NPL4/YBR170C Protein Information Help

Standard Name Npl4p 1
Systematic Name Ybr170cp
Alias Hrd4p
ORF Classification Verified
Description Substrate-recruiting cofactor of the Cdc48p-Npl4p-Ufd1p segregase; assists Cdc48p in the dislocation of misfolded, polyubiquitinated ERAD substrates that are subsequently delivered to the proteasome for degradation; also involved in the regulated destruction of resident ER membrane proteins, such as HMG-CoA reductase (Hmg1/2p) and cytoplasmic proteins (Fbp1p); role in mobilizing membrane bound transcription factors by regulated ubiquitin/proteasome-dependent processing (RUP) (2, 3, 4, 5, 6, 7)
Name Description Nuclear Protein Localization 1
Experimental Data
Molecules/cell 1050 8
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 580
Molecular Weight (Da) 65,782
Isoelectric Point (pI) 5.57

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Npl4p (InterPro)
Physical Interactions There are 73 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000053184 | P33755
MIPS: YBR170C
NCBI: 312610 | 402608 | 462739 | 536514 | 6319647 | NP_009729.1
GenBank/EMBL/DDBJ: DAA07286.1 | X72224 | X74437 | Z36039
Amino Acid Sequence (or in FASTA format)
 
       1  MLIRFRSKNG THRVSCQEND LFGTVIEKLV GNLDPNADVD TFTVCEKPGQ
      51  GIHAVSELAD RTVMDLGLKH GDMLILNYSD KPANEKDGVN VEIGSVGIDS
     101  KGIRQHRYGP LRIKELAVDE ELEKEDGLIP RQKSKLCKHG DRGMCEYCSP
     151  LPPWDKEYHE KNKIKHISFH SYLKKLNENA NKKENGSSYI SPLSEPDFRI
     201  NKRCHNGHEP WPRGICSKCQ PSAITLQQQE FRMVDHVEFQ KSEIINEFIQ
     251  AWRYTGMQRF GYMYGSYSKY DNTPLGIKAV VEAIYEPPQH DEQDGLTMDV
     301  EQVKNEMLQI DRQAQEMGLS RIGLIFTDLS DAGAGDGSVF CKRHKDSFFL
     351  SSLEVIMAAR HQTRHPNVSK YSEQGFFSSK FVTCVISGNL EGEIDISSYQ
     401  VSTEAEALVT ADMISGSTFP SMAYINDTTD ERYVPEIFYM KSNEYGITVK
     451  ENAKPAFPVD YLLVTLTHGF PNTDTETNSK FVSSTGFPWS NRQAMGQSQD
     501  YQELKKYLFN VASSGDFNLL HEKISNFHLL LYINSLQILS PDEWKLLIES
     551  AVKNEWEESL LKLVSSAGWQ TLVMILQESG *

external links for Npl4p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
Aspergillus (AspGD) BioPIXIE MIPS YeastRC Public Image Repository
Candida (CGD) CYC2008 (complexes) Pfam domains
Candida (CandidaDB) Complexome YeastRC Structure Prediction (Seattle)
YGOB DIP

YOGY GeneMANIA

References cited on this page View Complete Literature Guide for Npl4p
1) Bossie MA, et al.  (1992) A mutant nuclear protein with similarity to RNA binding proteins interferes with nuclear import in yeast. Mol Biol Cell 3(8):875-93
2) 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
3) Bays NW, et al.  (2001) HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins. Mol Biol Cell 12(12):4114-28
4) Ye Y, et al.  (2003) Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J Cell Biol 162(1):71-84
5) 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
6) 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
7) Heo JM, et al.  (2010) A stress-responsive system for mitochondrial protein degradation. Mol Cell 40(3):465-80
8) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41