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Protein

NAP1-binding protein 2

Gene

NBP2

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

Negatively regulates the high-osmolarity glycerol (HOG) pathway through its negative regulation of the HOG1 kinase activity. Mediates the binding between the PTC1 phosphatase and the PBS2 MAP/ERK kinase (MEK). With PTC1, regulates endoplasmic reticulum inheritance through the cell wall integrity (CWI) MAPK pathway by modulating the MAPK, SLT2.3 Publications

GO - Molecular functioni

  • protein binding, bridging Source: SGD

GO - Biological processi

  • hyperosmotic response Source: SGD
  • inactivation of MAPK activity involved in cell wall organization or biogenesis Source: SGD
  • inactivation of MAPK activity involved in osmosensory signaling pathway Source: SGD
  • negative regulation of protein kinase activity Source: SGD
  • response to heat Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-29752-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
NAP1-binding protein 2
Gene namesi
Name:NBP2
Ordered Locus Names:YDR162C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR162C.
SGDiS000002569. NBP2.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 236236NAP1-binding protein 2PRO_0000257822Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021PhosphoserineCombined sources
Modified residuei196 – 1961PhosphoserineCombined sources
Modified residuei235 – 2351PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12163.

PTM databases

iPTMnetiQ12163.

Interactioni

Subunit structurei

Interacts with PBS2 and PTC1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AIM21P405634EBI-34713,EBI-25376
CLA4P485623EBI-34713,EBI-4750
PBS2P080182EBI-34713,EBI-12972
PTC1P351824EBI-34713,EBI-12784
STE20Q034975EBI-34713,EBI-18285

GO - Molecular functioni

  • protein binding, bridging Source: SGD

Protein-protein interaction databases

BioGridi32213. 295 interactions.
DIPiDIP-1538N.
IntActiQ12163. 12 interactions.
MINTiMINT-392639.

Structurei

Secondary structure

1
236
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi113 – 1175Combined sources
Beta strandi136 – 1449Combined sources
Beta strandi147 – 1515Combined sources
Beta strandi158 – 1625Combined sources
Helixi163 – 1653Combined sources
Beta strandi166 – 1683Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YN8X-ray1.70A/B/C/D/E/F113-170[»]
2LCSNMR-A110-172[»]
ProteinModelPortaliQ12163.
SMRiQ12163. Positions 110-172.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12163.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini110 – 17162SH3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

HOGENOMiHOG000065953.
InParanoidiQ12163.
OMAiYAYDESN.
OrthoDBiEOG7X3R1P.

Family and domain databases

InterProiIPR001452. SH3_domain.
[Graphical view]
PfamiPF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12163-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATMETTTQK DTNILKSGLK KTIGVLNEAV LQNGREVEAV QAGNSDTMED
60 70 80 90 100
TETTTIGYIS IKDYAYADSN PLHYGYFDGD NEEDEMVSDS SNGEDTYNKR
110 120 130 140 150
QSITLPDDYI VNQRAVALYD FEPENDNELR LAEGDIVFIS YKHGQGWLVA
160 170 180 190 200
ENESGSKTGL VPEEFVSYIQ PEDGENEVEN KARPFYLTHL ITQSVSPKNN
210 220 230
IDNTNEDEYD DNDEWEDIDD VAEVEADMKT KLDISD
Length:236
Mass (Da):26,571
Last modified:November 1, 1996 - v1
Checksum:iA7458854D5000EA6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D43693 Genomic DNA. Translation: BAA07790.1.
Z50046 Genomic DNA. Translation: CAA90382.1.
AY557678 Genomic DNA. Translation: AAS56004.1.
BK006938 Genomic DNA. Translation: DAA12002.1.
PIRiS57986.
RefSeqiNP_010446.3. NM_001180469.3.

Genome annotation databases

EnsemblFungiiYDR162C; YDR162C; YDR162C.
GeneIDi851740.
KEGGisce:YDR162C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D43693 Genomic DNA. Translation: BAA07790.1.
Z50046 Genomic DNA. Translation: CAA90382.1.
AY557678 Genomic DNA. Translation: AAS56004.1.
BK006938 Genomic DNA. Translation: DAA12002.1.
PIRiS57986.
RefSeqiNP_010446.3. NM_001180469.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YN8X-ray1.70A/B/C/D/E/F113-170[»]
2LCSNMR-A110-172[»]
ProteinModelPortaliQ12163.
SMRiQ12163. Positions 110-172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32213. 295 interactions.
DIPiDIP-1538N.
IntActiQ12163. 12 interactions.
MINTiMINT-392639.

PTM databases

iPTMnetiQ12163.

Proteomic databases

MaxQBiQ12163.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR162C; YDR162C; YDR162C.
GeneIDi851740.
KEGGisce:YDR162C.

Organism-specific databases

EuPathDBiFungiDB:YDR162C.
SGDiS000002569. NBP2.

Phylogenomic databases

HOGENOMiHOG000065953.
InParanoidiQ12163.
OMAiYAYDESN.
OrthoDBiEOG7X3R1P.

Enzyme and pathway databases

BioCyciYEAST:G3O-29752-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ12163.
PROiQ12163.

Family and domain databases

InterProiIPR001452. SH3_domain.
[Graphical view]
PfamiPF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Okuda A., Fujii-Nakata T., Kikuchi A.
    Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: SFY526.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Yeast Nap1-binding protein Nbp2p is required for mitotic growth at high temperatures and for cell wall integrity."
    Ohkuni K., Okuda A., Kikuchi A.
    Genetics 165:517-529(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK pathway."
    Mapes J., Ota I.M.
    EMBO J. 23:302-311(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PTC1 AND PBS2.
  8. "Ptc1p regulates cortical ER inheritance via Slt2p."
    Du Y., Walker L., Novick P., Ferro-Novick S.
    EMBO J. 25:4413-4422(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "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-196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "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-196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-102; SER-196 AND SER-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-102 AND SER-196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNBP2_YEAST
AccessioniPrimary (citable) accession number: Q12163
Secondary accession number(s): D6VSE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 521 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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