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Q99383

- HRP1_YEAST

UniProt

Q99383 - HRP1_YEAST

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Protein

Nuclear polyadenylated RNA-binding protein 4

Gene

HRP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

RNA-binding protein, which is involved in the polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor CFIA complex and the cleavage and polyadenylation factor (CPF) complex. May be involved in regulation of poly(A) site selection. Is involved in nonsense-mediated mRNA decay. Seems to bind to an RNA downstream sequence element (DSE) located 3' of a nonsense codon and may mark the transcript for decay.4 Publications

GO - Molecular functioni

  1. mRNA binding Source: SGD
  2. nucleotide binding Source: InterPro
  3. RNA binding Source: SGD

GO - Biological processi

  1. mRNA cleavage Source: SGD
  2. mRNA polyadenylation Source: SGD
  3. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB-KW
  4. response to DNA damage checkpoint signaling Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA processing, Nonsense-mediated mRNA decay

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33519-MONOMER.
ReactomeiREACT_189250. AUF1 (hnRNP D0) destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear polyadenylated RNA-binding protein 4
Alternative name(s):
Cleavage factor IB
Short name:
CFIB
Gene namesi
Name:HRP1
Synonyms:NAB4, NAB5
Ordered Locus Names:YOL123W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XV

Organism-specific databases

CYGDiYOL123w.
SGDiS000005483. HRP1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. cytoplasmic stress granule Source: SGD
  3. mRNA cleavage factor complex Source: SGD
  4. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 534534Nuclear polyadenylated RNA-binding protein 4PRO_0000081658Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Phosphoserine3 Publications
Modified residuei3 – 31Phosphoserine3 Publications
Modified residuei206 – 2061Phosphoserine1 Publication
Modified residuei458 – 4581Phosphothreonine1 Publication
Modified residuei462 – 4621Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ99383.
PaxDbiQ99383.
PeptideAtlasiQ99383.

Expressioni

Gene expression databases

GenevestigatoriQ99383.

Interactioni

Subunit structurei

Interacts with NAM7.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NAB2P325053EBI-11783,EBI-11770

Protein-protein interaction databases

BioGridi34252. 61 interactions.
DIPiDIP-1371N.
IntActiQ99383. 33 interactions.
MINTiMINT-395353.

Structurei

Secondary structure

1
534
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi157 – 1593Combined sources
Beta strandi160 – 1634Combined sources
Helixi172 – 1798Combined sources
Turni180 – 1823Combined sources
Beta strandi185 – 1895Combined sources
Turni194 – 1963Combined sources
Beta strandi203 – 2097Combined sources
Helixi211 – 2188Combined sources
Beta strandi223 – 2264Combined sources
Helixi236 – 2416Combined sources
Beta strandi243 – 2508Combined sources
Helixi256 – 2649Combined sources
Beta strandi265 – 2673Combined sources
Beta strandi270 – 2734Combined sources
Beta strandi277 – 2815Combined sources
Beta strandi284 – 29310Combined sources
Helixi294 – 3029Combined sources
Beta strandi304 – 3063Combined sources
Beta strandi308 – 3114Combined sources
Beta strandi313 – 3175Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CJKNMR-A156-322[»]
2KM8NMR-C156-322[»]
ProteinModelPortaliQ99383.
SMRiQ99383. Positions 117-322.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99383.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini159 – 24183RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini243 – 32078RRM 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000118873.
HOGENOMiHOG000248803.
InParanoidiQ99383.
KOiK14411.
OMAiYQKMQEY.
OrthoDBiEOG706125.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99383-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSDEEDFND IYGDDKPTTT EEVKKEEEQN KAGSGTSQLD QLAALQALSS
60 70 80 90 100
SLNKLNNPNS NNSSSNNSNQ DTSSSKQDGT ANDKEGSNED TKNEKKQESA
110 120 130 140 150
TSANANANAS SAGPSGLPWE QLQQTMSQFQ QPSSQSPPQQ QVTQTKEERS
160 170 180 190 200
KADLSKESCK MFIGGLNWDT TEDNLREYFG KYGTVTDLKI MKDPATGRSR
210 220 230 240 250
GFGFLSFEKP SSVDEVVKTQ HILDGKVIDP KRAIPRDEQD KTGKIFVGGI
260 270 280 290 300
GPDVRPKEFE EFFSQWGTII DAQLMLDKDT GQSRGFGFVT YDSADAVDRV
310 320 330 340 350
CQNKFIDFKD RKIEIKRAEP RHMQQKSSNN GGNNGGNNMN RRGGNFGNQG
360 370 380 390 400
DFNQMYQNPM MGGYNPMMNP QAMTDYYQKM QEYYQQMQKQ TGMDYTQMYQ
410 420 430 440 450
QQMQQMAMMM PGFAMPPNAM TLNQPQQDSN ATQGSPAPSD SDNNKSNDVQ
460 470 480 490 500
TIGNTSNTDS GSPPLNLPNG PKGPSQYNDD HNSGYGYNRD RGDRDRNDRD
510 520 530
RDYNHRSGGN HRRNGRGGRG GYNRRNNGYH PYNR
Length:534
Mass (Da):59,650
Last modified:November 1, 1997 - v1
Checksum:i1B231069437B093D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35737 Genomic DNA. Translation: AAA79097.1.
U38535 Genomic DNA. Translation: AAB18142.1.
X95258 Genomic DNA. Translation: CAA64546.1.
Z74865 Genomic DNA. Translation: CAA99142.1.
BK006948 Genomic DNA. Translation: DAA10661.1.
PIRiS66820.
RefSeqiNP_014518.1. NM_001183377.1.

Genome annotation databases

EnsemblFungiiYOL123W; YOL123W; YOL123W.
GeneIDi853997.
KEGGisce:YOL123W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35737 Genomic DNA. Translation: AAA79097.1 .
U38535 Genomic DNA. Translation: AAB18142.1 .
X95258 Genomic DNA. Translation: CAA64546.1 .
Z74865 Genomic DNA. Translation: CAA99142.1 .
BK006948 Genomic DNA. Translation: DAA10661.1 .
PIRi S66820.
RefSeqi NP_014518.1. NM_001183377.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CJK NMR - A 156-322 [» ]
2KM8 NMR - C 156-322 [» ]
ProteinModelPortali Q99383.
SMRi Q99383. Positions 117-322.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34252. 61 interactions.
DIPi DIP-1371N.
IntActi Q99383. 33 interactions.
MINTi MINT-395353.

Proteomic databases

MaxQBi Q99383.
PaxDbi Q99383.
PeptideAtlasi Q99383.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YOL123W ; YOL123W ; YOL123W .
GeneIDi 853997.
KEGGi sce:YOL123W.

Organism-specific databases

CYGDi YOL123w.
SGDi S000005483. HRP1.

Phylogenomic databases

eggNOGi COG0724.
GeneTreei ENSGT00760000118873.
HOGENOMi HOG000248803.
InParanoidi Q99383.
KOi K14411.
OMAi YQKMQEY.
OrthoDBi EOG706125.

Enzyme and pathway databases

BioCyci YEAST:G3O-33519-MONOMER.
Reactomei REACT_189250. AUF1 (hnRNP D0) destabilizes mRNA.

Miscellaneous databases

EvolutionaryTracei Q99383.
NextBioi 975491.
PROi Q99383.

Gene expression databases

Genevestigatori Q99383.

Family and domain databases

Gene3Di 3.30.70.330. 2 hits.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF00076. RRM_1. 2 hits.
[Graphical view ]
SMARTi SM00360. RRM. 2 hits.
[Graphical view ]
PROSITEi PS50102. RRM. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Oberdorf A.M., Anderson J.T., Devore D.R., Swanson M.S.
    Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Potential RNA binding proteins in Saccharomyces cerevisiae identified as suppressors of temperature-sensitive mutations in NPL3."
    Henry M., Borland C.Z., Bossie M., Silver P.A.
    Genetics 142:103-115(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "DNA sequence analysis of a 10 624 bp fragment of the left arm of chromosome XV from Saccharomyces cerevisiae reveals a RNA binding protein, a mitochondrial protein, two ribosomal proteins and two new open reading frames."
    Lafuente M.J., Gamo F.-J., Gancedo C.
    Yeast 12:1041-1045(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "Hrp1, a sequence-specific RNA-binding protein that shuttles between the nucleus and the cytoplasm, is required for mRNA 3'-end formation in yeast."
    Kessler M.M., Henry M.F., Shen E., Zhao J., Gross S., Silver P.A., Moore C.L.
    Genes Dev. 11:2545-2556(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 182-189 AND 245-257, FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.
  7. "Control of cleavage site selection during mRNA 3' end formation by a yeast hnRNP."
    Minvielle-Sebastia L., Beyer K., Krecic A.M., Hector R.E., Swanson M.S., Keller W.
    EMBO J. 17:7454-7468(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "A specific RNA-protein interaction at yeast polyadenylation efficiency elements."
    Chen S., Hyman L.E.
    Nucleic Acids Res. 26:4965-4974(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING.
  9. "The yeast hnRNP-like protein Hrp1/Nab4 marks a transcript for nonsense-mediated mRNA decay."
    Gonzalez C.I., Ruiz-Echevarria M.J., Vasudevan S., Henry M.F., Peltz S.W.
    Mol. Cell 5:489-499(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NMD, INTERACTION WITH NAM7.
  10. "Five subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I."
    Gross S., Moore C.
    Proc. Natl. Acad. Sci. U.S.A. 98:6080-6085(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PRE-MRNA 3'-END FORMATION.
  11. Cited for: SUBCELLULAR LOCATION.
  12. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  13. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-3; SER-206; THR-458 AND SER-462, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-3 AND SER-462, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHRP1_YEAST
AccessioniPrimary (citable) accession number: Q99383
Secondary accession number(s): D6W1U5, Q02741
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 26, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3