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O75643

- U520_HUMAN

UniProt

O75643 - U520_HUMAN

Protein

U5 small nuclear ribonucleoprotein 200 kDa helicase

Gene

SNRNP200

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (07 Dec 2004)
      Previous versions | rss
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    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.4 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi503 – 5108ATP1 PublicationPROSITE-ProRule annotation
    Nucleotide bindingi1350 – 13578ATP1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent helicase activity Source: HGNC
    3. ATP-dependent RNA helicase activity Source: UniProtKB
    4. identical protein binding Source: IntAct
    5. poly(A) RNA binding Source: UniProtKB
    6. protein binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cis assembly of pre-catalytic spliceosome Source: HGNC
    3. gene expression Source: Reactome
    4. mRNA splicing, via spliceosome Source: UniProtKB
    5. osteoblast differentiation Source: UniProt
    6. RNA splicing Source: Reactome

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    ATP-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:
    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 namesi
    Name:SNRNP200
    Synonyms:ASCC3L1, HELIC2, KIAA0788
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:30859. SNRNP200.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. membrane Source: UniProt
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProt
    5. spliceosomal complex Source: UniProtKB
    6. U5 snRNP Source: HGNC

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Involvement in diseasei

    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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti681 – 6811R → C in RP33. 1 Publication
    VAR_065587
    Natural varianti681 – 6811R → H in RP33. 1 Publication
    VAR_065588
    Natural varianti683 – 6831V → L in RP33; unknown pathological significance. 1 Publication
    VAR_065589
    Natural varianti689 – 6891Y → C in RP33. 1 Publication
    VAR_065590
    Natural varianti1087 – 10871S → L in RP33; strongly reduced RNA helicase activity. 3 Publications
    VAR_063539
    Natural varianti1090 – 10901R → L in RP33. 1 Publication
    VAR_063540

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi603 – 6031R → A: Strongly decreased ATP-dependent RNA helicase activity. 1 Publication
    Mutagenesisi637 – 6371R → A: Strongly decreased ATP-dependent RNA helicase activity. 1 Publication
    Mutagenesisi1544 – 15441K → A: Decreased ATP-dependent RNA helicase activity. 1 Publication
    Mutagenesisi1548 – 15481H → A: Strongly decreased ATP-dependent RNA helicase activity. 1 Publication
    Mutagenesisi1578 – 15781T → A: Decreased ATP-dependent RNA helicase activity. 1 Publication

    Keywords - Diseasei

    Disease mutation, Retinitis pigmentosa

    Organism-specific databases

    MIMi610359. phenotype.
    Orphaneti791. Retinitis pigmentosa.
    PharmGKBiPA164726004.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 21362136U5 small nuclear ribonucleoprotein 200 kDa helicasePRO_0000102087Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei26 – 261Phosphoserine2 Publications
    Modified residuei225 – 2251Phosphoserine6 Publications
    Modified residuei709 – 7091PhosphotyrosineBy similarity
    Cross-linki944 – 944Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei971 – 9711N6-acetyllysine; alternate1 Publication
    Cross-linki971 – 971Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
    Cross-linki1071 – 1071Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki1199 – 1199Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei1765 – 17651PhosphothreonineBy similarity
    Cross-linki2091 – 2091Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei2131 – 21311Phosphothreonine2 Publications
    Modified residuei2133 – 21331Phosphoserine2 Publications
    Modified residuei2135 – 21351Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO75643.
    PaxDbiO75643.
    PeptideAtlasiO75643.
    PRIDEiO75643.

    PTM databases

    PhosphoSiteiO75643.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiO75643.
    BgeeiO75643.
    CleanExiHS_SNRNP200.
    GenevestigatoriO75643.

    Organism-specific databases

    HPAiHPA029321.

    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, NHP2L1, EFTUD2, SART1 and USP39. Identified in the spliceosome C complex.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-1045395,EBI-1045395
    RNF113AO155412EBI-1045395,EBI-2130294

    Protein-protein interaction databases

    BioGridi116661. 122 interactions.
    IntActiO75643. 37 interactions.
    MINTiMINT-5003904.
    STRINGi9606.ENSP00000317123.

    Structurei

    Secondary structure

    1
    2136
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi411 – 4144
    Helixi419 – 4213
    Beta strandi436 – 4383
    Beta strandi440 – 4478
    Turni464 – 4663
    Helixi469 – 4713
    Helixi483 – 4875
    Helixi489 – 4935
    Beta strandi499 – 5024
    Helixi510 – 52112
    Helixi522 – 5243
    Beta strandi537 – 5415
    Helixi545 – 55915
    Turni560 – 5634
    Beta strandi566 – 5683
    Helixi580 – 5823
    Beta strandi584 – 5885
    Helixi590 – 5967
    Helixi603 – 6064
    Beta strandi609 – 6146
    Helixi617 – 6215
    Helixi625 – 64218
    Beta strandi647 – 6526
    Helixi658 – 6647
    Helixi669 – 6724
    Beta strandi673 – 6753
    Helixi678 – 6803
    Beta strandi685 – 6884
    Helixi697 – 71216
    Beta strandi716 – 7183
    Beta strandi721 – 7244
    Turni728 – 7314
    Helixi732 – 74413
    Beta strandi752 – 7543
    Turni756 – 7583
    Helixi761 – 7644
    Helixi772 – 7776
    Turni778 – 7814
    Beta strandi782 – 7854
    Beta strandi787 – 7893
    Helixi792 – 80211
    Beta strandi808 – 8114
    Helixi813 – 8186
    Beta strandi823 – 8297
    Beta strandi832 – 8354
    Turni836 – 8394
    Beta strandi840 – 8434
    Helixi846 – 8538
    Turni859 – 8613
    Beta strandi865 – 8739
    Turni874 – 8774
    Helixi878 – 8825
    Turni883 – 8853
    Turni893 – 8964
    Helixi897 – 90610
    Helixi913 – 92210
    Helixi924 – 9318
    Turni933 – 9375
    Helixi940 – 9456
    Helixi950 – 96617
    Beta strandi969 – 9724
    Turni974 – 9763
    Beta strandi978 – 9814
    Helixi983 – 9908
    Helixi995 – 100410
    Helixi1011 – 10199
    Helixi1022 – 10243
    Helixi1031 – 10333
    Helixi1034 – 104310
    Beta strandi1044 – 10463
    Helixi1055 – 106713
    Helixi1075 – 110127
    Helixi1105 – 112016
    Beta strandi1124 – 11263
    Helixi1128 – 11314
    Helixi1137 – 11448
    Helixi1150 – 11556
    Helixi1158 – 11658
    Helixi1168 – 11703
    Helixi1171 – 11788
    Beta strandi1184 – 120623
    Turni1212 – 12143
    Beta strandi1218 – 12269
    Beta strandi1232 – 124211
    Helixi1243 – 12453
    Beta strandi1250 – 12578
    Beta strandi1264 – 127512
    Beta strandi1279 – 12857
    Helixi1309 – 13113
    Helixi1315 – 13184
    Turni1319 – 13246
    Beta strandi1326 – 13283
    Helixi1330 – 134011
    Beta strandi1346 – 13494
    Helixi1357 – 137014
    Beta strandi1376 – 13794
    Helixi1383 – 139715
    Turni1398 – 14003
    Beta strandi1405 – 14073
    Helixi1412 – 142110
    Beta strandi1423 – 14275
    Helixi1429 – 14368
    Turni1437 – 14415
    Helixi1443 – 14464
    Beta strandi1449 – 14535
    Helixi1456 – 14605
    Helixi1464 – 147916
    Beta strandi1481 – 14833
    Beta strandi1486 – 14927
    Helixi1497 – 15048
    Beta strandi1511 – 15133
    Helixi1516 – 15183
    Beta strandi1523 – 15308
    Helixi1535 – 15406
    Helixi1543 – 155311
    Beta strandi1555 – 15573
    Beta strandi1559 – 15657
    Helixi1566 – 158217
    Turni1586 – 15894
    Helixi1594 – 16018
    Helixi1607 – 16148
    Beta strandi1617 – 16204
    Helixi1626 – 163813
    Beta strandi1639 – 16413
    Beta strandi1643 – 16475
    Helixi1648 – 16503
    Beta strandi1651 – 16533
    Beta strandi1658 – 16647
    Beta strandi1666 – 16705
    Turni1671 – 16744
    Beta strandi1675 – 16784
    Helixi1681 – 16888
    Turni1694 – 16963
    Beta strandi1700 – 17078
    Helixi1708 – 17103
    Helixi1711 – 17177
    Helixi1728 – 17303
    Helixi1733 – 17419
    Helixi1748 – 17558
    Helixi1760 – 17667
    Helixi1768 – 17703
    Helixi1778 – 179821
    Beta strandi1801 – 18055
    Turni1806 – 18083
    Beta strandi1809 – 18124
    Helixi1814 – 18218
    Helixi1826 – 183510
    Helixi1842 – 18509
    Helixi1853 – 18553
    Helixi1865 – 187410
    Beta strandi1875 – 18773
    Helixi1887 – 189913
    Helixi1906 – 193227
    Helixi1936 – 195116
    Helixi1959 – 19624
    Helixi1968 – 19769
    Helixi1982 – 19876
    Helixi1990 – 19978
    Helixi2001 – 201111
    Beta strandi2017 – 20237
    Helixi2026 – 20283
    Beta strandi2033 – 204311
    Beta strandi2056 – 20583
    Beta strandi2064 – 20707
    Turni2071 – 20744
    Beta strandi2075 – 20828
    Beta strandi2085 – 209511
    Beta strandi2098 – 211215
    Beta strandi2118 – 212710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Q0ZX-ray2.00X1808-2136[»]
    4F91X-ray2.70B402-2125[»]
    4F92X-ray2.66B402-2125[»]
    4F93X-ray2.92B402-2125[»]
    4KITX-ray3.60B395-2129[»]
    ProteinModelPortaliO75643.
    SMRiO75643. Positions 402-2129.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75643.

    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
    Domaini981 – 1286306SEC63 1Add
    BLAST
    Domaini1337 – 1512176Helicase ATP-binding 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1545 – 1753209Helicase C-terminal 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1812 – 2124313SEC63 2Add
    BLAST

    Coiled coil

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

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi615 – 6184DEIH box
    Motifi1454 – 14574DEVH box

    Domaini

    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.1 Publication

    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

    eggNOGiCOG1204.
    HOVERGENiHBG051896.
    InParanoidiO75643.
    KOiK12854.
    OMAiKKMENWW.
    PhylomeDBiO75643.
    TreeFamiTF300056.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    3.40.50.300. 4 hits.
    InterProiIPR003593. 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]
    PfamiPF00270. DEAD. 2 hits.
    PF00271. Helicase_C. 2 hits.
    PF02889. Sec63. 2 hits.
    [Graphical view]
    SMARTiSM00382. AAA. 2 hits.
    SM00487. DEXDc. 2 hits.
    SM00490. HELICc. 2 hits.
    SM00611. SEC63. 2 hits.
    SM00973. Sec63. 2 hits.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 4 hits.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 2 hits.
    PS51194. HELICASE_CTER. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75643-1) [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

    MADVTARSLQ YEYKANSNLV LQADRSLIDR TRRDEPTGEV LSLVGKLEGT     50
    RMGDKAQRTK PQMQEERRAK RRKRDEDRHD INKMKGYTLL SEGIDEMVGI 100
    IYKPKTKETR ETYEVLLSFI QAALGDQPRD ILCGAADEVL AVLKNEKLRD 150
    KERRKEIDLL LGQTDDTRYH VLVNLGKKIT DYGGDKEIQN MDDNIDETYG 200
    VNVQFESDEE EGDEDVYGEV REEASDDDME GDEAVVRCTL SANLVASGEL 250
    MSSKKKDLHP RDIDAFWLQR QLSRFYDDAI VSQKKADEVL EILKTASDDR 300
    ECENQLVLLL GFNTFDFIKV LRQHRMMILY CTLLASAQSE AEKERIMGKM 350
    EADPELSKFL YQLHETEKED LIREERSRRE RVRQSRMDTD LETMDLDQGG 400
    EALAPRQVLD LEDLVFTQGS HFMANKRCQL PDGSFRRQRK GYEEVHVPAL 450
    KPKPFGSEEQ LLPVEKLPKY AQAGFEGFKT LNRIQSKLYR AALETDENLL 500
    LCAPTGAGKT NVALMCMLRE IGKHINMDGT INVDDFKIIY IAPMRSLVQE 550
    MVGSFGKRLA TYGITVAELT GDHQLCKEEI SATQIIVCTP EKWDIITRKG 600
    GERTYTQLVR LIILDEIHLL HDDRGPVLEA LVARAIRNIE MTQEDVRLIG 650
    LSATLPNYED VATFLRVDPA KGLFYFDNSF RPVPLEQTYV GITEKKAIKR 700
    FQIMNEIVYE KIMEHAGKNQ VLVFVHSRKE TGKTARAIRD MCLEKDTLGL 750
    FLREGSASTE VLRTEAEQCK NLELKDLLPY GFAIHHAGMT RVDRTLVEDL 800
    FADKHIQVLV STATLAWGVN LPAHTVIIKG TQVYSPEKGR WTELGALDIL 850
    QMLGRAGRPQ YDTKGEGILI TSHGELQYYL SLLNQQLPIE SQMVSKLPDM 900
    LNAEIVLGNV QNAKDAVNWL GYAYLYIRML RSPTLYGISH DDLKGDPLLD 950
    QRRLDLVHTA ALMLDKNNLV KYDKKTGNFQ VTELGRIASH YYITNDTVQT 1000
    YNQLLKPTLS EIELFRVFSL SSEFKNITVR EEEKLELQKL LERVPIPVKE 1050
    SIEEPSAKIN VLLQAFISQL KLEGFALMAD MVYVTQSAGR LMRAIFEIVL 1100
    NRGWAQLTDK TLNLCKMIDK RMWQSMCPLR QFRKLPEEVV KKIEKKNFPF 1150
    ERLYDLNHNE IGELIRMPKM GKTIHKYVHL FPKLELSVHL QPITRSTLKV 1200
    ELTITPDFQW DEKVHGSSEA FWILVEDVDS EVILHHEYFL LKAKYAQDEH 1250
    LITFFVPVFE PLPPQYFIRV VSDRWLSCET QLPVSFRHLI LPEKYPPPTE 1300
    LLDLQPLPVS ALRNSAFESL YQDKFPFFNP IQTQVFNTVY NSDDNVFVGA 1350
    PTGSGKTICA EFAILRMLLQ SSEGRCVYIT PMEALAEQVY MDWYEKFQDR 1400
    LNKKVVLLTG ETSTDLKLLG KGNIIISTPE KWDILSRRWK QRKNVQNINL 1450
    FVVDEVHLIG GENGPVLEVI CSRMRYISSQ IERPIRIVAL SSSLSNAKDV 1500
    AHWLGCSATS TFNFHPNVRP VPLELHIQGF NISHTQTRLL SMAKPVYHAI 1550
    TKHSPKKPVI VFVPSRKQTR LTAIDILTTC AADIQRQRFL HCTEKDLIPY 1600
    LEKLSDSTLK ETLLNGVGYL HEGLSPMERR LVEQLFSSGA IQVVVASRSL 1650
    CWGMNVAAHL VIIMDTQYYN GKIHAYVDYP IYDVLQMVGH ANRPLQDDEG 1700
    RCVIMCQGSK KDFFKKFLYE PLPVESHLDH CMHDHFNAEI VTKTIENKQD 1750
    AVDYLTWTFL YRRMTQNPNY YNLQGISHRH LSDHLSELVE QTLSDLEQSK 1800
    CISIEDEMDV APLNLGMIAA YYYINYTTIE LFSMSLNAKT KVRGLIEIIS 1850
    NAAEYENIPI RHHEDNLLRQ LAQKVPHKLN NPKFNDPHVK TNLLLQAHLS 1900
    RMQLSAELQS DTEEILSKAI RLIQACVDVL SSNGWLSPAL AAMELAQMVT 1950
    QAMWSKDSYL KQLPHFTSEH IKRCTDKGVE SVFDIMEMED EERNALLQLT 2000
    DSQIADVARF CNRYPNIELS YEVVDKDSIR SGGPVVVLVQ LEREEEVTGP 2050
    VIAPLFPQKR EEGWWVVIGD AKSNSLISIK RLTLQQKAKV KLDFVAPATG 2100
    AHNYTLYFMS DAYMGCDQEY KFSVDVKEAE TDSDSD 2136
    Length:2,136
    Mass (Da):244,508
    Last modified:December 7, 2004 - v2
    Checksum:i3F3811BDCCC9DDB7
    GO
    Isoform 2 (identifier: O75643-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         561-2071: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:625
    Mass (Da):71,472
    Checksum:iEDC83DE90411A495
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti588 – 5881C → F in AAH65924. (PubMed:15489334)Curated
    Sequence conflicti613 – 6131I → V in CAA94089. (PubMed:8670905)Curated
    Sequence conflicti802 – 8021A → G in CAA94089. (PubMed:8670905)Curated
    Sequence conflicti840 – 8401R → H in BAB14906. (PubMed:14702039)Curated
    Sequence conflicti1322 – 13221Q → R in BAB14906. (PubMed:14702039)Curated
    Sequence conflicti1371 – 13711S → N in CAA94089. (PubMed:8670905)Curated
    Sequence conflicti1383 – 13864EALA → RLWQ in CAA94089. (PubMed:8670905)Curated
    Sequence conflicti1476 – 14761Y → N in BAB14906. (PubMed:14702039)Curated
    Sequence conflicti1547 – 15471Y → F in CAA94089. (PubMed:8670905)Curated
    Sequence conflicti1667 – 16671Q → L in CAA94089. (PubMed:8670905)Curated
    Sequence conflicti1956 – 19561K → E in CAA94089. (PubMed:8670905)Curated
    Sequence conflicti1961 – 19622KQ → RR in CAA94089. (PubMed:8670905)Curated
    Sequence conflicti1965 – 19717HFTSEHI → PFPSGLF in CAA94089. (PubMed:8670905)Curated
    Sequence conflicti2031 – 20311S → R in BAB14906. (PubMed:14702039)Curated
    Sequence conflicti2065 – 20651W → L in AAH65924. (PubMed:15489334)Curated
    Sequence conflicti2101 – 21044AHNY → GRHN in CAA94089. (PubMed:8670905)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti681 – 6811R → C in RP33. 1 Publication
    VAR_065587
    Natural varianti681 – 6811R → H in RP33. 1 Publication
    VAR_065588
    Natural varianti683 – 6831V → L in RP33; unknown pathological significance. 1 Publication
    VAR_065589
    Natural varianti689 – 6891Y → C in RP33. 1 Publication
    VAR_065590
    Natural varianti1087 – 10871S → L in RP33; strongly reduced RNA helicase activity. 3 Publications
    VAR_063539
    Natural varianti1090 – 10901R → L in RP33. 1 Publication
    VAR_063540
    Natural varianti1736 – 17361F → L in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035943

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei561 – 20711511Missing in isoform 2. 1 PublicationVSP_026622Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS2020.1. [O75643-1]
    RefSeqiNP_054733.2. NM_014014.4. [O75643-1]
    UniGeneiHs.246112.

    Genome annotation databases

    EnsembliENST00000323853; ENSP00000317123; ENSG00000144028. [O75643-1]
    GeneIDi23020.
    KEGGihsa:23020.
    UCSCiuc002svu.3. human. [O75643-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS2020.1. [O75643-1 ]
    RefSeqi NP_054733.2. NM_014014.4. [O75643-1 ]
    UniGenei Hs.246112.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Q0Z X-ray 2.00 X 1808-2136 [» ]
    4F91 X-ray 2.70 B 402-2125 [» ]
    4F92 X-ray 2.66 B 402-2125 [» ]
    4F93 X-ray 2.92 B 402-2125 [» ]
    4KIT X-ray 3.60 B 395-2129 [» ]
    ProteinModelPortali O75643.
    SMRi O75643. Positions 402-2129.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116661. 122 interactions.
    IntActi O75643. 37 interactions.
    MINTi MINT-5003904.
    STRINGi 9606.ENSP00000317123.

    PTM databases

    PhosphoSitei O75643.

    Proteomic databases

    MaxQBi O75643.
    PaxDbi O75643.
    PeptideAtlasi O75643.
    PRIDEi O75643.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000323853 ; ENSP00000317123 ; ENSG00000144028 . [O75643-1 ]
    GeneIDi 23020.
    KEGGi hsa:23020.
    UCSCi uc002svu.3. human. [O75643-1 ]

    Organism-specific databases

    CTDi 23020.
    GeneCardsi GC02M096940.
    GeneReviewsi SNRNP200.
    H-InvDB HIX0002273.
    HGNCi HGNC:30859. SNRNP200.
    HPAi HPA029321.
    MIMi 601664. gene.
    610359. phenotype.
    neXtProti NX_O75643.
    Orphaneti 791. Retinitis pigmentosa.
    PharmGKBi PA164726004.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1204.
    HOVERGENi HBG051896.
    InParanoidi O75643.
    KOi K12854.
    OMAi KKMENWW.
    PhylomeDBi O75643.
    TreeFami TF300056.

    Enzyme and pathway databases

    Reactomei REACT_1753. mRNA Splicing - Minor Pathway.
    REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    ChiTaRSi SNRNP200. human.
    EvolutionaryTracei O75643.
    GeneWikii ASCC3L1.
    GenomeRNAii 23020.
    NextBioi 43966.
    PROi O75643.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75643.
    Bgeei O75643.
    CleanExi HS_SNRNP200.
    Genevestigatori O75643.

    Family and domain databases

    Gene3Di 2.60.40.150. 1 hit.
    3.40.50.300. 4 hits.
    InterProi IPR003593. 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 ]
    Pfami PF00270. DEAD. 2 hits.
    PF00271. Helicase_C. 2 hits.
    PF02889. Sec63. 2 hits.
    [Graphical view ]
    SMARTi SM00382. AAA. 2 hits.
    SM00487. DEXDc. 2 hits.
    SM00490. HELICc. 2 hits.
    SM00611. SEC63. 2 hits.
    SM00973. Sec63. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 4 hits.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 2 hits.
    PS51194. HELICASE_CTER. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. 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. 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.

    Entry informationi

    Entry nameiU520_HUMAN
    AccessioniPrimary (citable) accession number: O75643
    Secondary accession number(s): O94884
    , Q6NZY0, Q6PX59, Q8NBE6, Q96IF2, Q9H7S0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 153 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3