MMI1_SCHPO - dbPTM
MMI1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MMI1_SCHPO
UniProt AC O74958
Protein Name YTH domain-containing protein mmi1
Gene Name mmi1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 488
Subcellular Localization Nucleus .
Protein Description RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non-coding RNAs (By similarity). Required for elemination of certain meiosis-specific mRNAs in an early event following transcription. May bind to the cis-acting region (DSR) of the mRNA, activating the nuclear exosome which may lead to the degradation of the transcript from the 3' region. [PubMed: 16823445]
Protein Sequence MSNTNFSTSRSSKSIPELPNLEALRSLWPPPSLNESGDTRSVWTTHTGEPVASSVLSTSGSNNFSSPLKRPAPESHDAPIGRRLMVDDPRLIKHGKYDFSRHCTDYGHSYEWPYFRSLRRESMLYHTSGSYPESQPPYSSYSTDAPHYYHAGSESSAYYDSRSRLHGIQPPPKRRTLSPPPRRLADPVVVGSSRYVEEEVYRRPPYTLASEVPSSASAYQAGYSSYPVRSSPQLSHEDTRHGIASSGSTRYPFVPANTRASHSPSLLEPYAHSLPSSVAPVGAYPEKSSYLLSNSSNDSASRKEKPKARASTPPPLNFSRASEHRNEKGERISMINPRVVLDENGISHRSRYFIMLCDNETAIAHAKKTSIWAVKKDSSKRISDAYKKASVYFIFVAQQTYNALGYAQVVSDLNSTELPFWSDSSHAGGVRIKWIKTCNLFSAEISEIVSHMDHGSEARDGMEMMYDEGSRLCTLINYAIMKRIGRDR
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
11PhosphorylationTNFSTSRSSKSIPEL
CCCCCCCCCCCCCCC
41.7225720772
12PhosphorylationNFSTSRSSKSIPELP
CCCCCCCCCCCCCCC
29.3425720772
14PhosphorylationSTSRSSKSIPELPNL
CCCCCCCCCCCCCCH
45.3725720772
65PhosphorylationTSGSNNFSSPLKRPA
CCCCCCCCCCCCCCC
32.9229996109
66PhosphorylationSGSNNFSSPLKRPAP
CCCCCCCCCCCCCCC
30.0729996109
176PhosphorylationQPPPKRRTLSPPPRR
CCCCCCCCCCCCCCC
35.3028889911
178PhosphorylationPPKRRTLSPPPRRLA
CCCCCCCCCCCCCCC
34.4528889911
226PhosphorylationYQAGYSSYPVRSSPQ
HHCCCCCCCCCCCCC
10.3729996109
230PhosphorylationYSSYPVRSSPQLSHE
CCCCCCCCCCCCCCC
46.7528889911
231PhosphorylationSSYPVRSSPQLSHED
CCCCCCCCCCCCCCC
13.2028889911
235PhosphorylationVRSSPQLSHEDTRHG
CCCCCCCCCCCCCCC
21.4229996109
239PhosphorylationPQLSHEDTRHGIASS
CCCCCCCCCCCCCCC
22.9129996109
258PhosphorylationYPFVPANTRASHSPS
CCCCCCCCCCCCCCC
29.7129996109
261PhosphorylationVPANTRASHSPSLLE
CCCCCCCCCCCCHHH
22.6228889911
263PhosphorylationANTRASHSPSLLEPY
CCCCCCCCCCHHHCC
17.4328889911
265PhosphorylationTRASHSPSLLEPYAH
CCCCCCCCHHHCCCC
48.9128889911
270PhosphorylationSPSLLEPYAHSLPSS
CCCHHHCCCCCCCCC
13.9429996109
273PhosphorylationLLEPYAHSLPSSVAP
HHHCCCCCCCCCCCC
33.5329996109
276PhosphorylationPYAHSLPSSVAPVGA
CCCCCCCCCCCCCCC
42.6229996109
277PhosphorylationYAHSLPSSVAPVGAY
CCCCCCCCCCCCCCC
21.9929996109
296PhosphorylationSYLLSNSSNDSASRK
HEECCCCCCCCHHCC
49.2425720772
299PhosphorylationLSNSSNDSASRKEKP
CCCCCCCCHHCCCCC
32.1825720772
301PhosphorylationNSSNDSASRKEKPKA
CCCCCCHHCCCCCCH
48.0825720772
311PhosphorylationEKPKARASTPPPLNF
CCCCHHCCCCCCCCC
35.5728889911
312PhosphorylationKPKARASTPPPLNFS
CCCHHCCCCCCCCCC
38.5428889911
319PhosphorylationTPPPLNFSRASEHRN
CCCCCCCCCCHHHCC
26.3421712547
322PhosphorylationPLNFSRASEHRNEKG
CCCCCCCHHHCCCCC
32.5921712547

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 MMI1_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MMI1_SCHPO !!

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 MMI1_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAB2_SCHPOpab2physical
20512112
PAP_SCHPOpla1physical
20512112
YLP3_SCHPOred1physical
21317872
YLP3_SCHPOred1physical
23980030
XRN2_SCHPOdhp1physical
26631744
REC8_SCHPOrec8genetic
28199302
CRS1_SCHPOcrs1genetic
28199302
SCC3_SCHPOpsc3genetic
28199302
DBP2_SCHPOdbp2physical
26670050
MPG1_SCHPOmpg1physical
26670050
YBI8_SCHPOoga1physical
26670050
CG23_SCHPOcdc13physical
26670050
6PGD_SCHPOSPBC660.16physical
26670050
GBLP_SCHPOcpc2physical
26670050
PYRG_SCHPOcts1physical
26670050
RAD24_SCHPOrad24physical
26670050
YGMH_SCHPOSPBC19G7.17physical
26670050
PUB3_SCHPOpub3physical
26670050
RLA0_SCHPOrpp0physical
26670050
RL38A_SCHPOrpl3801physical
26670050
TPZ1_SCHPOtpz1physical
26670050
RL7A_SCHPOrlp7physical
26670050
YFFH_SCHPOSPAC1687.17cphysical
26670050
YHFA_SCHPOSPBC1734.10cphysical
26670050
YORF_SCHPOmpe1physical
26670050
SWS2_SCHPOSPCC1795.07physical
26670050
POP5_SCHPOpop5physical
26670050
ATG12_SCHPOatg12physical
26670050
HOB1_SCHPOhob1physical
26670050
NAA35_SCHPOmak10physical
26670050
MVP1_SCHPOmvp1physical
26670050
REC8_SCHPOrec8physical
27851962

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MMI1_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-176; SER-178; SER-230;SER-231; SER-261; SER-263; SER-265; SER-311 AND THR-312, AND MASSSPECTROMETRY.

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