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Protein

Serine/threonine-protein kinase KIN2

Gene

KIN2

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

Serine/threonine protein kinase involved in the regulation of exocytosis. Induces phosphorylation of SEC9 and its release from the plasma membrane to the cytosol.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei128 – 1281ATPPROSITE-ProRule annotation
Active sitei248 – 2481Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi105 – 1139ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  1. exocytosis Source: SGD
  2. protein autophosphorylation Source: SGD
  3. protein phosphorylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Exocytosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32246-MONOMER.
BRENDAi2.7.11.1. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase KIN2 (EC:2.7.11.1)
Gene namesi
Name:KIN2
Ordered Locus Names:YLR096W
ORF Names:L8004.3
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

CYGDiYLR096w.
EuPathDBiFungiDB:YLR096W.
SGDiS000004086. KIN2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11471147Serine/threonine-protein kinase KIN2PRO_0000086133Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221Phosphoserine1 Publication
Modified residuei146 – 1461Phosphoserine1 Publication
Modified residuei549 – 5491Phosphoserine3 Publications
Modified residuei609 – 6091Phosphoserine1 Publication
Modified residuei888 – 8881Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP13186.
PaxDbiP13186.
PeptideAtlasiP13186.

Expressioni

Gene expression databases

GenevestigatoriP13186.

Interactioni

Subunit structurei

Interacts with SEC9 and SRO7.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
BCK2P333064EBI-9723,EBI-3480
BUD14P276373EBI-9723,EBI-20747
RIM15P435652EBI-9723,EBI-15150

Protein-protein interaction databases

BioGridi31369. 153 interactions.
DIPiDIP-6276N.
IntActiP13186. 52 interactions.
MINTiMINT-604572.
STRINGi4932.YLR096W.

Structurei

3D structure databases

ProteinModelPortaliP13186.
SMRiP13186. Positions 93-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini99 – 377279Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini1098 – 114750KA1PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi527 – 53610Poly-Gln

Sequence similaritiesi

Contains 1 KA1 (kinase-associated) domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000122014.
HOGENOMiHOG000207352.
InParanoidiP13186.
KOiK08286.
OrthoDBiEOG793BK1.

Family and domain databases

Gene3Di3.30.310.80. 2 hits.
InterProiIPR028375. 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.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF103243. SSF103243. 2 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50032. KA1. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13186-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNPNTADYL VNPNFRTSKG GSLSPTPEAF NDTRVAAPAT LRMMGKQSGP
60 70 80 90 100
RNDQQQAPLM PPADIKQGKE QAAQRQNDAS RPNGAVELRQ FHRRSLGDWE
110 120 130 140 150
FLETVGAGSM GKVKLVKHRQ TKEICVIKIV NRASKAYLHK QHSLPSPKNE
160 170 180 190 200
SEILERQKRL EKEIARDKRT VREASLGQIL YHPHICRLFE MCTMSNHFYM
210 220 230 240 250
LFEYVSGGQL LDYIIQHGSL KEHHARKFAR GIASALQYLH ANNIVHRDLK
260 270 280 290 300
IENIMISSSG EIKIIDFGLS NIFDYRKQLH TFCGSLYFAA PELLKAQPYT
310 320 330 340 350
GPEVDIWSFG IVLYVLVCGK VPFDDENSSI LHEKIKKGKV DYPSHLSIEV
360 370 380 390 400
ISLLTRMIVV DPLRRATLKN VVEHPWMNRG YDFKAPSYVP NRVPLTPEMI
410 420 430 440 450
DSQVLKEMYR LEFIDDIEDT RRSLIRLVTE KEYIQLSQEY WDKLSNAKGL
460 470 480 490 500
SSSLNNNYLN STAQQTLIQN HITSNPSQSG YNEPDSNFED PTLAYHPLLS
510 520 530 540 550
IYHLVSEMVA RKLAKLQRRQ ALALQAQAQQ RQQQQQVALG TKVALNNNSP
560 570 580 590 600
DIMTKMRSPQ KEVVPNPGIF QVPAIGTSGT SNNTNTSNKP PLHVMVPPKL
610 620 630 640 650
TIPEQAHTSP TSRKSSDIHT ELNGVLKSTP VPVSGEYQQR SASPVVGEHQ
660 670 680 690 700
EKNTIGGIFR RISQSGQSQH PTRQQEPLPE REPPTYMSKS NEISIKVPKS
710 720 730 740 750
HSRTISDYIP SARRYPSYVP NSVDVKQKPA KNTTIAPPIR SVSQKQNSDL
760 770 780 790 800
PALPQNAELI VQKQRQKLLQ ENLDKLQIND NDNNNVNAVV DGINNDNSDH
810 820 830 840 850
YLSVPKGRKL HPSARAKSVG HARRESLKFT RPPIPAALPP SDMTNDNGFL
860 870 880 890 900
GEANKERYNP VSSNFSTVPE DSTTYSNDTN NRLTSVYSQE LTEKQILEEA
910 920 930 940 950
SKAPPGSMPS IDYPKSMFLK GFFSVQTTSS KPLPIVRHNI ISVLTRMNID
960 970 980 990 1000
FKEVKGGFIC VQQRPSIETA AVPVITTTGV GLDSGKAMDL QNSLDSQLSS
1010 1020 1030 1040 1050
SYHSTASSAS RNSSIKRQGS YKRGQNNIPL TPLATNTHQR NSSIPMSPNY
1060 1070 1080 1090 1100
GNQSNGTSGE LSSMSLDYVQ QQDDILTTSR AQNINNVNGQ TEQTNTSGIK
1110 1120 1130 1140
ERPPIKFEIH IVKVRIVGLA GVHFKKVSGN TWLYKELASY ILKELNL
Length:1,147
Mass (Da):128,338
Last modified:December 15, 1998 - v3
Checksum:iAC2660BF3CA69600
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti216 – 2172QH → HD in AAA34723 (PubMed:2957690).Curated
Sequence conflicti675 – 70733QEPLP…RTISD → SGTYSSKENLQHICQNQMKF PSKYRKAIVVLYQT (PubMed:2957690).CuratedAdd
BLAST
Sequence conflicti756 – 7583NAE → KRQ in AAA34723 (PubMed:2957690).Curated
Sequence conflicti805 – 8051P → PLSVP (PubMed:2957690).Curated
Sequence conflicti1034 – 10374ATNT → TTNSI (PubMed:2957690).Curated
Sequence conflicti1041 – 10422NS → KT in AAA34723 (PubMed:2957690).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS64930.
RefSeqiNP_013197.1. NM_001181983.1.

Genome annotation databases

EnsemblFungiiYLR096W; YLR096W; YLR096W.
GeneIDi850785.
KEGGisce:YLR096W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS64930.
RefSeqiNP_013197.1. NM_001181983.1.

3D structure databases

ProteinModelPortaliP13186.
SMRiP13186. Positions 93-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31369. 153 interactions.
DIPiDIP-6276N.
IntActiP13186. 52 interactions.
MINTiMINT-604572.
STRINGi4932.YLR096W.

Proteomic databases

MaxQBiP13186.
PaxDbiP13186.
PeptideAtlasiP13186.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR096W; YLR096W; YLR096W.
GeneIDi850785.
KEGGisce:YLR096W.

Organism-specific databases

CYGDiYLR096w.
EuPathDBiFungiDB:YLR096W.
SGDiS000004086. KIN2.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000122014.
HOGENOMiHOG000207352.
InParanoidiP13186.
KOiK08286.
OrthoDBiEOG793BK1.

Enzyme and pathway databases

BioCyciYEAST:G3O-32246-MONOMER.
BRENDAi2.7.11.1. 984.

Miscellaneous databases

NextBioi966981.
PROiP13186.

Gene expression databases

GenevestigatoriP13186.

Family and domain databases

Gene3Di3.30.310.80. 2 hits.
InterProiIPR028375. 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.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF103243. SSF103243. 2 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50032. KA1. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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. 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].

Entry informationi

Entry nameiKIN2_YEAST
AccessioniPrimary (citable) accession number: P13186
Secondary accession number(s): D6VY96, Q12384
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: December 15, 1998
Last modified: April 29, 2015
This is version 151 of the entry and version 3 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

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 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.