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Protein

Serine/threonine-protein kinase CLA4

Gene

CLA4

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

Functioni

Involved in budding and cytokinesis.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei594 – 5941ATPPROSITE-ProRule annotation
Active sitei693 – 6931Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi552 – 5609ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • kinase activity Source: SGD
  • protein serine/threonine kinase activity Source: SGD
  • receptor signaling protein serine/threonine kinase activity Source: GO_Central

GO - Biological processi

  • negative regulation of gene expression Source: SGD
  • negative regulation of sterol import by negative regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of protein import into nucleus Source: SGD
  • protein phosphorylation Source: SGD
  • regulation of exit from mitosis Source: SGD
  • response to pheromone Source: SGD
  • septin ring organization Source: SGD
  • sterol import Source: SGD
  • vacuole inheritance Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33286-MONOMER.
BRENDAi2.7.11.1. 984.
ReactomeiR-SCE-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-SCE-399954. Sema3A PAK dependent Axon repulsion.
R-SCE-5627123. RHO GTPases activate PAKs.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase CLA4 (EC:2.7.11.1)
Gene namesi
Name:CLA4
Ordered Locus Names:YNL298W
ORF Names:N0450
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL298W.
SGDiS000005242. CLA4.

Subcellular locationi

GO - Cellular componenti

  • cellular bud Source: SGD
  • fungal-type vacuole Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 842842Serine/threonine-protein kinase CLA4PRO_0000085865Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei29 – 291PhosphoserineCombined sources
Modified residuei46 – 461PhosphoserineCombined sources
Modified residuei351 – 3511PhosphoserineCombined sources
Modified residuei367 – 3671PhosphoserineCombined sources
Modified residuei425 – 4251PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP48562.

PTM databases

iPTMnetiP48562.

Interactioni

Subunit structurei

Interacts with CDC42.

Binary interactionsi

WithEntry#Exp.IntActNotes
BEM1P293663EBI-4750,EBI-3508
MYO5Q044393EBI-4750,EBI-11687
NBP2Q121633EBI-4750,EBI-34713

Protein-protein interaction databases

BioGridi35540. 626 interactions.
DIPiDIP-2276N.
IntActiP48562. 42 interactions.
MINTiMINT-582371.

Structurei

3D structure databases

ProteinModelPortaliP48562.
SMRiP48562. Positions 184-222, 484-838.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 179119PHPROSITE-ProRule annotationAdd
BLAST
Domaini184 – 19714CRIBPROSITE-ProRule annotationAdd
BLAST
Domaini546 – 825280Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi136 – 1449Poly-Ser
Compositional biasi372 – 38716Poly-GlnAdd
BLAST

Sequence similaritiesi

Contains 1 CRIB domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00840000129768.
HOGENOMiHOG000234202.
InParanoidiP48562.
KOiK19833.
OMAiTHIPTES.
OrthoDBiEOG708W7W.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.90.810.10. 1 hit.
InterProiIPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00786. PBD. 1 hit.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00285. PBD. 1 hit.
SM00233. PH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50108. CRIB. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48562-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSAAANKI SDNDFQNIGP APRPPSSNSQ GRTCYNQTQP ITKLMSQLDL
60 70 80 90 100
TSASHLGTST SKKKSGWVSY KDDGILSFIW QKRYLMLHDS YVALYKNDKQ
110 120 130 140 150
NDDAILKIPL TSIISVSRTQ LKQYCFELVR CSDRNSVSSG SSSSLNVSSD
160 170 180 190 200
SNSKKSIYIA TKTESDLHSW LDAIFAKCPL LSGVSSPTNF THKVHVGFDP
210 220 230 240 250
ETGSFVGMPT NWEKLLKHSR ITGEDWNNNS AAVIQVLQFY QEYNGAGNPT
260 270 280 290 300
NTLDKPQSGE TSSSQKSLPN SYNDNKLRNN SVNSKSSSGV SSSMVSQRKT
310 320 330 340 350
SQPPNTKSPV SLGSGSLPPI NTKLPTSQSN IPRHLQNVPN QQYPKMRNGH
360 370 380 390 400
SPTNGQFPRG PMHPNNSQRS LQQQQQQQQQ QKQQHQQYPY HHQGPSPSPS
410 420 430 440 450
PSPSPLNPYR PHHNMINPYS KQPQSPLSSQ STQNQAIPRY AQNSSPTAAH
460 470 480 490 500
FQPQRTAPKP PISAPRAPYP SNQNATSNTH VQPVAPKNDQ STPQTMRQAP
510 520 530 540 550
KRPDADVAQP GGVAKPKKPA RPTMSTAEIM SKLKKVTVNA DPSQCFKVIE
560 570 580 590 600
KAGQGASGSV YLAERTHIPT ESNMIELINN DIDEPHVGDK VAIKQMVLSK
610 620 630 640 650
QPRKELIVNE ILVMKDSRHK NIVNFLEAYL RTDDDLWVVM EFMEGGSLTD
660 670 680 690 700
IIENSPTNDN SHSPLTEPQI AYIVRETCQG LKFLHDKHII HRDIKSDNVL
710 720 730 740 750
LDTRARVKIT DFGFCARLTD KRSKRATMVG TPYWMAPEVV KQREYDEKID
760 770 780 790 800
VWSLGIMTIE MLEGEPPYLN EDPLKALYLI ATNGTPKLKH PESLSLEIKR
810 820 830 840
FLSVCLCVDV RYRASTEELL HHGFFNMACD PKDLTSLLEW KE
Length:842
Mass (Da):93,909
Last modified:February 1, 1996 - v1
Checksum:i3A2AB86414561DC6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti390 – 3901Y → I in CAA57879 (PubMed:7649470).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82499 Genomic DNA. Translation: CAA57879.1.
U23084 Genomic DNA. Translation: AAC49100.1.
Z71574 Genomic DNA. Translation: CAA96216.1.
BK006947 Genomic DNA. Translation: DAA10262.1.
PIRiS60402.
RefSeqiNP_014101.1. NM_001183136.1.

Genome annotation databases

EnsemblFungiiYNL298W; YNL298W; YNL298W.
GeneIDi855418.
KEGGisce:YNL298W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82499 Genomic DNA. Translation: CAA57879.1.
U23084 Genomic DNA. Translation: AAC49100.1.
Z71574 Genomic DNA. Translation: CAA96216.1.
BK006947 Genomic DNA. Translation: DAA10262.1.
PIRiS60402.
RefSeqiNP_014101.1. NM_001183136.1.

3D structure databases

ProteinModelPortaliP48562.
SMRiP48562. Positions 184-222, 484-838.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35540. 626 interactions.
DIPiDIP-2276N.
IntActiP48562. 42 interactions.
MINTiMINT-582371.

PTM databases

iPTMnetiP48562.

Proteomic databases

MaxQBiP48562.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL298W; YNL298W; YNL298W.
GeneIDi855418.
KEGGisce:YNL298W.

Organism-specific databases

EuPathDBiFungiDB:YNL298W.
SGDiS000005242. CLA4.

Phylogenomic databases

GeneTreeiENSGT00840000129768.
HOGENOMiHOG000234202.
InParanoidiP48562.
KOiK19833.
OMAiTHIPTES.
OrthoDBiEOG708W7W.

Enzyme and pathway databases

BioCyciYEAST:G3O-33286-MONOMER.
BRENDAi2.7.11.1. 984.
ReactomeiR-SCE-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-SCE-399954. Sema3A PAK dependent Axon repulsion.
R-SCE-5627123. RHO GTPases activate PAKs.

Miscellaneous databases

PROiP48562.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.90.810.10. 1 hit.
InterProiIPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00786. PBD. 1 hit.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00285. PBD. 1 hit.
SM00233. PH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50108. CRIB. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Ste20-like protein kinases are required for normal localization of cell growth and for cytokinesis in budding yeast."
    Cvrckova F., de Virgilio C., Manser E., Pringle J.R., Nasmyth K.
    Genes Dev. 9:1817-1830(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K1107.
  2. "Sequence analysis of a 30 kb DNA segment from yeast chromosome XIV carrying a ribosomal protein gene cluster, the genes encoding a plasma membrane protein and a subunit of replication factor C, and a novel putative serine/threonine protein kinase gene."
    Maurer K.C.T., Urbanus J.H.M., Planta R.J.
    Yeast 11:1303-1310(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "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-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  6. "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-46 AND SER-425, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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-29; SER-351 AND SER-367, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCLA4_YEAST
AccessioniPrimary (citable) accession number: P48562
Secondary accession number(s): D6W0P6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 6, 2016
This is version 171 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

Complete proteome, Reference proteome

Documents

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