51573.1. CH471178 Genomic DNA. Translation: EAW51574.1. BC002360 mRNA. Translation: AAH02360.1.
IPI	IPI00003519.
RefSeq	NP_001136077.1. NM_001142605.1. NP_004238.3. NM_004247.3.
UniGene	Hs.151787.
3D structure databases
ProteinModelPortal	Q15029.
SMR	Q15029. Positions 112-955.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15029. 20 interactions.
MINT	MINT-1161890.
STRING	Q15029.
PTM databases
PhosphoSite	Q15029.
Polymorphism databases
DMDM	18202501.
Proteomic databases
PeptideAtlas	Q15029.
PRIDE	Q15029.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262414; ENSP00000262414; ENSG00000108883. ENST00000426333; ENSP00000392094; ENSG00000108883.
GeneID	9343.
KEGG	hsa:9343.
UCSC	uc002ihn.1. human.
Organism-specific databases
CTD	9343.
GeneCards	GC17M042927.
H-InvDB	HIX0013887.
HGNC	HGNC:30858. EFTUD2.
HPA	HPA022021.
MIM	603892. gene.
neXtProt	NX_Q15029.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07288.
HOGENOM	HBG737692.
HOVERGEN	HBG001838.
InParanoid	Q15029.
OMA	WVLIEGI.
OrthoDB	EOG4001HJ.
PhylomeDB	Q15029.
Enzyme and pathway databases
Reactome	REACT_1675. mRNA Processing. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q15029.
Bgee	Q15029.
CleanEx	HS_EFTUD2.
Genevestigator	Q15029.
GermOnline	ENSG00000108883. Homo sapiens.
Family and domain databases
InterPro	IPR009022. Elongation_fac_G/III/V. IPR000795. ProtSyn_GTP-bd. IPR020568. Ribosomal_S5_D2-typ_fold. IPR014721. Ribosomal_S5_D2-typ_fold_subgr. IPR005225. Small_GTP-bd_dom. IPR000640. Transl_elong_EFG/EF2_C. IPR005517. Transl_elong_EFG/EF2_IV. IPR004161. Transl_elong_EFTu/EF1A_2. IPR009000. Transl_elong_init/rib_B-barrel. [Graphical view]
Gene3D	G3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit. G3DSA:3.30.70.240. Transl_elong_EFG/EF2_C. 1 hit.
KO	K12852.
Pfam	PF00679. EFG_C. 1 hit. PF03764. EFG_IV. 1 hit. PF00009. GTP_EFTU. 1 hit. PF03144. GTP_EFTU_D2. 1 hit. [Graphical view]
PRINTS	PR00315. ELONGATNFCT.
SMART	SM00838. EFG_C. 1 hit. SM00889. EFG_IV. 1 hit. [Graphical view]
SUPFAM	SSF54980. EFG_III_V. 2 hits. SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit. SSF50447. Translat_factor. 1 hit.
TIGRFAMs	TIGR00231. Small_GTP. 1 hit.
PROSITE	PS00301. EFACTOR_GTP. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	34995.
SOURCE	Search...

Entry information

Entry name

U5S1_HUMAN

Accession

Primary (citable) accession number: Q15029
Secondary accession number(s): D3DX58, Q9BUR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 136 of the entry and version 1 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.

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List of human entries with polymorphisms or disease mutations

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Index of human polymorphisms and disease mutations

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Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents