Reviewed, UniProtKB/Swiss-Prot P50623 (UBC9_YEAST)

Names and origin

Protein names

Recommended name:
    SUMO-conjugating enzyme UBC9
    EC=6.3.2.-
Alternative name(s):
    Ubiquitin-conjugating enzyme E2-18 kDa
    Ubiquitin-protein ligase
    Ubiquitin carrier protein 9

Gene names

Name:	UBC9
Ordered Locus Names:	YDL064W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	157 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	E2 ubiquitin-like--protein ligase mediating SUMO/Smt3 attachment to septins and PCNA. Seems to be involved in degradation of S- (CLB5) and M-phase cyclins (CLB2). Ref.3 Ref.4
Catalytic activity	ATP + SUMO + protein lysine = AMP + diphosphate + protein N-SUMOyllysine.
Pathway	Protein modification; protein sumoylation.
Subunit structure	Interacts with SIZ1. Ref.4 Ref.5
Subcellular location	Nucleus.
Miscellaneous	Present with 2600 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Ubl conjugation pathway
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	G2/M transition of mitotic cell cycle Traceable author statement. Source: SGD cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW mitotic spindle elongation Ref.1 Inferred from mutant phenotype. Source: SGD modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein sumoylation Ref.3 Inferred from direct assay. Source: SGD regulation of protein metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	condensed nuclear chromosome Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW SUMO ligase activity Ref.3 Inferred from direct assay. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-19760,EBI-19760
SMT3	Q12306	2	EBI-19760,EBI-17490

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 157

157

SUMO-conjugating enzyme UBC9

PRO_0000082556

Sites

Active site

93

1

Glycyl thioester intermediate By similarity

Secondary structure

1

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157

Helix Strand Turn

Details...

Helix

4 – 18

15

Beta strand

25 – 30

6

Beta strand

36 – 46

11

Turn

52 – 55

4

Beta strand

57 – 63

7

Turn

66 – 70

5

Beta strand

74 – 76

3

Helix

95 – 97

3

Turn

99 – 102

4

Helix

109 – 121

13

Helix

131 – 139

9

Helix

141 – 154

14

Sequences

	Sequence		Length	Mass (Da)
	P50623-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: D74EE9845BB677B4	FASTA	157	17,911
	10 20 30 40 50 60 MSSLCLQRLQ EERKKWRKDH PFGFYAKPVK KADGSMDLQK WEAGIPGKEG TNWAGGVYPI 70 80 90 100 110 120 TVEYPNEYPS KPPKVKFPAG FYHPNVYPSG TICLSILNED QDWRPAITLK QIVLGVQDLL 130 140 150 DSPNPNSPAQ EPAWRSFSRN KAEYDKKVLL QAKQYSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins." Seufert W., Futcher B., Jentsch S. Nature 373:78-81(1995) [PubMed: 7800043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p." Johnson E.S., Blobel G. J. Biol. Chem. 272:26799-26802(1997) [PubMed: 9341106] [Abstract] Cited for: FUNCTION.
[4]	"An E3-like factor that promotes SUMO conjugation to the yeast septins." Johnson E.S., Gupta A.A. Cell 106:735-744(2001) [PubMed: 11572779] [Abstract] Cited for: INTERACTION WITH SIZ1, FUNCTION.
[5]	"A novel factor required for the SUMO1/Smt3 conjugation of yeast septins." Takahashi Y., Toh-e A., Kikuchi Y. Gene 275:223-231(2001) [PubMed: 11587849] [Abstract] Cited for: INTERACTION WITH SIZ1.
[6]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X82538 Genomic DNA. Translation: CAA57888.1.
Z74112 Genomic DNA. Translation: CAA98629.1.

PIR

S52414.

RefSeq

NP_010219.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EKE	X-ray	1.90	A/B	1-157	[»]
2GJD	X-ray	1.75	A/B/C/D	1-157	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1531N.

IntAct

P50623. 7 interactions.

STRING

P50623.

Proteomic databases

PeptideAtlas

P50623.

PRIDE

P50623.

Genome annotation databases

Ensembl

YDL064W; YDL064W; YDL064W; Saccharomyces cerevisiae. [Genome view]

GeneID

851495.

KEGG

sce:YDL064W.

NMPDR

fig|4932.3.peg.959.

Organism-specific databases

CYGD

YDL064w.

SGD

S000002222. UBC9.

Phylogenomic databases

HOGENOM

P50623.

OMA

KQWRKDH

OrthoDB

EOG9QVDVD

Gene expression databases

ArrayExpress

P50623.

Genevestigator

P50623.

GermOnline

YDL064W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR016135. UBQ-conjugat/RWD-like.
IPR000608. UBQ-conjugat_E2.
[Graphical view]

Gene3D

G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.

Pfam

PF00179. UQ_con. 1 hit.
[Graphical view]

SMART

SM00212. UBCc. 1 hit.
[Graphical view]

PROSITE

PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

968831.

Entry information

Entry name

UBC9_YEAST

Accession

Primary (citable) accession number: P50623

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 24, 2009
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)