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P34217 (PIN4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA-binding protein PIN4
Alternative name(s):
Psi inducibility protein 4
Gene names
Name:PIN4
Synonyms:MDT1
Ordered Locus Names:YBL051C
ORF Names:YBL0506, YBL0516
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length668 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Subunit structure

Interacts with RAD53. Ref.6

Subcellular location

Cytoplasm Ref.4.

Post-translational modification

Hyperphosphorylated in response to DNA damage by MEC1. Ref.6

Miscellaneous

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

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RAD53P222163EBI-21256,EBI-17843

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 668668RNA-binding protein PIN4
PRO_0000082028

Regions

Domain85 – 16379RRM

Amino acid modifications

Modified residue561Phosphoserine Ref.11
Modified residue651Phosphoserine Ref.11
Modified residue1891Phosphoserine Ref.8 Ref.9 Ref.10
Modified residue1901Phosphoserine Ref.9 Ref.11
Modified residue1911Phosphoserine Ref.11
Modified residue1941Phosphoserine Ref.10 Ref.11
Modified residue1971Phosphoserine Ref.11
Modified residue1991Phosphoserine Ref.11
Modified residue2621Phosphoserine Ref.11
Modified residue3051Phosphothreonine; by ATR
Modified residue3971Phosphoserine Ref.11
Modified residue3991Phosphoserine Ref.11
Modified residue4001Phosphotyrosine Ref.11
Modified residue4021Phosphoserine Ref.11
Modified residue4541Phosphoserine Ref.11
Modified residue4661Phosphoserine Ref.7 Ref.8 Ref.11
Modified residue5261Phosphotyrosine Ref.11
Modified residue5411Phosphoserine Ref.7
Modified residue5791Phosphoserine Ref.11
Modified residue6291Phosphoserine Ref.11
Modified residue6361Phosphoserine Ref.10 Ref.11
Modified residue6381Phosphoserine Ref.7 Ref.10 Ref.11
Modified residue6401Phosphoserine Ref.10 Ref.11
Modified residue6531Phosphoserine Ref.10 Ref.11
Modified residue6551Phosphoserine Ref.7 Ref.10 Ref.11

Experimental info

Mutagenesis3051T → A: No interaction with RAD53. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P34217 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: EA8EE581286436CB

FASTA66873,776
        10         20         30         40         50         60 
METSSFENAP PAAINDAQDN NINTETNDQE TNQQSIETRD AIDKENGVQT ETGENSAKNA 

        70         80         90        100        110        120 
EQNVSSTNLN NAPTNGALDD DVIPNAIVIK NIPFAIKKEQ LLDIIEEMDL PLPYAFNYHF 

       130        140        150        160        170        180 
DNGIFRGLAF ANFTTPEETT QVITSLNGKE ISGRKLKVEY KKMLPQAERE RIEREKREKR 

       190        200        210        220        230        240 
GQLEEQHRSS SNLSLDSLSK MSGSGNNNTS NNQLFSTLMN GINANSMMNS PMNNTINNNS 

       250        260        270        280        290        300 
SNNNNSGNII LNQPSLSAQH TSSSLYQTNV NNQAQMSTER FYAPLPSTST LPLPPQQLDF 

       310        320        330        340        350        360 
NDPDTLEIYS QLLLFKDREK YYYELAYPMG ISASHKRIIN VLCSYLGLVE VYDPRFIIIR 

       370        380        390        400        410        420 
RKILDHANLQ SHLQQQGQMT SAHPLQPNST GGSMNRSQSY TSLLQAHAAA AANSISNQAV 

       430        440        450        460        470        480 
NNSSNSNTIN SNNGNGNNVI INNNSASSTP KISSQGQFSM QPTLTSPKMN IHHSSQYNSA 

       490        500        510        520        530        540 
DQPQQPQPQT QQNVQSAAQQ QQSFLRQQAT LTPSSRIPSG YSANHYQINS VNPLLRNSQI 

       550        560        570        580        590        600 
SPPNSQIPIN SQTLSQAQPP AQSQTQQRVP VAYQNASLSS QQLYNLNGPS SANSQSQLLP 

       610        620        630        640        650        660 
QHTNGSVHSN FSYQSYHDES MLSAHNLNSA DLIYKSLSHS GLDDGLEQGL NRSLSGLDLQ 


NQNKKNLW 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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-466; SER-541; SER-638 AND SER-655, MASS SPECTROMETRY.
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, MASS SPECTROMETRY.
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-189 AND SER-190, MASS SPECTROMETRY.
[10]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-194; SER-636; SER-638; SER-640; SER-653 AND SER-655, MASS SPECTROMETRY.
[11]"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-65; SER-190; SER-191; SER-194; SER-197; SER-199; SER-262; SER-397; SER-399; TYR-400; SER-402; SER-454; SER-466; TYR-526; SER-579; SER-629; SER-636; SER-638; SER-640; SER-653 AND SER-655, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z23261 Genomic DNA. Translation: CAA80795.1.
Z35812 Genomic DNA. Translation: CAA84871.1.
BK006936 Genomic DNA. Translation: DAA07068.1.
PIRS39836.
RefSeqNP_009502.1. NM_001178291.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2A0TNMR-B301-310[»]
ProteinModelPortalP34217.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1905N.
IntActP34217. 42 interactions.
MINTMINT-388641.
STRING4932.YBL051C.

Proteomic databases

PaxDbP34217.
PeptideAtlasP34217.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBL051C; YBL051C; YBL051C.
GeneID852229.
KEGGsce:YBL051C.

Organism-specific databases

CYGDYBL051c.
SGDS000000147. PIN4.

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000115549.
OMAKKMLPQA.
OrthoDBEOG4QG0PB.

Gene expression databases

GenevestigatorP34217.
GermOnlineYBL051C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP34217.
NextBio970760.

Entry information

Entry namePIN4_YEAST
AccessionPrimary (citable) accession number: P34217
Secondary accession number(s): D6VPU8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: May 1, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families