Q8TBC4 (UBA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	UBA3
Synonyms:	UBE1C

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Cell cycle Ubl conjugation pathway
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein modification process Traceable author statement Ref.7. Source: ProtInc endomitotic cell cycle Inferred from electronic annotation. Source: Ensembl protein neddylation Inferred from electronic annotation. Source: UniProtKB-UniPathway proteolysis Traceable author statement Ref.7. Source: ProtInc regulation of cell cycle Inferred from electronic annotation. Source: Ensembl
Cellular_component	nucleus Inferred from direct assay. Source: LIFEdb
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acid-amino acid ligase activity Inferred from electronic annotation. Source: InterPro protein heterodimerization activity Inferred from physical interaction Ref.8. Source: UniProtKB small protein activating enzyme activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RAD23B	P54727	2	EBI-717567,EBI-954531
UBE2M	P61081	2	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.10

Chain

2 – 463

462

NEDD8-activating enzyme E1 catalytic subunit

PRO_0000194941

Regions

Nucleotide binding

100 – 124

25

ATP

Nucleotide binding

148 – 171

24

ATP

Region

53 – 70

18

Interaction with UBE2M N-terminus

Region

157 – 161

5

Interaction with UBE2M N-terminus

Region

192 – 217

26

Interaction with UBE2M N-terminus

Region

227 – 229

3

Interaction with NEDD8

Region

242 – 248

7

Interaction with NAE1

Region

292 – 295

4

Interaction with NAE1

Region

331 – 338

8

Interaction with UBE2M N-terminus

Region

352 – 357

6

Interaction with NEDD8

Region

368 – 463

96

Interaction with UBE2M core domain

Sites

Active site

237

1

Glycyl thioester intermediate

Site

211

1

Determines specificity for NEDD8

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.10

Natural variations

Alternative sequence

8 – 21

14

Missing in isoform 2.

VSP_041127

Natural variant

9

1

K → R. Ref.5 Ref.6
Corresponds to variant rs17852113 [ dbSNP | Ensembl ].

VAR_023945

Experimental info

Mutagenesis

65

1

F → G: Reduces affinity for UBE2M. Ref.13

Mutagenesis

148

1

I → A: No effect on NEDD8 adenylation. Ref.12

Mutagenesis

160 – 161

2

HI → AA: Reduces affinity for UBE2M.

Mutagenesis

167

1

D → A: Abolishes NEDD8 adenylation. Ref.12

Mutagenesis

192

1

P → A: Reduces affinity for UBE2M; when associated with A-195 and A-197. Ref.13

Mutagenesis

195

1

I → A: Reduces affinity for UBE2M; when associated with A-192 and A-197. Ref.13

Mutagenesis

197

1

P → A: Reduces affinity for UBE2M; when associated with A-192 and A-195. Ref.13

Mutagenesis

211

1

R → Q: Abolishes specificity for NEDD8. Ref.11

Mutagenesis

214

1

L → A: Reduces affinity for UBE2M; when associated with A-217. Ref.13

Mutagenesis

217

1

M → A: Reduces affinity for UBE2M; when associated with A-214. Ref.13

Mutagenesis

227 – 228

2

LY → DD: Strongly reduces NEDD8 adenylation.

Mutagenesis

237

1

C → S: Abolishes thioester intermediate formation. Ref.6

Mutagenesis

238

1

T → A: No effect on NEDD8 adenylation; impairs thioester intermediate formation. Ref.12

Mutagenesis

310

1

I → A: No effect on NEDD8 adenylation or thioester intermediate formation; impairs NEDD8 transfer to UBE2M. Ref.12

Mutagenesis

331

1

I → A: Reduces affinity for UBE2M. Ref.13

Mutagenesis

352 – 357

6

YTYTFE → ATATA: Abolishes NEDD8 adenylation. Ref.12

Mutagenesis

368

1

S → P: Impairs NEDD8 transfer to UBE2M. Ref.14

Mutagenesis

369

1

Q → P: No effect on NEDD8 transfer to UBE2M. Ref.14

Mutagenesis

370

1

L → P: Impairs NEDD8 transfer to UBE2M. Ref.14

Mutagenesis

412

1

T → A: Impairs NEDD8 transfer to UBE2M. Ref.14

Mutagenesis

415

1

L → A: Impairs NEDD8 transfer to UBE2M. Ref.14

Mutagenesis

418

1

V → A: Impairs NEDD8 transfer to UBE2M. Ref.14

Mutagenesis

421

1

I → A: Impairs NEDD8 transfer to UBE2M. Ref.14

Mutagenesis

424

1

R → A: No effect on NEDD8 transfer to UBE2M. Ref.14

Sequence conflict

146

1

N → Y in CAB55996. Ref.1

Sequence conflict

271

1

D → G in CAB55996. Ref.1

Secondary structure

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463

Helix Strand Turn

Details...

Turn

35 – 38

4

Helix

39 – 46

8

Helix

62 – 68

7

Beta strand

72 – 75

4

Helix

80 – 90

11

Beta strand

96 – 100

5

Helix

106 – 108

3

Turn

109 – 111

3

Helix

117 – 119

3

Helix

124 – 135

12

Beta strand

142 – 146

5

Helix

148 – 150

3

Helix

153 – 156

4

Beta strand

160 – 164

5

Helix

169 – 181

13

Beta strand

185 – 188

4

Beta strand

189 – 191

3

Helix

192 – 194

3

Beta strand

198 – 204

7

Beta strand

207 – 213

7

Turn

215 – 217

3

Helix

221 – 227

7

Helix

236 – 241

6

Helix

246 – 255

10

Helix

257 – 260

4

Helix

275 – 291

17

Helix

299 – 306

8

Helix

314 – 333

20

Beta strand

341 – 346

6

Beta strand

348 – 350

3

Beta strand

352 – 356

5

Turn

365 – 367

3

Beta strand

372 – 376

5

Beta strand

377 – 379

3

Helix

382 – 391

10

Turn

393 – 395

3

Beta strand

401 – 406

6

Beta strand

409 – 414

6

Helix

419 – 430

12

Beta strand

431 – 433

3

Helix

434 – 436

3

Helix

437 – 440

4

Beta strand

443 – 447

5

Beta strand

451 – 453

3

Beta strand

455 – 460

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 6, 2005. Version 2. Checksum: 4C16DC0EEDE31A76	FASTA	463	51,852
	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
	Isoform 2 [UniParc]. Checksum: C624B0B917B2482B	FASTA	449	50,072
	10 20 30 40 50 60 MADGEEPMAV DGGCGDTGDW EGRWNHVKKF LERSGPFTHP DFEPSTESLQ FLLDTCKVLV 70 80 90 100 110 120 IGAGGLGCEL LKNLALSGFR QIHVIDMDTI DVSNLNRQFL FRPKDIGRPK AEVAAEFLND 130 140 150 160 170 180 RVPNCNVVPH FNKIQDFNDT FYRQFHIIVC GLDSIIARRW INGMLISLLN YEDGVLDPSS 190 200 210 220 230 240 IVPLIDGGTE GFKGNARVIL PGMTACIECT LELYPPQVNF PMCTIASMPR LPEHCIEYVR 250 260 270 280 290 300 MLQWPKEQPF GEGVPLDGDD PEHIQWIFQK SLERASQYNI RGVTYRLTQG VVKRIIPAVA 310 320 330 340 350 360 STNAVIAAVC ATEVFKIATS AYIPLNNYLV FNDVDGLYTY TFEAERKENC PACSQLPQNI 370 380 390 400 410 420 QFSPSAKLQE VLDYLTNSAS LQMKSPAITA TLEGKNRTLY LQSVTSIEER TRPNLSKTLK 430 440 ELGLVDGQEL AVADVTTPQT VLFKLHFTS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	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. , 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.

PIR

T17306.

RefSeq

NP_003959.3. NM_003968.3.
NP_937838.1. NM_198195.1.

UniGene

Hs.154320.

3D structure databases

PDBe
RCSB PDB
PDBj

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	368-463	[»]
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	[»]

ProteinModelPortal

Q8TBC4.

SMR

Q8TBC4. Positions 33-463.

ModBase

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MobiDB

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Protein-protein interaction databases

BioGrid

114503. 26 interactions.

IntAct

Q8TBC4. 12 interactions.

MINT

MINT-1375257.

STRING

9606.ENSP00000354340.

Chemistry

ChEMBL

CHEMBL2016430.

PTM databases

PhosphoSite

Q8TBC4.

Polymorphism databases

DMDM

83305811.

Proteomic databases

PaxDb

Q8TBC4.

PRIDE

Q8TBC4.

Protocols and materials databases

DNASU

9039.

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000349511; ENSP00000340041; ENSG00000144744. [Q8TBC4-2]
ENST00000361055; ENSP00000354340; ENSG00000144744. [Q8TBC4-1]

GeneID

9039.

KEGG

hsa:9039.

UCSC

uc003dno.3. human. [Q8TBC4-1]
uc003dnq.3. human. [Q8TBC4-2]

Organism-specific databases

CTD

9039.

GeneCards

GC03M069103.

HGNC

HGNC:12470. UBA3.

HPA

HPA034873.
HPA034874.

MIM

603172. gene.

neXtProt

NX_Q8TBC4.

PharmGKB

PA162407622.

GenAtlas

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Phylogenomic databases

eggNOG

COG0476.

HOGENOM

HOG000166793.

HOVERGEN

HBG082736.

InParanoid

Q8TBC4.

KO

K10686.

OMA

DHIQWIF.

PhylomeDB

Q8TBC4.

TreeFam

TF300499.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

UniPathway

UPA00885.

Gene expression databases

ArrayExpress

Q8TBC4.

Bgee

Q8TBC4.

CleanEx

HS_UBA3.

Genevestigator

Q8TBC4.

Family and domain databases

Gene3D

1.10.10.520. 1 hit.
3.10.20.260. 1 hit.
3.40.50.720. 2 hits.

InterPro

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]

Pfam

PF08825. E2_bind. 1 hit.
PF00899. ThiF. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 1 hit.
[Graphical view]

SUPFAM

SSF69572. SSF69572. 1 hit.

PROSITE

PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

UBA3. human.

EvolutionaryTrace

Q8TBC4.

GeneWiki

UBE1C.

GenomeRNAi

9039.

NextBio

33859.

PRO

Q8TBC4.

SOURCE

Search...

Entry information

Entry name

UBA3_HUMAN

Accession

Primary (citable) accession number: Q8TBC4
Secondary accession number(s): A6NLB5 , A8K027, O76088, Q9NTU3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	December 6, 2005
Last modified:	April 16, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.