NPL4/YBR170C Gene Ontology Annotations Help

This page displays GO annotations in different sections according to the annotation method used to add that annotation to SGD.

NPL4 Manually curated*:

Last Reviewed on: 2012-07-03    Molecular Function | Biological Process | Cellular Component

Manually curated Molecular Function
Annotation(s) Evidence Reference(s) Assigned By
molecular_function
unknown
ND: No Biological Data Available
Assigned on 2012-06-29
SGD  (2002) Use of the ND evidence code for Gene Ontology (GO) terms in SGD () SGD

Manually curated Biological Process
Annotation(s) Evidence Reference(s) Assigned By
cytoplasm-associated proteasomal ubiquitin-dependent protein catabolic process IMP: Inferred from Mutant Phenotype
Assigned on 2011-02-15
Metzger MB, et al.  (2008) Degradation of a Cytosolic Protein Requires Endoplasmic Reticulum-associated Degradation Machinery. J Biol Chem 283(47):32302-16 SGD
ER-associated misfolded protein catabolic process IMP: Inferred from Mutant Phenotype
Assigned on 2012-06-22
Ye Y, et al.  (2001) The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414(6864):652-6 SGD
IMP: Inferred from Mutant Phenotype
Assigned on 2012-06-22
Jarosch E, et al.  (2002) Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat Cell Biol 4(2):134-9 SGD
ER-associated protein catabolic process IMP: Inferred from Mutant Phenotype
Assigned on 2003-10-10
Bays NW, et al.  (2001) HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins. Mol Biol Cell 12(12):4114-28 SGD
mitochondria-associated protein catabolic process IMP: Inferred from Mutant Phenotype
Assigned on 2011-02-23
Heo JM, et al.  (2010) A stress-responsive system for mitochondrial protein degradation. Mol Cell 40(3):465-80 SGD
mitotic spindle disassembly IMP: Inferred from Mutant Phenotype
Assigned on 2012-06-27
Cao K, et al.  (2003) The AAA-ATPase Cdc48/p97 regulates spindle disassembly at the end of mitosis. Cell 115(3):355-67 SGD
positive regulation of protein localization to nucleus IMP: Inferred from Mutant Phenotype
Assigned on 2012-06-26
Rape M, et al.  (2001) Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Cell 107(5):667-77 SGD
IMP: Inferred from Mutant Phenotype
Assigned on 2012-06-26
Hitchcock AL, et al.  (2001) The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation. Mol Biol Cell 12(10):3226-41 SGD
proteasomal ubiquitin-dependent protein catabolic process IMP: Inferred from Mutant Phenotype
Assigned on 2012-06-29
Barbin L, et al.  (2010) The Cdc48-Ufd1-Npl4 complex is central in ubiquitin-proteasome triggered catabolite degradation of fructose-1,6-bisphosphatase. Biochem Biophys Res Commun 394(2):335-41 SGD
retrograde protein transport, ER to cytosol IMP: Inferred from Mutant Phenotype
Assigned on 2012-06-22
Ye Y, et al.  (2001) The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414(6864):652-6 SGD

Manually curated Cellular Component
Annotation(s) Evidence Reference(s) Assigned By
Cdc48p-Npl4p-Ufd1p AAA ATPase complex IDA: Inferred from Direct Assay
Assigned on 2012-06-26
Rape M, et al.  (2001) Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Cell 107(5):667-77 SGD
IDA: Inferred from Direct Assay
Assigned on 2012-06-26
Hitchcock AL, et al.  (2001) The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation. Mol Biol Cell 12(10):3226-41 SGD
Cdc48p-Npl4p-Vms1p AAA ATPase complex IDA: Inferred from Direct Assay
Assigned on 2012-07-03
Heo JM, et al.  (2010) A stress-responsive system for mitochondrial protein degradation. Mol Cell 40(3):465-80 SGD
Doa10p ubiquitin ligase complex IDA: Inferred from Direct Assay
Assigned on 2008-02-06
Carvalho P, et al.  (2006) Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Cell 126(2):361-73 SGD
nuclear outer membrane-endoplasmic reticulum membrane network IDA: Inferred from Direct Assay
Assigned on 2003-10-10
Hitchcock AL, et al.  (2001) The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation. Mol Biol Cell 12(10):3226-41 SGD

* Manually curated GO annotations reflect our best understanding of the basic molecular function, biological process, and cellular component for this gene product. Manually curated annotations are assigned by SGD curators based on published papers when available, or by curatorial statements if necessary. Curators periodically review all Manually curated GO annotations for accuracy and completeness. The "Last Reviewed on:" date at the top of this section indicates when these annotations were last reviewed.


NPL4 High-throughput**:

Cellular Component

High-throughput Cellular Component
Annotation(s) Evidence Reference(s) Assigned By
cytoplasm IDA: Inferred from Direct Assay
Assigned on 2012-12-12
Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76 SGD
integral to membrane ISM: Inferred from Sequence Model
Assigned on 2011-05-31
De Hertogh B, et al.  (2002) Phylogenetic classification of transporters and other membrane proteins from Saccharomyces cerevisiae. Funct Integr Genomics 2(4-5):154-70 SGD
nucleus IDA: Inferred from Direct Assay
Assigned on 2012-12-12
Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76 SGD

** GO annotations from High-throughput experiments are made based on a variety of large scale high-throughput experiments, including genome-wide experiments. Many of these annotations are made based on GO annotations (or mappings to GO annotations) assigned by the authors, rather than SGD curators. While SGD curators read these publications and often work closely with authors to incorporate the information, each individual annotation may not necessarily be reviewed by a curator. GO Annotations from high-throughput experiments will be assigned only when this type of data is available, and thus may not be assigned in all three aspects of the Gene Ontologies.


NPL4 Computational***:

Biological Process | Cellular Component

Computational Biological Process
Annotation(s) Evidence Reference(s) Assigned By
mRNA transport IEA: Inferred from Electronic Annotation
with EBI:KW-0509
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries. UniProtKB
protein transport IEA: Inferred from Electronic Annotation
with EBI:KW-0653
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries. UniProtKB
transport IEA: Inferred from Electronic Annotation
with EBI:KW-0813, EBI:KW-0811
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries. UniProtKB

Computational Cellular Component
Annotation(s) Evidence Reference(s) Assigned By
cytoplasm IEA: Inferred from Electronic Annotation
with EBI:KW-0963
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries. UniProtKB
endoplasmic reticulum IEA: Inferred from Electronic Annotation
with EBI:KW-0256
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries. UniProtKB
endoplasmic reticulum membrane IEA: Inferred from Electronic Annotation
with EBI:SL-0097
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries. UniProtKB
membrane IEA: Inferred from Electronic Annotation
with EBI:KW-0472
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries. UniProtKB
nuclear membrane IEA: Inferred from Electronic Annotation
with EBI:SL-0182
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries. UniProtKB
nucleus IEA: Inferred from Electronic Annotation
with EBI:KW-0539
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries. UniProtKB
perinuclear region of cytoplasm IEA: Inferred from Electronic Annotation
with EBI:SL-0198
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries. UniProtKB

*** Computational GO Annotations are predictions. These annotations are NOT reviewed by a curator. Currently, all computational GO annotations for S. cerevisiae are assigned by an external source (for example, the Gene Ontology Annotation (GOA) project of the European Bioinformatics Institute (EBI)).