Reviewed, UniProtKB/Swiss-Prot P48606 (TBCA_YEAST)

Names and origin

Protein names

Recommended name:
    Tubulin-specific chaperone A
Alternative name(s):
    Tubulin-folding cofactor A
      Short name=CFA

Gene names

Name:	RBL2
Ordered Locus Names:	YOR265W

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

General annotation (Comments)

Function	Tubulin-folding protein; involved in the early step of the tubulin folding pathway.
Subcellular location	Cytoplasm › cytoskeleton.
Miscellaneous	Present with 1760 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the TBCA family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Molecular function	Chaperone
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	microtubule cytoskeleton organization Inferred from mutant phenotype. Source: SGD post-chaperonin tubulin folding pathway Traceable author statement. Source: SGD tubulin complex assembly Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from direct assay. Source: SGD microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	beta-tubulin binding Inferred from mutant phenotype. Source: SGD unfolded protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
JSN1	P47135	1	EBI-18991,EBI-9422
TUB2	P02557	1	EBI-18991,EBI-18986
VPS54	Q12071	1	EBI-18991,EBI-36751

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 106

106

Tubulin-specific chaperone A

PRO_0000080045

Amino acid modifications

Modified residue

94

1

Phosphoserine Ref.6 Ref.7 Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

106

Helix Strand Turn

Details...

Helix

5 – 39

35

Helix

45 – 81

37

Beta strand

85 – 87

3

Helix

90 – 104

15

Sequences

	Sequence		Length	Mass (Da)
	P48606-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 3F649CCB78AB3EF3	FASTA	106	12,379
	10 20 30 40 50 60 MAPTQLDIKV KALKRLTKEE GYYQQELKDQ EAHVAKLKED KSVDPYDLKK QEEVLDDTKR 70 80 90 100 LLPTLYEKIR EFKEDLEQFL KTYQGTEDVS DARSAITSAQ ELLDSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Rbl2p, a yeast protein that binds to beta-tubulin and participates in microtubule function in vivo." Archer J.E., Vega L.R., Solomon F. Cell 82:425-434(1995) [PubMed: 7634332] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1 and VPH1." Poirey R., Jauniaux J.-C. Yeast 13:483-487(1997) [PubMed: 9153759] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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].
[6]	"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: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, MASS SPECTROMETRY.
[7]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U30184 Genomic DNA. Translation: AAB08525.1.
Z75173 Genomic DNA. Translation: CAA99488.1.
AY692767 Genomic DNA. Translation: AAT92786.1.

PIR

S64649.

RefSeq

NP_014908.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QSD	X-ray	2.20	A/B	1-106	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:4101N.

IntAct

P48606. 4 interactions.

STRING

P48606.

Proteomic databases

PeptideAtlas

P48606.

Genome annotation databases

Ensembl

YOR265W; YOR265W; YOR265W; Saccharomyces cerevisiae. [Genome view]

GeneID

854439.

KEGG

sce:YOR265W.

NMPDR

fig|4932.3.peg.6020.

Organism-specific databases

CYGD

YOR265w.

SGD

S000005791. RBL2.

Phylogenomic databases

HOGENOM

P48606.

OMA

EESQRMV

OrthoDB

EOG912NNH

Gene expression databases

ArrayExpress

P48606.

Genevestigator

P48606.

GermOnline

YOR265W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR004226. CofA_tubulin_bd.
[Graphical view]

PANTHER

PTHR21500. CofA_tubulin_bd. 1 hit.

Pfam

PF02970. TBCA. 1 hit.
[Graphical view]

ProDom

PD010430. CofA_tubulin_bd. 1 hit.
[Graphical view] [Entries sharing at least one domain]

ProtoNet

Search...

Other Resources

NextBio

976679.

Entry information

Entry name

TBCA_YEAST

Accession

Primary (citable) accession number: P48606

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	November 24, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)