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Protein

Ubiquitin-like modifier-activating enzyme 1

Gene

UBA1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system. 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. Essential for the formation of radiation-induced foci, timely DNA repair and for response to replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at DNA damage sites.By similarity

Catalytic activityi

ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.By similarity

Pathwayi: protein ubiquitination

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei478 – 4781ATP; via amide nitrogenBy similarity
Binding sitei504 – 5041ATPBy similarity
Binding sitei515 – 5151ATPBy similarity
Binding sitei528 – 5281ATPBy similarity
Active sitei632 – 6321Glycyl thioester intermediatePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi576 – 5772ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-like modifier-activating enzyme 1 (EC:6.2.1.45By similarity)
Alternative name(s):
Ubiquitin-activating enzyme E1
Gene namesi
Name:UBA1
Synonyms:UBE1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome X

Subcellular locationi

  • Cytoplasm By similarity
  • Mitochondrion By similarity
  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 10581057Ubiquitin-like modifier-activating enzyme 1PRO_0000328362Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei4 – 41PhosphoserineBy similarity
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei21 – 211PhosphoserineBy similarity
Modified residuei24 – 241PhosphoserineBy similarity
Modified residuei46 – 461PhosphoserineBy similarity
Modified residuei55 – 551PhosphotyrosineBy similarity
Modified residuei528 – 5281N6-succinyllysineBy similarity
Modified residuei671 – 6711N6-acetyllysineBy similarity
Modified residuei800 – 8001PhosphothreonineBy similarity
Modified residuei810 – 8101PhosphoserineBy similarity
Modified residuei816 – 8161PhosphoserineBy similarity
Modified residuei820 – 8201PhosphoserineBy similarity
Modified residuei835 – 8351PhosphoserineBy similarity
Modified residuei980 – 9801N6-acetyllysineBy similarity

Post-translational modificationi

ISGylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiA3KMV5.
PRIDEiA3KMV5.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi159880. 2 interactions.
STRINGi9913.ENSBTAP00000022299.

Structurei

3D structure databases

ProteinModelPortaliA3KMV5.
SMRiA3KMV5. Positions 48-1057.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati63 – 1991371-1Add
BLAST
Repeati459 – 6111531-2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni63 – 6115492 approximate repeatsAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2012. Eukaryota.
COG0476. LUCA.
GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
HOVERGENiHBG054199.
InParanoidiA3KMV5.
KOiK03178.
OMAiKGIPLCT.
OrthoDBiEOG74R1PV.
TreeFamiTF300586.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.
InterProiIPR032420. E1_4HB.
IPR032418. E1_FCCH.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_E1_C.
IPR019572. UBA_E1_Cys.
IPR018075. UBQ-activ_enz_E1.
IPR018074. UBQ-activ_enz_E1_CS.
IPR033127. UBQ-activ_enz_E1_Cys_AS.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamiPF16191. E1_4HB. 1 hit.
PF16190. E1_FCCH. 1 hit.
PF09358. E1_UFD. 1 hit.
PF00899. ThiF. 2 hits.
PF10585. UBA_e1_thiolCys. 1 hit.
[Graphical view]
PRINTSiPR01849. UBIQUITINACT.
SMARTiSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 2 hits.
TIGRFAMsiTIGR01408. Ube1. 1 hit.
PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A3KMV5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSPLSKKR RVSGPDPKPG SNCSPAHSVL SEVPSVPANG MAKNVSDADI
60 70 80 90 100
DEGLYSRQLY VLGHEAMKRL QTSSVLVSGL RGLGVEIAKN IILGGVKAVT
110 120 130 140 150
LHDQGTAQWA DLSSQFYLRE EDIGKNRAEV SQPRLAELNS YVPVSAYTGP
160 170 180 190 200
LVEDFLSDFQ VVVLTNSPLE DQLRVGEFCH SHGIKLVVAD TRGLFGQLFC
210 220 230 240 250
DFGEEMILTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH GFESGDFVSF
260 270 280 290 300
SEVQGMIELN GSQPMEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK
310 320 330 340 350
ISFKSLPASL AEPDFVMTDF AKYSRPAQLH IGFQALHHFC AQHGRSPRPH
360 370 380 390 400
NEEDAAELVT IAQAVNARSL PAVQQGSLDE DLIRKLAYVA AGDLAPINAF
410 420 430 440 450
IGGLAAQEVM KACSGKFMPI MQWLYFDALE CLPEDKEALT EDKCLPRQNR
460 470 480 490 500
YDGQVAVFGS DLQERLGKQK YFLVGAGAIG CELLKNFAMI GLGCAEDGEI
510 520 530 540 550
VVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN PHIRVTSHQN
560 570 580 590 600
RVGPDTERIY DDDFFQNLDG VTNALDNVDA RMYMDRRCVY YRKPLLESGT
610 620 630 640 650
LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD
660 670 680 690 700
EFEGLFKQPA ENVNQYLTDP KFVERTLRLA GTQPLEVLEA VQRSLVLQRP
710 720 730 740 750
QTWADCVTWA CHHWHTQYSN NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH
760 770 780 790 800
PLTFDVSNPL HLDYVIAAAN LFAQTYGLTG SQDRAAVATL LQSVQVPEFT
810 820 830 840 850
PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPEKLP GFKMYPIDFE
860 870 880 890 900
KDDDTNFHMD FIVAASNLRA ENYDIPPADR HKSKLIAGKI IPAIATTTAA
910 920 930 940 950
VVGLVCLELY KVVQGHRQLN SYKNGFLNLA LPFFGFSEPL AAPRHQYYNQ
960 970 980 990 1000
EWTLWDRFEV QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF
1010 1020 1030 1040 1050
FMPAAKLKER LDQPMTEIVS RVSKRKLGRH VRALVLELCC NDESGEDVEV

PYVRYTIR
Length:1,058
Mass (Da):117,830
Last modified:April 3, 2007 - v1
Checksum:iD723D3903025D982
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC133293 mRNA. Translation: AAI33294.1.
RefSeqiNP_001095947.1. NM_001102477.1.
XP_005228124.1. XM_005228067.3.
XP_005228125.1. XM_005228068.2.
XP_005228126.1. XM_005228069.2.
UniGeneiBt.48363.

Genome annotation databases

EnsembliENSBTAT00000022299; ENSBTAP00000022299; ENSBTAG00000016764.
GeneIDi282869.
KEGGibta:282869.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC133293 mRNA. Translation: AAI33294.1.
RefSeqiNP_001095947.1. NM_001102477.1.
XP_005228124.1. XM_005228067.3.
XP_005228125.1. XM_005228068.2.
XP_005228126.1. XM_005228069.2.
UniGeneiBt.48363.

3D structure databases

ProteinModelPortaliA3KMV5.
SMRiA3KMV5. Positions 48-1057.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi159880. 2 interactions.
STRINGi9913.ENSBTAP00000022299.

Proteomic databases

PaxDbiA3KMV5.
PRIDEiA3KMV5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000022299; ENSBTAP00000022299; ENSBTAG00000016764.
GeneIDi282869.
KEGGibta:282869.

Organism-specific databases

CTDi7317.

Phylogenomic databases

eggNOGiKOG2012. Eukaryota.
COG0476. LUCA.
GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
HOVERGENiHBG054199.
InParanoidiA3KMV5.
KOiK03178.
OMAiKGIPLCT.
OrthoDBiEOG74R1PV.
TreeFamiTF300586.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-BTA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

NextBioi20806397.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.
InterProiIPR032420. E1_4HB.
IPR032418. E1_FCCH.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_E1_C.
IPR019572. UBA_E1_Cys.
IPR018075. UBQ-activ_enz_E1.
IPR018074. UBQ-activ_enz_E1_CS.
IPR033127. UBQ-activ_enz_E1_Cys_AS.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamiPF16191. E1_4HB. 1 hit.
PF16190. E1_FCCH. 1 hit.
PF09358. E1_UFD. 1 hit.
PF00899. ThiF. 2 hits.
PF10585. UBA_e1_thiolCys. 1 hit.
[Graphical view]
PRINTSiPR01849. UBIQUITINACT.
SMARTiSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 2 hits.
TIGRFAMsiTIGR01408. Ube1. 1 hit.
PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal muscle.

Entry informationi

Entry nameiUBA1_BOVIN
AccessioniPrimary (citable) accession number: A3KMV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: April 3, 2007
Last modified: April 13, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.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.