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O75643

- U520_HUMAN

UniProt

O75643 - U520_HUMAN

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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

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

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
Complete GO annotation...

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
Complete GO annotation...

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.7 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti502 – 5021C → R in RP33. 1 Publication
VAR_071689
Natural varianti542 – 5421A → V in RP33. 1 Publication
VAR_071690
Natural varianti681 – 6811R → C in RP33 AND RP33. 2 Publications
VAR_065587
Natural varianti681 – 6811R → H in RP33 AND RP33. 2 Publications
VAR_065588
Natural varianti682 – 6821P → S in RP33. 1 Publication
VAR_071691
Natural varianti683 – 6831V → L in RP33; unknown pathological significance. 1 Publication
VAR_065589
Natural varianti689 – 6891Y → C in RP33. 1 Publication
VAR_065590
Natural varianti698 – 6981I → V in RP33. 1 Publication
VAR_071692
Natural varianti885 – 8851Q → E in RP33. 1 Publication
VAR_071693
Natural varianti1087 – 10871S → L in RP33 AND RP33; strongly reduced RNA helicase activity. 4 Publications
VAR_063539
Natural varianti1090 – 10901R → L in RP33. 1 Publication
VAR_063540
Natural varianti1779 – 17791R → H in RP33. 1 Publication
VAR_071694

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

BgeeiO75643.
CleanExiHS_SNRNP200.
ExpressionAtlasiO75643. baseline and differential.
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. 129 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.
GeneTreeiENSGT00640000091272.
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. DEAD/DEAH_box_helicase_dom.
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

        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
KERRKEIDLL 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 LIILDEIHLL 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 DEKVHGSSEA FWILVEDVDS EVILHHEYFL LKAKYAQDEH
1260 1270 1280 1290 1300
LITFFVPVFE PLPPQYFIRV VSDRWLSCET QLPVSFRHLI LPEKYPPPTE
1310 1320 1330 1340 1350
LLDLQPLPVS ALRNSAFESL YQDKFPFFNP IQTQVFNTVY NSDDNVFVGA
1360 1370 1380 1390 1400
PTGSGKTICA EFAILRMLLQ SSEGRCVYIT PMEALAEQVY MDWYEKFQDR
1410 1420 1430 1440 1450
LNKKVVLLTG ETSTDLKLLG KGNIIISTPE KWDILSRRWK QRKNVQNINL
1460 1470 1480 1490 1500
FVVDEVHLIG GENGPVLEVI CSRMRYISSQ IERPIRIVAL SSSLSNAKDV
1510 1520 1530 1540 1550
AHWLGCSATS TFNFHPNVRP VPLELHIQGF NISHTQTRLL SMAKPVYHAI
1560 1570 1580 1590 1600
TKHSPKKPVI VFVPSRKQTR LTAIDILTTC AADIQRQRFL HCTEKDLIPY
1610 1620 1630 1640 1650
LEKLSDSTLK ETLLNGVGYL HEGLSPMERR LVEQLFSSGA IQVVVASRSL
1660 1670 1680 1690 1700
CWGMNVAAHL VIIMDTQYYN GKIHAYVDYP IYDVLQMVGH ANRPLQDDEG
1710 1720 1730 1740 1750
RCVIMCQGSK KDFFKKFLYE PLPVESHLDH CMHDHFNAEI VTKTIENKQD
1760 1770 1780 1790 1800
AVDYLTWTFL YRRMTQNPNY YNLQGISHRH LSDHLSELVE QTLSDLEQSK
1810 1820 1830 1840 1850
CISIEDEMDV APLNLGMIAA YYYINYTTIE LFSMSLNAKT KVRGLIEIIS
1860 1870 1880 1890 1900
NAAEYENIPI RHHEDNLLRQ LAQKVPHKLN NPKFNDPHVK TNLLLQAHLS
1910 1920 1930 1940 1950
RMQLSAELQS DTEEILSKAI RLIQACVDVL SSNGWLSPAL AAMELAQMVT
1960 1970 1980 1990 2000
QAMWSKDSYL KQLPHFTSEH IKRCTDKGVE SVFDIMEMED EERNALLQLT
2010 2020 2030 2040 2050
DSQIADVARF CNRYPNIELS YEVVDKDSIR SGGPVVVLVQ LEREEEVTGP
2060 2070 2080 2090 2100
VIAPLFPQKR EEGWWVVIGD AKSNSLISIK RLTLQQKAKV KLDFVAPATG
2110 2120 2130
AHNYTLYFMS DAYMGCDQEY KFSVDVKEAE TDSDSD
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 varianti502 – 5021C → R in RP33. 1 Publication
VAR_071689
Natural varianti542 – 5421A → V in RP33. 1 Publication
VAR_071690
Natural varianti681 – 6811R → C in RP33 AND RP33. 2 Publications
VAR_065587
Natural varianti681 – 6811R → H in RP33 AND RP33. 2 Publications
VAR_065588
Natural varianti682 – 6821P → S in RP33. 1 Publication
VAR_071691
Natural varianti683 – 6831V → L in RP33; unknown pathological significance. 1 Publication
VAR_065589
Natural varianti689 – 6891Y → C in RP33. 1 Publication
VAR_065590
Natural varianti698 – 6981I → V in RP33. 1 Publication
VAR_071692
Natural varianti885 – 8851Q → E in RP33. 1 Publication
VAR_071693
Natural varianti1087 – 10871S → L in RP33 AND RP33; strongly reduced RNA helicase activity. 4 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
Natural varianti1779 – 17791R → H in RP33. 1 Publication
VAR_071694
Natural varianti1995 – 19951A → T.1 Publication
VAR_071695

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. 129 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.
GeneTreei ENSGT00640000091272.
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

Bgeei O75643.
CleanExi HS_SNRNP200.
ExpressionAtlasi O75643. baseline and differential.
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. DEAD/DEAH_box_helicase_dom.
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

« Hide 'large scale' publications
  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.
  27. "A novel missense SNRNP200 mutation associated with autosomal dominant retinitis pigmentosa in a Chinese family."
    Liu T., Jin X., Zhang X., Yuan H., Cheng J., Lee J., Zhang B., Zhang M., Wu J., Wang L., Tian G., Wang W.
    PLoS ONE 7:E45464-E45464(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RP33 GLU-885.
  28. "Contribution of SNRNP200 sequence variations to retinitis pigmentosa."
    Zhang X., Lai T.Y., Chiang S.W., Tam P.O., Liu D.T., Chan C.K., Pang C.P., Zhao C., Chen L.J.
    Eye 27:1204-1213(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS RP33 ARG-502; VAL-698 AND HIS-1779, VARIANT THR-1995.
  29. "Mutations in the small nuclear riboprotein 200 kDa gene (SNRNP200) cause 1.6% of autosomal dominant retinitis pigmentosa."
    Bowne S.J., Sullivan L.S., Avery C.E., Sasser E.M., Roorda A., Duncan J.L., Wheaton D.H., Birch D.G., Branham K.E., Heckenlively J.R., Sieving P.A., Daiger S.P.
    Mol. Vis. 19:2407-2417(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS RP33 VAL-542; CYS-681; HIS-681; SER-682 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 29, 2014
This is version 154 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

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