P46595 (UBC4_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 4
EC=6.3.2.19

Alternative name(s):
Ubiquitin carrier protein 4
Ubiquitin-protein ligase 4

Gene names

Name:	ubc4
ORF Names:	SPBC119.02

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the covalent attachment of ubiquitin to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. Mediates ubiquitination of PEX5 By similarity.
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cyclin catabolic process Inferred from genetic interaction PubMed 12724408. Source: PomBase mitotic sister chromatid segregation Inferred from mutant phenotype PubMed 8972853. Source: PomBase nucleus-associated proteasomal ubiquitin-dependent protein catabolic process Inferred from mutant phenotype PubMed 21324894. Source: PomBase protein polyubiquitination Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytosol Inferred from direct assay PubMed 16823372. Source: PomBase nucleus Inferred from direct assay PubMed 16823372PubMed 21324894. Source: PomBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 147

147

Ubiquitin-conjugating enzyme E2 4

PRO_0000082569

Sites

Active site

85

1

Glycyl thioester intermediate By similarity

Secondary structure

1

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147

Helix Strand Turn

Details...

Helix

2 – 14

13

Beta strand

20 – 26

7

Beta strand

29 – 38

10

Turn

44 – 47

4

Beta strand

49 – 55

7

Turn

58 – 62

5

Beta strand

66 – 69

4

Helix

87 – 89

3

Turn

90 – 92

3

Helix

99 – 111

13

Helix

121 – 129

9

Helix

131 – 145

15

Sequences

	Sequence		Length	Mass (Da)
	P46595 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 3E8BADFF494A91EB	FASTA	147	16,476
	10 20 30 40 50 60 MALKRINREL ADLGKDPPSS CSAGPVGDDL FHWQATIMGP ADSPYAGGVF FLSIHFPTDY 70 80 90 100 110 120 PFKPPKVNFT TRIYHPNINS NGSICLDILR DQWSPALTIS KVLLSICSLL TDPNPDDPLV 130 140 PEIAHVYKTD RSRYELSARE WTRKYAI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Schizosaccharomyces pombe and Candida albicans cDNA homologues of the Saccharomyces cerevisiae UBC4 gene." Damagnez V., Rolfe M., Cottarel G. Gene 155:137-138(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L37384 mRNA. No translation available.
CU329671 Genomic DNA. Translation: CAA17917.1.

PIR

T39300.

RefSeq

NP_595283.1. NM_001021190.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4II2	X-ray	2.20	C	1-147	[»]

ProteinModelPortal

P46595.

SMR

P46595. Positions 1-147.

ModBase

Search...

Protein-protein interaction databases

IntAct

P46595. 1 interaction.

MINT

MINT-4690340.

STRING

4896.SPBC119.02-1.

Proteomic databases

PaxDb

P46595.

PRIDE

P46595.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

SPBC119.02.1; SPBC119.02.1:pep; SPBC119.02.

GeneID

2540083.

KEGG

spo:SPBC119.02.

Organism-specific databases

PomBase

SPBC119.02.

Phylogenomic databases

eggNOG

COG5078.

HOGENOM

HOG000233455.

KO

K06689.

OMA

KVNFTTR.

OrthoDB

EOG4KM2CF.

Enzyme and pathway databases

UniPathway

UPA00143.

Family and domain databases

Gene3D

3.10.110.10. 1 hit.

InterPro

IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]

Pfam

PF00179. UQ_con. 1 hit.
[Graphical view]

SUPFAM

SSF54495. UBQ-conjugat/RWD-like. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

NextBio

20801220.

Entry information

Entry name

UBC4_SCHPO

Accession

Primary (citable) accession number: P46595

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 29, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program