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Protein

116 kDa U5 small nuclear ribonucleoprotein component

Gene

EFTUD2

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

Functioni

Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex required for pre-mRNA splicing. Binds GTP.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi136 – 1438GTPSequence Analysis
Nucleotide bindingi204 – 2085GTPSequence Analysis
Nucleotide bindingi258 – 2614GTPSequence Analysis

GO - Molecular functioni

  1. GTPase activity Source: ProtInc
  2. GTP binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA processing Source: ProtInc
  3. mRNA splicing, via spliceosome Source: UniProtKB
  4. RNA splicing Source: Reactome
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1753. mRNA Splicing - Minor Pathway.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
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 namesi
Name:EFTUD2
Synonyms:KIAA0031, SNRP116
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:30858. EFTUD2.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. Cajal body Source: BHF-UCL
  2. catalytic step 2 spliceosome Source: UniProtKB
  3. cytoplasm Source: HPA
  4. membrane Source: UniProtKB
  5. nuclear speck Source: BHF-UCL
  6. nucleoplasm Source: HPA
  7. spliceosomal complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Involvement in diseasei

Mandibulofacial dysostosis with microcephaly1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA rare syndrome characterized by progressive microcephaly, midface and malar hypoplasia, micrognathia, microtia, dysplastic ears, preauricular skin tags, significant developmental delay, and speech delay. Many patients have major sequelae, including choanal atresia that results in respiratory difficulties, conductive hearing loss, and cleft palate.

See also OMIM:610536
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti262 – 2621R → W in MFDM. 1 Publication
VAR_067580
Natural varianti476 – 4761C → R in MFDM. 1 Publication
VAR_067581
Natural varianti637 – 6371L → R in MFDM. 1 Publication
VAR_067582

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi610536. phenotype.
Orphaneti79113. Mandibulofacial dysostosis-microcephaly syndrome.
PharmGKBiPA142671915.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 972972116 kDa U5 small nuclear ribonucleoprotein componentPRO_0000091563Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei19 – 191Phosphoserine4 Publications
Modified residuei86 – 861Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15029.
PaxDbiQ15029.
PeptideAtlasiQ15029.
PRIDEiQ15029.

PTM databases

PhosphoSiteiQ15029.

Expressioni

Gene expression databases

BgeeiQ15029.
CleanExiHS_EFTUD2.
ExpressionAtlasiQ15029. baseline and differential.
GenevestigatoriQ15029.

Organism-specific databases

HPAiHPA022021.

Interactioni

Subunit structurei

Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, NHP2L1, EFTUD2, SART1 and USP39. Identified in the spliceosome C complex. Interacts with ERBB4 and PRPF8.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSPB1P047922EBI-357897,EBI-352682
IKQ131232EBI-357897,EBI-713456
MYCP011065EBI-357897,EBI-447544
PRPF8Q6P2Q92EBI-357897,EBI-538479
SF3B4Q154272EBI-357897,EBI-348469

Protein-protein interaction databases

BioGridi114749. 125 interactions.
IntActiQ15029. 42 interactions.
MINTiMINT-1161890.
STRINGi9606.ENSP00000262414.

Structurei

3D structure databases

ProteinModelPortaliQ15029.
SMRiQ15029. Positions 114-954.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini127 – 409283tr-type GPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0480.
GeneTreeiENSGT00770000120583.
HOGENOMiHOG000231589.
HOVERGENiHBG001838.
InParanoidiQ15029.
KOiK12852.
OMAiPTDTSIK.
OrthoDBiEOG7WDN1S.
PhylomeDBiQ15029.
TreeFamiTF105703.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR000795. EF_GTP-bd_dom.
IPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR005517. Transl_elong_EFG/EF2_IV.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SMARTiSM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15029-1) [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
MDTDLYDEFG NYIGPELDSD EDDDELGRET KDLDEMDDDD DDDDVGDHDD
60 70 80 90 100
DHPGMEVVLH EDKKYYPTAE EVYGPEVETI VQEEDTQPLT EPIIKPVKTK
110 120 130 140 150
KFTLMEQTLP VTVYEMDFLA DLMDNSELIR NVTLCGHLHH GKTCFVDCLI
160 170 180 190 200
EQTHPEIRKR YDQDLCYTDI LFTEQERGVG IKSTPVTVVL PDTKGKSYLF
210 220 230 240 250
NIMDTPGHVN FSDEVTAGLR ISDGVVLFID AAEGVMLNTE RLIKHAVQER
260 270 280 290 300
LAVTVCINKI DRLILELKLP PTDAYYKLRH IVDEVNGLIS MYSTDENLIL
310 320 330 340 350
SPLLGNVCFS SSQYSICFTL GSFAKIYADT FGDINYQEFA KRLWGDIYFN
360 370 380 390 400
PKTRKFTKKA PTSSSQRSFV EFILEPLYKI LAQVVGDVDT SLPRTLDELG
410 420 430 440 450
IHLTKEELKL NIRPLLRLVC KKFFGEFTGF VDMCVQHIPS PKVGAKPKIE
460 470 480 490 500
HTYTGGVDSD LGEAMSDCDP DGPLMCHTTK MYSTDDGVQF HAFGRVLSGT
510 520 530 540 550
IHAGQPVKVL GENYTLEDEE DSQICTVGRL WISVARYHIE VNRVPAGNWV
560 570 580 590 600
LIEGVDQPIV KTATITEPRG NEEAQIFRPL KFNTTSVIKI AVEPVNPSEL
610 620 630 640 650
PKMLDGLRKV NKSYPSLTTK VEESGEHVIL GTGELYLDCV MHDLRKMYSE
660 670 680 690 700
IDIKVADPVV TFCETVVETS SLKCFAETPN KKNKITMIAE PLEKGLAEDI
710 720 730 740 750
ENEVVQITWN RKKLGEFFQT KYDWDLLAAR SIWAFGPDAT GPNILVDDTL
760 770 780 790 800
PSEVDKALLG SVKDSIVQGF QWGTREGPLC DELIRNVKFK ILDAVVAQEP
810 820 830 840 850
LHRGGGQIIP TARRVVYSAF LMATPRLMEP YYFVEVQAPA DCVSAVYTVL
860 870 880 890 900
ARRRGHVTQD APIPGSPLYT IKAFIPAIDS FGFETDLRTH TQGQAFSLSV
910 920 930 940 950
FHHWQIVPGD PLDKSIVIRP LEPQPAPHLA REFMIKTRRR KGLSEDVSIS
960 970
KFFDDPMLLE LAKQDVVLNY PM
Length:972
Mass (Da):109,436
Last modified:November 1, 1996 - v1
Checksum:i862BD6CA7993F118
GO
Isoform 2 (identifier: Q15029-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.

Show »
Length:937
Mass (Da):105,384
Checksum:iC754AB346695B0C3
GO
Isoform 3 (identifier: Q15029-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     143-152: Missing.

Note: No experimental confirmation available.

Show »
Length:962
Mass (Da):108,283
Checksum:i6EF1ECDE3BDA0784
GO

Sequence cautioni

The sequence BAA04699.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti321 – 3211G → V in AAH02360 (PubMed:15489334).Curated
Sequence conflicti619 – 6191T → S in BAG59832 (PubMed:14702039).Curated
Sequence conflicti955 – 9551D → G in BAG59832 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti262 – 2621R → W in MFDM. 1 Publication
VAR_067580
Natural varianti476 – 4761C → R in MFDM. 1 Publication
VAR_067581
Natural varianti637 – 6371L → R in MFDM. 1 Publication
VAR_067582
Natural varianti773 – 7731G → V.
Corresponds to variant rs1056505 [ dbSNP | Ensembl ].
VAR_014931

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3535Missing in isoform 2. 1 PublicationVSP_044282Add
BLAST
Alternative sequencei143 – 15210Missing in isoform 3. 1 PublicationVSP_055175

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21163 mRNA. Translation: BAA04699.2. Different initiation.
AK296367 mRNA. Translation: BAG59042.1.
AK297392 mRNA. Translation: BAG59832.1.
AK316098 mRNA. Translation: BAH14469.1.
AC015936 Genomic DNA. No translation available.
CH471178 Genomic DNA. Translation: EAW51573.1.
CH471178 Genomic DNA. Translation: EAW51574.1.
BC002360 mRNA. Translation: AAH02360.1.
CCDSiCCDS11489.1. [Q15029-1]
CCDS45707.1. [Q15029-2]
CCDS59295.1. [Q15029-3]
RefSeqiNP_001136077.1. NM_001142605.1. [Q15029-2]
NP_001245282.1. NM_001258353.1. [Q15029-1]
NP_001245283.1. NM_001258354.1. [Q15029-3]
NP_004238.3. NM_004247.3. [Q15029-1]
UniGeneiHs.151787.

Genome annotation databases

EnsembliENST00000402521; ENSP00000385873; ENSG00000108883. [Q15029-2]
ENST00000426333; ENSP00000392094; ENSG00000108883. [Q15029-1]
ENST00000591382; ENSP00000467805; ENSG00000108883. [Q15029-1]
ENST00000592576; ENSP00000465058; ENSG00000108883. [Q15029-3]
GeneIDi9343.
KEGGihsa:9343.
UCSCiuc002ihn.2. human. [Q15029-1]

Polymorphism databases

DMDMi18202501.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21163 mRNA. Translation: BAA04699.2. Different initiation.
AK296367 mRNA. Translation: BAG59042.1.
AK297392 mRNA. Translation: BAG59832.1.
AK316098 mRNA. Translation: BAH14469.1.
AC015936 Genomic DNA. No translation available.
CH471178 Genomic DNA. Translation: EAW51573.1.
CH471178 Genomic DNA. Translation: EAW51574.1.
BC002360 mRNA. Translation: AAH02360.1.
CCDSiCCDS11489.1. [Q15029-1]
CCDS45707.1. [Q15029-2]
CCDS59295.1. [Q15029-3]
RefSeqiNP_001136077.1. NM_001142605.1. [Q15029-2]
NP_001245282.1. NM_001258353.1. [Q15029-1]
NP_001245283.1. NM_001258354.1. [Q15029-3]
NP_004238.3. NM_004247.3. [Q15029-1]
UniGeneiHs.151787.

3D structure databases

ProteinModelPortaliQ15029.
SMRiQ15029. Positions 114-954.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114749. 125 interactions.
IntActiQ15029. 42 interactions.
MINTiMINT-1161890.
STRINGi9606.ENSP00000262414.

PTM databases

PhosphoSiteiQ15029.

Polymorphism databases

DMDMi18202501.

Proteomic databases

MaxQBiQ15029.
PaxDbiQ15029.
PeptideAtlasiQ15029.
PRIDEiQ15029.

Protocols and materials databases

DNASUi9343.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000402521; ENSP00000385873; ENSG00000108883. [Q15029-2]
ENST00000426333; ENSP00000392094; ENSG00000108883. [Q15029-1]
ENST00000591382; ENSP00000467805; ENSG00000108883. [Q15029-1]
ENST00000592576; ENSP00000465058; ENSG00000108883. [Q15029-3]
GeneIDi9343.
KEGGihsa:9343.
UCSCiuc002ihn.2. human. [Q15029-1]

Organism-specific databases

CTDi9343.
GeneCardsiGC17M042927.
H-InvDBHIX0135614.
HGNCiHGNC:30858. EFTUD2.
HPAiHPA022021.
MIMi603892. gene.
610536. phenotype.
neXtProtiNX_Q15029.
Orphaneti79113. Mandibulofacial dysostosis-microcephaly syndrome.
PharmGKBiPA142671915.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0480.
GeneTreeiENSGT00770000120583.
HOGENOMiHOG000231589.
HOVERGENiHBG001838.
InParanoidiQ15029.
KOiK12852.
OMAiPTDTSIK.
OrthoDBiEOG7WDN1S.
PhylomeDBiQ15029.
TreeFamiTF105703.

Enzyme and pathway databases

ReactomeiREACT_1753. mRNA Splicing - Minor Pathway.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiEFTUD2. human.
GeneWikiiEFTUD2.
GenomeRNAii9343.
NextBioi34995.
PROiQ15029.
SOURCEiSearch...

Gene expression databases

BgeeiQ15029.
CleanExiHS_EFTUD2.
ExpressionAtlasiQ15029. baseline and differential.
GenevestigatoriQ15029.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR000795. EF_GTP-bd_dom.
IPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR005517. Transl_elong_EFG/EF2_IV.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SMARTiSM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Thalamus.
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 1).
    Tissue: Muscle.
  6. "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] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRPF8.
  8. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  9. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP."
    Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.
    RNA 12:1418-1430(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  12. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, SUBCELLULAR LOCATION.
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND THR-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. Cited for: VARIANTS MFDM TRP-262; ARG-476 AND ARG-637.

Entry informationi

Entry nameiU5S1_HUMAN
AccessioniPrimary (citable) accession number: Q15029
Secondary accession number(s): B4DK30
, B4DMC0, D3DX58, K7EJ81, Q9BUR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: November 1, 1996
Last modified: March 4, 2015
This is version 171 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.