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Protein

U5 small nuclear ribonucleoprotein 200 kDa helicase

Gene

Snrnp200

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

RNA helicase that plays an essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes. Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome (By similarity).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi503 – 5108ATPPROSITE-ProRule annotation
Nucleotide bindingi1353 – 13608ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
U5 small nuclear ribonucleoprotein 200 kDa helicase (EC:3.6.4.13)
Alternative name(s):
BRR2 homolog
U5 snRNP-specific 200 kDa protein
Short name:
U5-200KD
Gene namesi
Name:Snrnp200
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1561120. Snrnp200.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21392139U5 small nuclear ribonucleoprotein 200 kDa helicasePRO_0000422050Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171PhosphoserineBy similarity
Modified residuei26 – 261PhosphoserineBy similarity
Modified residuei225 – 2251PhosphoserineCombined sources
Modified residuei389 – 3891PhosphothreonineBy similarity
Modified residuei709 – 7091PhosphotyrosineCombined sources
Cross-linki944 – 944Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei971 – 9711N6-acetyllysine; alternateBy similarity
Cross-linki971 – 971Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki1071 – 1071Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki1199 – 1199Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei1431 – 14311PhosphothreonineBy similarity
Modified residuei1768 – 17681PhosphothreonineBy similarity
Modified residuei2005 – 20051PhosphoserineBy similarity
Cross-linki2094 – 2094Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei2134 – 21341PhosphothreonineBy similarity
Modified residuei2136 – 21361PhosphoserineBy similarity
Modified residuei2138 – 21381PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiF1LNJ2.
PRIDEiF1LNJ2.

PTM databases

iPTMnetiF1LNJ2.

Interactioni

Subunit structurei

Component of a core complex containing at least PRPF8, SNRNP200, EFTUD2 and SNRNP40. 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, SNU13, EFTUD2, SART1 and USP39. Identified in the spliceosome C complex (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000048598.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini490 – 673184Helicase ATP-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini684 – 921238Helicase C-terminal 1PROSITE-ProRule annotationAdd
BLAST
Domaini982 – 1289308SEC63 1Add
BLAST
Domaini1340 – 1515176Helicase ATP-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini1548 – 1756209Helicase C-terminal 2PROSITE-ProRule annotationAdd
BLAST
Domaini1815 – 2127313SEC63 2Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili54 – 8431Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi615 – 6184DEAH box
Motifi1457 – 14604DEAH box

Domaini

Contains two helicase domains. The N-terminal helicase domain has catalytic activity by itself, contrary to C-terminal helicase domain that may have a regulatory role and enhance the activity of the first helicase domain.By similarity

Sequence similaritiesi

Belongs to the helicase family. SKI2 subfamily.Curated
Contains 2 helicase ATP-binding domains.PROSITE-ProRule annotation
Contains 2 helicase C-terminal domains.PROSITE-ProRule annotation
Contains 2 SEC63 domains.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG0952. Eukaryota.
COG1204. LUCA.
InParanoidiF1LNJ2.
TreeFamiTF300056.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
3.40.50.300. 4 hits.
InterProiIPR000008. C2_dom.
IPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014756. Ig_E-set.
IPR027417. P-loop_NTPase.
IPR004179. Sec63-dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00270. DEAD. 2 hits.
PF00271. Helicase_C. 1 hit.
PF02889. Sec63. 2 hits.
[Graphical view]
SMARTiSM00487. DEXDc. 2 hits.
SM00490. HELICc. 2 hits.
SM00973. Sec63. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 2 hits.
SSF52540. SSF52540. 4 hits.
SSF81296. SSF81296. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 2 hits.
PS51194. HELICASE_CTER. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

F1LNJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADVTARSLQ YEYKANSNLV LQADRSLIDR TRRDEPTGEV LSLVGKLEGT
60 70 80 90 100
RMGDKAQRTK PQMQEERRAK RRKRDEDRHD INKMKGYTLL SEGIDEMVGI
110 120 130 140 150
IYKPKTKETR ETYEVLLSFI QAALGDQPRD ILCGAADEVL AVLKNEKLRD
160 170 180 190 200
KERRREIDLL LGQTDDTRYH VLVNLGKKIT DYGGDKEIQN MDDNIDETYG
210 220 230 240 250
VNVQFESDEE EGDEDVYGEV REEASDDDME GDEAVVRCTL SANLVASGEL
260 270 280 290 300
MSSKKKDLHP RDIDAFWLQR QLSRFYDDAI VSQKKADEVL EILKTASDDR
310 320 330 340 350
ECENQLVLLL GFNTFDFIKV LRQHRMMILY CTLLASAQSE AEKERIMGKM
360 370 380 390 400
EADPELSKFL YQLHETEKED LIREERSRRE RVRQSRMDTD LETMDLDQGG
410 420 430 440 450
EALAPRQVLD LEDLVFTQGS HFMANKRCQL PDGSFRRQRK GYEEVHVPAL
460 470 480 490 500
KPKPFGSEEQ LLPVEKLPKY AQAGFEGFKT LNRIQSKLYR AALETDENLL
510 520 530 540 550
LCAPTGAGKT NVALMCMLRE IGKHINMDGT INVDDFKIIY IAPMRSLVQE
560 570 580 590 600
MVGSFGKRLA TYGITVAELT GDHQLCKEEI SATQIIVCTP EKWDIITRKG
610 620 630 640 650
GERTYTQLVR LIVLDEIHLL HDDRGPVLEA LVARAIRNIE MTQEDVRLIG
660 670 680 690 700
LSATLPNYED VATFLRVDPA KGLFYFDNSF RPVPLEQTYV GITEKKAIKR
710 720 730 740 750
FQIMNEIVYE KIMEHAGKNQ VLVFVHSRKE TGKTARAIRD MCLEKDTLGL
760 770 780 790 800
FLREGSASTE VLRTEAEQCK NLELKDLLPY GFAIHHAGMT RVDRTLVEDL
810 820 830 840 850
FADKHIQVLV STATLAWGVN LPAHTVIIKG TQVYSPEKGR WTELGALDIL
860 870 880 890 900
QMLGRAGRPQ YDTKGEGILI TSHGELQYYL SLLNQQLPIE SQMVSKLPDM
910 920 930 940 950
LNAEIVLGNV QNAKDAVNWL GYAYLYIRML RSPTLYGISH DDLKGDPLLD
960 970 980 990 1000
QRRLDLVHTA ALMLDKNNLV KYDKKTGNFQ VTELGRIASH YYITNDTVQT
1010 1020 1030 1040 1050
YNQLLKPTLS EIELFRVFSL SSEFKNITVR EEEKLELQKL LERVPIPVKE
1060 1070 1080 1090 1100
SIEEPSAKIN VLLQAFISQL KLEGFALMAD MVYVTQSAGR LMRAIFEIVL
1110 1120 1130 1140 1150
NRGWAQLTDK TLNLCKMIDK RMWQSMCPLR QFRKLPEEVV KKIEKKNFPF
1160 1170 1180 1190 1200
ERLYDLNHNE IGELIRMPKM GKTIHKYVHL FPKLELSVHL QPITRSTLKV
1210 1220 1230 1240 1250
ELTITPDFQW DEKARLVHGS SEAFWILVED VDSEVILHHE YFLLKAKYAQ
1260 1270 1280 1290 1300
DEHLITFFVP VFEPLPPQYF IRVVSDRWLS CETQLPVSFR HLILPEKYPP
1310 1320 1330 1340 1350
PTELLDLQPL PVSALRNSAF ESLYQDKFPF FNPIQTQVFN TVYNSDDNVF
1360 1370 1380 1390 1400
VGAPTGSGKT ICAEFAILRM LLQNSEGRCV YITPMEALAE QVYMDWYEKF
1410 1420 1430 1440 1450
QDRLNKKVVL LTGETSTDLK LLGKGNIIIS TPEKWDILSR RWKQRKNVQN
1460 1470 1480 1490 1500
INLFVVDEVH LIGGENGPVL EVICSRMRYI SSQIERPIRI VALSSSLSNA
1510 1520 1530 1540 1550
KDVAHWLGCS ATSTFNFHPN VRPVPLELHI QGFNISHTQT RLLSMAKPVY
1560 1570 1580 1590 1600
HAITKHSPKK PVIVFVPSRK QTRLTAIDIL TTCAADIQRQ RFLHCTEKDL
1610 1620 1630 1640 1650
IPYLEKLSDS TLKETLLNGV GYLHEGLSPM ERRLVEQLFS SGAIQVVVAS
1660 1670 1680 1690 1700
RSLCWGMNVA AHLVIIMDTQ YYNGKIHAYV DYPIYDVLQM VGHANRPLQD
1710 1720 1730 1740 1750
DEGRCVIMCQ GSKKDFFKKF LYEPLPVESH LDHCMHDHFN AEIVTKTIEN
1760 1770 1780 1790 1800
KQDAVDYLTW TFLYRRMTQN PNYYNLQGIS HRHLSDHLSE LVEQTLSDLE
1810 1820 1830 1840 1850
QSKCISIEDE MDVAPLNLGM IAAYYYINYT TIELFSMSLN AKTKVRGLIE
1860 1870 1880 1890 1900
IISNAAEYEN IPIRHHEDNL LRQLAQKVPH KLNNPKFNDP HVKTNLLLQA
1910 1920 1930 1940 1950
HLSRMQLSAE LQSDTEEILS KAIRLIQACV DVLSSNGWLS PALAAMELAQ
1960 1970 1980 1990 2000
MVTQAMWSKD SYLKQLPHFT SEHIKRCTDK GVESVFDIME MEDEERNALL
2010 2020 2030 2040 2050
QLTDSQIADV ARFCNRYPNI ELSYEVVDKD SIRSGGPVVV LVQLEREEEV
2060 2070 2080 2090 2100
TGPVIAPLFP QKREEGWWVV IGDAKSNSLI SIKRLTLQQK AKVKLDFVAP
2110 2120 2130
ATGGHNYTLY FMSDAYMGCD QEYKFSVDVK EAETDSDSD
Length:2,139
Mass (Da):244,875
Last modified:May 3, 2011 - v1
Checksum:iC85E398D8032F98B
GO

Sequence databases

UniGeneiRn.76239.

Cross-referencesi

Sequence databases

UniGeneiRn.76239.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000048598.

PTM databases

iPTMnetiF1LNJ2.

Proteomic databases

PaxDbiF1LNJ2.
PRIDEiF1LNJ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi1561120. Snrnp200.

Phylogenomic databases

eggNOGiKOG0952. Eukaryota.
COG1204. LUCA.
InParanoidiF1LNJ2.
TreeFamiTF300056.

Miscellaneous databases

PROiF1LNJ2.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
3.40.50.300. 4 hits.
InterProiIPR000008. C2_dom.
IPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014756. Ig_E-set.
IPR027417. P-loop_NTPase.
IPR004179. Sec63-dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00270. DEAD. 2 hits.
PF00271. Helicase_C. 1 hit.
PF02889. Sec63. 2 hits.
[Graphical view]
SMARTiSM00487. DEXDc. 2 hits.
SM00490. HELICc. 2 hits.
SM00973. Sec63. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 2 hits.
SSF52540. SSF52540. 4 hits.
SSF81296. SSF81296. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 2 hits.
PS51194. HELICASE_CTER. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-709, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiU520_RAT
AccessioniPrimary (citable) accession number: F1LNJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2013
Last sequence update: May 3, 2011
Last modified: July 6, 2016
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.