AIR1_YEAST - dbPTM
AIR1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AIR1_YEAST
UniProt AC P40507
Protein Name Protein AIR1
Gene Name AIR1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 360
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Component of the TRAMP (TRF4) and TRAMP5 complexes which have a poly(A) RNA polymerase activity and are 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. AIR1 also inhibits the methylation of NPL3 mediated by HMT1 through its interaction with HMT1..
Protein Sequence MSTLLSEVESIDTLPYVKDTTPTGSDSSSFNKLLAPSIEDVDANPEELRTLRGQGRYFGITDYDSNGAIMEAEPKCNNCSQRGHLKRNCPHVICTYCGFMDDHYSQHCPKAIICTNCNANGHYKSQCPHKWKKVFCTLCNSKRHSRERCPSIWRSYLLKTKDANQGDFDFQTVFCYNCGNAGHFGDDCAERRSSRVPNTDGSAFCGDNLATKFKQHYFNQLKDYKREASQRQHFDNEHEFNLLDYEYNDDAYDLPGSRTYRDKMKWKGKVQSTRNKNSSNNRYESSNNRKKKSPFSAQNYKVTKNKRVQTHPLDFPRSSQNNRTNDYSSQFSYNRDDFPKGPKNKRGRSSSNKSQRNGRY
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
6Phosphorylation--MSTLLSEVESIDT
--CCCHHHHHEECCC		42.5828889911
10PhosphorylationTLLSEVESIDTLPYV
CHHHHHEECCCCCCC		30.8228889911
16PhosphorylationESIDTLPYVKDTTPT
EECCCCCCCCCCCCC		24.2028132839
20PhosphorylationTLPYVKDTTPTGSDS
CCCCCCCCCCCCCCC		29.0222890988
21PhosphorylationLPYVKDTTPTGSDSS
CCCCCCCCCCCCCCH		29.0525521595
23PhosphorylationYVKDTTPTGSDSSSF
CCCCCCCCCCCCHHH		47.4222890988
25PhosphorylationKDTTPTGSDSSSFNK
CCCCCCCCCCHHHHH		36.4822890988
27PhosphorylationTTPTGSDSSSFNKLL
CCCCCCCCHHHHHHH		29.5822890988
28PhosphorylationTPTGSDSSSFNKLLA
CCCCCCCHHHHHHHC		43.8922890988
29PhosphorylationPTGSDSSSFNKLLAP
CCCCCCHHHHHHHCC		36.4722890988
37PhosphorylationFNKLLAPSIEDVDAN
HHHHHCCCHHHCCCC		32.7625752575
141PhosphorylationVFCTLCNSKRHSRER
HHHHHHCCCCCCHHH		30.0328889911
272PhosphorylationKWKGKVQSTRNKNSS
CCCCEECCCCCCCCC		32.1128889911
273PhosphorylationWKGKVQSTRNKNSSN
CCCEECCCCCCCCCC		22.5928889911
293PhosphorylationSNNRKKKSPFSAQNY
CCCCCCCCCCCCCCC		39.8021440633
328PhosphorylationNNRTNDYSSQFSYNR
CCCCCCCCCCCCCCC		22.1130377154
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 AIR1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AIR1_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 AIR1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAP2_YEASTPAP2physical
11805837
NOP3_YEASTNPL3physical
11805837
HRB1_YEASTHRB1physical
11805837
IMDH4_YEASTIMD4physical
11805837
DED1_YEASTDED1physical
11805837
AIR2_YEASTAIR2physical
15935759
PAP2_YEASTPAP2physical
15935759
PAP2_YEASTPAP2physical
15828860
MTR4_YEASTMTR4physical
15828860
AIR2_YEASTAIR2genetic
10896665
PAP2_YEASTPAP2physical
16554755
FHL1_YEASTFHL1genetic
19061648
ATG17_YEASTATG17physical
18719252
PBP2_YEASTPBP2physical
18719252
NAB2_YEASTNAB2physical
18719252
AIR2_YEASTAIR2genetic
18591258
MFT1_YEASTMFT1genetic
18591258
THP2_YEASTTHP2genetic
18591258
THO2_YEASTTHO2genetic
18591258
NOP13_YEASTNOP13genetic
18591258
SSF2_YEASTSSF2genetic
18591258
SQS1_YEASTSQS1genetic
18591258
MPP6_YEASTMPP6genetic
18591258
TOM1_YEASTTOM1genetic
18591258
END3_YEASTEND3genetic
18591258
AIR2_YEASTAIR2genetic
18408161
MPP6_YEASTMPP6genetic
18408161
MFT1_YEASTMFT1genetic
18408161
THP2_YEASTTHP2genetic
18408161
NOT3_YEASTNOT3genetic
19547744
CHD1_YEASTCHD1genetic
19547744
PSP1_YEASTPSP1genetic
18591258
CHD1_YEASTCHD1genetic
18591258
SPT2_YEASTSPT2genetic
18591258
SEM1_YEASTSEM1genetic
18591258
YJ26_YEASTYJR056Cgenetic
18591258
ISW1_YEASTISW1genetic
18591258
PAN2_YEASTPAN2genetic
18591258
AIR2_YEASTAIR2genetic
21878619
PAP2_YEASTPAP2physical
21878619
RNH1_YEASTRNH1genetic
22195970
AIR2_YEASTAIR2genetic
22923767
SWI6_YEASTSWI6genetic
27708008
AIR2_YEASTAIR2genetic
27708008
SSF1_YEASTSSF1genetic
27708008
VAC14_YEASTVAC14genetic
27708008
MSC1_YEASTMSC1genetic
27708008
TMA23_YEASTTMA23genetic
27708008
YO024_YEASTYOL024Wgenetic
27708008
NOP12_YEASTNOP12genetic
27708008
SYH1_YEASTSYH1genetic
27708008
YP084_YEASTYPR084Wgenetic
27708008
NAB3_YEASTNAB3genetic
25775092
PAP2_YEASTPAP2genetic
25775092
AIR2_YEASTAIR2genetic
25159613
CEP70_HUMANCEP70physical
27107014
ZN250_HUMANZNF250physical
27107014
RBMX_HUMANRBMXphysical
27107014
KHDR2_HUMANKHDRBS2physical
27107014
DVL2_HUMANDVL2physical
27107014
CCD33_HUMANCCDC33physical
27107014
HNRPC_HUMANHNRNPCphysical
27107014
TRI41_HUMANTRIM41physical
27107014
ZN473_HUMANZNF473physical
27107014
GMCL1_HUMANGMCL1physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AIR1_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-21 AND SER-37, AND MASSSPECTROMETRY.

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