Kelch repeat-containing protein 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P38853 (KEL1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 119. History...

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

Documents (3) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Kelch repeat-containing protein 1

Gene names

Name:	KEL1
Ordered Locus Names:	YHR158C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1164 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has a role in cell morphogenesis and cell fusion and may antagonize the PKC1 pathway.
Subunit structure	Interacts with KEL2.
Miscellaneous	Present with 1350 molecules/cell in log phase SD medium.
Sequence similarities	Contains 5 Kelch repeats.

Ontologies

Keywords
Domain	Coiled coil Kelch repeat Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell morphogenesis Traceable author statement PubMed 11079560. Source: SGD cytogamy Inferred from physical interaction Ref.4. Source: SGD negative regulation of exit from mitosis Inferred from mutant phenotype PubMed 12234925. Source: SGD plasma membrane fusion Traceable author statement PubMed 11079560. Source: SGD regulation of cell shape Inferred from mutant phenotype Ref.4. Source: SGD
Cellular_component	cellular bud neck Inferred from direct assay Ref.4. Source: SGD cellular bud tip Inferred from direct assay Ref.4. Source: SGD cytoplasm Inferred from direct assay PubMed 11914276. Source: SGD mating projection tip Inferred from direct assay PubMed 19053807 Ref.4. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
itself		5	EBI-9619,EBI-9619
BCK2	P33306	2	EBI-9619,EBI-3480
KEL2	P50090	4	EBI-9619,EBI-9630
LTE1	P07866	4	EBI-9619,EBI-10243
PAC1	P39946	3	EBI-9619,EBI-12838

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1164

1164

Kelch repeat-containing protein 1

PRO_0000119096

Regions

Repeat

139 – 186

Kelch 1

Repeat

253 – 307

Kelch 2

Repeat

308 – 357

Kelch 3

Repeat

359 – 409

Kelch 4

Repeat

411 – 460

Kelch 5

Coiled coil

777 – 931

155

Potential

Coiled coil

974 – 1163

190

Potential

Amino acid modifications

Modified residue

Phosphoserine Ref.9 Ref.10

Modified residue

Phosphoserine Ref.9 Ref.10

Modified residue

Phosphoserine Ref.10

Modified residue

Phosphoserine Ref.6 Ref.10

Modified residue

Phosphoserine Ref.6

Modified residue

165

Phosphothreonine Ref.10

Modified residue

465

Phosphothreonine Ref.10

Modified residue

467

Phosphothreonine Ref.10

Modified residue

477

Phosphothreonine Ref.7

Modified residue

486

Phosphothreonine Ref.10

Modified residue

503

Phosphoserine Ref.10

Modified residue

565

Phosphothreonine Ref.9

Modified residue

596

Phosphoserine Ref.10

Modified residue

597

Phosphoserine Ref.10

Modified residue

604

Phosphothreonine Ref.10

Modified residue

613

Phosphoserine Ref.6 Ref.7 Ref.9 Ref.10

Modified residue

626

Phosphothreonine Ref.10

Modified residue

647

Phosphoserine Ref.10

Modified residue

688

Phosphoserine Ref.10

Modified residue

689

Phosphoserine Ref.9 Ref.10

Modified residue

691

Phosphoserine Ref.7 Ref.10

Modified residue

703

Phosphoserine Ref.10

Modified residue

704

Phosphoserine Ref.10

Modified residue

707

Phosphoserine Ref.10

Modified residue

748

Phosphoserine Ref.10

Modified residue

837

Phosphoserine Ref.10

Modified residue

997

Phosphoserine Ref.10

Modified residue

1001

Phosphothreonine Ref.10

Modified residue

1003

Phosphoserine Ref.6 Ref.8 Ref.10

Modified residue

1019

Phosphoserine Ref.8 Ref.10

Modified residue

1020

Phosphoserine Ref.10

Modified residue

1022

Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10

Modified residue

1048

Phosphoserine Ref.10

Experimental info

Sequence conflict

447

D → A in AAT92822. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P38853 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 43D0FC570F1D5E4D
Show »

FASTA

1,164

131,094

        10         20         30         40         50         60 
MAGFSFAKKF THKKHGKTPS DASISDQSRE ASLSTPPNEK FFTKQETPQK GRQFSQGYHS 

        70         80         90        100        110        120 
NVNKTSSPPM FARKQVSESR IQPSAVPPQQ RNVSGPSTTL HKQLSKQREY TVWNRIKLQN 

       130        140        150        160        170        180 
SPFPRYRHVA SAYVTDKNQI YVIGGLHDQS VYGDTWILTA FDNATRFSTT TIDISEATPP 

       190        200        210        220        230        240 
PRVGHAAVLC GNAFVVFGGD THKVNKEGLM DDDIYLLNIN SYKWTVPAPV GPRPLGRYGH 

       250        260        270        280        290        300 
KISIIATTQM KTKLYVFGGQ FDDTYFNDLA VYDLSSFRRP DSHWEFLKPR TFTPPPITNF 

       310        320        330        340        350        360 
TMISYDSKLW VFGGDTLQGL VNDVFMYDPA INDWFIIDTT GEKPPPVQEH ATVVYNDLMC 

       370        380        390        400        410        420 
VVGGKDEHDA YLNSVYFLNL KSRKWFKLPV FTAGIPQGRS GHSLTLLKND KILIMGGDKF 

       430        440        450        460        470        480 
DYARVEEYDL HTSDIDMQRG TIVYTLDLAR IKDLCPGVMD VPTDTPTPRN GNLDLATPVT 

       490        500        510        520        530        540 
PTSHQTKNMN VPISAAPLAS APSPAPKDFS DADRLNREVH NRNVSTEHQN QSHPVNSESH 

       550        560        570        580        590        600 
LIAEPNILTP YVPSESSQTP VMKITSNKPF DTPTIQKEPD LSETMDPTVG NQRIPSSIYG 

       610        620        630        640        650        660 
DNLTPANQIK NNSPILETLP SNEIKTPQNG NIEEIKHLPD ADEKIDSTTT FDQEINGDKL 

       670        680        690        700        710        720 
GTSSMSKVEE DGNVADEDDE IGVAQMASSP SKDQFKIKHY NESSELSQNN TEIDKLSEPV 

       730        740        750        760        770        780 
DITIKKSDTA GHDSANHVID ASDEKNVSPM GDVPTDTKNE EASVPINRDA TTEVVDRALF 

       790        800        810        820        830        840 
EKLRSELQSL KELTHEKALE AGAHIKELET ELWQLKSQKN SGTTKEIDEL DSVRLQSKCE 

       850        860        870        880        890        900 
ILEADNHSLE DKVNELEELV NSKFLDIENL NEVIQFQNEK IKSLELEPNY KEKLEELQIE 

       910        920        930        940        950        960 
HENLSRENER LKNESKQHNE DIINNVANYS SQLGSLISHW KENRANSSFL ESSSSLISVS 

       970        980        990       1000       1010       1020 
DENGEKTVGE PYGDQSRHHR VVINKLTNRL DDLLERSQEL TISKEKLSSE YHALKMEHSS 

      1030       1040       1050       1060       1070       1080 
LSQDVLVKEN EIKKIQNDYK ESISSMDSAS KALMVSQREL EKYKSLNKKL IDELDELKFK 

      1090       1100       1110       1120       1130       1140 
NGVCSENFEN GLRSTEESSN NVKNSNSIRE NQFNIKINDL KAELFITNQE RDDLKSEVLE 

      1150       1160 
LKKRLLNLEN NTKQVNEDAD SDLL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. Vaudin M. Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Identification of Kel1p, a kelch domain-containing protein involved in cell fusion and morphology in Saccharomyces cerevisiae." Philips J., Herskowitz I. J. Cell Biol. 143:375-389(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[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]	"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-67; SER-94; SER-613 AND SER-1003, MASS SPECTROMETRY. Strain: YAL6B.
[7]	"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 THR-477; SER-613; SER-691 AND SER-1022, MASS SPECTROMETRY. Strain: ADR376.
[8]	"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-1003; SER-1019 AND SER-1022, MASS SPECTROMETRY.
[9]	"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-20; SER-23; THR-565; SER-613; SER-689 AND SER-1022, MASS SPECTROMETRY.
[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-20; SER-23; SER-25; SER-67; THR-165; THR-465; THR-467; THR-486; SER-503; SER-596; SER-597; THR-604; SER-613; THR-626; SER-647; SER-688; SER-689; SER-691; SER-703; SER-704; SER-707; SER-748; SER-837; SER-997; THR-1001; SER-1003; SER-1019; SER-1020; SER-1022 AND SER-1048, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U10397 Genomic DNA. Translation: AAB68991.1. AY692803 Genomic DNA. Translation: AAT92822.1. BK006934 Genomic DNA. Translation: DAA06851.1.
PIR	S46769.
RefSeq	NP_012028.1. NM_001179289.1.
3D structure databases
ProteinModelPortal	P38853.
SMR	P38853. Positions 253-419.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1403N.
IntAct	P38853. 30 interactions.
MINT	MINT-385237.
STRING	4932.YHR158C.
2D gel databases
COMPLUYEAST-2DPAGE	P38853.
Proteomic databases
PaxDb	P38853.
PeptideAtlas	P38853.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YHR158C; YHR158C; YHR158C.
GeneID	856563.
KEGG	sce:YHR158C.
Organism-specific databases
CYGD	YHR158c.
SGD	S000001201. KEL1.
Phylogenomic databases
eggNOG	NOG145020.
GeneTree	ENSGT00700000104199.
HOGENOM	HOG000000942.
OMA	GGQLEND.
OrthoDB	EOG42NN7R.
Gene expression databases
Genevestigator	P38853.
GermOnline	YHR158C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	2.120.10.80. 1 hit.
InterPro	IPR015915. Kelch-typ_b-propeller. IPR006652. Kelch_1. [Graphical view]
Pfam	PF01344. Kelch_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	982393.

Entry information

Entry name

KEL1_YEAST

Accession

Primary (citable) accession number: P38853
Secondary accession number(s): D3DLA7, E9P8X4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 119 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 VIII

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

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel 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