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Entry version 180 (08 May 2019)
Sequence version 1 (01 Feb 1994)
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Protein

Pre-mRNA-splicing factor 8

Gene

PRP8

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for association of BRR2 with the spliceosomal U5 snRNP, and the subsequent assembly of the U4/U6-U5 tri-snRNP complex. Functions as scaffold that positions spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so that splicing can occur. Interacts with both the 5' and the 3' splice site, as well as the branch region. Has a role in branch site-3' splice site selection. Associates with the branch site-3' splice 3'-exon region. Also has a role in cell cycle.8 Publications

Miscellaneous

Present with 468 molecules/cell in log phase SD medium.1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionRibonucleoprotein, RNA-binding
Biological processmRNA processing, mRNA splicing

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
YEAST:G3O-31199-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.1.13.2 984

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Pre-mRNA-splicing factor 8
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PRP8
Synonyms:DBF3, DNA39, RNA8, SLT21, USA2
Ordered Locus Names:YHR165C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome VIII

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
FungiDB:YHR165C

Saccharomyces Genome Database

More...
SGDi
S000001208 PRP8

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus, Spliceosome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1658H → S: No effect on viability. 1 Publication1
Mutagenesisi1684E → Q: No effect on viability. 1 Publication1
Mutagenesisi1687H → S: No effect on viability. 1 Publication1
Mutagenesisi1700D → N: No effect on viability. 1 Publication1
Mutagenesisi1735D → N: No effect on viability. 1 Publication1
Mutagenesisi1853D → A: Alters protein folding. Severely impaired growth. Strongly reduced growth at 35 degrees Celsius; when associated with A-1854. 3 Publications1
Mutagenesisi1853D → N: Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. 3 Publications1
Mutagenesisi1854D → A: Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. Strongly reduced growth at 35 degrees Celsius; when associated with A-1853. 2 Publications1
Mutagenesisi1854D → N: Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. 2 Publications1
Mutagenesisi1855T → A: Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. 1 Publication1
Mutagenesisi1936T → A: Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. 1 Publication1
Mutagenesisi1937R → K: Severely impaired growth. Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000970421 – 2413Pre-mRNA-splicing factor 8Add BLAST2413

Proteomic databases

MaxQB - The MaxQuant DataBase

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MaxQBi
P33334

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P33334

PRoteomics IDEntifications database

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PRIDEi
P33334

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P33334

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P33334

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1. Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with PRP40 and SNP1. Interacts (via SCwid domain) with CWC21. Interacts (via SCwid domain) with SNU114 (via N-terminus). Interacts (via RNase H homology domain and MPN domain) with BRR2; this modulates BRR2 ATPase and helicase activity. Interacts (via RNase H homology domain) with AAR2. AAR2 and BRR2 compete for PRP8 binding, and during U5 snRNP maturation BRR2 displaces the initially bound AAR2. Is associated with snRNP U5, together with SNU114 and BRR2.10 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
36599, 238 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1651 PRP19-associated complex
CPX-25 U4/U6.U5 tri-snRNP complex
CPX-29 U5 snRNP
CPX-30 Aar2-U5 snRNP

Database of interacting proteins

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DIPi
DIP-2427N

Protein interaction database and analysis system

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IntActi
P33334, 67 interactors

Molecular INTeraction database

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MINTi
P33334

STRING: functional protein association networks

More...
STRINGi
4932.YHR165C

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

12413
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OG4X-ray2.00A2147-2397[»]
3E66X-ray2.05A/B1822-2095[»]
3E9OX-ray2.00A1836-2087[»]
3E9PX-ray2.10A/B1833-2087[»]
3JCMelectron microscopy3.80A1-2413[»]
3SBGX-ray3.28A1836-2397[»]
3SBTX-ray1.80A1836-2092[»]
3ZEFX-ray3.10B/E885-2413[»]
4BGDX-ray3.10C2148-2395[»]
4I43X-ray2.00B885-2413[»]
4ILGX-ray2.10B1836-2090[»]
C2147-2413[»]
4ILHX-ray1.85A1836-2090[»]
4ILJX-ray2.00A/B1836-2090[»]
5DCAX-ray2.80J2148-2398[»]
5GAMelectron microscopy3.70A1-735[»]
5GANelectron microscopy3.60A1-2413[»]
5GAOelectron microscopy3.60A2147-2413[»]
5GAPelectron microscopy3.60A1-2413[»]
5GM6electron microscopy3.50A128-2413[»]
5GMKelectron microscopy3.40A1-2413[»]
5LJ3electron microscopy3.80A1-2413[»]
5LJ5electron microscopy3.80A1-2413[»]
5LQWelectron microscopy5.80A1-2413[»]
5M52X-ray3.40C/D2147-2413[»]
5M5PX-ray4.20B/D2147-2413[»]
5MPSelectron microscopy3.85A1-2413[»]
5MQ0electron microscopy4.17A1-2413[»]
5NRLelectron microscopy7.20A1-2413[»]
5WSGelectron microscopy4.00A1-2413[»]
5Y88electron microscopy3.70A1-2413[»]
5YLZelectron microscopy3.60A1-2413[»]
5ZWMelectron microscopy3.40A1-2413[»]
5ZWOelectron microscopy3.90A1-2413[»]
6BK8electron microscopy3.30A1-2413[»]
6EXNelectron microscopy3.70A1-2413[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P33334

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P33334

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini2182 – 2311MPNPROSITE-ProRule annotationAdd BLAST130

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni253 – 543SNU114/CWC21 interacting domain (SCwid)Add BLAST291
Regioni885 – 1375Reverse transcriptase homology domainAdd BLAST491
Regioni1376 – 1649LinkerAdd BLAST274
Regioni1585 – 1598Important for branch point selectionAdd BLAST14
Regioni1653 – 1824Restriction endonuclease homology domainAdd BLAST172
Regioni1839 – 2092RNase H homology domainAdd BLAST254

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi5 – 9Poly-Pro5
Compositional biasi20 – 27Poly-Pro8
Compositional biasi50 – 56Poly-Pro7
Compositional biasi72 – 78Poly-Pro7

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The MPN (JAB/Mov34) domain has structural similarity with deubiquitinating enzymes, but lacks the residues that would bind the catalytic metal ion.
Contains a region with structural similarity to reverse transcripase, presenting the classical thumb, fingers and palm architecture, but lacks enzyme activity, since the essential metal-binding residues are not conserved.
Contains a region with structural similarity to type-2 restriction endonucleases, but the residues that would bind catalytic metal ions in endonucleases are instead involved in hydrogen bonds that stabilize a highly conserved loop.
Contains a region with structural similarity to RNase H, but lacks RNase H activity.

Phylogenomic databases

Ensembl GeneTree

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GeneTreei
ENSGT00390000015210

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000184103

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P33334

KEGG Orthology (KO)

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KOi
K12856

Identification of Orthologs from Complete Genome Data

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OMAi
QWATMWV

Family and domain databases

Conserved Domains Database

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CDDi
cd13838 RNase_H_like_Prp8_IV, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000555 JAMM/MPN+_dom
IPR037518 MPN
IPR012591 PRO8NT
IPR012592 PROCN
IPR012984 PROCT
IPR027652 PRP8
IPR021983 PRP8_domainIV
IPR019581 Prp8_U5-snRNA-bd
IPR019580 Prp8_U6-snRNA-bd
IPR012337 RNaseH-like_sf
IPR019582 RRM_spliceosomal_PrP8

The PANTHER Classification System

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PANTHERi
PTHR11140 PTHR11140, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF08082 PRO8NT, 1 hit
PF08083 PROCN, 1 hit
PF08084 PROCT, 1 hit
PF12134 PRP8_domainIV, 1 hit
PF10598 RRM_4, 1 hit
PF10597 U5_2-snRNA_bdg, 1 hit
PF10596 U6-snRNA_bdg, 1 hit

ProDom; a protein domain database

More...
ProDomi
View protein in ProDom or Entries sharing at least one domain
PD149576 Pre-mRNA-splicing_factor-8, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00232 JAB_MPN, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF53098 SSF53098, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50249 MPN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P33334-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGLPPPPPG FEEDSDLALP PPPPPPPGYE IEELDNPMVP SSVNEDTFLP
60 70 80 90 100
PPPPPPSNFE INAEEIVDFT LPPPPPPPGL DELETKAEKK VELHGKRKLD
110 120 130 140 150
IGKDTFVTRK SRKRAKKMTK KAKRSNLYTP KAEMPPEHLR KIINTHSDMA
160 170 180 190 200
SKMYNTDKKA FLGALKYLPH AILKLLENMP HPWEQAKEVK VLYHTSGAIT
210 220 230 240 250
FVNETPRVIE PVYTAQWSAT WIAMRREKRD RTHFKRMRFP PFDDDEPPLS
260 270 280 290 300
YEQHIENIEP LDPINLPLDS QDDEYVKDWL YDSRPLEEDS KKVNGTSYKK
310 320 330 340 350
WSFDLPEMSN LYRLSTPLRD EVTDKNYYYL FDKKSFFNGK ALNNAIPGGP
360 370 380 390 400
KFEPLYPREE EEDYNEFNSI DRVIFRVPIR SEYKVAFPHL YNSRPRSVRI
410 420 430 440 450
PWYNNPVSCI IQNDEEYDTP ALFFDPSLNP IPHFIDNNSS LNVSNTKENG
460 470 480 490 500
DFTLPEDFAP LLAEEEELIL PNTKDAMSLY HSPFPFNRTK GKMVRAQDVA
510 520 530 540 550
LAKKWFLQHP DEEYPVKVKV SYQKLLKNYV LNELHPTLPT NHNKTKLLKS
560 570 580 590 600
LKNTKYFQQT TIDWVEAGLQ LCRQGHNMLN LLIHRKGLTY LHLDYNFNLK
610 620 630 640 650
PTKTLTTKER KKSRLGNSFH LMRELLKMMK LIVDTHVQFR LGNVDAFQLA
660 670 680 690 700
DGIHYILNHI GQLTGIYRYK YKVMHQIRAC KDLKHIIYYK FNKNLGKGPG
710 720 730 740 750
CGFWQPAWRV WLNFLRGTIP LLERYIGNLI TRQFEGRSNE IVKTTTKQRL
760 770 780 790 800
DAYYDLELRN SVMDDILEMM PESIRQKKAR TILQHLSEAW RCWKANIPWD
810 820 830 840 850
VPGMPAPIKK IIERYIKSKA DAWVSAAHYN RERIKRGAHV EKTMVKKNLG
860 870 880 890 900
RLTRLWIKNE QERQRQIQKN GPEITPEEAT TIFSVMVEWL ESRSFSPIPF
910 920 930 940 950
PPLTYKNDTK ILVLALEDLK DVYASKVRLN ASEREELALI EEAYDNPHDT
960 970 980 990 1000
LNRIKKYLLT QRVFKPVDIT MMENYQNISP VYSVDPLEKI TDAYLDQYLW
1010 1020 1030 1040 1050
YEADQRKLFP NWIKPSDSEI PPLLVYKWTQ GINNLSEIWD VSRGQSAVLL
1060 1070 1080 1090 1100
ETTLGEMAEK IDFTLLNRLL RLIVDPNIAD YITAKNNVVI NFKDMSHVNK
1110 1120 1130 1140 1150
YGLIRGLKFA SFIFQYYGLV IDLLLLGQER ATDLAGPANN PNEFMQFKSK
1160 1170 1180 1190 1200
EVEKAHPIRL YTRYLDRIYM LFHFEEDEGE ELTDEYLAEN PDPNFENSIG
1210 1220 1230 1240 1250
YNNRKCWPKD SRMRLIRQDV NLGRAVFWEI QSRVPTSLTS IKWENAFVSV
1260 1270 1280 1290 1300
YSKNNPNLLF SMCGFEVRIL PRQRMEEVVS NDEGVWDLVD ERTKQRTAKA
1310 1320 1330 1340 1350
YLKVSEEEIK KFDSRIRGIL MASGSTTFTK VAAKWNTSLI SLFTYFREAI
1360 1370 1380 1390 1400
VATEPLLDIL VKGETRIQNR VKLGLNSKMP TRFPPAVFYT PKELGGLGMI
1410 1420 1430 1440 1450
SASHILIPAS DLSWSKQTDT GITHFRAGMT HEDEKLIPTI FRYITTWENE
1460 1470 1480 1490 1500
FLDSQRVWAE YATKRQEAIQ QNRRLAFEEL EGSWDRGIPR ISTLFQRDRH
1510 1520 1530 1540 1550
TLAYDRGHRI RREFKQYSLE RNSPFWWTNS HHDGKLWNLN AYRTDVIQAL
1560 1570 1580 1590 1600
GGIETILEHT LFKGTGFNSW EGLFWEKASG FEDSMQFKKL THAQRTGLSQ
1610 1620 1630 1640 1650
IPNRRFTLWW SPTINRANVY VGFLVQLDLT GIFLHGKIPT LKISLIQIFR
1660 1670 1680 1690 1700
AHLWQKIHES IVFDICQILD GELDVLQIES VTKETVHPRK SYKMNSSAAD
1710 1720 1730 1740 1750
ITMESVHEWE VSKPSLLHET NDSFKGLITN KMWFDVQLRY GDYDSHDISR
1760 1770 1780 1790 1800
YVRAKFLDYT TDNVSMYPSP TGVMIGIDLA YNMYDAYGNW FNGLKPLIQN
1810 1820 1830 1840 1850
SMRTIMKANP ALYVLRERIR KGLQIYQSSV QEPFLNSSNY AELFNNDIKL
1860 1870 1880 1890 1900
FVDDTNVYRV TVHKTFEGNV ATKAINGCIF TLNPKTGHLF LKIIHTSVWA
1910 1920 1930 1940 1950
GQKRLSQLAK WKTAEEVSAL VRSLPKEEQP KQIIVTRKAM LDPLEVHMLD
1960 1970 1980 1990 2000
FPNIAIRPTE LRLPFSAAMS IDKLSDVVMK ATEPQMVLFN IYDDWLDRIS
2010 2020 2030 2040 2050
SYTAFSRLTL LLRALKTNEE SAKMILLSDP TITIKSYHLW PSFTDEQWIT
2060 2070 2080 2090 2100
IESQMRDLIL TEYGRKYNVN ISALTQTEIK DIILGQNIKA PSVKRQKMAE
2110 2120 2130 2140 2150
LEAARSEKQN DEEAAGASTV MKTKTINAQG EEIVVVASAD YESQTFSSKN
2160 2170 2180 2190 2200
EWRKSAIANT LLYLRLKNIY VSADDFVEEQ NVYVLPKNLL KKFIEISDVK
2210 2220 2230 2240 2250
IQVAAFIYGM SAKDHPKVKE IKTVVLVPQL GHVGSVQISN IPDIGDLPDT
2260 2270 2280 2290 2300
EGLELLGWIH TQTEELKFMA ASEVATHSKL FADKKRDCID ISIFSTPGSV
2310 2320 2330 2340 2350
SLSAYNLTDE GYQWGEENKD IMNVLSEGFE PTFSTHAQLL LSDRITGNFI
2360 2370 2380 2390 2400
IPSGNVWNYT FMGTAFNQEG DYNFKYGIPL EFYNEMHRPV HFLQFSELAG
2410
DEELEAEQID VFS
Length:2,413
Mass (Da):279,504
Last modified:February 1, 1994 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8F4F6F89D34D3508
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti388 – 420PHLYN…EYDTP → LIYIIPGPVQCAYHGIIIQC RVLSRTMRSTTRL in AAA67044 (PubMed:7838707).CuratedAdd BLAST33
Sequence conflicti1132T → S in AAA67044 (PubMed:7838707).Curated1
Sequence conflicti1575W → C in AAA67044 (PubMed:7838707).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z24732 Genomic DNA Translation: CAA80854.1
L29421 Genomic DNA Translation: AAA67044.1
U00027 Genomic DNA Translation: AAB68011.1
BK006934 Genomic DNA Translation: DAA06858.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S34670

NCBI Reference Sequences

More...
RefSeqi
NP_012035.1, NM_001179296.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YHR165C_mRNA; YHR165C_mRNA; YHR165C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
856570

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YHR165C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z24732 Genomic DNA Translation: CAA80854.1
L29421 Genomic DNA Translation: AAA67044.1
U00027 Genomic DNA Translation: AAB68011.1
BK006934 Genomic DNA Translation: DAA06858.1
PIRiS34670
RefSeqiNP_012035.1, NM_001179296.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OG4X-ray2.00A2147-2397[»]
3E66X-ray2.05A/B1822-2095[»]
3E9OX-ray2.00A1836-2087[»]
3E9PX-ray2.10A/B1833-2087[»]
3JCMelectron microscopy3.80A1-2413[»]
3SBGX-ray3.28A1836-2397[»]
3SBTX-ray1.80A1836-2092[»]
3ZEFX-ray3.10B/E885-2413[»]
4BGDX-ray3.10C2148-2395[»]
4I43X-ray2.00B885-2413[»]
4ILGX-ray2.10B1836-2090[»]
C2147-2413[»]
4ILHX-ray1.85A1836-2090[»]
4ILJX-ray2.00A/B1836-2090[»]
5DCAX-ray2.80J2148-2398[»]
5GAMelectron microscopy3.70A1-735[»]
5GANelectron microscopy3.60A1-2413[»]
5GAOelectron microscopy3.60A2147-2413[»]
5GAPelectron microscopy3.60A1-2413[»]
5GM6electron microscopy3.50A128-2413[»]
5GMKelectron microscopy3.40A1-2413[»]
5LJ3electron microscopy3.80A1-2413[»]
5LJ5electron microscopy3.80A1-2413[»]
5LQWelectron microscopy5.80A1-2413[»]
5M52X-ray3.40C/D2147-2413[»]
5M5PX-ray4.20B/D2147-2413[»]
5MPSelectron microscopy3.85A1-2413[»]
5MQ0electron microscopy4.17A1-2413[»]
5NRLelectron microscopy7.20A1-2413[»]
5WSGelectron microscopy4.00A1-2413[»]
5Y88electron microscopy3.70A1-2413[»]
5YLZelectron microscopy3.60A1-2413[»]
5ZWMelectron microscopy3.40A1-2413[»]
5ZWOelectron microscopy3.90A1-2413[»]
6BK8electron microscopy3.30A1-2413[»]
6EXNelectron microscopy3.70A1-2413[»]
SMRiP33334
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36599, 238 interactors
ComplexPortaliCPX-1651 PRP19-associated complex
CPX-25 U4/U6.U5 tri-snRNP complex
CPX-29 U5 snRNP
CPX-30 Aar2-U5 snRNP
DIPiDIP-2427N
IntActiP33334, 67 interactors
MINTiP33334
STRINGi4932.YHR165C

PTM databases

CarbonylDBiP33334
iPTMnetiP33334

Proteomic databases

MaxQBiP33334
PaxDbiP33334
PRIDEiP33334

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR165C_mRNA; YHR165C_mRNA; YHR165C
GeneIDi856570
KEGGisce:YHR165C

Organism-specific databases

EuPathDBiFungiDB:YHR165C
SGDiS000001208 PRP8

Phylogenomic databases

GeneTreeiENSGT00390000015210
HOGENOMiHOG000184103
InParanoidiP33334
KOiK12856
OMAiQWATMWV

Enzyme and pathway databases

BioCyciYEAST:G3O-31199-MONOMER
BRENDAi3.1.13.2 984

Miscellaneous databases

EvolutionaryTraceiP33334

Protein Ontology

More...
PROi
PR:P33334

Family and domain databases

CDDicd13838 RNase_H_like_Prp8_IV, 1 hit
InterProiView protein in InterPro
IPR000555 JAMM/MPN+_dom
IPR037518 MPN
IPR012591 PRO8NT
IPR012592 PROCN
IPR012984 PROCT
IPR027652 PRP8
IPR021983 PRP8_domainIV
IPR019581 Prp8_U5-snRNA-bd
IPR019580 Prp8_U6-snRNA-bd
IPR012337 RNaseH-like_sf
IPR019582 RRM_spliceosomal_PrP8
PANTHERiPTHR11140 PTHR11140, 1 hit
PfamiView protein in Pfam
PF08082 PRO8NT, 1 hit
PF08083 PROCN, 1 hit
PF08084 PROCT, 1 hit
PF12134 PRP8_domainIV, 1 hit
PF10598 RRM_4, 1 hit
PF10597 U5_2-snRNA_bdg, 1 hit
PF10596 U6-snRNA_bdg, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD149576 Pre-mRNA-splicing_factor-8, 1 hit
SMARTiView protein in SMART
SM00232 JAB_MPN, 1 hit
SUPFAMiSSF53098 SSF53098, 2 hits
PROSITEiView protein in PROSITE
PS50249 MPN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPRP8_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P33334
Secondary accession number(s): D3DLB4
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: May 8, 2019
This is version 180 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names
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