P52488 (UBA2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-activating enzyme E1-like

Alternative name(s):
Polymerase-interacting protein 2
SMT3-activating enzyme subunit 2

Gene names

Name:	UBA2
Synonyms:	PIP2, UAL1
Ordered Locus Names:	YDR390C
ORF Names:	D9509.10

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	636 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The dimeric enzyme acts as a SMT3 E1 ligase. It mediates ATP-dependent activation of SMT3 and formation of a thioester with a conserved cysteine residue on AOS1. Ref.6
Pathway	Protein modification; protein sumoylation.
Subunit structure	Heterodimer of UBA2 and AOS1. The complex binds SMT3.
Subcellular location	Nucleus.
Post-translational modification	Multiubiquitinated in vivo.
Miscellaneous	Present with 18800 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the ubiquitin-activating E1 family.
Sequence caution	The sequence CAA82980.1 differs from that shown. Reason: Frameshift at positions 180 and 268.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Nucleus
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein sumoylation Inferred from direct assay Ref.6. Source: SGD
Cellular_component	SUMO activating enzyme complex Inferred from physical interaction Ref.6. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW SUMO activating enzyme activity Inferred from physical interaction Ref.6. Source: SGD ligase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 636

636

Ubiquitin-activating enzyme E1-like

PRO_0000194979

Regions

Nucleotide binding

28 – 33

6

ATP By similarity

Nucleotide binding

60 – 63

4

ATP By similarity

Nucleotide binding

121 – 126

6

ATP By similarity

Motif

619 – 622

4

Nuclear localization signal Potential

Sites

Active site

177

1

Glycyl thioester intermediate By similarity

Metal binding

162

1

Zinc By similarity

Metal binding

165

1

Zinc By similarity

Metal binding

435

1

Zinc By similarity

Metal binding

438

1

Zinc By similarity

Binding site

52

1

ATP By similarity

Binding site

76

1

ATP By similarity

Amino acid modifications

Modified residue

288

1

Phosphothreonine Ref.8

Modified residue

439

1

Phosphoserine Ref.8

Experimental info

Mutagenesis

177

1

C → A or S: Loss of function.

Secondary structure

1

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636

Helix Strand Turn

Details...

Beta strand

442 – 448

7

Helix

450 – 455

6

Helix

458 – 469

12

Beta strand

473 – 479

7

Turn

480 – 483

4

Beta strand

484 – 488

5

Turn

493 – 496

4

Turn

499 – 503

5

Beta strand

509 – 515

7

Beta strand

518 – 522

5

Beta strand

525 – 531

7

Beta strand

535 – 538

4

Beta strand

549 – 551

3

Sequences

	Sequence		Length	Mass (Da)
	P52488 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: DBF800E1458B3B10	FASTA	636	71,259
	10 20 30 40 50 60 MPRETSLVTI IGEDSYKKLR SSRCLLVGAG GIGSELLKDI ILMEFGEIHI VDLDTIDLSN 70 80 90 100 110 120 LNRQFLFRQK DIKQPKSTTA VKAVQHFNNS KLVPYQGNVM DISTFPLHWF EQFDIIFNAL 130 140 150 160 170 180 DNLAARRYVN KISQFLSLPL IESGTAGFDG YMQPIIPGKT ECFECTKKET PKTFPVCTIR 190 200 210 220 230 240 STPSQPIHCI VWAKNFLFNQ LFASETSGNE DDNNQDWGTD DAEEIKRIKQ ETNELYELQK 250 260 270 280 290 300 IIISRDASRI PEILNKLFIQ DINKLLAIEN LWKTRTKPVP LSDSQINTPT KTAQSASNSV 310 320 330 340 350 360 GTIQEQISNF INITQKLMDR YPKEQNHIEF DKDDADTLEF VATAANIRSH IFNIPMKSVF 370 380 390 400 410 420 DIKQIAGNII PAIATTNAIV AGASSLISLR VLNLLKYAPT TKYTDLNMAF TAKASNLSQN 430 440 450 460 470 480 RYLSNPKLAP PNKNCPVCSK VCRGVIKLSS DCLNKMKLSD FVVLIREKYS YPQDISLLDA 490 500 510 520 530 540 SNQRLLFDYD FEDLNDRTLS EINLGNGSII LFSDEEGDTM IRKAIELFLD VDDELPCNTC 550 560 570 580 590 600 SLPDVEVPLI KANNSPSKNE EEEKNEKGAD VVATTNSHGK DGIVILDDDE GEITIDAEPI 610 620 630 NGSKKRPVDT EISEAPSNKR TKLVNEPTNS DIVELD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An essential yeast gene encoding a homolog of ubiquitin-activating enzyme." Dohmen R.J., Stappen R., McGrath J.P., Forrova H., Kolarov J., Goffeau A., Varshavsky A. J. Biol. Chem. 270:18099-18109(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Kolarov J. Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	del Olmo M., Gross S., Moore C.L. Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 200060 / W303.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer." Johnson E.S., Schwienhorst I., Dohmen R.J., Blobel G. EMBO J. 16:5509-5519(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-288 AND SER-439, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z48725 Genomic DNA. Translation: CAA88617.1.
Z30326 Genomic DNA. Translation: CAA82980.1. Frameshift.
U17263 Genomic DNA. Translation: AAB46626.1.
U32274 Genomic DNA. Translation: AAB64832.1.
BK006938 Genomic DNA. Translation: DAA12234.1.

PIR

A57178.

RefSeq

NP_010678.3. NM_001180698.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ONG	X-ray	2.30	A/C	439-563	[»]
3ONH	X-ray	1.60	A	439-563	[»]

ProteinModelPortal

P52488.

SMR

P52488. Positions 19-552.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2296N.

IntAct

P52488. 7 interactions.

MINT

MINT-657883.

STRING

4932.YDR390C.

Proteomic databases

PaxDb

P52488.

PeptideAtlas

P52488.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR390C; YDR390C; YDR390C.

GeneID

851998.

KEGG

sce:YDR390C.

Organism-specific databases

CYGD

YDR390c.

SGD

S000002798. UBA2.

Phylogenomic databases

eggNOG

COG0476.

GeneTree

ENSGT00550000074924.

HOGENOM

HOG000216514.

KO

K10685.

OMA

YGEIHIV.

OrthoDB

EOG43BQX3.

Enzyme and pathway databases

BioCyc

YEAST:G3O-29938-MONOMER.

UniPathway

UPA00886.

Gene expression databases

Genevestigator

P52488.

GermOnline

YDR390C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.10.3240.10. 1 hit.
3.40.50.720. 2 hits.

InterPro

IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR023280. Ub-like_act_enz_cat_cys_dom.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018074. UBQ-activ_enz_E1_AS.
[Graphical view]

Pfam

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

SUPFAM

SSF69572. MoeB. 1 hit.

PROSITE

PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

970178.

Entry information

Entry name

UBA2_YEAST

Accession

Primary (citable) accession number: P52488
Secondary accession number(s): D6VT24

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 128 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program