Reviewed, UniProtKB/Swiss-Prot Q12476 (AIR2_YEAST)

Names and origin

Protein names

Recommended name:
    Protein AIR2
Alternative name(s):
    Arginine methyltransferase-interacting RING finger protein 2

Gene names

Name:	AIR2
Ordered Locus Names:	YDL175C

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

General annotation (Comments)

Function	Component of the TRAMP (TRF4) complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates like cryptic transcripts generated by RNA polymerase II and III, or hypomethylated pre-tRNAi-Met. Both complexes polyadenylate RNA processing and degradation intermediates of snRNAs, snoRNAs and mRNAs that accumulate in strains lacking a functional exosome. AIR2 also inhibits the methylation of NPL3 mediated by HMT1 through its interaction with HMT1. Ref.2 Ref.5 Ref.6 Ref.8
Subunit structure	Component of the TRAMP complex (also called TRF4 complex) composed of at least HUL4, MTR4, PAP2/TRF4 and either AIR1 or AIR2. Interacts with HMT1 and NPL3. The interaction with NPL3 requires the presence of HMT1. Ref.2
Subcellular location	Nucleus.
Miscellaneous	Present with 1800 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the AIR1 family. Contains 3 CCHC-type zinc fingers.

Ontologies

Keywords
Cellular component	Nucleus
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ncRNA polyadenylation Ref.5 Ref.8 Inferred from direct assay. Source: SGD nuclear mRNA surveillance of mRNA 3'-end processing Inferred from genetic interaction. Source: SGD nuclear polyadenylation-dependent CUT catabolic process Inferred from genetic interaction. Source: SGD nuclear polyadenylation-dependent rRNA catabolic process Ref.5 Inferred from genetic interaction. Source: SGD nuclear polyadenylation-dependent snRNA catabolic process Ref.5 Inferred from genetic interaction. Source: SGD nuclear polyadenylation-dependent snoRNA catabolic process Ref.5 Inferred from genetic interaction. Source: SGD nuclear polyadenylation-dependent tRNA catabolic process Ref.5 Ref.8 Inferred from direct assay. Source: SGD
Cellular component	TRAMP complex Ref.5 Ref.6 Ref.8 Inferred from direct assay. Source: SGD nucleolus Inferred from direct assay. Source: SGD
Molecular function	nucleic acid binding Inferred from electronic annotation. Source: InterPro protein binding Ref.5 Ref.6 Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P38800	1	EBI-31475,EBI-24597
MTR4	P47047	1	EBI-31475,EBI-11592
PAP2	P53632	1	EBI-31475,EBI-19517
PAT1	P25644	1	EBI-31475,EBI-204

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 344	344	Protein AIR2		PRO_0000227604
Regions
	Zinc finger	61 – 78	18	CCHC-type 1
	Zinc finger	99 – 116	18	CCHC-type 2
	Zinc finger	162 – 179	18	CCHC-type 3
Amino acid modifications
	Modified residue	15	1	Phosphothreonine Ref.10 Ref.11
	Modified residue	16	1	Phosphothreonine Ref.10 Ref.11 Ref.7
	Modified residue	31	1	Phosphoserine Ref.11
	Modified residue	49	1	Phosphoserine Ref.10 Ref.11 Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Q12476-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 5915C97FA39D6AFC	FASTA	344	39,344
	10 20 30 40 50 60 MEKNTAPFVV DTAPTTPPDK LVAPSIEEVN SNPNELRALR GQGRYFGVSD DDKDAIKEAA 70 80 90 100 110 120 PKCNNCSQRG HLKKDCPHII CSYCGATDDH YSRHCPKAIQ CSKCDEVGHY RSQCPHKWKK 130 140 150 160 170 180 VQCTLCKSKK HSKERCPSIW RAYILVDDNE KAKPKVLPFH TIYCYNCGGK GHFGDDCKEK 190 200 210 220 230 240 RSSRVPNEDG SAFTGSNLSV ELKQEYYRHM NRNSDENEDY QFSESIYDED PLPRPSHKRH 250 260 270 280 290 300 SQNDHSHSGR NKRRASNFHP PPYQKSNVIQ PTIRGETLSL NNNISKNSRY QNTKVNVSSI 310 320 330 340 SENMYGSRYN PSTYVDNNSI SNSSNYRNYN SYQPYRSGTL GKRR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"Novel RING finger proteins, Air1p and Air2p, interact with Hmt1p and inhibit the arginine methylation of Npl3p." Inoue K., Mizuno T., Wada K., Hagiwara M. J. Biol. Chem. 275:32793-32799(2000) [PubMed: 10896665] [Abstract] Cited for: FUNCTION, INTERACTION WITH HMT1 AND NPL3.
[3]	"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].
[4]	"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].
[5]	"RNA degradation by the exosome is promoted by a nuclear polyadenylation complex." LaCava J., Houseley J., Saveanu C., Petfalski E., Thompson E., Jacquier A., Tollervey D. Cell 121:713-724(2005) [PubMed: 15935758] [Abstract] Cited for: IDENTIFICATION IN TRAMP COMPLEX, FUNCTION OF THE TRAMP COMPLEX.
[6]	"Cryptic pol II transcripts are degraded by a nuclear quality control pathway involving a new poly(A) polymerase." Wyers F., Rougemaille M., Badis G., Rousselle J.-C., Dufour M.-E., Boulay J., Regnault B., Devaux F., Namane A., Seraphin B., Libri D., Jacquier A. Cell 121:725-737(2005) [PubMed: 15935759] [Abstract] Cited for: IDENTIFICATION IN THE TRF4 COMPLEX, MASS SPECTROMETRY, FUNCTION OF THE TRF4 COMPLEX.
[7]	"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 THR-16, MASS SPECTROMETRY.
[8]	"A new yeast poly(A) polymerase complex involved in RNA quality control." Vanacova S., Wolf J., Martin G., Blank D., Dettwiler S., Friedlein A., Langen H., Keith G., Keller W. PLoS Biol. 3:986-997(2005) [PubMed: 15828860] [Abstract] Cited for: IDENTIFICATION IN THE TRF4 COMPLEX, MASS SPECTROMETRY, FUNCTION OF THE TRF4 COMPLEX.
[9]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, MASS SPECTROMETRY.
[10]	"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 THR-15; THR-16 AND SER-49, MASS SPECTROMETRY.
[11]	"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 THR-15; THR-16; SER-31 AND SER-49, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z74223 Genomic DNA. Translation: CAA98749.1. Z67750 Genomic DNA. Translation: CAA91570.1.
PIR	S61037.
RefSeq	NP_010106.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2543N.
IntAct	Q12476. 74 interactions.
STRING	Q12476.
Proteomic databases
PeptideAtlas	Q12476.
Genome annotation databases
Ensembl	YDL175C; YDL175C; YDL175C; Saccharomyces cerevisiae. [Genome view]
GeneID	851379.
KEGG	sce:YDL175C.
NMPDR	fig|4932.3.peg.840.
Organism-specific databases
CYGD	YDL175c.
SGD	S000002334. AIR2.
Phylogenomic databases
HOGENOM	Q12476.
OrthoDB	EOG93FJCZ
Gene expression databases
ArrayExpress	Q12476.
Genevestigator	Q12476.
GermOnline	YDL175C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR016713. PolA_Pol_cplx_Air1/2_su. IPR001878. Znf_CCHC. [Graphical view]
Pfam	PF00098. zf-CCHC. 3 hits. [Graphical view]
PIRSF	PIRSF018162. PolyA_pol_Air1/2. 1 hit.
SMART	SM00343. ZnF_C2HC. 5 hits. [Graphical view]
PROSITE	PS50158. ZF_CCHC. 3 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	968516.

Entry information

Entry name

AIR2_YEAST

Accession

Primary (citable) accession number: Q12476

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	November 1, 1996
Last modified:	November 24, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)