NIF1_SCHPO - dbPTM
NIF1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NIF1_SCHPO
UniProt AC P87159
Protein Name Mitosis inhibitor nif1
Gene Name nif1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 681
Subcellular Localization Cytoplasm .
Protein Description Functions as a negative regulator of mitosis. It interacts with the C-terminal of nim1, thereby inhibiting its kinase activity which phosphorylates wee1..
Protein Sequence METMQSRTYAGLTKLNTTTALLNKKDGNDDDKAEHSKRSGYHGLSPLDALALKHRDLNRKLNLRAMMSKSEDNLQILKETTSGSSSDLLNIESPASPAEASSPFTVRTPTVHDPEHYFVAQKLSSVFGTPDLEDETDFFDYFSAAPDVHPNDIFDSYNSNNIAESFDDDNYYNSLLPPNAPYYHEIEPPRTASNTSPTPNSIKSAHPAEPPKRPAFTRSATSPDKILPTRIKSKDTVSSGDSTPLSGSSSSKGMLMSMSTSENHSLSSNPELSNSNLLAKNESPADVSNNESGNESSKEPDKEHSTPIHPTTPVSRCARPSSRQQTISILQAQSPFLKKSDKERANLNKTMVSINKSINIHQSIHEISCPHHSSSDNCLFILISLMDRLHSPVLKQLDVSLQSLTMTAIRYIDLNYVDVQYTNLRGGAYGNGNNSESSDNAQLKKEEHLNLAIHFHLLNDHDKCFWHTGMASSYEDYTATFIYGLYLRHGLACSPKTHVSFLFLLKTATQLLNKLVECLHSSDLGLNDTTPNEKLSTEYNQQRLLLALILYELGVCFMHGWGITRDRYLALHLIKLSGAWGDADAQFEAGLQMSLGAVSDKDSHMAAYYYRLAGFQGISPPSKCKWVYKSKYSLAANHKVPAASEVAYVSAIVENLESHSLKFSTKPKAKLRSLITSVRYL
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
45PhosphorylationRSGYHGLSPLDALAL
HHCCCCCCHHHHHHH		28.1925720772
68PhosphorylationLNLRAMMSKSEDNLQ
HCHHHHHCCCHHHHH		21.6825720772
70PhosphorylationLRAMMSKSEDNLQIL
HHHHHCCCHHHHHHH		42.7628889911
82PhosphorylationQILKETTSGSSSDLL
HHHHHHCCCCHHHCC		44.0627738172
96PhosphorylationLNIESPASPAEASSP
CCCCCCCCHHHCCCC		28.2027738172
108PhosphorylationSSPFTVRTPTVHDPE
CCCCEECCCCCCCHH		20.9829996109
110PhosphorylationPFTVRTPTVHDPEHY
CCEECCCCCCCHHHH		29.8429996109
193PhosphorylationIEPPRTASNTSPTPN
CCCCCCCCCCCCCCC		39.7729996109
195PhosphorylationPPRTASNTSPTPNSI
CCCCCCCCCCCCCCC		33.3229996109
196PhosphorylationPRTASNTSPTPNSIK
CCCCCCCCCCCCCCC		30.9028889911
198PhosphorylationTASNTSPTPNSIKSA
CCCCCCCCCCCCCCC		34.5629996109
204PhosphorylationPTPNSIKSAHPAEPP
CCCCCCCCCCCCCCC		30.0924763107
219PhosphorylationKRPAFTRSATSPDKI
CCCCCCCCCCCCCCC		32.6125720772
221PhosphorylationPAFTRSATSPDKILP
CCCCCCCCCCCCCCC		41.8824763107
222PhosphorylationAFTRSATSPDKILPT
CCCCCCCCCCCCCCC		30.7129996109
250PhosphorylationTPLSGSSSSKGMLMS
CCCCCCCCCCCEEEE		37.4525720772
251PhosphorylationPLSGSSSSKGMLMSM
CCCCCCCCCCEEEEC		34.8725720772
288PhosphorylationNESPADVSNNESGNE
CCCCCCCCCCCCCCC		34.1921712547
292PhosphorylationADVSNNESGNESSKE
CCCCCCCCCCCCCCC		49.3824763107
296PhosphorylationNNESGNESSKEPDKE
CCCCCCCCCCCCCCC		51.1921712547
297PhosphorylationNESGNESSKEPDKEH
CCCCCCCCCCCCCCC		34.5529996109
305PhosphorylationKEPDKEHSTPIHPTT
CCCCCCCCCCCCCCC		36.6529996109
306PhosphorylationEPDKEHSTPIHPTTP
CCCCCCCCCCCCCCC		28.3329996109
312PhosphorylationSTPIHPTTPVSRCAR
CCCCCCCCCHHHCCC		26.5829996109
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 NIF1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NIF1_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 NIF1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDR1_SCHPOcdr1physical
9135149
RAD57_SCHPOrad57genetic
18931302
TLG2_SCHPOtlg2genetic
18931302
SKB1_SCHPOskb1genetic
23615447
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NIF1_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 SER-70 AND SER-196, AND MASSSPECTROMETRY.

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