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O75643 (U520_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
U5 small nuclear ribonucleoprotein 200 kDa helicase

EC=3.6.4.13
Alternative name(s):
Activating signal cointegrator 1 complex subunit 3-like 1
BRR2 homolog
U5 snRNP-specific 200 kDa protein
Short name=U5-200KD
Gene names
Name:SNRNP200
Synonyms:ASCC3L1, HELIC2, KIAA0788
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2136 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5 Ref.7 Ref.22

Catalytic activity

ATP + H2O = ADP + phosphate. Ref.22

Subunit structure

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, NHP2L1, EFTUD2, SART1 and USP39. Identified in the spliceosome C complex. Ref.1 Ref.5 Ref.8

Subcellular location

Nucleus Ref.7.

Tissue specificity

Widely expressed. Ref.24

Domain

Contains two helicase domains. The N-terminal helicase domain has catalytic activity by itself, contrary to the C-terminal helicase domain that may have a regulatory role and enhance the activity of the first helicase domain. Ref.22

Involvement in disease

Retinitis pigmentosa 33 (RP33) [MIM:610359]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.22 Ref.24 Ref.25 Ref.26

Sequence similarities

Belongs to the helicase family. SKI2 subfamily.

Contains 2 helicase ATP-binding domains.

Contains 2 helicase C-terminal domains.

Contains 2 SEC63 domains.

Sequence caution

The sequence BAB14906.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
Spliceosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Retinitis pigmentosa
   DomainCoiled coil
Repeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.22Ref.7. Source: GOC

RNA splicing

Traceable author statement. Source: Reactome

cis assembly of pre-catalytic spliceosome

Inferred by curator Ref.7. Source: HGNC

gene expression

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Inferred from direct assay Ref.5. Source: UniProtKB

osteoblast differentiation

Inferred from direct assay PubMed 16210410. Source: UniProt

   Cellular_componentU5 snRNP

Inferred from direct assay Ref.7. Source: HGNC

catalytic step 2 spliceosome

Inferred from direct assay Ref.8. Source: UniProtKB

membrane

Inferred from direct assay PubMed 16210410. Source: UniProt

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 22720776. Source: UniProt

spliceosomal complex

Inferred from direct assay Ref.5. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent RNA helicase activity

Inferred from direct assay Ref.22. Source: UniProtKB

ATP-dependent helicase activity

Inferred from direct assay Ref.7. Source: HGNC

identical protein binding

Inferred from physical interaction PubMed 22365833. Source: IntAct

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 18951082. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-1045395,EBI-1045395
RNF113AO155412EBI-1045395,EBI-2130294

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75643-1)

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.
Isoform 2 (identifier: O75643-2)

The sequence of this isoform differs from the canonical sequence as follows:
     561-2071: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21362136U5 small nuclear ribonucleoprotein 200 kDa helicase
PRO_0000102087

Regions

Domain490 – 673184Helicase ATP-binding 1
Domain684 – 921238Helicase C-terminal 1
Domain981 – 1286306SEC63 1
Domain1337 – 1512176Helicase ATP-binding 2
Domain1545 – 1753209Helicase C-terminal 2
Domain1812 – 2124313SEC63 2
Nucleotide binding503 – 5108ATP
Nucleotide binding1350 – 13578ATP
Coiled coil54 – 8431 Potential
Motif615 – 6184DEIH box
Motif1454 – 14574DEVH box

Amino acid modifications

Modified residue261Phosphoserine Ref.13 Ref.18
Modified residue2251Phosphoserine Ref.10 Ref.11 Ref.12 Ref.14 Ref.18 Ref.20
Modified residue7091Phosphotyrosine By similarity
Modified residue9711N6-acetyllysine; alternate Ref.17
Modified residue17651Phosphothreonine By similarity
Modified residue21311Phosphothreonine Ref.13 Ref.16
Modified residue21331Phosphoserine Ref.13 Ref.16
Modified residue21351Phosphoserine Ref.13 Ref.16
Cross-link944Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.9
Cross-link971Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.9
Cross-link1071Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.9
Cross-link1199Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.9
Cross-link2091Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.9

Natural variations

Alternative sequence561 – 20711511Missing in isoform 2.
VSP_026622
Natural variant6811R → C in RP33. Ref.26
VAR_065587
Natural variant6811R → H in RP33. Ref.26
VAR_065588
Natural variant6831V → L in RP33; unknown pathological significance. Ref.26
VAR_065589
Natural variant6891Y → C in RP33. Ref.26
VAR_065590
Natural variant10871S → L in RP33; strongly reduced RNA helicase activity. Ref.1 Ref.22 Ref.24 Ref.26
VAR_063539
Natural variant10901R → L in RP33. Ref.25
VAR_063540
Natural variant17361F → L in a colorectal cancer sample; somatic mutation. Ref.23
VAR_035943

Experimental info

Mutagenesis6031R → A: Strongly decreased ATP-dependent RNA helicase activity. Ref.22
Mutagenesis6371R → A: Strongly decreased ATP-dependent RNA helicase activity. Ref.22
Mutagenesis15441K → A: Decreased ATP-dependent RNA helicase activity. Ref.22
Mutagenesis15481H → A: Strongly decreased ATP-dependent RNA helicase activity. Ref.22
Mutagenesis15781T → A: Decreased ATP-dependent RNA helicase activity. Ref.22
Sequence conflict5881C → F in AAH65924. Ref.6
Sequence conflict6131I → V in CAA94089. Ref.5
Sequence conflict8021A → G in CAA94089. Ref.5
Sequence conflict8401R → H in BAB14906. Ref.2
Sequence conflict13221Q → R in BAB14906. Ref.2
Sequence conflict13711S → N in CAA94089. Ref.5
Sequence conflict1383 – 13864EALA → RLWQ in CAA94089. Ref.5
Sequence conflict14761Y → N in BAB14906. Ref.2
Sequence conflict15471Y → F in CAA94089. Ref.5
Sequence conflict16671Q → L in CAA94089. Ref.5
Sequence conflict19561K → E in CAA94089. Ref.5
Sequence conflict1961 – 19622KQ → RR in CAA94089. Ref.5
Sequence conflict1965 – 19717HFTSEHI → PFPSGLF in CAA94089. Ref.5
Sequence conflict20311S → R in BAB14906. Ref.2
Sequence conflict20651W → L in AAH65924. Ref.6
Sequence conflict2101 – 21044AHNY → GRHN in CAA94089. Ref.5

Secondary structure

................................................................................................................................................................................................................................................................................................................... 2136
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 7, 2004. Version 2.
Checksum: 3F3811BDCCC9DDB7

FASTA2,136244,508
        10         20         30         40         50         60 
MADVTARSLQ YEYKANSNLV LQADRSLIDR TRRDEPTGEV LSLVGKLEGT RMGDKAQRTK 

        70         80         90        100        110        120 
PQMQEERRAK RRKRDEDRHD INKMKGYTLL SEGIDEMVGI IYKPKTKETR ETYEVLLSFI 

       130        140        150        160        170        180 
QAALGDQPRD ILCGAADEVL AVLKNEKLRD KERRKEIDLL LGQTDDTRYH VLVNLGKKIT 

       190        200        210        220        230        240 
DYGGDKEIQN MDDNIDETYG VNVQFESDEE EGDEDVYGEV REEASDDDME GDEAVVRCTL 

       250        260        270        280        290        300 
SANLVASGEL MSSKKKDLHP RDIDAFWLQR QLSRFYDDAI VSQKKADEVL EILKTASDDR 

       310        320        330        340        350        360 
ECENQLVLLL GFNTFDFIKV LRQHRMMILY CTLLASAQSE AEKERIMGKM EADPELSKFL 

       370        380        390        400        410        420 
YQLHETEKED LIREERSRRE RVRQSRMDTD LETMDLDQGG EALAPRQVLD LEDLVFTQGS 

       430        440        450        460        470        480 
HFMANKRCQL PDGSFRRQRK GYEEVHVPAL KPKPFGSEEQ LLPVEKLPKY AQAGFEGFKT 

       490        500        510        520        530        540 
LNRIQSKLYR AALETDENLL LCAPTGAGKT NVALMCMLRE IGKHINMDGT INVDDFKIIY 

       550        560        570        580        590        600 
IAPMRSLVQE MVGSFGKRLA TYGITVAELT GDHQLCKEEI SATQIIVCTP EKWDIITRKG 

       610        620        630        640        650        660 
GERTYTQLVR LIILDEIHLL HDDRGPVLEA LVARAIRNIE MTQEDVRLIG LSATLPNYED 

       670        680        690        700        710        720 
VATFLRVDPA KGLFYFDNSF RPVPLEQTYV GITEKKAIKR FQIMNEIVYE KIMEHAGKNQ 

       730        740        750        760        770        780 
VLVFVHSRKE TGKTARAIRD MCLEKDTLGL FLREGSASTE VLRTEAEQCK NLELKDLLPY 

       790        800        810        820        830        840 
GFAIHHAGMT RVDRTLVEDL FADKHIQVLV STATLAWGVN LPAHTVIIKG TQVYSPEKGR 

       850        860        870        880        890        900 
WTELGALDIL QMLGRAGRPQ YDTKGEGILI TSHGELQYYL SLLNQQLPIE SQMVSKLPDM 

       910        920        930        940        950        960 
LNAEIVLGNV QNAKDAVNWL GYAYLYIRML RSPTLYGISH DDLKGDPLLD QRRLDLVHTA 

       970        980        990       1000       1010       1020 
ALMLDKNNLV KYDKKTGNFQ VTELGRIASH YYITNDTVQT YNQLLKPTLS EIELFRVFSL 

      1030       1040       1050       1060       1070       1080 
SSEFKNITVR EEEKLELQKL LERVPIPVKE SIEEPSAKIN VLLQAFISQL KLEGFALMAD 

      1090       1100       1110       1120       1130       1140 
MVYVTQSAGR LMRAIFEIVL NRGWAQLTDK TLNLCKMIDK RMWQSMCPLR QFRKLPEEVV 

      1150       1160       1170       1180       1190       1200 
KKIEKKNFPF ERLYDLNHNE IGELIRMPKM GKTIHKYVHL FPKLELSVHL QPITRSTLKV 

      1210       1220       1230       1240       1250       1260 
ELTITPDFQW DEKVHGSSEA FWILVEDVDS EVILHHEYFL LKAKYAQDEH LITFFVPVFE 

      1270       1280       1290       1300       1310       1320 
PLPPQYFIRV VSDRWLSCET QLPVSFRHLI LPEKYPPPTE LLDLQPLPVS ALRNSAFESL 

      1330       1340       1350       1360       1370       1380 
YQDKFPFFNP IQTQVFNTVY NSDDNVFVGA PTGSGKTICA EFAILRMLLQ SSEGRCVYIT 

      1390       1400       1410       1420       1430       1440 
PMEALAEQVY MDWYEKFQDR LNKKVVLLTG ETSTDLKLLG KGNIIISTPE KWDILSRRWK 

      1450       1460       1470       1480       1490       1500 
QRKNVQNINL FVVDEVHLIG GENGPVLEVI CSRMRYISSQ IERPIRIVAL SSSLSNAKDV 

      1510       1520       1530       1540       1550       1560 
AHWLGCSATS TFNFHPNVRP VPLELHIQGF NISHTQTRLL SMAKPVYHAI TKHSPKKPVI 

      1570       1580       1590       1600       1610       1620 
VFVPSRKQTR LTAIDILTTC AADIQRQRFL HCTEKDLIPY LEKLSDSTLK ETLLNGVGYL 

      1630       1640       1650       1660       1670       1680 
HEGLSPMERR LVEQLFSSGA IQVVVASRSL CWGMNVAAHL VIIMDTQYYN GKIHAYVDYP 

      1690       1700       1710       1720       1730       1740 
IYDVLQMVGH ANRPLQDDEG RCVIMCQGSK KDFFKKFLYE PLPVESHLDH CMHDHFNAEI 

      1750       1760       1770       1780       1790       1800 
VTKTIENKQD AVDYLTWTFL YRRMTQNPNY YNLQGISHRH LSDHLSELVE QTLSDLEQSK 

      1810       1820       1830       1840       1850       1860 
CISIEDEMDV APLNLGMIAA YYYINYTTIE LFSMSLNAKT KVRGLIEIIS NAAEYENIPI 

      1870       1880       1890       1900       1910       1920 
RHHEDNLLRQ LAQKVPHKLN NPKFNDPHVK TNLLLQAHLS RMQLSAELQS DTEEILSKAI 

      1930       1940       1950       1960       1970       1980 
RLIQACVDVL SSNGWLSPAL AAMELAQMVT QAMWSKDSYL KQLPHFTSEH IKRCTDKGVE 

      1990       2000       2010       2020       2030       2040 
SVFDIMEMED EERNALLQLT DSQIADVARF CNRYPNIELS YEVVDKDSIR SGGPVVVLVQ 

      2050       2060       2070       2080       2090       2100 
LEREEEVTGP VIAPLFPQKR EEGWWVVIGD AKSNSLISIK RLTLQQKAKV KLDFVAPATG 

      2110       2120       2130 
AHNYTLYFMS DAYMGCDQEY KFSVDVKEAE TDSDSD 

« Hide

Isoform 2 [UniParc].

Checksum: EDC83DE90411A495
Show »

FASTA62571,472

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, VARIANT RP33 LEU-1087.
[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. expand/collapse author list , 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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 264-2136 (ISOFORM 1).
Tissue: Cerebellum and Placenta.
[3]"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 111-2136 (ISOFORM 1).
Tissue: Brain.
[4]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[5]"The HeLa 200 kDa U5 snRNP-specific protein and its homologue in Saccharomyces cerevisiae are members of the DEXH-box protein family of putative RNA helicases."
Lauber J., Fabrizio P., Teigelkamp S., Lane W.S., Hartmann E., Luehrmann R.
EMBO J. 15:4001-4015(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 436-2136, PROTEIN SEQUENCE OF 672-690; 1200-1213; 1295-1317; 1326-1338 AND 1717-1728, FUNCTION, SUBUNIT.
Tissue: Fetal brain.
[6]"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] OF 316-2136.
Tissue: Placenta and Skin.
[7]"The human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in vitro."
Laggerbauer B., Achsel T., Luehrmann R.
Proc. Natl. Acad. Sci. U.S.A. 95:4188-4192(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[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]"A proteomic study of SUMO-2 target proteins."
Vertegaal A.C.O., Ogg S.C., Jaffray E., Rodriguez M.S., Hay R.T., Andersen J.S., Mann M., Lamond A.I.
J. Biol. Chem. 279:33791-33798(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-944; LYS-971; LYS-1071; LYS-1199 AND LYS-2091.
Tissue: Cervix carcinoma.
[10]"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-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[12]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; THR-2131; SER-2133 AND SER-2135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[15]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2131; SER-2133 AND SER-2135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-971, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26 AND SER-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Crystal structure of Q9P172/SEC63 from Homo sapiens."
Northeast structural genomics consortium (NESG)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1808-2136.
[22]"Structural basis for functional cooperation between tandem helicase cassettes in Brr2-mediated remodeling of the spliceosome."
Santos K.F., Jovin S.M., Weber G., Pena V., Luhrmann R., Wahl M.C.
Proc. Natl. Acad. Sci. U.S.A. 109:17418-17423(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) OF 402-2125 IN COMPLEX WITH ATP, CATALYTIC ACTIVITY, FUNCTION, DOMAIN, CHARACTERIZATION OF VARIANT RP33 LEU-1087, MUTAGENESIS OF ARG-603; ARG-637; LYS-1544; HIS-1548 AND THR-1578.
[23]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-1736.
[24]"Autosomal-dominant retinitis pigmentosa caused by a mutation in SNRNP200, a gene required for unwinding of U4/U6 snRNAs."
Zhao C., Bellur D.L., Lu S., Zhao F., Grassi M.A., Bowne S.J., Sullivan L.S., Daiger S.P., Chen L.J., Pang C.P., Zhao K., Staley J.P., Larsson C.
Am. J. Hum. Genet. 85:617-627(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP33 LEU-1087, TISSUE SPECIFICITY.
[25]"Mutations in ASCC3L1 on 2q11.2 are associated with autosomal dominant retinitis pigmentosa in a Chinese family."
Li N., Mei H., MacDonald I.M., Jiao X., Hejtmancik J.F.
Invest. Ophthalmol. Vis. Sci. 51:1036-1043(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP33 LEU-1090.
[26]"Next generation sequencing of pooled samples reveals new SNRNP200 mutations associated with retinitis pigmentosa."
Benaglio P., McGee T.L., Capelli L.P., Harper S., Berson E.L., Rivolta C.
Hum. Mutat. 32:E2246-E2258(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RP33 CYS-681; HIS-681; LEU-683; CYS-689 AND LEU-1087.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY572488 mRNA. Translation: AAS78571.1.
AK024391 mRNA. Translation: BAB14906.1. Different initiation.
AK090671 mRNA. Translation: BAC03499.1.
AB018331 mRNA. Translation: BAA34508.2.
Z70200 Genomic DNA. Translation: CAA94089.1.
BC065924 mRNA. Translation: AAH65924.1.
BC007577 mRNA. Translation: AAH07577.1.
CCDSCCDS2020.1. [O75643-1]
RefSeqNP_054733.2. NM_014014.4. [O75643-1]
UniGeneHs.246112.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q0ZX-ray2.00X1808-2136[»]
4F91X-ray2.70B402-2125[»]
4F92X-ray2.66B402-2125[»]
4F93X-ray2.92B402-2125[»]
4KITX-ray3.60B395-2129[»]
ProteinModelPortalO75643.
SMRO75643. Positions 402-2129.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116661. 122 interactions.
IntActO75643. 37 interactions.
MINTMINT-5003904.
STRING9606.ENSP00000317123.

PTM databases

PhosphoSiteO75643.

Proteomic databases

MaxQBO75643.
PaxDbO75643.
PeptideAtlasO75643.
PRIDEO75643.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323853; ENSP00000317123; ENSG00000144028. [O75643-1]
GeneID23020.
KEGGhsa:23020.
UCSCuc002svu.3. human. [O75643-1]

Organism-specific databases

CTD23020.
GeneCardsGC02M096940.
GeneReviewsSNRNP200.
H-InvDBHIX0002273.
HGNCHGNC:30859. SNRNP200.
HPAHPA029321.
MIM601664. gene.
610359. phenotype.
neXtProtNX_O75643.
Orphanet791. Retinitis pigmentosa.
PharmGKBPA164726004.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1204.
HOVERGENHBG051896.
InParanoidO75643.
KOK12854.
OMAKKMENWW.
PhylomeDBO75643.
TreeFamTF300056.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressO75643.
BgeeO75643.
CleanExHS_SNRNP200.
GenevestigatorO75643.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
3.40.50.300. 4 hits.
InterProIPR003593. AAA+_ATPase.
IPR000008. C2_dom.
IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014756. Ig_E-set.
IPR027417. P-loop_NTPase.
IPR004179. Sec63-dom.
[Graphical view]
PfamPF00270. DEAD. 2 hits.
PF00271. Helicase_C. 2 hits.
PF02889. Sec63. 2 hits.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
SM00487. DEXDc. 2 hits.
SM00490. HELICc. 2 hits.
SM00611. SEC63. 2 hits.
SM00973. Sec63. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 4 hits.
SSF81296. SSF81296. 1 hit.
PROSITEPS51192. HELICASE_ATP_BIND_1. 2 hits.
PS51194. HELICASE_CTER. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSNRNP200. human.
EvolutionaryTraceO75643.
GeneWikiASCC3L1.
GenomeRNAi23020.
NextBio43966.
PROO75643.
SOURCESearch...

Entry information

Entry nameU520_HUMAN
AccessionPrimary (citable) accession number: O75643
Secondary accession number(s): O94884 expand/collapse secondary AC list , Q6NZY0, Q6PX59, Q8NBE6, Q96IF2, Q9H7S0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 7, 2004
Last modified: July 9, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM