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Protein

U4/U6 small nuclear ribonucleoprotein Prp31

Gene

PRPF31

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

Functioni

Involved in pre-mRNA splicing. Required for the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei247 – 2471Interaction with U4 snRNA
Sitei270 – 2701Interaction with U4 snRNA

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. ribonucleoprotein complex binding Source: MGI
  3. snRNP binding Source: BHF-UCL

GO - Biological processi

  1. mRNA splicing, via spliceosome Source: BHF-UCL
  2. spliceosomal tri-snRNP complex assembly Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
U4/U6 small nuclear ribonucleoprotein Prp31
Alternative name(s):
Pre-mRNA-processing factor 31
Serologically defined breast cancer antigen NY-BR-99
U4/U6 snRNP 61 kDa protein
Short name:
Protein 61K
Short name:
hPrp31
Gene namesi
Name:PRPF31
Synonyms:PRP31
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19, UP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:15446. PRPF31.

Subcellular locationi

Nucleus speckle. NucleusCajal body
Note: Predominantly found in speckles and in Cajal bodies.

GO - Cellular componenti

  1. Cajal body Source: MGI
  2. MLL1 complex Source: UniProtKB
  3. nuclear speck Source: MGI
  4. nucleus Source: HPA
  5. U2-type spliceosomal complex Source: BHF-UCL
  6. U4/U6 x U5 tri-snRNP complex Source: InterPro
  7. U4atac snRNP Source: BHF-UCL
  8. U4 snRNP Source: BHF-UCL
  9. viral nucleocapsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Involvement in diseasei

Retinitis pigmentosa 113 Publications

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

Disease descriptionA 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.

See also OMIM:600138
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti111 – 1144Missing in RP11; high penetrance. 1 Publication
VAR_025629
Natural varianti194 – 1941A → E in RP11; mislocation of the protein in the cytoplasm and reduced interaction with PRPF6; the result may be a deficiency in splicing function in the retina. 3 Publications
VAR_025630
Natural varianti216 – 2161A → P in RP11; mislocation of the protein in the cytoplasm, but no effect on interaction with PRPF6; the result may be a deficiency in splicing function in the retina. 4 Publications
VAR_025631

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi270 – 2701H → A or K: Reduces binding to the complex formed by U4 snRNA and NHP2L1. 1 Publication
Mutagenesisi351 – 36414Missing : Abolishes nuclear localization. 1 PublicationAdd
BLAST

Keywords - Diseasei

Disease mutation, Retinitis pigmentosa

Organism-specific databases

MIMi600138. phenotype.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA33814.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499U4/U6 small nuclear ribonucleoprotein Prp31PRO_0000227799Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei379 – 3791Phosphoserine1 Publication
Modified residuei395 – 3951Phosphoserine1 Publication
Modified residuei438 – 4381N6-acetyllysineBy similarity
Modified residuei450 – 4501Phosphoserine1 Publication
Modified residuei455 – 4551Phosphothreonine4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8WWY3.
PaxDbiQ8WWY3.
PRIDEiQ8WWY3.

PTM databases

PhosphoSiteiQ8WWY3.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ8WWY3.
CleanExiHS_PRPF31.
ExpressionAtlasiQ8WWY3. baseline and differential.
GenevestigatoriQ8WWY3.

Organism-specific databases

HPAiHPA041939.
HPA061873.

Interactioni

Subunit structurei

Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, NHP2L1, EFTUD2, SART1 and USP39. Interacts with a complex formed by NHP2L1 and U4 snRNA, but not with NHP2L1 or U4 snRNA alone. Interacts with PRPF6/U5 snRNP-associated 102 kDa protein. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts (via its NLS) with CTNNBL1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PRPF6O949062EBI-1567797,EBI-536755

Protein-protein interaction databases

BioGridi117563. 97 interactions.
IntActiQ8WWY3. 20 interactions.
MINTiMINT-3047742.
STRINGi9606.ENSP00000324122.

Structurei

Secondary structure

1
499
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi89 – 11830Combined sources
Turni119 – 1213Combined sources
Helixi125 – 1284Combined sources
Helixi132 – 14211Combined sources
Helixi146 – 1483Combined sources
Helixi149 – 1513Combined sources
Helixi155 – 1573Combined sources
Helixi161 – 17212Combined sources
Helixi181 – 21535Combined sources
Helixi217 – 23519Combined sources
Helixi238 – 2425Combined sources
Helixi246 – 2494Combined sources
Turni250 – 2534Combined sources
Turni273 – 2764Combined sources
Helixi278 – 2814Combined sources
Helixi285 – 2873Combined sources
Helixi288 – 30720Combined sources
Helixi315 – 33117Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OZBX-ray2.60B/E78-333[»]
3SIUX-ray2.63B/E85-333[»]
3SIVX-ray3.30B/E/H/K85-333[»]
ProteinModelPortaliQ8WWY3.
SMRiQ8WWY3. Positions 86-332.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WWY3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini215 – 333119NopPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili85 – 120361 PublicationAdd
BLAST
Coiled coili181 – 215351 PublicationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi351 – 36414Nuclear localization signal (NLS)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi16 – 194Poly-Glu
Compositional biasi25 – 295Poly-Glu

Domaini

Interacts with the snRNP via the Nop domain.
The coiled coil domain is formed by two non-contiguous helices.

Sequence similaritiesi

Belongs to the PRP31 family.Curated
Contains 1 Nop domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG1498.
GeneTreeiENSGT00550000075069.
HOGENOMiHOG000207983.
HOVERGENiHBG082193.
InParanoidiQ8WWY3.
KOiK12844.
OMAiEYRLIVA.
PhylomeDBiQ8WWY3.
TreeFamiTF300677.

Family and domain databases

InterProiIPR002687. Nop_dom.
IPR012976. NOSIC.
IPR027105. Prp31.
IPR019175. Prp31_C.
[Graphical view]
PANTHERiPTHR13904. PTHR13904. 1 hit.
PfamiPF01798. Nop. 1 hit.
PF08060. NOSIC. 1 hit.
PF09785. Prp31_C. 1 hit.
[Graphical view]
SMARTiSM00931. NOSIC. 1 hit.
[Graphical view]
PROSITEiPS51358. NOP. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8WWY3-1) [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
MSLADELLAD LEEAAEEEEG GSYGEEEEEP AIEDVQEETQ LDLSGDSVKT
60 70 80 90 100
IAKLWDSKMF AEIMMKIEEY ISKQAKASEV MGPVEAAPEY RVIVDANNLT
110 120 130 140 150
VEIENELNII HKFIRDKYSK RFPELESLVP NALDYIRTVK ELGNSLDKCK
160 170 180 190 200
NNENLQQILT NATIMVVSVT ASTTQGQQLS EEELERLEEA CDMALELNAS
210 220 230 240 250
KHRIYEYVES RMSFIAPNLS IIIGASTAAK IMGVAGGLTN LSKMPACNIM
260 270 280 290 300
LLGAQRKTLS GFSSTSVLPH TGYIYHSDIV QSLPPDLRRK AARLVAAKCT
310 320 330 340 350
LAARVDSFHE STEGKVGYEL KDEIERKFDK WQEPPPVKQV KPLPAPLDGQ
360 370 380 390 400
RKKRGGRRYR KMKERLGLTE IRKQANRMSF GEIEEDAYQE DLGFSLGHLG
410 420 430 440 450
KSGSGRVRQT QVNEATKARI SKTLQRTLQK QSVVYGGKST IRDRSSGTAS
460 470 480 490
SVAFTPLQGL EIVNPQAAEK KVAEANQKYF SSMAEFLKVK GEKSGLMST
Length:499
Mass (Da):55,456
Last modified:March 21, 2006 - v2
Checksum:i7B50EC4C3393795C
GO
Isoform 2 (identifier: Q8WWY3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     333-364: EPPPVKQVKPLPAPLDGQRKKRGGRRYRKMKE → RRRWLRPTRSISPAWLSSSRSRARRVALCPPE
     365-499: Missing.

Note: No experimental confirmation available.

Show »
Length:364
Mass (Da):40,779
Checksum:i799839F6D6489EEB
GO
Isoform 3 (identifier: Q8WWY3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: Missing.
     359-499: Missing.

Note: No experimental confirmation available.

Show »
Length:278
Mass (Da):30,966
Checksum:i9FCE9E591AF0B586
GO
Isoform 4 (identifier: Q8WWY3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     426-499: RTLQKQSVVY...KGEKSGLMST → VWARPRWGWG...PSPHSRAWRL

Note: No experimental confirmation available.

Show »
Length:491
Mass (Da):54,909
Checksum:i78141E2A6DB6B1FB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881E → D in AAK77986 (PubMed:11867543).Curated
Sequence conflicti235 – 2351A → G in AAG48270 (PubMed:12747765).Curated
Sequence conflicti244 – 2441M → V in CAB43677 (PubMed:11230166).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti111 – 1144Missing in RP11; high penetrance. 1 Publication
VAR_025629
Natural varianti194 – 1941A → E in RP11; mislocation of the protein in the cytoplasm and reduced interaction with PRPF6; the result may be a deficiency in splicing function in the retina. 3 Publications
VAR_025630
Natural varianti216 – 2161A → P in RP11; mislocation of the protein in the cytoplasm, but no effect on interaction with PRPF6; the result may be a deficiency in splicing function in the retina. 4 Publications
VAR_025631

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8080Missing in isoform 3. 1 PublicationVSP_017581Add
BLAST
Alternative sequencei333 – 36432EPPPV…RKMKE → RRRWLRPTRSISPAWLSSSR SRARRVALCPPE in isoform 2. 1 PublicationVSP_017582Add
BLAST
Alternative sequencei359 – 499141Missing in isoform 3. 1 PublicationVSP_017583Add
BLAST
Alternative sequencei365 – 499135Missing in isoform 2. 1 PublicationVSP_017584Add
BLAST
Alternative sequencei426 – 49974RTLQK…GLMST → VWARPRWGWGPRDTRWGEPR SQPPCPPHSGPCRSRASYMA GSPPSATAPRARPPAWPSPH SRAWRL in isoform 4. 1 PublicationVSP_057390Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY040822 mRNA. Translation: AAK77986.1.
AF308303 mRNA. Translation: AAG48270.1.
AL050369 mRNA. Translation: CAB43677.1.
AK098547 mRNA. Translation: BAC05329.1.
AB593024 mRNA. Translation: BAJ83978.1.
AC012314 Genomic DNA. No translation available.
AC245052 Genomic DNA. No translation available.
BC117389 mRNA. Translation: AAI17390.1.
CCDSiCCDS12879.1. [Q8WWY3-1]
RefSeqiNP_056444.3. NM_015629.3. [Q8WWY3-1]
XP_005258786.1. XM_005258729.1.
XP_005277128.1. XM_005277071.1.
XP_005277306.1. XM_005277249.1.
XP_005278315.1. XM_005278258.1.
XP_006723200.1. XM_006723137.1. [Q8WWY3-1]
XP_006725704.1. XM_006725641.1. [Q8WWY3-1]
XP_006725830.1. XM_006725767.1. [Q8WWY3-1]
XP_006725831.1. XM_006725768.1.
XP_006725931.1. XM_006725868.1. [Q8WWY3-1]
XP_006725932.1. XM_006725869.1.
XP_006726019.1. XM_006725956.1. [Q8WWY3-1]
XP_006726020.1. XM_006725957.1.
XP_006726118.1. XM_006726055.1. [Q8WWY3-1]
XP_006726119.1. XM_006726056.1.
XP_006726216.1. XM_006726153.1. [Q8WWY3-1]
XP_006726217.1. XM_006726154.1.
XP_006726256.1. XM_006726193.1. [Q8WWY3-1]
XP_006726257.1. XM_006726194.1.
XP_006726336.1. XM_006726273.1. [Q8WWY3-1]
XP_006726372.1. XM_006726309.1. [Q8WWY3-1]
UniGeneiHs.515598.

Genome annotation databases

EnsembliENST00000321030; ENSP00000324122; ENSG00000105618. [Q8WWY3-1]
ENST00000419967; ENSP00000405166; ENSG00000105618. [Q8WWY3-4]
ENST00000610903; ENSP00000484896; ENSG00000277154. [Q8WWY3-1]
ENST00000612749; ENSP00000478804; ENSG00000276421. [Q8WWY3-4]
ENST00000613693; ENSP00000483929; ENSG00000275885. [Q8WWY3-1]
ENST00000614518; ENSP00000484151; ENSG00000274651. [Q8WWY3-4]
ENST00000615175; ENSP00000479700; ENSG00000274144. [Q8WWY3-4]
ENST00000616732; ENSP00000485017; ENSG00000276421. [Q8WWY3-1]
ENST00000618595; ENSP00000483382; ENSG00000274894. [Q8WWY3-4]
ENST00000618937; ENSP00000480434; ENSG00000274651. [Q8WWY3-1]
ENST00000619220; ENSP00000484834; ENSG00000277953. [Q8WWY3-4]
ENST00000619391; ENSP00000480636; ENSG00000275885. [Q8WWY3-4]
ENST00000619439; ENSP00000480725; ENSG00000274894. [Q8WWY3-1]
ENST00000619956; ENSP00000481201; ENSG00000275117. [Q8WWY3-1]
ENST00000620142; ENSP00000482626; ENSG00000274144. [Q8WWY3-1]
ENST00000620861; ENSP00000480726; ENSG00000277707. [Q8WWY3-1]
ENST00000621588; ENSP00000481708; ENSG00000277154. [Q8WWY3-4]
ENST00000622300; ENSP00000481654; ENSG00000277953. [Q8WWY3-1]
ENST00000622387; ENSP00000483982; ENSG00000275117. [Q8WWY3-4]
ENST00000622636; ENSP00000477787; ENSG00000277707. [Q8WWY3-4]
GeneIDi26121.
KEGGihsa:26121.
UCSCiuc002qdh.2. human. [Q8WWY3-1]
uc021vbi.1. human.

Polymorphism databases

DMDMi90101442.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY040822 mRNA. Translation: AAK77986.1.
AF308303 mRNA. Translation: AAG48270.1.
AL050369 mRNA. Translation: CAB43677.1.
AK098547 mRNA. Translation: BAC05329.1.
AB593024 mRNA. Translation: BAJ83978.1.
AC012314 Genomic DNA. No translation available.
AC245052 Genomic DNA. No translation available.
BC117389 mRNA. Translation: AAI17390.1.
CCDSiCCDS12879.1. [Q8WWY3-1]
RefSeqiNP_056444.3. NM_015629.3. [Q8WWY3-1]
XP_005258786.1. XM_005258729.1.
XP_005277128.1. XM_005277071.1.
XP_005277306.1. XM_005277249.1.
XP_005278315.1. XM_005278258.1.
XP_006723200.1. XM_006723137.1. [Q8WWY3-1]
XP_006725704.1. XM_006725641.1. [Q8WWY3-1]
XP_006725830.1. XM_006725767.1. [Q8WWY3-1]
XP_006725831.1. XM_006725768.1.
XP_006725931.1. XM_006725868.1. [Q8WWY3-1]
XP_006725932.1. XM_006725869.1.
XP_006726019.1. XM_006725956.1. [Q8WWY3-1]
XP_006726020.1. XM_006725957.1.
XP_006726118.1. XM_006726055.1. [Q8WWY3-1]
XP_006726119.1. XM_006726056.1.
XP_006726216.1. XM_006726153.1. [Q8WWY3-1]
XP_006726217.1. XM_006726154.1.
XP_006726256.1. XM_006726193.1. [Q8WWY3-1]
XP_006726257.1. XM_006726194.1.
XP_006726336.1. XM_006726273.1. [Q8WWY3-1]
XP_006726372.1. XM_006726309.1. [Q8WWY3-1]
UniGeneiHs.515598.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OZBX-ray2.60B/E78-333[»]
3SIUX-ray2.63B/E85-333[»]
3SIVX-ray3.30B/E/H/K85-333[»]
ProteinModelPortaliQ8WWY3.
SMRiQ8WWY3. Positions 86-332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117563. 97 interactions.
IntActiQ8WWY3. 20 interactions.
MINTiMINT-3047742.
STRINGi9606.ENSP00000324122.

PTM databases

PhosphoSiteiQ8WWY3.

Polymorphism databases

DMDMi90101442.

Proteomic databases

MaxQBiQ8WWY3.
PaxDbiQ8WWY3.
PRIDEiQ8WWY3.

Protocols and materials databases

DNASUi26121.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321030; ENSP00000324122; ENSG00000105618. [Q8WWY3-1]
ENST00000419967; ENSP00000405166; ENSG00000105618. [Q8WWY3-4]
ENST00000610903; ENSP00000484896; ENSG00000277154. [Q8WWY3-1]
ENST00000612749; ENSP00000478804; ENSG00000276421. [Q8WWY3-4]
ENST00000613693; ENSP00000483929; ENSG00000275885. [Q8WWY3-1]
ENST00000614518; ENSP00000484151; ENSG00000274651. [Q8WWY3-4]
ENST00000615175; ENSP00000479700; ENSG00000274144. [Q8WWY3-4]
ENST00000616732; ENSP00000485017; ENSG00000276421. [Q8WWY3-1]
ENST00000618595; ENSP00000483382; ENSG00000274894. [Q8WWY3-4]
ENST00000618937; ENSP00000480434; ENSG00000274651. [Q8WWY3-1]
ENST00000619220; ENSP00000484834; ENSG00000277953. [Q8WWY3-4]
ENST00000619391; ENSP00000480636; ENSG00000275885. [Q8WWY3-4]
ENST00000619439; ENSP00000480725; ENSG00000274894. [Q8WWY3-1]
ENST00000619956; ENSP00000481201; ENSG00000275117. [Q8WWY3-1]
ENST00000620142; ENSP00000482626; ENSG00000274144. [Q8WWY3-1]
ENST00000620861; ENSP00000480726; ENSG00000277707. [Q8WWY3-1]
ENST00000621588; ENSP00000481708; ENSG00000277154. [Q8WWY3-4]
ENST00000622300; ENSP00000481654; ENSG00000277953. [Q8WWY3-1]
ENST00000622387; ENSP00000483982; ENSG00000275117. [Q8WWY3-4]
ENST00000622636; ENSP00000477787; ENSG00000277707. [Q8WWY3-4]
GeneIDi26121.
KEGGihsa:26121.
UCSCiuc002qdh.2. human. [Q8WWY3-1]
uc021vbi.1. human.

Organism-specific databases

CTDi26121.
GeneCardsiGC19P054618.
GeneReviewsiPRPF31.
H-InvDBHIX0027609.
HIX0137464.
HGNCiHGNC:15446. PRPF31.
HPAiHPA041939.
HPA061873.
MIMi600138. phenotype.
606419. gene.
neXtProtiNX_Q8WWY3.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA33814.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1498.
GeneTreeiENSGT00550000075069.
HOGENOMiHOG000207983.
HOVERGENiHBG082193.
InParanoidiQ8WWY3.
KOiK12844.
OMAiEYRLIVA.
PhylomeDBiQ8WWY3.
TreeFamiTF300677.

Miscellaneous databases

EvolutionaryTraceiQ8WWY3.
GeneWikiiPRPF31.
GenomeRNAii26121.
NextBioi35500158.
PROiQ8WWY3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WWY3.
CleanExiHS_PRPF31.
ExpressionAtlasiQ8WWY3. baseline and differential.
GenevestigatoriQ8WWY3.

Family and domain databases

InterProiIPR002687. Nop_dom.
IPR012976. NOSIC.
IPR027105. Prp31.
IPR019175. Prp31_C.
[Graphical view]
PANTHERiPTHR13904. PTHR13904. 1 hit.
PfamiPF01798. Nop. 1 hit.
PF08060. NOSIC. 1 hit.
PF09785. Prp31_C. 1 hit.
[Graphical view]
SMARTiSM00931. NOSIC. 1 hit.
[Graphical view]
PROSITEiPS51358. NOP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

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  1. "Protein 61K, encoded by a gene (PRPF31) linked to autosomal dominant retinitis pigmentosa, is required for U4/U6.U5 tri-snRNP formation and pre-mRNA splicing."
    Makarova O.V., Makarov E.M., Liu S., Vornlocher H.-P., Luehrmann R.
    EMBO J. 21:1148-1157(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH C20ORF14.
  2. "Humoral immunity to human breast cancer: antigen definition and quantitative analysis of mRNA expression."
    Scanlan M.J., Gout I., Gordon C.M., Williamson B., Stockert E., Gure A.O., Jaeger D., Chen Y.-T., Mackay A., O'Hare M.J., Old L.J.
    Cancer Immun. 1:4-4(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Mammary gland.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney.
  4. "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).
    Tissue: Testis.
  5. "Full-length transcriptome analysis of human retina-derived cell lines ARPE-19 and Y79 using the vector-capping method."
    Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S., Usami R., Ohtoko K., Kato S.
    Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Retinoblastoma.
  6. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  8. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
    Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
    Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
  9. "The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP."
    Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.
    RNA 12:1418-1430(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450 AND THR-455, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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 SER-379 AND THR-455, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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 THR-455, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "CTNNBL1 is a novel nuclear localization sequence-binding protein that recognizes RNA-splicing factors CDC5L and Prp31."
    Ganesh K., Adam S., Taylor B., Simpson P., Rada C., Neuberger M.
    J. Biol. Chem. 286:17091-17102(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTNNBL1.
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395 AND THR-455, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP."
    Liu S., Li P., Dybkov O., Nottrott S., Hartmuth K., Luehrmann R., Carlomagno T., Wahl M.C.
    Science 316:115-120(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 78-333 IN COMPLEX WITH NHP2L1 AND STEM-LOOP RNA OF U4 SNRNA, COILED-COIL DOMAIN, INTERACTION WITH PRPF6, CHARACTERIZATION OF VARIANTS RP11 GLU-194 AND PRO-216, MUTAGENESIS OF HIS-270.
  17. "Evidence for a major retinitis pigmentosa locus on 19q13.4 (RP11) and association with a unique bimodal expressivity phenotype."
    Al-Maghtheh M., Vithana E., Tarttelin E., Jay M., Evans K., Moore T., Bhattacharya S., Inglehearn C.F.
    Am. J. Hum. Genet. 59:864-871(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RP11 PRO-216.
  18. "A human homolog of yeast pre-mRNA splicing gene, PRP31, underlies autosomal dominant retinitis pigmentosa on chromosome 19q13.4 (RP11)."
    Vithana E.N., Abu-Safieh L., Allen M.J., Carey A., Papaioannou M., Chakarova C., Al-Maghtheh M., Ebenezer N.D., Willis C., Moore A.T., Bird A.C., Hunt D.M., Bhattacharya S.S.
    Mol. Cell 8:375-381(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS RP11 GLU-194 AND RP11 PRO-216, TISSUE SPECIFICITY.
  19. "Disease mechanism for retinitis pigmentosa (RP11) caused by mutations in the splicing factor gene PRPF31."
    Deery E.C., Vithana E.N., Newbold R.J., Gallon V.A., Bhattacharya S.S., Warren M.J., Hunt D.M., Wilkie S.E.
    Hum. Mol. Genet. 11:3209-3219(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS RP11 GLU-194 AND PRO-216, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 351-ARG--GLU-364.
  20. "Novel deletion in the pre-mRNA splicing gene PRPF31 causes autosomal dominant retinitis pigmentosa in a large Chinese family."
    Wang L., Ribaudo M., Zhao K., Yu N., Chen Q., Sun Q., Wang L., Wang Q.
    Am. J. Med. Genet. A 121:235-239(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RP11 111-HIS--ILE-114 DEL.

Entry informationi

Entry nameiPRP31_HUMAN
AccessioniPrimary (citable) accession number: Q8WWY3
Secondary accession number(s): E7ESA8
, F1T0A4, Q17RB4, Q8N7F9, Q9H271, Q9Y439
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: March 4, 2015
This is version 115 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, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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

Similar proteinsi

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