NTR2_YEAST - dbPTM
NTR2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NTR2_YEAST
UniProt AC P36118
Protein Name Pre-mRNA-splicing factor NTR2
Gene Name NTR2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 322
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Involved in pre-mRNA splicing and spliceosome disassembly. Promotes release of excised lariat intron from the spliceosome by acting as a receptor for PRP43. This targeting of PRP43 leads to disassembly of the spliceosome with the separation of the U2, U5, U6 snRNPs and the NTC complex..
Protein Sequence MAIKKRNKIRLPSGSPEEVGIDGSAHKPMQQIKPLVSNDSEDDDNDICVLQPIKFKKVPKRDITFDGEQAIKEDNSHYEDLYHSKKNTNASTRNKDDLLILNMEDLMEGNHHLLSDSSEAGSSSEGEHISSIPTRGEIAKLKAQKSLSRRKISESDVTTERDYVKLLDSEDKREIMETIRLNGGLKRNNEKEITNFSDDEMQGFQDEMLALTDNQIAIQKDSKRKIIEKAINEVPYRTNEEWETQLLSKGNINKSNEKIITPLPVLFPDDDESGNSIERINEMVSKICLQRKKVEMRLQALEKTKIDLEKSKASLINKLIGN
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
13PhosphorylationRNKIRLPSGSPEEVG
CCCCCCCCCCHHHCC
57.4024961812
15PhosphorylationKIRLPSGSPEEVGID
CCCCCCCCHHHCCCC
33.2121440633
37PhosphorylationQQIKPLVSNDSEDDD
HHCCCCCCCCCCCCC
42.4720377248
40PhosphorylationKPLVSNDSEDDDNDI
CCCCCCCCCCCCCCE
47.3722369663
72UbiquitinationFDGEQAIKEDNSHYE
CCHHHHHCCCCCCHH
63.1317644757
146PhosphorylationAKLKAQKSLSRRKIS
HHHHHHHHHHCCCCC
21.3524961812
148PhosphorylationLKAQKSLSRRKISES
HHHHHHHHCCCCCHH
36.8124961812
153PhosphorylationSLSRRKISESDVTTE
HHHCCCCCHHHCCCH
33.8024961812
155PhosphorylationSRRKISESDVTTERD
HCCCCCHHHCCCHHH
30.5020377248
169PhosphorylationDYVKLLDSEDKREIM
HHHHHCCHHHHHHHH
47.8923749301
186UbiquitinationIRLNGGLKRNNEKEI
HHHCCCCCCCCCCCC
57.2521427232
194PhosphorylationRNNEKEITNFSDDEM
CCCCCCCCCCCHHHH
31.1621440633
197PhosphorylationEKEITNFSDDEMQGF
CCCCCCCCHHHHHCH
46.3421440633
212PhosphorylationQDEMLALTDNQIAIQ
HHHHHHHCCCCEEEC
27.5730377154
229AcetylationSKRKIIEKAINEVPY
HHHHHHHHHHHHCCC
44.1324489116

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 NTR2_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NTR2_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 NTR2_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YBB0_YEASTYBL010Cphysical
10688190
SP382_YEASTSPP382physical
10688190
POF1_YEASTPOF1physical
16554755
PRP8_YEASTPRP8physical
16554755
PSMD9_YEASTNAS2physical
16554755
PYRE_YEASTURA5physical
16554755
SYF1_YEASTSYF1physical
16357217
CEF1_YEASTCEF1physical
16357217
CLF1_YEASTCLF1physical
16357217
SYF2_YEASTSYF2physical
16357217
ISY1_YEASTISY1physical
16357217
SN309_YEASTSNT309physical
16357217
NTC20_YEASTNTC20physical
16357217
SP382_YEASTSPP382physical
16357217
PRP43_YEASTPRP43physical
16357217
SP382_YEASTSPP382physical
16880513
PRP8_YEASTPRP8physical
16880513
YBB0_YEASTYBL010Cphysical
11283351
SP382_YEASTSPP382physical
11283351
BRR2_YEASTBRR2physical
17893323
SAC3_YEASTSAC3genetic
19061648
NU120_YEASTNUP120genetic
19061648
SYDM_YEASTMSD1genetic
19061648
SYMM_YEASTMSM1genetic
19061648
PUF2_YEASTPUF2genetic
19061648
NNF1_YEASTNNF1physical
22875988
SKA1_HUMANSKA1physical
27107014

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NTR2_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 SER-40 AND SER-153, AND MASSSPECTROMETRY.

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