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Protein

NEDD8-activating enzyme E1 catalytic subunit

Gene

Uba3

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

Functioni

Catalytic 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. Down-regulates steroid receptor activity. Necessary for cell cycle progression.1 Publication

Enzyme regulationi

Binding of TP53BP2 to the regulatory subunit NAE1 decreases 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei211 – 2111Determines specificity for NEDD8By similarity
Active sitei237 – 2371Glycyl thioester intermediatePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi100 – 12425ATPBy similarityAdd
BLAST
Nucleotide bindingi148 – 17124ATPBy similarityAdd
BLAST

GO - Molecular functioni

  • acid-amino acid ligase activity Source: InterPro
  • ATP binding Source: UniProtKB-KW
  • ligand-dependent nuclear receptor binding Source: RGD
  • NEDD8 activating enzyme activity Source: RGD
  • protein heterodimerization activity Source: RGD

GO - Biological processi

  • endomitotic cell cycle Source: Ensembl
  • negative regulation of transcription, DNA-templated Source: RGD
  • protein neddylation Source: RGD
  • regulation of cell cycle Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-RNO-5676590. NIK-->noncanonical NF-kB signaling.
R-RNO-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00885.

Names & Taxonomyi

Protein namesi
Recommended name:
NEDD8-activating enzyme E1 catalytic subunit (EC:6.3.2.-)
Alternative name(s):
NEDD8-activating enzyme E1C
Ubiquitin-activating enzyme E1C
Ubiquitin-like modifier-activating enzyme 3
Short name:
Ubiquitin-activating enzyme 3
Gene namesi
Name:Uba3
Synonyms:Ube1c
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi621084. Uba3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 462461NEDD8-activating enzyme E1 catalytic subunitPRO_0000194944Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ99MI7.
PRIDEiQ99MI7.

PTM databases

iPTMnetiQ99MI7.
PhosphoSiteiQ99MI7.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

ExpressionAtlasiQ99MI7. baseline and differential.
GenevisibleiQ99MI7. RN.

Interactioni

Subunit structurei

Heterodimer of UBA3 and NAE1. Interacts with NEDD8, UBE2F and UBE2M (By similarity). Binds ESR1 and ESR2 with bound steroid ligand. Interacts with TBATA (By similarity).By similarity

GO - Molecular functioni

  • ligand-dependent nuclear receptor binding Source: RGD
  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi250766. 2 interactions.
STRINGi10116.ENSRNOP00000008893.

Structurei

3D structure databases

ProteinModelPortaliQ99MI7.
SMRiQ99MI7. Positions 33-462.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 7018Interaction with UBE2M N-terminusBy similarityAdd
BLAST
Regioni157 – 1615Interaction with UBE2M N-terminusBy similarity
Regioni192 – 21726Interaction with UBE2M N-terminusBy similarityAdd
BLAST
Regioni227 – 2293Interaction with NEDD8By similarity
Regioni242 – 2487Interaction with NAE1By similarity
Regioni292 – 2954Interaction with NAE1By similarity
Regioni331 – 3388Interaction with UBE2M N-terminusBy similarity
Regioni352 – 3576Interaction with NEDD8By similarity
Regioni368 – 46295Interaction with UBE2M core domainBy similarityAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2015. Eukaryota.
COG0476. LUCA.
HOGENOMiHOG000166793.
HOVERGENiHBG082736.
InParanoidiQ99MI7.
KOiK10686.
OrthoDBiEOG78WKRM.
PhylomeDBiQ99MI7.
TreeFamiTF300499.

Family and domain databases

Gene3Di1.10.10.520. 1 hit.
3.10.20.260. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR014929. E2_binding.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR023318. Ub_act_enz_dom_a.
IPR030468. Uba3.
IPR033127. UBQ-activ_enz_E1_Cys_AS.
[Graphical view]
PANTHERiPTHR10953:SF6. PTHR10953:SF6. 1 hit.
PfamiPF08825. E2_bind. 1 hit.
PF00899. ThiF. 1 hit.
[Graphical view]
SMARTiSM01181. E2_bind. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
PROSITEiPS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q99MI7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADGEEPEKK RRRIEELLAE KMAVDGGCGD TGDWEGRWNH VKKFLERSGP
60 70 80 90 100
FTHPDFEPST ESLQFLLDTC KVLVIGAGGL GCELLKNLAL SGFRQIHVID
110 120 130 140 150
MDTIDVSNLN RQFLFRPKDV GRPKAEVAAE FLNDRVPNCN VVPHFNKIQD
160 170 180 190 200
FNDTFYRQFH IIVCGLDSII ARRWINGMLI SLLNYEDGVL DPSSIVPLID
210 220 230 240 250
GGTEGFKGNA RVILPGMTAC IECTLELYPP QVNFPMCTIA SMPRLPEHCI
260 270 280 290 300
EYVRMLQWPK EQPFGDGVPL DGDDPEHIQW IFQKSVERAS QYNIRGVTYR
310 320 330 340 350
LTQGVVKRII PAVASTNAVI AAVCATEVFK IATSAYIPLN NYLVFNDVDG
360 370 380 390 400
LYTYTFEAER KENCPACSQL PQNIQFSPSA KLQEVLDYLT NSASLQMKSP
410 420 430 440 450
AITATLEGKN RTLYLQSVTS IEERTRPNLS KTLKELGLVD GQELAVADVT
460
TPQTVLFKLH FT
Length:462
Mass (Da):51,723
Last modified:June 1, 2001 - v1
Checksum:i183FAB8C44486645
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF336829 mRNA. Translation: AAK21298.1.
BC081743 mRNA. Translation: AAH81743.1.
RefSeqiNP_476553.1. NM_057205.2.
UniGeneiRn.162761.

Genome annotation databases

EnsembliENSRNOT00000008893; ENSRNOP00000008893; ENSRNOG00000006221.
GeneIDi117553.
KEGGirno:117553.
UCSCiRGD:621084. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF336829 mRNA. Translation: AAK21298.1.
BC081743 mRNA. Translation: AAH81743.1.
RefSeqiNP_476553.1. NM_057205.2.
UniGeneiRn.162761.

3D structure databases

ProteinModelPortaliQ99MI7.
SMRiQ99MI7. Positions 33-462.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250766. 2 interactions.
STRINGi10116.ENSRNOP00000008893.

PTM databases

iPTMnetiQ99MI7.
PhosphoSiteiQ99MI7.

Proteomic databases

PaxDbiQ99MI7.
PRIDEiQ99MI7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000008893; ENSRNOP00000008893; ENSRNOG00000006221.
GeneIDi117553.
KEGGirno:117553.
UCSCiRGD:621084. rat.

Organism-specific databases

CTDi9039.
RGDi621084. Uba3.

Phylogenomic databases

eggNOGiKOG2015. Eukaryota.
COG0476. LUCA.
HOGENOMiHOG000166793.
HOVERGENiHBG082736.
InParanoidiQ99MI7.
KOiK10686.
OrthoDBiEOG78WKRM.
PhylomeDBiQ99MI7.
TreeFamiTF300499.

Enzyme and pathway databases

UniPathwayiUPA00885.
ReactomeiR-RNO-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-RNO-5676590. NIK-->noncanonical NF-kB signaling.
R-RNO-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiQ99MI7.

Gene expression databases

ExpressionAtlasiQ99MI7. baseline and differential.
GenevisibleiQ99MI7. RN.

Family and domain databases

Gene3Di1.10.10.520. 1 hit.
3.10.20.260. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR014929. E2_binding.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR023318. Ub_act_enz_dom_a.
IPR030468. Uba3.
IPR033127. UBQ-activ_enz_E1_Cys_AS.
[Graphical view]
PANTHERiPTHR10953:SF6. PTHR10953:SF6. 1 hit.
PfamiPF08825. E2_bind. 1 hit.
PF00899. ThiF. 1 hit.
[Graphical view]
SMARTiSM01181. E2_bind. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
PROSITEiPS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESR1 AND ESR2, TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Uterus.
  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: Lung.

Entry informationi

Entry nameiUBA3_RAT
AccessioniPrimary (citable) accession number: Q99MI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Arg-211 acts as a selectivity gate, preventing misactivation of ubiquitin by this NEDD8-specific E1 complex.By similarity

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.