AIR2_YEAST - dbPTM
AIR2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AIR2_YEAST
UniProt AC Q12476
Protein Name Protein AIR2
Gene Name AIR2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 344
Subcellular Localization Nucleus .
Protein Description 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..
Protein Sequence MEKNTAPFVVDTAPTTPPDKLVAPSIEEVNSNPNELRALRGQGRYFGVSDDDKDAIKEAAPKCNNCSQRGHLKKDCPHIICSYCGATDDHYSRHCPKAIQCSKCDEVGHYRSQCPHKWKKVQCTLCKSKKHSKERCPSIWRAYILVDDNEKAKPKVLPFHTIYCYNCGGKGHFGDDCKEKRSSRVPNEDGSAFTGSNLSVELKQEYYRHMNRNSDENEDYQFSESIYDEDPLPRPSHKRHSQNDHSHSGRNKRRASNFHPPPYQKSNVIQPTIRGETLSLNNNISKNSRYQNTKVNVSSISENMYGSRYNPSTYVDNNSISNSSNYRNYNSYQPYRSGTLGKRR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
3Ubiquitination-----MEKNTAPFVV
-----CCCCCCCEEE		59.3015699485
5Phosphorylation---MEKNTAPFVVDT
---CCCCCCCEEECC		46.9328889911
12PhosphorylationTAPFVVDTAPTTPPD
CCCEEECCCCCCCCC		23.9521440633
15PhosphorylationFVVDTAPTTPPDKLV
EEECCCCCCCCCCCC		49.8522369663
16PhosphorylationVVDTAPTTPPDKLVA
EECCCCCCCCCCCCC		31.5922369663
20UbiquitinationAPTTPPDKLVAPSIE
CCCCCCCCCCCCCHH		51.1115699485
25PhosphorylationPDKLVAPSIEEVNSN
CCCCCCCCHHHHCCC		32.6621440633
31PhosphorylationPSIEEVNSNPNELRA
CCHHHHCCCHHHHHH		59.8624961812
49PhosphorylationQGRYFGVSDDDKDAI
CCCCCCCCCCCHHHH		35.3822369663
241PhosphorylationRPSHKRHSQNDHSHS
CCCCCCCCCCCCCCC		34.4130377154
256PhosphorylationGRNKRRASNFHPPPY
CCCCCCHHCCCCCCC		37.9128889911
266PhosphorylationHPPPYQKSNVIQPTI
CCCCCCCCCCCCCCC		22.3226447709
272PhosphorylationKSNVIQPTIRGETLS
CCCCCCCCCCCCEEE		13.6126447709
277PhosphorylationQPTIRGETLSLNNNI
CCCCCCCEEECCCCC		25.1926447709
279PhosphorylationTIRGETLSLNNNISK
CCCCCEEECCCCCCC		36.1530377154
319PhosphorylationSTYVDNNSISNSSNY
CCCCCCCCCCCCCCC		33.3830377154
329PhosphorylationNSSNYRNYNSYQPYR
CCCCCCCCCCCCCCC		9.1127017623
331PhosphorylationSNYRNYNSYQPYRSG
CCCCCCCCCCCCCCC		18.1327017623
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of AIR2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AIR2_YEAST !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of AIR2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DED1_YEASTDED1physical
11805837
SYSC_YEASTSES1physical
11805837
NOP3_YEASTNPL3physical
11805837
IMA1_YEASTSRP1physical
11805837
QCR2_YEASTQCR2physical
11805837
RT35_YEASTMRPS35physical
11805837
ADH2_YEASTADH2physical
11805837
PAP2_YEASTPAP2physical
15935759
AIR1_YEASTAIR1physical
15935759
MTR4_YEASTMTR4physical
15935758
PAP2_YEASTPAP2physical
15935758
TRF5_YEASTTRF5physical
15935758
PAP2_YEASTPAP2physical
15828860
MTR4_YEASTMTR4physical
15828860
MTR4_YEASTMTR4physical
16429126
NAB3_YEASTNAB3physical
16429126
PAP2_YEASTPAP2physical
16429126
PAT1_YEASTPAT1physical
11283351
NOP3_YEASTNPL3genetic
19061648
PAP2_YEASTPAP2genetic
19061648
RRP6_YEASTRRP6genetic
19061648
AIR1_YEASTAIR1genetic
19061648
ELP3_YEASTELP3genetic
19061648
KRR1_YEASTKRR1genetic
19061648
TAD3_YEASTTAD3genetic
19061648
LSM3_YEASTLSM3genetic
19061648
LHP1_YEASTLHP1genetic
19061648
ERF3_YEASTSUP35genetic
19061648
CWC21_YEASTCWC21genetic
19061648
POP8_YEASTPOP8genetic
19061648
RU1A_YEASTMUD1genetic
19061648
POP7_YEASTPOP7genetic
19061648
CSI1_YEASTCSI1genetic
19061648
NOP15_YEASTNOP15genetic
19061648
BRR1_YEASTBRR1genetic
19061648
IF2G_YEASTGCD11genetic
19061648
CHD1_YEASTCHD1genetic
19061648
AIR1_YEASTAIR1genetic
18408161
ELP3_YEASTELP3genetic
19547744
CWC21_YEASTCWC21genetic
19547744
CHD1_YEASTCHD1genetic
19547744
MTR4_YEASTMTR4physical
22402490
PAP2_YEASTPAP2physical
22402490
MTR4_YEASTMTR4physical
25175027
PAP2_YEASTPAP2physical
24097436
VAM7_YEASTVAM7genetic
27708008
YJ90_YEASTYJR120Wgenetic
27708008
PET8_YEASTPET8genetic
27708008
PRI1_YEASTPRI1genetic
27708008
BET3_YEASTBET3genetic
27708008
SSL1_YEASTSSL1genetic
27708008
RPB2_YEASTRPB2genetic
27708008
DEP1_YEASTDEP1genetic
27708008
ERS1_YEASTERS1genetic
27708008
SAP1_YEASTSAP1genetic
27708008
G3P3_YEASTTDH3genetic
27708008
AIR1_YEASTAIR1genetic
27708008
CBF1_YEASTCBF1genetic
27708008
TDA4_YEASTTDA4genetic
27708008
YKK7_YEASTYKL107Wgenetic
27708008
SSH4_YEASTSSH4genetic
27708008
DCOR_YEASTSPE1genetic
27708008
YRA2_YEASTYRA2genetic
27708008
BPT1_YEASTBPT1genetic
27708008
CSF1_YEASTCSF1genetic
27708008
HRB1_YEASTHRB1genetic
27708008
RRP6_YEASTRRP6genetic
27708008
PMT3_YEASTPMT3genetic
27708008
HAT1_YEASTHAT1genetic
27708008
NAB3_YEASTNAB3genetic
25775092
PAP2_YEASTPAP2genetic
25775092
LZTS2_HUMANLZTS2physical
27107014
DVL2_HUMANDVL2physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AIR2_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15; THR-16; SER-31 ANDSER-49, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15; THR-16 AND SER-49,AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-16, AND MASSSPECTROMETRY.

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