TEA4_SCHPO - dbPTM
TEA4_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TEA4_SCHPO
UniProt AC O60132
Protein Name Tip elongation aberrant protein Tea4
Gene Name tea4 {ECO:0000312|PomBase:SPBC1706.01}
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 821
Subcellular Localization Cytoplasm, cytoskeleton . Through it's binding with tea1, is transported by the cytoplasmic microtubule system and is localized at cell tips, microtubule plus ends and cytoplasmic dots.
Protein Description Cell polarity factor essential for the bipolar localization and function of structures containing the cell-end marker tea1 during the normal cell cycle. Regulates cell polarity in complex with tea1 and together with the stress signaling MAPK cascade, contributes to cell polarity maintenance under stress conditions. Required for the localization of for3 at the cell tip specifically during initiation of bipolar growth. During the new end take off (NETO), formation of a protein complex that includes tea1, tea4 and for3 is necessary and sufficient for the establishment of cell polarity and localized actin assembly at new cell ends..
Protein Sequence MLHMNSASSADSMEIMESHFDPTQQNDSTIIESRYSPEEYLEQSFEIQRIISGENSEPQTVASQEISDSQEEDTTLTSSQFEDCGTEYNEVVEDDEFRSEDEDDFMDEEEEYALYEAELSSSPSIHEEVIDCNFVHAIRGFEATVEGQVDATKGDMMILLDDSNSYWWLVKMCKNLAIGYLPAEYIETPSERLARLNKYKNSETSNSQQSVTLPPLDIVEKTLEAPSPNFRIKRVTFTCSSNSSDDEMDSENDYEAMVNRTVAENGLEIEFSDSSDSSLSAEYRSESEDHVTDSPAYVDLTELEGGFNQFNSTSFQSTSPLGLEIVETEINGSSTTADSKNSHSPYSKFSSAYPDAENSNISKINISIAGNKELYGNATQSDPSLYSTWIANKHKTASSATVDSPLRRSLSVDAMQSNASFSSYSSTSNTDKSLRPSSYSAVSESSNFTHDVSRDNKEISLNAPKSIIVSQSDSFDTSNVTQDAPNDVEKEPISGQMPNNLSVQSLKQLEVYPIRHSVSIEMPSEKLLSPRLYSSSTPSSPTKGFQKDDEEDSENRKQADKVELSPSSLLRQMSLPVDSSSQSDAQCTTSSVYITAERKAFSQSSIDLSTLSNHHVNNEINRRSFAGGFTSLADELSEMRELLHESPAPLECNEEMVIPTPELDASSAIPSSSISHDEDLLPRKNTEESTSSSSFSSLITSPASLQYDENPFKQSVVAELNNNSSSVPFVDSAHASDIHAYDNDHVSTKNKEFNRRLREFILDPDSLSGLYWSVKSAGVRASRRVSRNIEGESVSSDLDDIFANVLKGLSDEMASLLNTNR
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
35PhosphorylationSTIIESRYSPEEYLE
CCCEECCCCHHHHHH		2.9228889911
36PhosphorylationTIIESRYSPEEYLEQ
CCEECCCCHHHHHHH		24.2728889911
40PhosphorylationSRYSPEEYLEQSFEI
CCCCHHHHHHHHEEE		37.3728889911
44PhosphorylationPEEYLEQSFEIQRII
HHHHHHHHEEEEEHH		46.4829996109
202PhosphorylationRLNKYKNSETSNSQQ
HHHHHCCCCCCCCCC		20.3125720772
204PhosphorylationNKYKNSETSNSQQSV
HHHCCCCCCCCCCCE		7.1025720772
205PhosphorylationKYKNSETSNSQQSVT
HHCCCCCCCCCCCEE		48.9725720772
207PhosphorylationKNSETSNSQQSVTLP
CCCCCCCCCCCEEEC		6.5225720772
210PhosphorylationETSNSQQSVTLPPLD
CCCCCCCCEEECCHH		19.1425720772
222PhosphorylationPLDIVEKTLEAPSPN
CHHHHHHHHCCCCCC		30.2729996109
227PhosphorylationEKTLEAPSPNFRIKR
HHHHCCCCCCCEEEE		3.5228889911
344PhosphorylationADSKNSHSPYSKFSS
CCCCCCCCCCHHHHH		17.2321712547
350PhosphorylationHSPYSKFSSAYPDAE
CCCCHHHHHCCCCCC		31.5624763107
359PhosphorylationAYPDAENSNISKINI
CCCCCCCCCCCEEEE		26.1325720772
362PhosphorylationDAENSNISKINISIA
CCCCCCCCEEEEEEC		7.6721712547
381PhosphorylationLYGNATQSDPSLYST
HCCCCCCCCHHHHHH		37.1421712547
396PhosphorylationWIANKHKTASSATVD
HHCCCCCCCCCCCCC		50.0225720772
398PhosphorylationANKHKTASSATVDSP
CCCCCCCCCCCCCCH		5.6925720772
399PhosphorylationNKHKTASSATVDSPL
CCCCCCCCCCCCCHH		21.1425720772
401PhosphorylationHKTASSATVDSPLRR
CCCCCCCCCCCHHHH		32.7125720772
404PhosphorylationASSATVDSPLRRSLS
CCCCCCCCHHHHHCC		34.9425720772
409PhosphorylationVDSPLRRSLSVDAMQ
CCCHHHHHCCHHHHH		5.3725720772
411PhosphorylationSPLRRSLSVDAMQSN
CHHHHHCCHHHHHCC		27.3325720772
433PhosphorylationSTSNTDKSLRPSSYS
CCCCCCCCCCCCCCC		24.0721712547
437PhosphorylationTDKSLRPSSYSAVSE
CCCCCCCCCCCCCCC		22.7821712547
438PhosphorylationDKSLRPSSYSAVSES
CCCCCCCCCCCCCCC		29.3629996109
439PhosphorylationKSLRPSSYSAVSESS
CCCCCCCCCCCCCCC		36.7121712547
440PhosphorylationSLRPSSYSAVSESSN
CCCCCCCCCCCCCCC		3.8229996109
443PhosphorylationPSSYSAVSESSNFTH
CCCCCCCCCCCCCCC		64.1525720772
445PhosphorylationSYSAVSESSNFTHDV
CCCCCCCCCCCCCCC		61.7925720772
446PhosphorylationYSAVSESSNFTHDVS
CCCCCCCCCCCCCCC		44.0325720772
502PhosphorylationGQMPNNLSVQSLKQL
CCCCCCCCCCCCCEE		3.2024763107
505PhosphorylationPNNLSVQSLKQLEVY
CCCCCCCCCCEEEEE		14.0124763107
517PhosphorylationEVYPIRHSVSIEMPS
EEEECCCEEEEECCC		20.5729996109
533PhosphorylationKLLSPRLYSSSTPSS
CCCCCCCCCCCCCCC		9.7025720772
534PhosphorylationLLSPRLYSSSTPSSP
CCCCCCCCCCCCCCC		57.8621712547
535PhosphorylationLSPRLYSSSTPSSPT
CCCCCCCCCCCCCCC		65.9629996109
536PhosphorylationSPRLYSSSTPSSPTK
CCCCCCCCCCCCCCC		58.7425720772
537PhosphorylationPRLYSSSTPSSPTKG
CCCCCCCCCCCCCCC		69.1224763107
539PhosphorylationLYSSSTPSSPTKGFQ
CCCCCCCCCCCCCCC		74.0521712547
540PhosphorylationYSSSTPSSPTKGFQK
CCCCCCCCCCCCCCC		60.2428889911
542PhosphorylationSSTPSSPTKGFQKDD
CCCCCCCCCCCCCCC		73.6721712547
565PhosphorylationQADKVELSPSSLLRQ
HHHHEEECHHHHHHH		15.7228889911
567PhosphorylationDKVELSPSSLLRQMS
HHEEECHHHHHHHCC		31.9325720772
568PhosphorylationKVELSPSSLLRQMSL
HEEECHHHHHHHCCC		28.1225720772
602PhosphorylationTAERKAFSQSSIDLS
EECCCHHCCCCCCHH		23.9329996109
604PhosphorylationERKAFSQSSIDLSTL
CCCHHCCCCCCHHHH		6.8225720772
610PhosphorylationQSSIDLSTLSNHHVN
CCCCCHHHHCCCCCC		41.0829996109
624PhosphorylationNNEINRRSFAGGFTS
CCCCHHCCCCCCHHH		5.6029996109
646PhosphorylationMRELLHESPAPLECN
HHHHHHCCCCCCCCC		2.8029996109
660PhosphorylationNEEMVIPTPELDASS
CCCCEECCCCCCCCC		26.7427738172
689PhosphorylationPRKNTEESTSSSSFS
CCCCCCCCCCCCCCH		16.1025720772
690PhosphorylationRKNTEESTSSSSFSS
CCCCCCCCCCCCCHH		19.7425720772
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 TEA4_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TEA4_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 TEA4_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FOR3_SCHPOfor3genetic
15809031
TEA1_SCHPOtea1physical
15809031
TEA1_SCHPOtea1physical
15936270
PP11_SCHPOdis2physical
21703453
POM1_SCHPOpom1physical
21703453
MYO52_SCHPOmyo52genetic
22137473
TIP1_SCHPOtip1physical
15809031
FOR3_SCHPOfor3physical
15809031
YD83_SCHPOSPAC1F3.03genetic
22681890
YOI5_SCHPOSPBC1778.05cgenetic
22681890
TCO89_SCHPOtco89genetic
22681890
DPH3_SCHPOdph3genetic
22681890
ELP6_SCHPOelp6genetic
22681890
YFY2_SCHPOSPAC9.02cgenetic
22681890
YN8E_SCHPOSPBP35G2.14genetic
22681890
NEM1_SCHPOnem1genetic
22681890
MBO1_SCHPOmto1genetic
22681890
CG121_SCHPOcgi121genetic
22681890
OXR1_SCHPOmug63genetic
22681890
ZIP1_SCHPOzip1genetic
22681890
DOM34_SCHPOdom34genetic
22681890
YBPC_SCHPOSPBC16H5.12cgenetic
22681890
GBB_SCHPOgit5genetic
22681890
VPS38_SCHPOvps38genetic
22681890
YEEB_SCHPOSPAC19A8.11cgenetic
22681890
MST2_SCHPOmst2genetic
22681890
TSR4_SCHPOSPBC25H2.15genetic
22681890
ERD11_SCHPOerd1genetic
22681890
SHR3_SCHPOpsh3genetic
22681890
YAM5_SCHPOmso1genetic
22681890
RFP2_SCHPOrfp2genetic
22681890
CTU2_SCHPOctu2genetic
22681890
CTU1_SCHPOctu1genetic
22681890
MUG73_SCHPOmug73genetic
22681890
TEA1_SCHPOtea1physical
23695164
RGA4_SCHPOrga4physical
24554432
TEA1_SCHPOtea1physical
26771498
GEF1_SCHPOgef1genetic
26246599
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TEA4_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 TYR-23; SER-24 AND TYR-28,AND MASS SPECTROMETRY.

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