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Q8TBC4

- UBA3_HUMAN

UniProt

Q8TBC4 - UBA3_HUMAN

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Protein

NEDD8-activating enzyme E1 catalytic subunit

Gene

UBA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequences (2)
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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.3 Publications

Enzyme regulationi

Binding of TP53BP2 to the regulatory subunit NAE1 decreases activity.

Pathwayi

Protein modification; protein neddylation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei211 – 2111Determines specificity for NEDD8
Active sitei237 – 2371Glycyl thioester intermediate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi100 – 12425ATP1 PublicationAdd
BLAST
Nucleotide bindingi148 – 17124ATP1 PublicationAdd
BLAST

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. NEDD8 activating enzyme activity Source: RefGenome
  4. protein heterodimerization activity Source: UniProtKB

GO - Biological processi

  1. cellular protein modification process Source: ProtInc
  2. endomitotic cell cycle Source: Ensembl
  3. protein neddylation Source: RefGenome
  4. proteolysis Source: ProtInc
  5. 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

ReactomeiREACT_75842. 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:12470. UBA3.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: RefGenome
  2. nucleus Source: LIFEdb
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi65 – 651F → G: Reduces affinity for UBE2M. 1 Publication
Mutagenesisi148 – 1481I → A: No effect on NEDD8 adenylation. 1 Publication
Mutagenesisi160 – 1612HI → AA: Reduces affinity for UBE2M. 1 Publication
Mutagenesisi167 – 1671D → A: Abolishes NEDD8 adenylation. 1 Publication
Mutagenesisi192 – 1921P → A: Reduces affinity for UBE2M; when associated with A-195 and A-197. 1 Publication
Mutagenesisi195 – 1951I → A: Reduces affinity for UBE2M; when associated with A-192 and A-197. 1 Publication
Mutagenesisi197 – 1971P → A: Reduces affinity for UBE2M; when associated with A-192 and A-195. 1 Publication
Mutagenesisi211 – 2111R → Q: Abolishes specificity for NEDD8. 1 Publication
Mutagenesisi214 – 2141L → A: Reduces affinity for UBE2M; when associated with A-217. 1 Publication
Mutagenesisi217 – 2171M → A: Reduces affinity for UBE2M; when associated with A-214. 1 Publication
Mutagenesisi227 – 2282LY → DD: Strongly reduces NEDD8 adenylation. 1 Publication
Mutagenesisi237 – 2371C → S: Abolishes thioester intermediate formation. 1 Publication
Mutagenesisi238 – 2381T → A: No effect on NEDD8 adenylation; impairs thioester intermediate formation. 1 Publication
Mutagenesisi310 – 3101I → A: No effect on NEDD8 adenylation or thioester intermediate formation; impairs NEDD8 transfer to UBE2M. 1 Publication
Mutagenesisi331 – 3311I → A: Reduces affinity for UBE2M. 1 Publication
Mutagenesisi352 – 3576YTYTFE → ATATA: Abolishes NEDD8 adenylation. 1 Publication
Mutagenesisi368 – 3681S → P: Impairs NEDD8 transfer to UBE2M. 1 Publication
Mutagenesisi369 – 3691Q → P: No effect on NEDD8 transfer to UBE2M. 1 Publication
Mutagenesisi370 – 3701L → P: Impairs NEDD8 transfer to UBE2M. 1 Publication
Mutagenesisi412 – 4121T → A: Impairs NEDD8 transfer to UBE2M. 1 Publication
Mutagenesisi415 – 4151L → A: Impairs NEDD8 transfer to UBE2M. 1 Publication
Mutagenesisi418 – 4181V → A: Impairs NEDD8 transfer to UBE2M. 1 Publication
Mutagenesisi421 – 4211I → A: Impairs NEDD8 transfer to UBE2M. 1 Publication
Mutagenesisi424 – 4241R → A: No effect on NEDD8 transfer to UBE2M. 1 Publication

Organism-specific databases

PharmGKBiPA162407622.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 463462NEDD8-activating enzyme E1 catalytic subunitPRO_0000194941Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8TBC4.
PaxDbiQ8TBC4.
PRIDEiQ8TBC4.

PTM databases

PhosphoSiteiQ8TBC4.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ8TBC4.
CleanExiHS_UBA3.
ExpressionAtlasiQ8TBC4. baseline and differential.
GenevestigatoriQ8TBC4.

Organism-specific databases

HPAiHPA034873.
HPA034874.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
RAD23BP547272EBI-717567,EBI-954531
UBE2MP610812EBI-717567,EBI-1041660

Protein-protein interaction databases

BioGridi114503. 28 interactions.
IntActiQ8TBC4. 12 interactions.
MINTiMINT-1375257.
STRINGi9606.ENSP00000354340.

Structurei

Secondary structure

1
463
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni35 – 384Combined sources
Helixi39 – 468Combined sources
Helixi62 – 687Combined sources
Beta strandi72 – 754Combined sources
Helixi80 – 9011Combined sources
Beta strandi96 – 1005Combined sources
Helixi106 – 1083Combined sources
Turni109 – 1113Combined sources
Helixi117 – 1193Combined sources
Helixi124 – 13512Combined sources
Beta strandi142 – 1465Combined sources
Helixi148 – 1503Combined sources
Helixi153 – 1564Combined sources
Beta strandi160 – 1645Combined sources
Helixi169 – 18113Combined sources
Beta strandi185 – 1884Combined sources
Beta strandi189 – 1913Combined sources
Helixi192 – 1943Combined sources
Beta strandi198 – 2047Combined sources
Beta strandi207 – 2137Combined sources
Turni215 – 2173Combined sources
Helixi221 – 2277Combined sources
Helixi236 – 2416Combined sources
Helixi246 – 25510Combined sources
Helixi257 – 2604Combined sources
Helixi275 – 29117Combined sources
Helixi299 – 3068Combined sources
Helixi314 – 33320Combined sources
Beta strandi341 – 3466Combined sources
Beta strandi348 – 3503Combined sources
Beta strandi352 – 3565Combined sources
Turni365 – 3673Combined sources
Beta strandi372 – 3765Combined sources
Beta strandi377 – 3793Combined sources
Helixi382 – 39110Combined sources
Turni393 – 3953Combined sources
Beta strandi401 – 4066Combined sources
Beta strandi409 – 4146Combined sources
Helixi419 – 43012Combined sources
Beta strandi431 – 4333Combined sources
Helixi434 – 4363Combined sources
Helixi437 – 4404Combined sources
Beta strandi443 – 4475Combined sources
Beta strandi451 – 4533Combined sources
Beta strandi455 – 4606Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R4MX-ray3.00B/D/F/H33-463[»]
1R4NX-ray3.60B/D/F/H33-463[»]
1TT5X-ray2.60B/D33-463[»]
1Y8XX-ray2.40B368-463[»]
1YOVX-ray2.60B/D22-463[»]
2LQ7NMR-A369-463[»]
2NVUX-ray2.80B33-463[»]
3DBHX-ray2.85B/D/F/H33-463[»]
3DBLX-ray2.90B/D/F/H33-463[»]
3DBRX-ray3.05B/D/F/H33-463[»]
3FN1X-ray2.50A368-463[»]
3GZNX-ray3.00B/D1-463[»]
ProteinModelPortaliQ8TBC4.
SMRiQ8TBC4. Positions 33-463.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8TBC4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 7018Interaction with UBE2M N-terminusAdd
BLAST
Regioni157 – 1615Interaction with UBE2M N-terminus
Regioni192 – 21726Interaction with UBE2M N-terminusAdd
BLAST
Regioni227 – 2293Interaction with NEDD8
Regioni242 – 2487Interaction with NAE1
Regioni292 – 2954Interaction with NAE1
Regioni331 – 3388Interaction with UBE2M N-terminus
Regioni352 – 3576Interaction with NEDD8
Regioni368 – 46396Interaction with UBE2M core domainAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family. UBA3 subfamily.Curated

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00550000074831.
HOGENOMiHOG000166793.
HOVERGENiHBG082736.
InParanoidiQ8TBC4.
KOiK10686.
OMAiQFNLVIC.
PhylomeDBiQ8TBC4.
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.
IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR023318. Ub_act_enz_dom_a.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018074. UBQ-activ_enz_E1_AS.
[Graphical view]
PfamiPF08825. E2_bind. 1 hit.
PF00899. ThiF. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
PROSITEiPS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8TBC4-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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 RQFLFRPKDI 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 EQPFGEGVPL DGDDPEHIQW IFQKSLERAS 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 FTS
Length:463
Mass (Da):51,852
Last modified:December 6, 2005 - v2
Checksum:i4C16DC0EEDE31A76
GO
Isoform 2 (identifier: Q8TBC4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     8-21: Missing.

Show »
Length:449
Mass (Da):50,072
Checksum:iC624B0B917B2482B
GO

Sequence cautioni

The sequence AAC27648.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461N → Y in CAB55996. (PubMed:11230166)Curated
Sequence conflicti271 – 2711D → G in CAB55996. (PubMed:11230166)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91K → R.2 Publications
Corresponds to variant rs17852113 [ dbSNP | Ensembl ].		VAR_023945

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei8 – 2114Missing in isoform 2. 1 PublicationVSP_041127Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL117566 mRNA. Translation: CAB55996.2.
AK002159 mRNA. Translation: BAG51021.1.
AK289392 mRNA. Translation: BAF82081.1.
AC092060 Genomic DNA. No translation available.
AC109587 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW65470.1.
BC022853 mRNA. Translation: AAH22853.1.
AF046024 mRNA. Translation: AAC27648.1. Different initiation.
AB012190 mRNA. Translation: BAA33144.1.
CCDSiCCDS2909.1. [Q8TBC4-1]
CCDS2910.1. [Q8TBC4-2]
PIRiT17306.
RefSeqiNP_003959.3. NM_003968.3. [Q8TBC4-1]
NP_937838.1. NM_198195.1. [Q8TBC4-2]
UniGeneiHs.154320.

Genome annotation databases

EnsembliENST00000349511; ENSP00000340041; ENSG00000144744. [Q8TBC4-2]
ENST00000361055; ENSP00000354340; ENSG00000144744. [Q8TBC4-1]
GeneIDi9039.
KEGGihsa:9039.
UCSCiuc003dno.3. human. [Q8TBC4-1]
uc003dnq.3. human. [Q8TBC4-2]

Polymorphism databases

DMDMi83305811.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 AL117566 mRNA. Translation: CAB55996.2 .
AK002159 mRNA. Translation: BAG51021.1 .
AK289392 mRNA. Translation: BAF82081.1 .
AC092060 Genomic DNA. No translation available.
AC109587 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW65470.1 .
BC022853 mRNA. Translation: AAH22853.1 .
AF046024 mRNA. Translation: AAC27648.1 . Different initiation.
AB012190 mRNA. Translation: BAA33144.1 .
CCDSi CCDS2909.1. [Q8TBC4-1 ]
CCDS2910.1. [Q8TBC4-2 ]
PIRi T17306.
RefSeqi NP_003959.3. NM_003968.3. [Q8TBC4-1 ]
NP_937838.1. NM_198195.1. [Q8TBC4-2 ]
UniGenei Hs.154320.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1R4M X-ray 3.00 B/D/F/H 33-463 [» ]
1R4N X-ray 3.60 B/D/F/H 33-463 [» ]
1TT5 X-ray 2.60 B/D 33-463 [» ]
1Y8X X-ray 2.40 B 368-463 [» ]
1YOV X-ray 2.60 B/D 22-463 [» ]
2LQ7 NMR - A 369-463 [» ]
2NVU X-ray 2.80 B 33-463 [» ]
3DBH X-ray 2.85 B/D/F/H 33-463 [» ]
3DBL X-ray 2.90 B/D/F/H 33-463 [» ]
3DBR X-ray 3.05 B/D/F/H 33-463 [» ]
3FN1 X-ray 2.50 A 368-463 [» ]
3GZN X-ray 3.00 B/D 1-463 [» ]
ProteinModelPortali Q8TBC4.
SMRi Q8TBC4. Positions 33-463.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114503. 28 interactions.
IntActi Q8TBC4. 12 interactions.
MINTi MINT-1375257.
STRINGi 9606.ENSP00000354340.

Chemistry

ChEMBLi CHEMBL2016430.

PTM databases

PhosphoSitei Q8TBC4.

Polymorphism databases

DMDMi 83305811.

Proteomic databases

MaxQBi Q8TBC4.
PaxDbi Q8TBC4.
PRIDEi Q8TBC4.

Protocols and materials databases

DNASUi 9039.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000349511 ; ENSP00000340041 ; ENSG00000144744 . [Q8TBC4-2 ]
ENST00000361055 ; ENSP00000354340 ; ENSG00000144744 . [Q8TBC4-1 ]
GeneIDi 9039.
KEGGi hsa:9039.
UCSCi uc003dno.3. human. [Q8TBC4-1 ]
uc003dnq.3. human. [Q8TBC4-2 ]

Organism-specific databases

CTDi 9039.
GeneCardsi GC03M069103.
HGNCi HGNC:12470. UBA3.
HPAi HPA034873.
HPA034874.
MIMi 603172. gene.
neXtProti NX_Q8TBC4.
PharmGKBi PA162407622.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0476.
GeneTreei ENSGT00550000074831.
HOGENOMi HOG000166793.
HOVERGENi HBG082736.
InParanoidi Q8TBC4.
KOi K10686.
OMAi QFNLVIC.
PhylomeDBi Q8TBC4.
TreeFami TF300499.

Enzyme and pathway databases

UniPathwayi UPA00885 .
Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSi UBA3. human.
EvolutionaryTracei Q8TBC4.
GeneWikii UBE1C.
GenomeRNAii 9039.
NextBioi 33859.
PROi Q8TBC4.
SOURCEi Search...

Gene expression databases

Bgeei Q8TBC4.
CleanExi HS_UBA3.
ExpressionAtlasi Q8TBC4. baseline and differential.
Genevestigatori Q8TBC4.

Family and domain databases

Gene3Di 1.10.10.520. 1 hit.
3.10.20.260. 1 hit.
3.40.50.720. 2 hits.
InterProi IPR014929. E2_binding.
IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR023318. Ub_act_enz_dom_a.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018074. UBQ-activ_enz_E1_AS.
[Graphical view ]
Pfami PF08825. E2_bind. 1 hit.
PF00899. ThiF. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 1 hit.
[Graphical view ]
SUPFAMi SSF69572. SSF69572. 1 hit.
PROSITEi PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Fetal kidney.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
  3. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1), VARIANT ARG-9.
    Tissue: Prostatic adenocarcinoma.
  6. "Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway."
    Gong L., Yeh E.T.H.
    J. Biol. Chem. 274:12036-12042(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-463 (ISOFORM 1), VARIANT ARG-9, FUNCTION, MUTAGENESIS OF CYS-237, TISSUE SPECIFICITY.
    Tissue: Placenta.
  7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-463, FUNCTION.
  8. "Conservation in the mechanism of Nedd8 activation by the human AppBp1-Uba3 heterodimer."
    Bohnsack R.N., Haas A.L.
    J. Biol. Chem. 278:26823-26830(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NAE1.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1."
    Walden H., Podgorski M.S., Huang D.T., Miller D.W., Howard R.J., Minor D.L. Jr., Holton J.M., Schulman B.A.
    Mol. Cell 12:1427-1437(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 33-463 IN COMPLEX WITH NAE1; NEDD8 AND ATP, MUTAGENESIS OF ARG-211.
  12. "Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8."
    Walden H., Podgorski M.S., Schulman B.A.
    Nature 422:330-334(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 24-463 IN COMPLEX WITH NAE1, MUTAGENESIS OF ILE-148; ASP-167; 227-LEU-TYR-228; THR-238; ILE-310 AND 352-TYR--TYR-357.
  13. "A unique E1-E2 interaction required for optimal conjugation of the ubiquitin-like protein NEDD8."
    Huang D.T., Miller D.W., Mathew R., Cassell R., Holton J.M., Roussel M.F., Schulman B.A.
    Nat. Struct. Mol. Biol. 11:927-935(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 33-463 IN COMPLEX WITH NAE1 AND UBE2M, MUTAGENESIS OF PHE-65; 160-HIS-ILE-161; PRO-192; ILE-195; PRO-197; LEU-214; MET-217 AND ILE-331.
  14. "Structural basis for recruitment of Ubc12 by an E2 binding domain in NEDD8's E1."
    Huang D.T., Paydar A., Zhuang M., Waddell M.B., Holton J.M., Schulman B.A.
    Mol. Cell 17:341-350(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 368-463 IN COMPLEX WITH UBE2M, MUTAGENESIS OF SER-368; GLN-369; LEU-370; THR-412; LEU-415; VAL-418; ILE-421 AND ARG-424.
  15. "E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification."
    Huang D.T., Ayrault O., Hunt H.W., Taherbhoy A.M., Duda D.M., Scott D.C., Borg L.A., Neale G., Murray P.J., Roussel M.F., Schulman B.A.
    Mol. Cell 33:483-495(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 368-420 IN COMPLEX WITH UBE2F.
+Additional computationally mapped references.

Entry informationi

Entry nameiUBA3_HUMAN
AccessioniPrimary (citable) accession number: Q8TBC4
Secondary accession number(s): A6NLB5
, A8K027, O76088, Q9NTU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: December 6, 2005
Last modified: January 7, 2015
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.
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