Heterogeneous nuclear rnp K-like protein 2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P38199 (HEK2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 89. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Heterogeneous nuclear rnp K-like protein 2

Alternative name(s):
KH domain-containing protein 1

Gene names

Name:	HEK2
Synonyms:	KHD1
Ordered Locus Names:	YBL032W
ORF Names:	YBL0418

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	RNA-binding protein involved in the correct localization of transcripts in the cell. RNA localization is a widespread mechanism for achieving localized protein synthesis. Required for the asymmetric localization to the daughter cell nucleus of the ASH1 transcript, encoding for a specific repressor of transcription. Overexpression inhibits translation of the ASH1 transcript. Involved in the stability of transcripts such as the MTL1 mRNA. Involved in structural and functional organization of telomeric chromatin and regulates silencing at the HMR locus. Ref.6 Ref.7 Ref.11 Ref.14 Ref.16 Ref.17
Subunit structure	Binds RNA.
Subcellular location	Cytoplasm. Cytoplasm › P-body. Nucleus. Chromosome › telomere Ref.7 Ref.8 Ref.14 Ref.17.
Post-translational modification	Phosphorylated by the plasma membrane-anchored casein kinase YCK1. Phosphorylation at its C-terminus reduces its RNA-binding capacity. Ref.11 Ref.12 Ref.13 Ref.15
Miscellaneous	Present with 15600 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Belongs to the HEK2 family. Contains 3 KH domains.

Ontologies

Keywords
Biological process	Translation regulation Transport mRNA transport
Cellular component	Chromosome Cytoplasm Nucleus Telomere
Domain	Repeat
Ligand	RNA-binding
Molecular function	Chromatin regulator
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW intracellular mRNA localization Inferred from mutant phenotype. Source: SGD mRNA stabilization Inferred from mutant phenotype Ref.17. Source: SGD mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW telomere maintenance via telomerase Inferred from mutant phenotype Ref.7. Source: SGD
Cellular component	cytoplasmic mRNA processing body Inferred from direct assay Ref.17. Source: SGD nuclear chromosome, telomeric region Inferred from direct assay Ref.7. Source: SGD
Molecular function	mRNA binding Inferred from direct assay Ref.6. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 381

381

Heterogeneous nuclear rnp K-like protein 2

PRO_0000050161

Regions

Domain

43 – 107

KH 1

Domain

156 – 221

KH 2

Domain

258 – 326

KH 3

Amino acid modifications

Modified residue

252

Phosphoserine Ref.13 Ref.15

Modified residue

358

Phosphoserine Ref.12 Ref.15

Modified residue

360

Phosphoserine Ref.13 Ref.15

Modified residue

362

Phosphoserine Ref.13 Ref.15

Modified residue

381

Phosphoserine Ref.15

Experimental info

Sequence conflict

362

S → P in AAT92833. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P38199 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 0A8752961EB77DC9
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FASTA

381

41,683

        10         20         30         40         50         60 
MSQFFEAATP VAIPTNNTNG GSSDAGSAAT GGAPVVGTTA QPTINHRLLL SLKEAAKIIG 

        70         80         90        100        110        120 
TKGSTISRIR AANAVKIGIS EKVPGCSDRI LSCAGNVINV ANAIGDIVDV LNKRNPENED 

       130        140        150        160        170        180 
AAEGEAEEHY YFHFLNHILP APSKDEIRDL QQLEDIGYVR LIVANSHISS IIGKAGATIK 

       190        200        210        220        230        240 
SLINKHGVKI VASKDFLPAS DERIIEIQGF PGSITNVLIE ISEIILSDVD VRFSTERSYF 

       250        260        270        280        290        300 
PHLKKSSGEP TSPSTSSNTR IELKIPELYV GAIIGRGMNR IKNLKTFTKT NIVVERKDDD 

       310        320        330        340        350        360 
DKDENFRKFI ITSKFPKNVK LAESMLLKNL NTEIEKRENY KRKLEAAEGD ATVVTERSDS 

       370        380 
ASFLEEKEEP QENHDNKEEQ S

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of a 17.4 kb DNA segment of yeast chromosome II encompassing the ribosomal protein L19 as well as proteins with homologies to components of the hnRNP and snRNP complexes and to the human proliferation-associated p120 antigen." van Dyck L., Jonniaux J.-L., Barreiros T.D.M., Kleine K., Goffeau A. Yeast 10:1663-1673(1994) [PubMed: 7725803] [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. Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [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]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"KH domain-containing proteins of yeast: absence of a fragile X gene homologue." Currie J.R., Brown W.T. Am. J. Med. Genet. 84:272-276(1999) [PubMed: 10331606] [Abstract] Cited for: DOMAIN.
[6]	"The Khd1 protein, which has three KH RNA-binding motifs, is required for proper localization of ASH1 mRNA in yeast." Irie K., Tadauchi T., Takizawa P.A., Vale R.D., Matsumoto K., Herskowitz I. EMBO J. 21:1158-1167(2002) [PubMed: 11867544] [Abstract] Cited for: RNA-BINDING, FUNCTION.
[7]	"Yeast hnRNP K-like genes are involved in regulation of the telomeric position effect and telomere length." Denisenko O., Bomsztyk K. Mol. Cell. Biol. 22:286-297(2002) [PubMed: 11739741] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"The binding activity of yeast RNAs to yeast Hek2p and mammalian hnRNP K proteins, determined using the three-hybrid system." Paziewska A., Wyrwicz L.S., Ostrowski J. Cell. Mol. Biol. Lett. 10:227-235(2005) [PubMed: 16010288] [Abstract] Cited for: RNA-BINDING.
[11]	"Local activation of yeast ASH1 mRNA translation through phosphorylation of Khd1p by the casein kinase Yck1p." Paquin N., Menade M., Poirier G., Donato D., Drouet E., Chartrand P. Mol. Cell 26:795-809(2007) [PubMed: 17588515] [Abstract] Cited for: FUNCTION, RNA-BINDING, PHOSPHORYLATION.
[12]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, MASS SPECTROMETRY.
[13]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252; SER-360 AND SER-362, MASS SPECTROMETRY.
[14]	"Epistatic interaction between the K-homology domain protein HEK2 and SIR1 at HMR and telomeres in yeast." Denisenko O., Bomsztyk K. J. Mol. Biol. 375:1178-1187(2008) [PubMed: 18067921] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[15]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252; SER-358; SER-360; SER-362 AND SER-381, MASS SPECTROMETRY.
[16]	"Distinct roles for Khd1p in the localization and expression of bud-localized mRNAs in yeast." Hasegawa Y., Irie K., Gerber A.P. RNA 14:2333-2347(2008) [PubMed: 18805955] [Abstract] Cited for: FUNCTION, RNA-BINDING.
[17]	"Stability control of MTL1 mRNA by the RNA-binding protein Khd1p in yeast." Mauchi N., Ohtake Y., Irie K. Cell Struct. Funct. 35:95-105(2010) [PubMed: 20953064] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X77291 Genomic DNA. Translation: CAA54496.1. Z35793 Genomic DNA. Translation: CAA84852.1. AY692814 Genomic DNA. Translation: AAT92833.1. BK006936 Genomic DNA. Translation: DAA07087.1.
PIR	S45766.
RefSeq	NP_009521.1. NM_001178272.1.
3D structure databases
ProteinModelPortal	P38199.
SMR	P38199. Positions 41-113, 158-226, 260-331.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3934N.
IntAct	P38199. 53 interactions.
MINT	MINT-506819.
STRING	P38199.
Proteomic databases
PeptideAtlas	P38199.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBL032W; YBL032W; YBL032W.
GeneID	852248.
KEGG	sce:YBL032W.
NMPDR	fig\|4932.3.peg.213.
Organism-specific databases
CYGD	YBL032w.
SGD	S000000128. HEK2.
Phylogenomic databases
eggNOG	fuNOG07095.
HOGENOM	HBG204258.
OrthoDB	EOG4Z65XM.
Gene expression databases
ArrayExpress	P38199.
Genevestigator	P38199.
GermOnline	YBL032W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004087. KH. IPR004088. KH_type_1. IPR018111. KH_type_1_subgr. [Graphical view]
Pfam	PF00013. KH_1. 3 hits. [Graphical view]
SMART	SM00322. KH. 3 hits. [Graphical view]
PROSITE	PS50084. KH_TYPE_1. 3 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	970814.

Entry information

Entry name

HEK2_YEAST

Accession

Primary (citable) accession number: P38199
Secondary accession number(s): D6VPW7, E9P8X5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	December 14, 2011
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal 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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents