Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

RNA-binding protein PIN4

Gene

PIN4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in normal G2/M phase transition of the mitotic cell cycle. In association with RAD53, also involved in checkpoint control in response to DNA damage.1 Publication

GO - Molecular functioni

GO - Biological processi

  • DNA damage checkpoint Source: SGD
  • G2/M transition of mitotic cell cycle Source: SGD
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-28950-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-binding protein PIN4
Alternative name(s):
Psi inducibility protein 4
Gene namesi
Name:PIN4
Synonyms:MDT1
Ordered Locus Names:YBL051C
ORF Names:YBL0506, YBL0516
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL051C.
SGDiS000000147. PIN4.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi305 – 3051T → A: No interaction with RAD53. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 668668RNA-binding protein PIN4PRO_0000082028Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei56 – 561PhosphoserineCombined sources
Modified residuei189 – 1891PhosphoserineCombined sources
Modified residuei191 – 1911PhosphoserineCombined sources
Modified residuei194 – 1941PhosphoserineCombined sources
Modified residuei197 – 1971PhosphoserineCombined sources
Modified residuei305 – 3051Phosphothreonine1 Publication
Modified residuei393 – 3931PhosphoserineCombined sources
Modified residuei466 – 4661PhosphoserineCombined sources
Modified residuei541 – 5411PhosphoserineCombined sources
Modified residuei636 – 6361PhosphoserineCombined sources
Modified residuei638 – 6381PhosphoserineCombined sources
Modified residuei640 – 6401PhosphoserineCombined sources
Modified residuei653 – 6531PhosphoserineCombined sources
Modified residuei655 – 6551PhosphoserineCombined sources

Post-translational modificationi

Hyperphosphorylated in response to DNA damage by MEC1.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP34217.

PTM databases

iPTMnetiP34217.

Interactioni

Subunit structurei

Interacts with RAD53.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RAD53P222163EBI-21256,EBI-17843

Protein-protein interaction databases

BioGridi32647. 91 interactions.
DIPiDIP-1905N.
IntActiP34217. 43 interactions.
MINTiMINT-388641.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A0TNMR-B301-310[»]
ProteinModelPortaliP34217.
SMRiP34217. Positions 123-163.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34217.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini85 – 16379RRMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000115549.
OMAiKKMLPQA.
OrthoDBiEOG7FFN1K.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P34217-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METSSFENAP PAAINDAQDN NINTETNDQE TNQQSIETRD AIDKENGVQT
60 70 80 90 100
ETGENSAKNA EQNVSSTNLN NAPTNGALDD DVIPNAIVIK NIPFAIKKEQ
110 120 130 140 150
LLDIIEEMDL PLPYAFNYHF DNGIFRGLAF ANFTTPEETT QVITSLNGKE
160 170 180 190 200
ISGRKLKVEY KKMLPQAERE RIEREKREKR GQLEEQHRSS SNLSLDSLSK
210 220 230 240 250
MSGSGNNNTS NNQLFSTLMN GINANSMMNS PMNNTINNNS SNNNNSGNII
260 270 280 290 300
LNQPSLSAQH TSSSLYQTNV NNQAQMSTER FYAPLPSTST LPLPPQQLDF
310 320 330 340 350
NDPDTLEIYS QLLLFKDREK YYYELAYPMG ISASHKRIIN VLCSYLGLVE
360 370 380 390 400
VYDPRFIIIR RKILDHANLQ SHLQQQGQMT SAHPLQPNST GGSMNRSQSY
410 420 430 440 450
TSLLQAHAAA AANSISNQAV NNSSNSNTIN SNNGNGNNVI INNNSASSTP
460 470 480 490 500
KISSQGQFSM QPTLTSPKMN IHHSSQYNSA DQPQQPQPQT QQNVQSAAQQ
510 520 530 540 550
QQSFLRQQAT LTPSSRIPSG YSANHYQINS VNPLLRNSQI SPPNSQIPIN
560 570 580 590 600
SQTLSQAQPP AQSQTQQRVP VAYQNASLSS QQLYNLNGPS SANSQSQLLP
610 620 630 640 650
QHTNGSVHSN FSYQSYHDES MLSAHNLNSA DLIYKSLSHS GLDDGLEQGL
660
NRSLSGLDLQ NQNKKNLW
Length:668
Mass (Da):73,776
Last modified:February 1, 1994 - v1
Checksum:iEA8EE581286436CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z23261 Genomic DNA. Translation: CAA80795.1.
Z35812 Genomic DNA. Translation: CAA84871.1.
BK006936 Genomic DNA. Translation: DAA07068.1.
PIRiS39836.
RefSeqiNP_009502.1. NM_001178291.1.

Genome annotation databases

EnsemblFungiiYBL051C; YBL051C; YBL051C.
GeneIDi852229.
KEGGisce:YBL051C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z23261 Genomic DNA. Translation: CAA80795.1.
Z35812 Genomic DNA. Translation: CAA84871.1.
BK006936 Genomic DNA. Translation: DAA07068.1.
PIRiS39836.
RefSeqiNP_009502.1. NM_001178291.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A0TNMR-B301-310[»]
ProteinModelPortaliP34217.
SMRiP34217. Positions 123-163.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32647. 91 interactions.
DIPiDIP-1905N.
IntActiP34217. 43 interactions.
MINTiMINT-388641.

PTM databases

iPTMnetiP34217.

Proteomic databases

MaxQBiP34217.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL051C; YBL051C; YBL051C.
GeneIDi852229.
KEGGisce:YBL051C.

Organism-specific databases

EuPathDBiFungiDB:YBL051C.
SGDiS000000147. PIN4.

Phylogenomic databases

HOGENOMiHOG000115549.
OMAiKKMLPQA.
OrthoDBiEOG7FFN1K.

Enzyme and pathway databases

BioCyciYEAST:G3O-28950-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP34217.
PROiP34217.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing and functional analysis of a 32,560 bp segment on the left arm of yeast chromosome II. Identification of 26 open reading frames, including the KIP1 and SEC17 genes."
    Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F.
    Yeast 9:1355-1371(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Mdt1, a novel Rad53 FHA1 domain-interacting protein, modulates DNA damage tolerance and G(2)/M cell cycle progression in Saccharomyces cerevisiae."
    Pike B.L., Yongkiettrakul S., Tsai M.-D., Heierhorst J.
    Mol. Cell. Biol. 24:2779-2788(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAD53, PHOSPHORYLATION, MUTAGENESIS OF THR-305.
  7. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541 AND SER-638, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  8. "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-189 AND SER-466, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  9. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-56; SER-653 AND SER-655, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-189; SER-191; SER-194; SER-197; SER-393; SER-466; SER-636; SER-638; SER-640; SER-653 AND SER-655, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPIN4_YEAST
AccessioniPrimary (citable) accession number: P34217
Secondary accession number(s): D6VPU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 6, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4630 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

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 one 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.