Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5U300 (UBA1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-like modifier-activating enzyme 1
Alternative name(s):
Ubiquitin-activating enzyme E1
Gene names
Name:Uba1
Synonyms:Ube1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1058 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP By similarity.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Monomer. Interacts with GAN (via BTB domain) By similarity. UniProtKB Q02053

Post-translational modification

ISGylated By similarity.

Miscellaneous

There are two active sites within the E1 molecule, allowing it to accommodate two ubiquitin moieties at a time, with a new ubiquitin forming an adenylate intermediate as the previous one is transferred to the thiol site.

Sequence similarities

Belongs to the ubiquitin-activating E1 family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein ubiquitination

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

small protein activating enzyme activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 10581057Ubiquitin-like modifier-activating enzyme 1
PRO_0000365096

Regions

Repeat63 – 1991371-1
Repeat459 – 6111531-2
Nucleotide binding478 – 50730ATP By similarity UniProtKB Q02053
Region63 – 6115492 approximate repeats

Sites

Active site6321Glycyl thioester intermediate By similarity UniProtKB Q02053

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue131Phosphoserine By similarity UniProtKB Q02053
Modified residue461Phosphoserine By similarity UniProtKB Q02053
Modified residue551Phosphotyrosine By similarity UniProtKB Q02053
Modified residue5281N6-succinyllysine By similarity
Modified residue6711N6-acetyllysine By similarity
Modified residue8001Phosphothreonine By similarity UniProtKB Q02053
Modified residue8101Phosphoserine By similarity
Modified residue8161Phosphoserine By similarity UniProtKB Q02053
Modified residue8201Phosphoserine By similarity UniProtKB Q02053
Modified residue8351Phosphoserine By similarity UniProtKB Q02053
Modified residue9801N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5U300 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: FAC21190A3014F79

FASTA1,058117,788
        10         20         30         40         50         60 
MSSSPLSKKR RVSGPDPKPG SNCSSAQSVL SEVSSVPTNG MAKNGSEADI DESLYSRQLY 

        70         80         90        100        110        120 
VLGHEAMKML QTSSVLVSGL RGLGVEIAKN IILGGVKAVT LHDQGTTQWA DLSSQFYLRE 

       130        140        150        160        170        180 
EDIGKNRAEV SQPRLAELNS YVPVTAYTGP LVEDFLSGFQ VVVLTNSPLE EQLRVGEFCH 

       190        200        210        220        230        240 
SRGIKLVVAD TRGLFGQLFC DFGEEMVLTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH 

       250        260        270        280        290        300 
GFETGDFVSF SEVQGMVQLN GCQPIEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK 

       310        320        330        340        350        360 
ISFKSLPASL AEPDFVMTDF AKYSRPAQLH IGFQALHQFC AQHNRPPRPR NEEDATELVT 

       370        380        390        400        410        420 
LAQAVNARSP PAVQQDNVDE DLIRKLAYVA AGDLAPINAF IGGLAAQEVM KACSGKFMPI 

       430        440        450        460        470        480 
MQWLYFDALE CLPEDKEALT EDKCLPRQNR YDGQVAVFGS DLQEKLGKQK YFLVGAGAIG 

       490        500        510        520        530        540 
CELLKNFAMI GLGCGEGGEV VVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN 

       550        560        570        580        590        600 
PYIQVTSHQN RVGPDTERIY DDDFFQNLDG VANALDNVDA RMYMDRRCVY YRKPLLESGT 

       610        620        630        640        650        660 
LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD EFEGLFKQPA 

       670        680        690        700        710        720 
ENVNQYLTDS KFVERTLRLA GTQPLEVLEA VQRSLVLQRP QTWGDCVTWA CHHWHTQYCN 

       730        740        750        760        770        780 
NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH PLTFDVNNTL HLDYVMAAAN LFAQTYGLTG 

       790        800        810        820        830        840 
SQDRAAVASL LQSVQVPEFT PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPDKLP 

       850        860        870        880        890        900 
GFKMYPIDFE KDDDSNFHMD FIVAASNLRA ENYDISPADR HKSKLIAGKI IPAIATTTAA 

       910        920        930        940        950        960 
VVGLVCLELY KVVQGHQQLD SYKNGFLNLA LPFFGFSEPL AAPRHQYYNQ EWTLWDRFEV 

       970        980        990       1000       1010       1020 
QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF FMPAAKLKER LDQPMTEIVS 

      1030       1040       1050 
RVSKRKLGRH VRALVLELCC NDESGEDVEV PYVRYTIR 

« Hide

References

« Hide 'large scale' references
[1]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Strain: Brown Norway.
Tissue: Kidney.
[3]Maurya D.K., Bhargava P.
Submitted (JAN-2009) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH474009 Genomic DNA. Translation: EDL97701.1.
CH474009 Genomic DNA. Translation: EDL97702.1.
BC085791 mRNA. Translation: AAH85791.1.
RefSeqNP_001014102.1. NM_001014080.1.
XP_006256674.1. XM_006256612.1.
UniGeneRn.11800.

3D structure databases

ProteinModelPortalQ5U300.
SMRQ5U300. Positions 48-1057.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid260716. 3 interactions.
STRING10116.ENSRNOP00000033950.

PTM databases

PhosphoSiteQ5U300.

Proteomic databases

PaxDbQ5U300.
PRIDEQ5U300.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000031115; ENSRNOP00000033950; ENSRNOG00000019164.
GeneID314432.
KEGGrno:314432.
UCSCRGD:1359327. rat.

Organism-specific databases

CTD7317.
RGD1359327. Uba1.

Phylogenomic databases

eggNOGCOG0476.
GeneTreeENSGT00390000016689.
HOGENOMHOG000167329.
HOVERGENHBG054199.
InParanoidQ5U300.
KOK03178.
OMAPFFAFSE.
OrthoDBEOG74R1PV.
TreeFamTF300586.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

GenevestigatorQ5U300.

Family and domain databases

Gene3D1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.
InterProIPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_e1_C.
IPR023280. Ub-like_act_enz_cat_cys_dom.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018075. UBQ-activ_enz_E1.
IPR018074. UBQ-activ_enz_E1_AS.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamPF00899. ThiF. 2 hits.
PF09358. UBA_e1_C. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 2 hits.
[Graphical view]
PRINTSPR01849. UBIQUITINACT.
SMARTSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMSSF69572. SSF69572. 2 hits.
TIGRFAMsTIGR01408. Ube1. 1 hit.
PROSITEPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio667673.
PROQ5U300.

Entry information

Entry nameUBA1_RAT
AccessionPrimary (citable) accession number: Q5U300
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: December 7, 2004
Last modified: March 19, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways