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P13186 (KIN2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Serine/threonine-protein kinase KIN2

EC=2.7.11.1
Gene names
Name:KIN2
Ordered Locus Names:YLR096W
ORF Names:L8004.3
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1147 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine protein kinase involved in the regulation of exocytosis. Induces phosphorylation of SEC9 and its release from the plasma membrane to the cytosol. Ref.5 Ref.6

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts with SEC9 and SRO7. Ref.6

Subcellular location

Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side Ref.4 Ref.6.

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. NIM1 subfamily.

Contains 1 KA1 (kinase-associated) domain.

Contains 1 protein kinase domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11471147Serine/threonine-protein kinase KIN2
PRO_0000086133

Regions

Domain99 – 377279Protein kinase
Domain1098 – 114750KA1
Nucleotide binding105 – 1139ATP By similarity
Compositional bias527 – 53610Poly-Gln

Sites

Active site2481Proton acceptor By similarity
Binding site1281ATP By similarity

Amino acid modifications

Modified residue221Phosphoserine Ref.10
Modified residue1461Phosphoserine Ref.8
Modified residue5491Phosphoserine Ref.7 Ref.9 Ref.10
Modified residue6091Phosphoserine Ref.7
Modified residue8881Phosphoserine Ref.7

Experimental info

Sequence conflict216 – 2172QH → HD in AAA34723. Ref.1
Sequence conflict675 – 70733QEPLP…RTISD → SGTYSSKENLQHICQNQMKF PSKYRKAIVVLYQT Ref.1
Sequence conflict756 – 7583NAE → KRQ in AAA34723. Ref.1
Sequence conflict8051P → PLSVP Ref.1
Sequence conflict1034 – 10374ATNT → TTNSI Ref.1
Sequence conflict1041 – 10422NS → KT in AAA34723. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P13186 [UniParc].

Last modified December 15, 1998. Version 3.
Checksum: AC2660BF3CA69600

FASTA1,147128,338
        10         20         30         40         50         60 
MPNPNTADYL VNPNFRTSKG GSLSPTPEAF NDTRVAAPAT LRMMGKQSGP RNDQQQAPLM 

        70         80         90        100        110        120 
PPADIKQGKE QAAQRQNDAS RPNGAVELRQ FHRRSLGDWE FLETVGAGSM GKVKLVKHRQ 

       130        140        150        160        170        180 
TKEICVIKIV NRASKAYLHK QHSLPSPKNE SEILERQKRL EKEIARDKRT VREASLGQIL 

       190        200        210        220        230        240 
YHPHICRLFE MCTMSNHFYM LFEYVSGGQL LDYIIQHGSL KEHHARKFAR GIASALQYLH 

       250        260        270        280        290        300 
ANNIVHRDLK IENIMISSSG EIKIIDFGLS NIFDYRKQLH TFCGSLYFAA PELLKAQPYT 

       310        320        330        340        350        360 
GPEVDIWSFG IVLYVLVCGK VPFDDENSSI LHEKIKKGKV DYPSHLSIEV ISLLTRMIVV 

       370        380        390        400        410        420 
DPLRRATLKN VVEHPWMNRG YDFKAPSYVP NRVPLTPEMI DSQVLKEMYR LEFIDDIEDT 

       430        440        450        460        470        480 
RRSLIRLVTE KEYIQLSQEY WDKLSNAKGL SSSLNNNYLN STAQQTLIQN HITSNPSQSG 

       490        500        510        520        530        540 
YNEPDSNFED PTLAYHPLLS IYHLVSEMVA RKLAKLQRRQ ALALQAQAQQ RQQQQQVALG 

       550        560        570        580        590        600 
TKVALNNNSP DIMTKMRSPQ KEVVPNPGIF QVPAIGTSGT SNNTNTSNKP PLHVMVPPKL 

       610        620        630        640        650        660 
TIPEQAHTSP TSRKSSDIHT ELNGVLKSTP VPVSGEYQQR SASPVVGEHQ EKNTIGGIFR 

       670        680        690        700        710        720 
RISQSGQSQH PTRQQEPLPE REPPTYMSKS NEISIKVPKS HSRTISDYIP SARRYPSYVP 

       730        740        750        760        770        780 
NSVDVKQKPA KNTTIAPPIR SVSQKQNSDL PALPQNAELI VQKQRQKLLQ ENLDKLQIND 

       790        800        810        820        830        840 
NDNNNVNAVV DGINNDNSDH YLSVPKGRKL HPSARAKSVG HARRESLKFT RPPIPAALPP 

       850        860        870        880        890        900 
SDMTNDNGFL GEANKERYNP VSSNFSTVPE DSTTYSNDTN NRLTSVYSQE LTEKQILEEA 

       910        920        930        940        950        960 
SKAPPGSMPS IDYPKSMFLK GFFSVQTTSS KPLPIVRHNI ISVLTRMNID FKEVKGGFIC 

       970        980        990       1000       1010       1020 
VQQRPSIETA AVPVITTTGV GLDSGKAMDL QNSLDSQLSS SYHSTASSAS RNSSIKRQGS 

      1030       1040       1050       1060       1070       1080 
YKRGQNNIPL TPLATNTHQR NSSIPMSPNY GNQSNGTSGE LSSMSLDYVQ QQDDILTTSR 

      1090       1100       1110       1120       1130       1140 
AQNINNVNGQ TEQTNTSGIK ERPPIKFEIH IVKVRIVGLA GVHFKKVSGN TWLYKELASY 


ILKELNL 

« Hide

References

« Hide 'large scale' references
[1]"Two yeast genes that encode unusual protein kinases."
Levin D.E., Hammond C.I., Ralston R.O., Bishop J.M.
Proc. Natl. Acad. Sci. U.S.A. 84:6035-6039(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"KIN1 and KIN2 protein kinases localize to the cytoplasmic face of the yeast plasma membrane."
Tibbetts M., Donovan M., Roe S., Stiltner A.M., Hammond C.I.
Exp. Cell Res. 213:93-99(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[5]"Characterization of the KIN2 gene product in Saccharomyces cerevisiae and comparison between the kinase activities of p145KIN1 and p145KIN2."
Donovan M., Romano P., Tibbetts M., Hammond C.I.
Yeast 10:113-124(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"The yeast par-1 homologs kin1 and kin2 show genetic and physical interactions with components of the exocytic machinery."
Elbert M., Rossi G., Brennwald P.
Mol. Biol. Cell 16:532-549(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SEC9 AND SRO7.
[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 SER-549; SER-609 AND SER-888, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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-549, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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-22 AND SER-549, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M69018 Genomic DNA. Translation: AAA34723.1.
Z73268 Genomic DNA. Translation: CAA97659.1.
Z73269 Genomic DNA. Translation: CAA97661.1.
U53876 Genomic DNA. Translation: AAB67540.1.
BK006945 Genomic DNA. Translation: DAA09412.1.
PIRS64930.
RefSeqNP_013197.1. NM_001181983.1.

3D structure databases

ProteinModelPortalP13186.
SMRP13186. Positions 93-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31369. 153 interactions.
DIPDIP-6276N.
IntActP13186. 52 interactions.
MINTMINT-604572.
STRING4932.YLR096W.

Proteomic databases

MaxQBP13186.
PaxDbP13186.
PeptideAtlasP13186.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR096W; YLR096W; YLR096W.
GeneID850785.
KEGGsce:YLR096W.

Organism-specific databases

CYGDYLR096w.
SGDS000004086. KIN2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000111001.
HOGENOMHOG000207352.
KOK08286.
OrthoDBEOG793BK1.

Enzyme and pathway databases

BioCycYEAST:G3O-32246-MONOMER.
BRENDA2.7.11.1. 984.

Gene expression databases

GenevestigatorP13186.

Family and domain databases

Gene3D3.30.310.80. 2 hits.
InterProIPR028375. KA1/Ssp2_C.
IPR001772. KA1_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF103243. SSF103243. 2 hits.
SSF56112. SSF56112. 2 hits.
PROSITEPS50032. KA1. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio966981.
PROP13186.

Entry information

Entry nameKIN2_YEAST
AccessionPrimary (citable) accession number: P13186
Secondary accession number(s): D6VY96, Q12384
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: December 15, 1998
Last modified: June 11, 2014
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families