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Q8TBC4 (UBA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:UBA3
Synonyms:UBE1C
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8

Enzyme regulation

Binding of TP53BP2 to the regulatory subunit NAE1 decreases activity.

Pathway

Protein modification; protein neddylation.

Subunit structure

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. Ref.8

Tissue specificity

Ubiquitously expressed. Ref.6

Miscellaneous

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

Sequence similarities

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

Sequence caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RAD23BP547272EBI-717567,EBI-954531
UBE2MP610812EBI-717567,EBI-1041660

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8TBC4-1)

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.
Isoform 2 (identifier: Q8TBC4-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 463462NEDD8-activating enzyme E1 catalytic subunit
PRO_0000194941

Regions

Nucleotide binding100 – 12425ATP
Nucleotide binding148 – 17124ATP
Region53 – 7018Interaction with UBE2M N-terminus
Region157 – 1615Interaction with UBE2M N-terminus
Region192 – 21726Interaction with UBE2M N-terminus
Region227 – 2293Interaction with NEDD8
Region242 – 2487Interaction with NAE1
Region292 – 2954Interaction with NAE1
Region331 – 3388Interaction with UBE2M N-terminus
Region352 – 3576Interaction with NEDD8
Region368 – 46396Interaction with UBE2M core domain

Sites

Active site2371Glycyl thioester intermediate
Site2111Determines specificity for NEDD8

Amino acid modifications

Modified residue21N-acetylalanine Ref.10

Natural variations

Alternative sequence8 – 2114Missing in isoform 2.
VSP_041127
Natural variant91K → R. Ref.5 Ref.6
Corresponds to variant rs17852113 [ dbSNP | Ensembl ].
VAR_023945

Experimental info

Mutagenesis651F → G: Reduces affinity for UBE2M. Ref.13
Mutagenesis1481I → A: No effect on NEDD8 adenylation. Ref.12
Mutagenesis160 – 1612HI → AA: Reduces affinity for UBE2M.
Mutagenesis1671D → A: Abolishes NEDD8 adenylation. Ref.12
Mutagenesis1921P → A: Reduces affinity for UBE2M; when associated with A-195 and A-197. Ref.13
Mutagenesis1951I → A: Reduces affinity for UBE2M; when associated with A-192 and A-197. Ref.13
Mutagenesis1971P → A: Reduces affinity for UBE2M; when associated with A-192 and A-195. Ref.13
Mutagenesis2111R → Q: Abolishes specificity for NEDD8. Ref.11
Mutagenesis2141L → A: Reduces affinity for UBE2M; when associated with A-217. Ref.13
Mutagenesis2171M → A: Reduces affinity for UBE2M; when associated with A-214. Ref.13
Mutagenesis227 – 2282LY → DD: Strongly reduces NEDD8 adenylation.
Mutagenesis2371C → S: Abolishes thioester intermediate formation. Ref.6
Mutagenesis2381T → A: No effect on NEDD8 adenylation; impairs thioester intermediate formation. Ref.12
Mutagenesis3101I → A: No effect on NEDD8 adenylation or thioester intermediate formation; impairs NEDD8 transfer to UBE2M. Ref.12
Mutagenesis3311I → A: Reduces affinity for UBE2M. Ref.13
Mutagenesis352 – 3576YTYTFE → ATATA: Abolishes NEDD8 adenylation. Ref.12
Mutagenesis3681S → P: Impairs NEDD8 transfer to UBE2M. Ref.14
Mutagenesis3691Q → P: No effect on NEDD8 transfer to UBE2M. Ref.14
Mutagenesis3701L → P: Impairs NEDD8 transfer to UBE2M. Ref.14
Mutagenesis4121T → A: Impairs NEDD8 transfer to UBE2M. Ref.14
Mutagenesis4151L → A: Impairs NEDD8 transfer to UBE2M. Ref.14
Mutagenesis4181V → A: Impairs NEDD8 transfer to UBE2M. Ref.14
Mutagenesis4211I → A: Impairs NEDD8 transfer to UBE2M. Ref.14
Mutagenesis4241R → A: No effect on NEDD8 transfer to UBE2M. Ref.14
Sequence conflict1461N → Y in CAB55996. Ref.1
Sequence conflict2711D → G in CAB55996. Ref.1

Secondary structure

................................................................................... 463
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 4C16DC0EEDE31A76

FASTA46351,852
        10         20         30         40         50         60 
MADGEEPEKK RRRIEELLAE KMAVDGGCGD TGDWEGRWNH VKKFLERSGP FTHPDFEPST 

        70         80         90        100        110        120 
ESLQFLLDTC KVLVIGAGGL GCELLKNLAL SGFRQIHVID MDTIDVSNLN RQFLFRPKDI 

       130        140        150        160        170        180 
GRPKAEVAAE FLNDRVPNCN VVPHFNKIQD FNDTFYRQFH IIVCGLDSII ARRWINGMLI 

       190        200        210        220        230        240 
SLLNYEDGVL DPSSIVPLID GGTEGFKGNA RVILPGMTAC IECTLELYPP QVNFPMCTIA 

       250        260        270        280        290        300 
SMPRLPEHCI EYVRMLQWPK EQPFGEGVPL DGDDPEHIQW IFQKSLERAS QYNIRGVTYR 

       310        320        330        340        350        360 
LTQGVVKRII PAVASTNAVI AAVCATEVFK IATSAYIPLN NYLVFNDVDG LYTYTFEAER 

       370        380        390        400        410        420 
KENCPACSQL PQNIQFSPSA KLQEVLDYLT NSASLQMKSP AITATLEGKN RTLYLQSVTS 

       430        440        450        460 
IEERTRPNLS KTLKELGLVD GQELAVADVT TPQTVLFKLH FTS 

« Hide

Isoform 2 [UniParc].

Checksum: C624B0B917B2482B
Show »

FASTA44950,072

References

« Hide 'large scale' references
[1]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A new NEDD8-ligating system for cullin-4A."
Osaka F., Kawasaki H., Aida N., Saeki M., Chiba T., Kawashima S., Tanaka K., Kato S.
Genes Dev. 12:2263-2268(1998) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2909.1. [Q8TBC4-1]
CCDS2910.1. [Q8TBC4-2]
PIRT17306.
RefSeqNP_003959.3. NM_003968.3. [Q8TBC4-1]
NP_937838.1. NM_198195.1. [Q8TBC4-2]
UniGeneHs.154320.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ8TBC4.
SMRQ8TBC4. Positions 33-463.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114503. 26 interactions.
IntActQ8TBC4. 12 interactions.
MINTMINT-1375257.
STRING9606.ENSP00000354340.

Chemistry

ChEMBLCHEMBL2016430.

PTM databases

PhosphoSiteQ8TBC4.

Polymorphism databases

DMDM83305811.

Proteomic databases

MaxQBQ8TBC4.
PaxDbQ8TBC4.
PRIDEQ8TBC4.

Protocols and materials databases

DNASU9039.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000349511; ENSP00000340041; ENSG00000144744. [Q8TBC4-2]
ENST00000361055; ENSP00000354340; ENSG00000144744. [Q8TBC4-1]
GeneID9039.
KEGGhsa:9039.
UCSCuc003dno.3. human. [Q8TBC4-1]
uc003dnq.3. human. [Q8TBC4-2]

Organism-specific databases

CTD9039.
GeneCardsGC03M069103.
HGNCHGNC:12470. UBA3.
HPAHPA034873.
HPA034874.
MIM603172. gene.
neXtProtNX_Q8TBC4.
PharmGKBPA162407622.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0476.
HOGENOMHOG000166793.
HOVERGENHBG082736.
InParanoidQ8TBC4.
KOK10686.
OMADHIQWIF.
PhylomeDBQ8TBC4.
TreeFamTF300499.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
UniPathwayUPA00885.

Gene expression databases

ArrayExpressQ8TBC4.
BgeeQ8TBC4.
CleanExHS_UBA3.
GenevestigatorQ8TBC4.

Family and domain databases

Gene3D1.10.10.520. 1 hit.
3.10.20.260. 1 hit.
3.40.50.720. 2 hits.
InterProIPR014929. 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]
PfamPF08825. E2_bind. 1 hit.
PF00899. ThiF. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 1 hit.
[Graphical view]
SUPFAMSSF69572. SSF69572. 1 hit.
PROSITEPS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBA3. human.
EvolutionaryTraceQ8TBC4.
GeneWikiUBE1C.
GenomeRNAi9039.
NextBio33859.
PROQ8TBC4.
SOURCESearch...

Entry information

Entry nameUBA3_HUMAN
AccessionPrimary (citable) accession number: Q8TBC4
Secondary accession number(s): A6NLB5 expand/collapse secondary AC list , A8K027, O76088, Q9NTU3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: December 6, 2005
Last modified: July 9, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM