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Q8WWY3 (PRP31_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

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

Names and origin

Protein namesRecommended name:
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 names
Name:PRPF31
Synonyms:PRP31
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Subunit structure

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. Ref.1 Ref.7 Ref.8 Ref.13 Ref.14

Subcellular location

Nucleus speckle. NucleusCajal body. Note: Predominantly found in speckles and in Cajal bodies. Ref.1 Ref.17

Tissue specificity

Ubiquitously expressed. Ref.16

Domain

Interacts with the snRNP via the Nop domain. Ref.14

The coiled coil domain is formed by two non-contiguous helices. Ref.14

Involvement in disease

Retinitis pigmentosa 11 (RP11) [MIM:600138]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Sequence similarities

Belongs to the PRP31 family.

Contains 1 Nop domain.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRPF6O949062EBI-1567797,EBI-536755

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8WWY3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8WWY3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     333-364: EPPPVKQVKPLPAPLDGQRKKRGGRRYRKMKE → RRRWLRPTRSISPAWLSSSRSRARRVALCPPE
     365-499: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8WWY3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: Missing.
     359-499: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 499499U4/U6 small nuclear ribonucleoprotein Prp31
PRO_0000227799

Regions

Domain215 – 333119Nop
Region351 – 36414Nuclear localization signal (NLS)
Coiled coil85 – 12036 Ref.14
Coiled coil181 – 21535 Ref.14
Compositional bias16 – 194Poly-Glu
Compositional bias25 – 295Poly-Glu

Sites

Site2471Interaction with U4 snRNA
Site2701Interaction with U4 snRNA

Amino acid modifications

Modified residue3791Phosphoserine Ref.10
Modified residue4381N6-acetyllysine By similarity
Modified residue4501Phosphoserine Ref.9
Modified residue4551Phosphothreonine Ref.9 Ref.10 Ref.11

Natural variations

Alternative sequence1 – 8080Missing in isoform 3.
VSP_017581
Alternative sequence333 – 36432EPPPV…RKMKE → RRRWLRPTRSISPAWLSSSR SRARRVALCPPE in isoform 2.
VSP_017582
Alternative sequence359 – 499141Missing in isoform 3.
VSP_017583
Alternative sequence365 – 499135Missing in isoform 2.
VSP_017584
Natural variant111 – 1144Missing in RP11; high penetrance.
VAR_025629
Natural variant1941A → 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. Ref.14 Ref.16 Ref.17
VAR_025630
Natural variant2161A → 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. Ref.14 Ref.15 Ref.16 Ref.17
VAR_025631

Experimental info

Mutagenesis2701H → A or K: Reduces binding to the complex formed by U4 snRNA and NHP2L1. Ref.14
Mutagenesis351 – 36414Missing: Abolishes nuclear localization. Ref.17
Sequence conflict1881E → D in AAK77986. Ref.1
Sequence conflict2351A → G in AAG48270. Ref.2
Sequence conflict2441M → V in CAB43677. Ref.3

Secondary structure

................................. 499
Helix Strand Turn

Details...

Sequences

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

Last modified March 21, 2006. Version 2.
Checksum: 7B50EC4C3393795C

FASTA49955,456
        10         20         30         40         50         60 
MSLADELLAD LEEAAEEEEG GSYGEEEEEP AIEDVQEETQ LDLSGDSVKT IAKLWDSKMF 

        70         80         90        100        110        120 
AEIMMKIEEY ISKQAKASEV MGPVEAAPEY RVIVDANNLT VEIENELNII HKFIRDKYSK 

       130        140        150        160        170        180 
RFPELESLVP NALDYIRTVK ELGNSLDKCK NNENLQQILT NATIMVVSVT ASTTQGQQLS 

       190        200        210        220        230        240 
EEELERLEEA CDMALELNAS KHRIYEYVES RMSFIAPNLS IIIGASTAAK IMGVAGGLTN 

       250        260        270        280        290        300 
LSKMPACNIM LLGAQRKTLS GFSSTSVLPH TGYIYHSDIV QSLPPDLRRK AARLVAAKCT 

       310        320        330        340        350        360 
LAARVDSFHE STEGKVGYEL KDEIERKFDK WQEPPPVKQV KPLPAPLDGQ RKKRGGRRYR 

       370        380        390        400        410        420 
KMKERLGLTE IRKQANRMSF GEIEEDAYQE DLGFSLGHLG KSGSGRVRQT QVNEATKARI 

       430        440        450        460        470        480 
SKTLQRTLQK QSVVYGGKST IRDRSSGTAS SVAFTPLQGL EIVNPQAAEK KVAEANQKYF 

       490 
SSMAEFLKVK GEKSGLMST 

« Hide

Isoform 2 [UniParc].

Checksum: 799839F6D6489EEB
Show »

FASTA36440,779
Isoform 3 [UniParc].

Checksum: 9FCE9E591AF0B586
Show »

FASTA27830,966

References

« Hide 'large scale' references
[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]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[5]"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. expand/collapse author list , 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].
[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] (ISOFORM 1).
Tissue: Brain.
[7]"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.
[8]"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.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450 AND THR-455, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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.
[11]"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.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY040822 mRNA. Translation: AAK77986.1.
AF308303 mRNA. Translation: AAG48270.1.
AL050369 mRNA. Translation: CAB43677.1.
AK098547 mRNA. Translation: BAC05329.1.
AC012314 Genomic DNA. No translation available.
BC117389 mRNA. Translation: AAI17390.1.
CCDSCCDS12879.1. [Q8WWY3-1]
RefSeqNP_056444.3. NM_015629.3. [Q8WWY3-1]
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_006725931.1. XM_006725868.1. [Q8WWY3-1]
XP_006726019.1. XM_006725956.1. [Q8WWY3-1]
XP_006726118.1. XM_006726055.1. [Q8WWY3-1]
XP_006726216.1. XM_006726153.1. [Q8WWY3-1]
XP_006726256.1. XM_006726193.1. [Q8WWY3-1]
XP_006726336.1. XM_006726273.1. [Q8WWY3-1]
XP_006726372.1. XM_006726309.1. [Q8WWY3-1]
UniGeneHs.515598.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OZBX-ray2.60B/E78-333[»]
3SIUX-ray2.63B/E85-333[»]
3SIVX-ray3.30B/E/H/K85-333[»]
ProteinModelPortalQ8WWY3.
SMRQ8WWY3. Positions 86-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117563. 48 interactions.
IntActQ8WWY3. 20 interactions.
MINTMINT-3047742.
STRING9606.ENSP00000324122.

PTM databases

PhosphoSiteQ8WWY3.

Polymorphism databases

DMDM90101442.

Proteomic databases

MaxQBQ8WWY3.
PaxDbQ8WWY3.
PRIDEQ8WWY3.

Protocols and materials databases

DNASU26121.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000321030; ENSP00000324122; ENSG00000105618. [Q8WWY3-1]
ENST00000574214; ENSP00000459844; ENSG00000273224. [Q8WWY3-1]
ENST00000604745; ENSP00000475036; ENSG00000271442. [Q8WWY3-1]
ENST00000608045; ENSP00000476271; ENSG00000273376. [Q8WWY3-1]
ENST00000609025; ENSP00000477190; ENSG00000273462. [Q8WWY3-1]
ENST00000609058; ENSP00000477070; ENSG00000272932. [Q8WWY3-1]
ENST00000609316; ENSP00000476892; ENSG00000273060. [Q8WWY3-1]
ENST00000609384; ENSP00000477049; ENSG00000272964. [Q8WWY3-1]
ENST00000609750; ENSP00000476631; ENSG00000273469. [Q8WWY3-1]
ENST00000610056; ENSP00000476508; ENSG00000273109. [Q8WWY3-1]
GeneID26121.
KEGGhsa:26121.
UCSCuc002qdh.2. human. [Q8WWY3-1]

Organism-specific databases

CTD26121.
GeneCardsGC19P054618.
GeneReviewsPRPF31.
H-InvDBHIX0027609.
HIX0137464.
HGNCHGNC:15446. PRPF31.
HPAHPA041939.
MIM600138. phenotype.
606419. gene.
neXtProtNX_Q8WWY3.
Orphanet791. Retinitis pigmentosa.
PharmGKBPA33814.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1498.
HOGENOMHOG000207983.
HOVERGENHBG082193.
InParanoidQ8WWY3.
KOK12844.
OMARKHANRM.
PhylomeDBQ8WWY3.
TreeFamTF300677.

Gene expression databases

ArrayExpressQ8WWY3.
BgeeQ8WWY3.
CleanExHS_PRPF31.
GenevestigatorQ8WWY3.

Family and domain databases

InterProIPR002687. Nop_dom.
IPR012976. NOSIC.
IPR027105. Prp31.
IPR019175. Prp31_C.
[Graphical view]
PANTHERPTHR13904. PTHR13904. 1 hit.
PfamPF01798. Nop. 1 hit.
PF08060. NOSIC. 1 hit.
PF09785. Prp31_C. 1 hit.
[Graphical view]
SMARTSM00931. NOSIC. 1 hit.
[Graphical view]
PROSITEPS51358. NOP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8WWY3.
GeneWikiPRPF31.
GenomeRNAi26121.
NextBio48131.
PROQ8WWY3.
SOURCESearch...

Entry information

Entry namePRP31_HUMAN
AccessionPrimary (citable) accession number: Q8WWY3
Secondary accession number(s): Q17RB4 expand/collapse secondary AC list , Q8N7F9, Q9H271, Q9Y439
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: July 9, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM