P36075 (CUE2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-binding protein CUE2

Alternative name(s):
Coupling of ubiquitin conjugation to ER degradation protein 2

Gene names

Name:	CUE2
Ordered Locus Names:	YKL090W

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	443 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Subunit structure	Binds to ubiquitin.
Sequence similarities	Contains 2 CUE domains. Contains 1 Smr domain.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Domain	Repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	ubiquitin binding Inferred from direct assay PubMed 12628920Ref.6. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 443

443

Ubiquitin-binding protein CUE2

PRO_0000079558

Regions

Domain

8 – 51

44

CUE 1

Domain

55 – 98

44

CUE 2

Domain

347 – 443

97

Smr

Amino acid modifications

Modified residue

109

1

Phosphoserine Ref.4 Ref.5

Modified residue

112

1

Phosphoserine Ref.4 Ref.5

Modified residue

411

1

Phosphoserine Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

443

Helix Strand Turn

Details...

Helix

9 – 19

11

Beta strand

21 – 23

3

Helix

25 – 34

10

Turn

35 – 37

3

Helix

40 – 49

10

Sequences

	Sequence		Length	Mass (Da)
	P36075 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 8B7BB872C2BDC734	FASTA	443	50,874
	10 20 30 40 50 60 MSMDNNDDHE SKLSILMDMF PAISKSKLQV HLLENNNDLD LTIGLLLKEN DDKSTVDNEL 70 80 90 100 110 120 HQLYDMFPQL DCSVIKDQFV INEKSVESTI SDLLNYETLQ KLKDNQANSP DSVKRNEKKN 130 140 150 160 170 180 NWESTNDHIE SIIKFTDAPK NIAQEYLAEN GFDTVKAIIK IILDYYDKRD FKKDVDTFKV 190 200 210 220 230 240 KRSPNTTVRG GRVQSSTGLA HVLKKGKESA NVAQESLKRP RSYKHSLDSP QMVELNELVA 250 260 270 280 290 300 DNRDLKAINH EFLQKCLQFY DGDVVKVLNI SSLLIEDDKN ITKTWNFDEG FTLTSRDNCK 310 320 330 340 350 360 QHLPKFSTPQ ISRRNEVGNT YKLPLHDKET PEGAVPVINN LFQTYRLDFH GFLPSEAVST 370 380 390 400 410 420 LKLALNKWWS KEVAERELNS HNINSYGSKV QFVSPLIVVT GRGIHSIGGI SKVRLQVKSF 430 440 LEKNHYIFWE ESSYFRIEGK KKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W. Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, MASS SPECTROMETRY. Strain: YAL6B.
[4]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-112, MASS SPECTROMETRY.
[5]	"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 SER-109 AND SER-112, MASS SPECTROMETRY.
[6]	"Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding." Kang R.S., Daniels C.M., Francis S.A., Shih S.C., Salerno W.J., Hicke L., Radhakrishnan I. Cell 113:621-630(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-54 IN COMPLEX WITH UBIQUITIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z28090 Genomic DNA. Translation: CAA81928.1.
BK006944 Genomic DNA. Translation: DAA09068.1.

PIR

S37915.

RefSeq

NP_012833.1. NM_001179656.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OTR	NMR	-	A	6-54	[»]

ProteinModelPortal

P36075.

SMR

P36075. Positions 6-54.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1917N.

IntAct

P36075. 4 interactions.

MINT

MINT-394365.

STRING

4932.YKL090W.

Proteomic databases

PaxDb

P36075.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YKL090W; YKL090W; YKL090W.

GeneID

853772.

KEGG

sce:YKL090W.

Organism-specific databases

CYGD

YKL090w.

SGD

S000001573. CUE2.

Phylogenomic databases

eggNOG

NOG262951.

OMA

LDFHGFL.

OrthoDB

EOG46T6B6.

Gene expression databases

Genevestigator

P36075.

GermOnline

YKL090W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR003892. CUE.
IPR002625. Smr/MutS2_C.
IPR009060. UBA-like.
[Graphical view]

Pfam

PF02845. CUE. 2 hits.
PF01713. Smr. 1 hit.
[Graphical view]

SMART

SM00546. CUE. 2 hits.
SM00463. SMR. 1 hit.
[Graphical view]

SUPFAM

SSF46934. UBA_like. 1 hit.

PROSITE

PS51140. CUE. 2 hits.
PS50828. SMR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P36075.

NextBio

974873.

Entry information

Entry name

CUE2_YEAST

Accession

Primary (citable) accession number: P36075
Secondary accession number(s): D6VXJ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program