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Protein

NEDD8-activating enzyme E1 regulatory subunit

Gene

Nae1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Necessary for cell cycle progression through the S-M checkpoint. Overexpression of NAE1 causes apoptosis through deregulation of NEDD8 conjugation.1 Publication

Enzyme regulationi

Binding of TP53BP2 to the regulatory subunit NAE1 decreases neddylation activity.By similarity

Pathwayi: protein neddylation

This protein is involved in the pathway protein neddylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein neddylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis, Cell cycle, Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00885.

Names & Taxonomyi

Protein namesi
Recommended name:
NEDD8-activating enzyme E1 regulatory subunit
Alternative name(s):
Amyloid beta precursor protein-binding protein 1, 59 kDa
Short name:
APP-BP1
Amyloid protein-binding protein 1
Gene namesi
Name:Nae1
Synonyms:Appbp1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619945. Nae1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 534533NEDD8-activating enzyme E1 regulatory subunitPRO_0000194954Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei6 – 61N6-acetyllysineBy similarity
Modified residuei341 – 3411N6-acetyllysineBy similarity

Post-translational modificationi

Ubiquitinated by TRIP12, leading to its degradation by the proteasome.By similarity

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

PaxDbiQ9Z1A5.
PRIDEiQ9Z1A5.

PTM databases

iPTMnetiQ9Z1A5.

Expressioni

Tissue specificityi

Expressed throughout the brain. In hippocampus, strongly expressed in granule cells and in the pyramidal cell layer. Strongly expressed in the piriform cortex. In the cerebellum, expressed only in Purkinje cells.1 Publication

Interactioni

Subunit structurei

Heterodimer of UBA3 and NAE1. The complex binds NEDD8 and UBE2M. Binds APP and TP53BP2.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei211 – 2111Interaction with UBA3By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000045593.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1A5.
SMRiQ9Z1A5. Positions 9-534.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni331 – 34414Interaction with UBA3By similarityAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2016. Eukaryota.
COG0476. LUCA.
HOGENOMiHOG000216537.
HOVERGENiHBG079761.
InParanoidiQ9Z1A5.
PhylomeDBiQ9Z1A5.

Family and domain databases

Gene3Di3.40.50.720. 3 hits.
InterProiIPR030667. APP-BP1.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
[Graphical view]
PIRSFiPIRSF039099. APP-BP1. 1 hit.
SUPFAMiSSF69572. SSF69572. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9Z1A5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQQGKILKE QKYDRQLRLW GDHGQEALES AHVCLINATA TGTEILKNLV
60 70 80 90 100
LPGIGSFTII DGNQVSGEDV GNNFFLQKCS IGKNRAQAAM EFLQELNSDV
110 120 130 140 150
SGSFVEESPE NLLDNDPSFF CRFTIVVATQ LLESTLLRLA DVLWNSQIPL
160 170 180 190 200
LICRTYGLVG YMRIIIKEHP VIESHPDNAL EDLRLDKPFP ELREHFQSYD
210 220 230 240 250
LDHMEKKDHS HTPWIVIIAK YLAQWYSETN GRIPKSYKEK EDFRELIRQG
260 270 280 290 300
ILKNENGAPE DEENFEEAIK NVNTALNTTQ IPSSIEDIFN DDRCINITKQ
310 320 330 340 350
TPSFWILARA LKEFVAKEGQ GNLPVRGTIP DMIADSNKYI KLQNVYREKA
360 370 380 390 400
KKDAAAVGNH VAKLLQSCGQ APESISEKEL KLLCSNSAFL RVVRCRSLAE
410 420 430 440 450
EYGLHTVNKD EIISSMDNPD NEIVLYLMLR AVDRFHKQHG RYPGVSNYQV
460 470 480 490 500
EEDIGKLKSC LTGFLQEYGL SVMVKDDYVH EFCRYGAAEP HTVAAFLGGA
510 520 530
AAQEVIKIIT KQFVIFNNTY IYSGMSQTSA TFQL
Length:534
Mass (Da):60,383
Last modified:May 1, 1999 - v1
Checksum:i5A759E170D7A99B2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90829 mRNA. Translation: AAD09247.1.
UniGeneiRn.4279.

Genome annotation databases

UCSCiRGD:619945. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90829 mRNA. Translation: AAD09247.1.
UniGeneiRn.4279.

3D structure databases

ProteinModelPortaliQ9Z1A5.
SMRiQ9Z1A5. Positions 9-534.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000045593.

PTM databases

iPTMnetiQ9Z1A5.

Proteomic databases

PaxDbiQ9Z1A5.
PRIDEiQ9Z1A5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:619945. rat.

Organism-specific databases

RGDi619945. Nae1.

Phylogenomic databases

eggNOGiKOG2016. Eukaryota.
COG0476. LUCA.
HOGENOMiHOG000216537.
HOVERGENiHBG079761.
InParanoidiQ9Z1A5.
PhylomeDBiQ9Z1A5.

Enzyme and pathway databases

UniPathwayiUPA00885.

Miscellaneous databases

NextBioi616573.
PROiQ9Z1A5.

Family and domain databases

Gene3Di3.40.50.720. 3 hits.
InterProiIPR030667. APP-BP1.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
[Graphical view]
PIRSFiPIRSF039099. APP-BP1. 1 hit.
SUPFAMiSSF69572. SSF69572. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Localization of the amyloid protein precursor binding protein, APP-BP1, in the developing central nervous system."
    Chow N., Mobley W.C., Dreger U.C., Coopersmith R., Neve R.L.
    Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  2. "APP-BP1, a novel protein that binds to the carboxyl-terminal region of the amyloid precursor protein."
    Chow N., Korenberg J.R., Chen X.-N., Neve R.L.
    J. Biol. Chem. 271:11339-11346(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  3. "APP-BP1 mediates APP-induced apoptosis and DNA synthesis and is increased in Alzheimer's disease brain."
    Chen Y., Liu W., McPhie D.L., Hassinger L., Neve R.L.
    J. Cell Biol. 163:27-33(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH APP, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiULA1_RAT
AccessioniPrimary (citable) accession number: Q9Z1A5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 1, 1999
Last modified: May 11, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.