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P15891

- ABP1_YEAST

UniProt

P15891 - ABP1_YEAST

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Protein
Actin-binding protein
Gene
ABP1, YCR088W, YCR88W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Regulates ARP2/3 complex-mediated actin assembly. Recruits ARP2/3 complex to sides of preexisting actin filaments, which may promote nucleation or stabilization of filament branches. Binds to actin filaments, but not actin monomers. Actin binding is required for ARP2/3 complex activation. May also have a role in linking the actin cytoskeleton to endocytosis. recruits components of the endocytotic machinery to cortical actin patches, known sites of endocytosis.1 Publication

GO - Molecular functioni

  1. actin filament binding Source: SGD
  2. protein binding Source: IntAct

GO - Biological processi

  1. actin cortical patch assembly Source: SGD
  2. barbed-end actin filament capping Source: SGD
  3. protein localization Source: SGD
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29382-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-binding protein
Gene namesi
Name:ABP1
Ordered Locus Names:YCR088W
ORF Names:YCR88W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome III

Organism-specific databases

SGDiS000000684. ABP1.

Subcellular locationi

Cytoplasmcytoskeletonactin patch
Note: Cortical actin patches.3 Publications

GO - Cellular componenti

  1. actin cortical patch Source: SGD
  2. cell cortex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211K → A in ABP1-1; moderately reduces actin binding and partially reduces ARP2/3 complex activation; when associated with A-24. 1 Publication
Mutagenesisi24 – 241R → A in ABP1-1; moderately reduces actin binding and partially reduces ARP2/3 complex activation; when associated with A-21. 1 Publication
Mutagenesisi80 – 801K → A in ABP1-2; strongly reduces actin binding and abolishes ARP2/3 complex activation. 1 Publication
Mutagenesisi94 – 941K → A in ABP1-3; reduces actin binding and abolishes ARP2/3 complex activation; when associated with A-96. 1 Publication
Mutagenesisi96 – 961R → A in ABP1-3; reduces actin binding and abolishes ARP2/3 complex activation; when associated with A-94. 1 Publication
Mutagenesisi122 – 1221D → A in ABP1-4; no effect; when associated with A-125. 1 Publication
Mutagenesisi125 – 1251D → A in ABP1-4; no effect; when associated with A-122. 1 Publication
Mutagenesisi134 – 1341K → A in ABP1-5; moderately reduces actin binding and abolishes ARP2/3 complex activation. 1 Publication
Mutagenesisi201 – 2033DDW → AAA: Abolishes ARP2/3 complex activation, but not actin binding. 1 Publication
Mutagenesisi437 – 4393DDW → AAA: Abolishes ARP2/3 complex activation, but not actin binding. 1 Publication
Mutagenesisi569 – 5691W → A: Abolishes protein binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 592591Actin-binding protein
PRO_0000064429Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei165 – 1651Phosphothreonine1 Publication
Modified residuei167 – 1671Phosphoserine1 Publication
Modified residuei169 – 1691Phosphoserine3 Publications
Modified residuei181 – 1811Phosphothreonine4 Publications
Modified residuei183 – 1831Phosphoserine3 Publications
Modified residuei313 – 3131Phosphoserine2 Publications
Modified residuei365 – 3651Phosphoserine3 Publications
Modified residuei389 – 3891Phosphoserine2 Publications
Modified residuei458 – 4581Phosphoserine1 Publication
Modified residuei481 – 4811Phosphoserine2 Publications

Post-translational modificationi

The actin depolymerizing factor homology (ADF) domain mediates actin filament binding.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP15891.
PaxDbiP15891.
PeptideAtlasiP15891.

Expressioni

Gene expression databases

GenevestigatoriP15891.

Interactioni

Subunit structurei

Binds F-actin, but not G-actin. Interacts with the ARP2/3 complex. Interacts with APP1, ARK1, PRK1, SCP1, SRV2 and YIR003W via its SH3 domain. Interacts with the SH3 domain of RVS167 and with SLA1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AIM21P4056310EBI-2036,EBI-25376
APP1P539339EBI-2036,EBI-28798
ARK1P5397411EBI-2036,EBI-9817
BSP1Q066042EBI-2036,EBI-37047
HUA2Q121343EBI-2036,EBI-37262
INP52P509422EBI-2036,EBI-28834
LSB3P436036EBI-2036,EBI-22980
PRK1P4049410EBI-2036,EBI-9703
RVS167P397436EBI-2036,EBI-14500
SCP1Q088736EBI-2036,EBI-33137
SLA1P327904EBI-2036,EBI-17313
SRV2P175559EBI-2036,EBI-4024
YSC84P327933EBI-2036,EBI-24460

Protein-protein interaction databases

BioGridi31060. 87 interactions.
DIPiDIP-534N.
IntActiP15891. 35 interactions.
MINTiMINT-370108.
STRINGi4932.YCR088W.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 2413
Beta strandi32 – 376
Beta strandi43 – 508
Helixi52 – 565
Beta strandi65 – 717
Beta strandi80 – 867
Helixi93 – 10917
Beta strandi115 – 1228
Helixi123 – 1264
Helixi128 – 1369
Beta strandi537 – 5415
Beta strandi546 – 5505
Beta strandi558 – 5636
Beta strandi566 – 5749
Turni575 – 5773
Beta strandi580 – 5845
Helixi585 – 5873
Beta strandi588 – 5903

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HQZX-ray2.101/2/3/4/5/6/7/8/91-141[»]
1JO8X-ray1.30A535-592[»]
2K3BNMR-A535-592[»]
2RPNNMR-A535-592[»]
DisProtiDP00634.
ProteinModelPortaliP15891.
SMRiP15891. Positions 3-141, 535-592.

Miscellaneous databases

EvolutionaryTraceiP15891.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 136130ADF-H
Add
BLAST
Repeati200 – 209101
Repeati436 – 445102
Domaini532 – 59261SH3
Add
BLAST
Repeati566 – 575103

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni200 – 5753763 X 10 AA approximate repeats (acidic)
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi518 – 5225Poly-Pro

Sequence similaritiesi

Belongs to the ABP1 family.
Contains 1 ADF-H domain.
Contains 1 SH3 domain.

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG265859.
HOGENOMiHOG000246671.
OMAiIINIEFV.
OrthoDBiEOG7B05P0.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00241. Cofilin_ADF. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00102. ADF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51263. ADF_H. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15891-1 [UniParc]FASTAAdd to Basket

« Hide

MALEPIDYTT HSREIDAEYL KIVRGSDPDT TWLIISPNAK KEYEPESTGS    50
SFHDFLQLFD ETKVQYGLAR VSPPGSDVEK IIIIGWCPDS APLKTRASFA 100
ANFAAVANNL FKGYHVQVTA RDEDDLDENE LLMKISNAAG ARYSIQTSSK 150
QQGKASTPPV KKSFTPSKSP APVSKKEPVK TPSPAPAAKI SSRVNDNNDD 200
DDWNEPELKE RDFDQAPLKP NQSSYKPIGK IDLQKVIAEE KAKEDPRLVQ 250
KPTAAGSKID PSSDIANLKN ESKLKRDSEF NSFLGTTKPP SMTESSLKND 300
DDKVIKGFRN EKSPAQLWAE RKAKQNSGNA ETKAEAPKPE VPEDEPEGEP 350
DVKDLKSKFE GLAASEKEEE EMENKFAPPP KKSEPTIISP KPFSKPQEPV 400
KAEEAEQPKT DYKKIGNPLP GMHIEADNEE EPEENDDDWD DDEDEAAQPP 450
LPSRNVASGA PVQKEEPEQE EIAPSLPSRN SIPAPKQEEA PEQAPEEEIE 500
EEAEEAAPQL PSRSSAAPPP PPRRATPEKK PKENPWATAE YDYDAAEDNE 550
LTFVENDKII NIEFVDDDWW LGELEKDGSK GLFPSNYVSL GN 592
Length:592
Mass (Da):65,576
Last modified:January 23, 2007 - v4
Checksum:i39523510704D94AA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581L → S in CAA36075. 1 Publication
Sequence conflicti312 – 3121K → I in CAA36075. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X51780 Genomic DNA. Translation: CAA36075.1.
X59720 Genomic DNA. Translation: CAA42253.1.
BK006937 Genomic DNA. Translation: DAA07557.1.
PIRiS19503. LLBY.
RefSeqiNP_010012.1. NM_001178794.1.

Genome annotation databases

EnsemblFungiiYCR088W; YCR088W; YCR088W.
GeneIDi850450.
KEGGisce:YCR088W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X51780 Genomic DNA. Translation: CAA36075.1 .
X59720 Genomic DNA. Translation: CAA42253.1 .
BK006937 Genomic DNA. Translation: DAA07557.1 .
PIRi S19503. LLBY.
RefSeqi NP_010012.1. NM_001178794.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HQZ X-ray 2.10 1/2/3/4/5/6/7/8/9 1-141 [» ]
1JO8 X-ray 1.30 A 535-592 [» ]
2K3B NMR - A 535-592 [» ]
2RPN NMR - A 535-592 [» ]
DisProti DP00634.
ProteinModelPortali P15891.
SMRi P15891. Positions 3-141, 535-592.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31060. 87 interactions.
DIPi DIP-534N.
IntActi P15891. 35 interactions.
MINTi MINT-370108.
STRINGi 4932.YCR088W.

Proteomic databases

MaxQBi P15891.
PaxDbi P15891.
PeptideAtlasi P15891.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YCR088W ; YCR088W ; YCR088W .
GeneIDi 850450.
KEGGi sce:YCR088W.

Organism-specific databases

SGDi S000000684. ABP1.

Phylogenomic databases

eggNOGi NOG265859.
HOGENOMi HOG000246671.
OMAi IINIEFV.
OrthoDBi EOG7B05P0.

Enzyme and pathway databases

BioCyci YEAST:G3O-29382-MONOMER.

Miscellaneous databases

EvolutionaryTracei P15891.
NextBioi 966066.
PROi P15891.

Gene expression databases

Genevestigatori P15891.

Family and domain databases

Gene3Di 3.40.20.10. 1 hit.
InterProi IPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00241. Cofilin_ADF. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
SMARTi SM00102. ADF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS51263. ADF_H. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I."
    Drubin D.G., Mulholland J., Zhu Z., Botstein D.
    Nature 343:288-290(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [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. Bienvenut W.V., Peters C.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13 AND 97-112, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "A conserved proline-rich region of the Saccharomyces cerevisiae cyclase-associated protein binds SH3 domains and modulates cytoskeletal localization."
    Freeman N.L., Lila T., Mintzer K.A., Chen Z., Pahk A.J., Ren R., Drubin D.G., Field J.
    Mol. Cell. Biol. 16:548-556(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRV2.
  6. "In vivo analysis of the domains of yeast Rvs167p suggests Rvs167p function is mediated through multiple protein interactions."
    Colwill K., Field D., Moore L., Friesen J., Andrews B.
    Genetics 152:881-893(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RVS167.
  7. "Activation of the Arp2/3 complex by the actin filament binding protein Abp1p."
    Goode B.L., Rodal A.A., Barnes G., Drubin D.G.
    J. Cell Biol. 153:627-634(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ACTIN AND ARP2/3 COMPLEX, MUTAGENESIS OF 201-ASP--TRP-203 AND 437-ASP--TRP-439.
  8. "Sla1p couples the yeast endocytic machinery to proteins regulating actin dynamics."
    Warren D.T., Andrews P.D., Gourlay C.W., Ayscough K.R.
    J. Cell Sci. 115:1703-1715(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLA1, SUBCELLULAR LOCATION.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. Cited for: INTERACTION WITH APP1; PRK1; SCP1 AND YIR003W.
  12. "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-181; SER-183; SER-365 AND SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  13. "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-169; THR-181; SER-183 AND SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-169; THR-181; SER-183; SER-313; SER-365; SER-389; SER-458 AND SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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 THR-165; SER-167; SER-169; THR-181; SER-313 AND SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis."
    Fazi B., Cope M.J.T.V., Douangamath A., Ferracuti S., Schirwitz K., Zucconi A., Drubin D.G., Wilmanns M., Cesareni G., Castagnoli L.
    J. Biol. Chem. 277:5290-5298(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF SH3 DOMAIN, MUTAGENESIS OF TRP-569, INTERACTION WITH ARK1 AND PRK1.
  19. "Structural and functional dissection of the Abp1 ADFH actin-binding domain reveals versatile in vivo adapter functions."
    Quintero-Monzon O., Rodal A.A., Strokopytov B., Almo S.C., Goode B.L.
    Mol. Biol. Cell 16:3128-3139(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF ADF DOMAIN, MUTAGENESIS OF LYS-21; ARG-24; LYS-80; LYS-94; ARG-96; ASP-122; ASP-125 AND LYS-134, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiABP1_YEAST
AccessioniPrimary (citable) accession number: P15891
Secondary accession number(s): D6VR88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 149 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 606 molecules/cell in log phase SD medium.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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 III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

External Data

Dasty 3

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