TIP41_YEAST - dbPTM
TIP41_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TIP41_YEAST
UniProt AC Q12199
Protein Name Type 2A phosphatase activator TIP41
Gene Name TIP41
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 356
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Involved in negative regulation of the TOR signaling pathway in response to type of available nitrogen source. Indirectly activates the PP2A phosphatase SIT4 via interaction with its suppressor TAP42. This interaction is enhanced under nitrogen limitation conditions. Also has a role in regulation of NPR1 in response to nitrogen limitation..
Protein Sequence MSKRNTPPLRSSGINTIQINAAREMHAQTVRARRMPMPTSGITTPSVQPTAAPATPPRHICNNPNNPQCLHCGSVIIPSPRATLPLEDNPSISINDWTISSRKKPILNSQELDIWENEKLKGLTLPEMIFGNNYIRIENSKQHWSIEFNALDALKEVQLQDSGIRVAYSNDWINSKKRQNSTNGAQRFTNDVNDDSLNIIHKYDWTYTTRYKGTESSPESKFRLDNDQKLPLDKLAVHDKILFYDDMILFEDELADNGISILNVKIRVMNERLLLLSRFFLRVDDVLVRVYDTRIYVEFDENVVIRESKEFEGKYQDVLAKHRLSQSHDPKAALRDSNWVAQNTPMIKRQCEIIQF
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--MSKRNTPPLRSSG
--CCCCCCCCCCCCC
30.2517563356
40PhosphorylationRRMPMPTSGITTPSV
HCCCCCCCCCCCCCC
23.4819779198
50PhosphorylationTTPSVQPTAAPATPP
CCCCCCCCCCCCCCC
20.5427017623
55PhosphorylationQPTAAPATPPRHICN
CCCCCCCCCCCCCCC
32.5427738172
74PhosphorylationPQCLHCGSVIIPSPR
CCCCCCCCEEECCCC
18.6119779198
79PhosphorylationCGSVIIPSPRATLPL
CCCEEECCCCCCCCC
19.3325704821
169PhosphorylationSGIRVAYSNDWINSK
CCCEEEEECCCCCCC
20.6921126336
214PhosphorylationYTTRYKGTESSPESK
EEEECCCCCCCCCHH
28.6627017623
216PhosphorylationTRYKGTESSPESKFR
EECCCCCCCCCHHCC
51.5427017623
217PhosphorylationRYKGTESSPESKFRL
ECCCCCCCCCHHCCC
26.8427017623

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 TIP41_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TIP41_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 TIP41_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP4C_YEASTPPH3physical
16085932
PP2A1_YEASTPPH21physical
16085932
PP2A2_YEASTPPH22physical
16085932
PP4R2_YEASTPSY4physical
16085932
PP4R3_YEASTPSY2physical
16085932
RPN5_YEASTRPN5physical
16554755
RPN9_YEASTRPN9physical
16554755
PP2A1_YEASTPPH21physical
11283351
PP2A2_YEASTPPH22physical
11283351
PP2A4_YEASTPPG1physical
11283351
TAP42_YEASTTAP42physical
17846631
PP2A1_YEASTPPH21physical
17846631
PP2A2_YEASTPPH22physical
17846631
SA155_YEASTSAP155genetic
11741537
YPK9_YEASTYPK9genetic
22457822
PDP2_YEASTPTC6genetic
23704987
ELP3_YEASTELP3genetic
28357221
URM1_YEASTURM1genetic
28357221

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TIP41_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-55, AND MASSSPECTROMETRY.
"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-6, AND MASSSPECTROMETRY.

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