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Protein

Nuclear protein localization protein 4 homolog

Gene

Nploc4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1L-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope.6 Publications

Pathwayi: proteasomal ubiquitin-dependent pathway

This protein is involved in the pathway proteasomal ubiquitin-dependent pathway, which is part of Protein degradation.
View all proteins of this organism that are known to be involved in the pathway proteasomal ubiquitin-dependent pathway and in Protein degradation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri580 – 60829RanBP2-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ATPase binding Source: ParkinsonsUK-UCL
  • protein complex binding Source: RGD
  • ubiquitin binding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: BHF-UCL
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00144.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear protein localization protein 4 homolog
Short name:
Protein NPL4
Gene namesi
Name:Nploc4
Synonyms:Npl4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620794. Nploc4.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • nucleus Source: RGD
  • UFD1-NPL4 complex Source: ParkinsonsUK-UCL
  • VCP-NPL4-UFD1 AAA ATPase complex Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 608607Nuclear protein localization protein 4 homologPRO_0000057943Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei179 – 1791N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9ES54.
PRIDEiQ9ES54.

PTM databases

PhosphoSiteiQ9ES54.

Interactioni

Subunit structurei

Heterodimer with UFD1L. The heterodimer binds ubiquitinated proteins. The heterodimer binds to VCP and inhibits Golgi membrane fusion.2 Publications

GO - Molecular functioni

  • ATPase binding Source: ParkinsonsUK-UCL
  • protein complex binding Source: RGD
  • ubiquitin binding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi250817. 8 interactions.
DIPiDIP-41365N.
IntActiQ9ES54. 5 interactions.
MINTiMINT-1610466.
STRINGi10116.ENSRNOP00000051856.

Structurei

Secondary structure

1
608
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi587 – 5893Combined sources
Beta strandi601 – 6033Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NJ3NMR-A580-608[»]
1Q5WNMR-A580-608[»]
ProteinModelPortaliQ9ES54.
SMRiQ9ES54. Positions 2-77, 578-608.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ES54.

Family & Domainsi

Domaini

Binds ubiquitinated proteins via its RanBP2-type zinc finger.

Sequence similaritiesi

Belongs to the NPL4 family.Curated
Contains 1 RanBP2-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri580 – 60829RanBP2-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2834. Eukaryota.
COG5100. LUCA.
HOGENOMiHOG000008139.
HOVERGENiHBG052659.
InParanoidiQ9ES54.
KOiK14015.
PhylomeDBiQ9ES54.

Family and domain databases

InterProiIPR016563. Npl4.
IPR007717. NPL4_C.
IPR024682. Npl4_Ub-like_dom.
IPR007716. NPL4_Zn-bd_put.
IPR029071. Ubiquitin-rel_dom.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF05021. NPL4. 1 hit.
PF11543. UN_NPL4. 1 hit.
PF05020. zf-NPL4. 1 hit.
[Graphical view]
PIRSFiPIRSF010052. Polyub_prc_Npl4. 1 hit.
SMARTiSM00547. ZnF_RBZ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF90209. SSF90209. 1 hit.
PROSITEiPS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9ES54-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAESIIIRVQ SPDGVKRITA TKRETAATFL KKVAKEFGFQ NNGFSVYINR
60 70 80 90 100
NKTGEITASS SKSLHLLKIK HGDLLFLFPS SLAGPSSEME TSTSVGLKAF
110 120 130 140 150
GAPHVVEDEI DQYLSKQDGK IYRSRDPQLC RHGPLGKCVH CVPLEPFDED
160 170 180 190 200
YLNHLEPPVK HMSFHAYIRK LTGGADKGKF VALENISCKI KSGCEGHLPW
210 220 230 240 250
PNGICTKCQP SAITLNRQKY RHVDNIMFEN HTVADRFLDF WRKTGNQHFG
260 270 280 290 300
YLYGRYTEHK DIPLGIRAEV AAIYEPPQIG TQNSLELLED PKAEVVDEIA
310 320 330 340 350
SKLGLRKVGW IFTDLVSEDT RKGTVRYSRN KDTYFLSSEE CITAGDFQNK
360 370 380 390 400
HPNICRLSPD GHFGSKFVTA VATGGPDNQV HFEGYQVSNQ CMALVRDECL
410 420 430 440 450
LPCKDAPELG YAKESSSEQY VPDVFYKDID KFGNEITQLA RPLPVEYLII
460 470 480 490 500
DITTTFPKDP VYTFSISQNP FPIENRDVLG ETQDFHSLAT YLSQNTSSVF
510 520 530 540 550
LDTISDFHLL LFLVTNEVMP LQDSISLLLE AVRTRNEELA QTWKKSEQWA
560 570 580 590 600
TIEQLCSTVG VQLPGLHEFG AVGGSARAAT SAMWACQHCT FMNQPGTGHC

EMCSLPRT
Length:608
Mass (Da):68,056
Last modified:January 23, 2007 - v3
Checksum:iF6F57DDEA53594A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF234600 mRNA. Translation: AAG27534.1.
BC101887 mRNA. Translation: AAI01888.1.
RefSeqiNP_542144.1. NM_080577.2.
UniGeneiRn.217306.

Genome annotation databases

GeneIDi140639.
KEGGirno:140639.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF234600 mRNA. Translation: AAG27534.1.
BC101887 mRNA. Translation: AAI01888.1.
RefSeqiNP_542144.1. NM_080577.2.
UniGeneiRn.217306.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NJ3NMR-A580-608[»]
1Q5WNMR-A580-608[»]
ProteinModelPortaliQ9ES54.
SMRiQ9ES54. Positions 2-77, 578-608.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250817. 8 interactions.
DIPiDIP-41365N.
IntActiQ9ES54. 5 interactions.
MINTiMINT-1610466.
STRINGi10116.ENSRNOP00000051856.

PTM databases

PhosphoSiteiQ9ES54.

Proteomic databases

PaxDbiQ9ES54.
PRIDEiQ9ES54.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi140639.
KEGGirno:140639.

Organism-specific databases

CTDi55666.
RGDi620794. Nploc4.

Phylogenomic databases

eggNOGiKOG2834. Eukaryota.
COG5100. LUCA.
HOGENOMiHOG000008139.
HOVERGENiHBG052659.
InParanoidiQ9ES54.
KOiK14015.
PhylomeDBiQ9ES54.

Enzyme and pathway databases

UniPathwayiUPA00144.

Miscellaneous databases

EvolutionaryTraceiQ9ES54.
NextBioi620604.
PROiQ9ES54.

Family and domain databases

InterProiIPR016563. Npl4.
IPR007717. NPL4_C.
IPR024682. Npl4_Ub-like_dom.
IPR007716. NPL4_Zn-bd_put.
IPR029071. Ubiquitin-rel_dom.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF05021. NPL4. 1 hit.
PF11543. UN_NPL4. 1 hit.
PF05020. zf-NPL4. 1 hit.
[Graphical view]
PIRSFiPIRSF010052. Polyub_prc_Npl4. 1 hit.
SMARTiSM00547. ZnF_RBZ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF90209. SSF90209. 1 hit.
PROSITEiPS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways."
    Meyer H.H., Shorter J.G., Seemann J., Pappin D., Warren G.
    EMBO J. 19:2181-2192(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 9-17; 24-31; 36-50; 71-116; 161-169; 222-236; 244-252; 357-316; 405-444; 459-477 AND 536-544, FUNCTION, HETERODIMERIZATION WITH UFD1L, INTERACTION WITH VCP, SUBCELLULAR LOCATION.
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  3. "Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly."
    Hetzer M., Meyer H.H., Walther T.C., Bilbao-Cortes D., Warren G., Mattaj I.W.
    Nat. Cell Biol. 3:1086-1091(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol."
    Ye Y., Meyer H.H., Rapoport T.A.
    Nature 414:652-656(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "The AAA-ATPase Cdc48/p97 regulates spindle disassembly at the end of mitosis."
    Cao K., Nakajima R., Meyer H.H., Zheng Y.
    Cell 115:355-367(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4."
    Meyer H.H., Wang Y., Warren G.
    EMBO J. 21:5645-5652(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 580-608, FUNCTION.
  7. "Structure and ubiquitin interactions of the conserved zinc finger domain of Npl4."
    Wang B., Alam S.L., Meyer H.H., Payne M., Stemmler T.L., Davis D.R., Sundquist W.I.
    J. Biol. Chem. 278:20225-20234(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, STRUCTURE BY NMR OF 580-608 IN COMPLEX WITH ZINC, INTERACTION WITH UBIQUITIN.

Entry informationi

Entry nameiNPL4_RAT
AccessioniPrimary (citable) accession number: Q9ES54
Secondary accession number(s): Q3T1J3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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.