TEA2_SCHPO - dbPTM
TEA2_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TEA2_SCHPO
UniProt AC Q1MTQ1
Protein Name Kinesin-like protein tea2
Gene Name tea2 {ECO:0000312|EMBL:CAA22353.1}
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 628
Subcellular Localization Cytoplasm, cytoskeleton . Localized in large clusters at cell tips and also in punctate dots within the cell that are coincident with the ends of cytoplasmic microtubules.
Protein Description Promotes microtubule growth, possibly through interactions with the microtubule end, and is important for establishing and maintaining polarized growth along the long axis of the cell. Acts as a kinesin motor protein that moves along microtubules and is required for proper localization of tea1 and tip1 to the cell tips and microtubules, respectively. ATPase activity stimulated via interaction with mal3..
Protein Sequence MSSSSSKPVNTGLVTPRRYSTMTGIRTGPSQSGTGSIPYSPTSPLSRNFSNYSIPMLRSNSTQTNVNGPTAFDLGVTEKLMSPGTLDRYTRPALYPSKDLDYLKNEYVNYESTTSQQTNSKGLKESNFVGSGIITSIRIRPIGKNQGVWSHGKLSNDPYGREYIRQQTSTSSSTIQQEYLFNNVFGMESKNYDIYKRSVKSVVRNVFSGYNGIVFAYGMTGTGKTYSMQGTENEPGIIPLAMNDLFEMVENNSDDDTFQIRISYLEIYNERIRDLIGNSDEEPRIRENASGEVNVTPLTRVLVTSPEEVSQVIEQCNAIRKTAATDFNTYSSRSHAILQVFLIRNNPTAHTSQISSLSLVDLAGSERASAHHERRKEGAFINKSLLTLGTVISRLSAAANPSLTSNSGHIPYRESKLTRLLQQSLSGQSQISLLATISIESNHTMETTNTLKFASRAQNLPQDIRQAEAVTNVQAELASLHSALEKNAQEVEYYASLVKQLTSDLEERDTYIAMLEAERSQGTAISRARLRMEELLSDHNFEIADLRDELQDKEQIIYALRYAQKQRDIADFNQSLAKFPHKILKKNVTRGSRSSSDQFSNETKTEILPDDQQQSKKDSVTQETQLLS
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
4Phosphorylation----MSSSSSKPVNT
----CCCCCCCCCCC
31.1829996109
15PhosphorylationPVNTGLVTPRRYSTM
CCCCCCCCCCCEECC
19.0029996109
20PhosphorylationLVTPRRYSTMTGIRT
CCCCCCEECCCCCCC
15.1929996109
40PhosphorylationGTGSIPYSPTSPLSR
CCCCCCCCCCCCCCC
19.1525720772
42PhosphorylationGSIPYSPTSPLSRNF
CCCCCCCCCCCCCCC
36.7225720772
43PhosphorylationSIPYSPTSPLSRNFS
CCCCCCCCCCCCCCC
27.5125720772
46PhosphorylationYSPTSPLSRNFSNYS
CCCCCCCCCCCCCCC
28.6727738172
50PhosphorylationSPLSRNFSNYSIPML
CCCCCCCCCCCCCEE
38.1125720772
52PhosphorylationLSRNFSNYSIPMLRS
CCCCCCCCCCCEECC
13.5325720772
53PhosphorylationSRNFSNYSIPMLRSN
CCCCCCCCCCEECCC
25.1925720772
59PhosphorylationYSIPMLRSNSTQTNV
CCCCEECCCCCCCCC
31.0429996109
61PhosphorylationIPMLRSNSTQTNVNG
CCEECCCCCCCCCCC
24.1225720772
62PhosphorylationPMLRSNSTQTNVNGP
CEECCCCCCCCCCCC
43.6025720772
64PhosphorylationLRSNSTQTNVNGPTA
ECCCCCCCCCCCCCE
41.0229996109
82PhosphorylationGVTEKLMSPGTLDRY
CCCCCCCCCCCCCCC
30.5228889911
589PhosphorylationKILKKNVTRGSRSSS
HHHHCCCCCCCCCCC
38.4121712547
592PhosphorylationKKNVTRGSRSSSDQF
HCCCCCCCCCCCCCC
26.2124763107
594PhosphorylationNVTRGSRSSSDQFSN
CCCCCCCCCCCCCCC
35.5724763107
595PhosphorylationVTRGSRSSSDQFSNE
CCCCCCCCCCCCCCC
36.5024763107
596PhosphorylationTRGSRSSSDQFSNET
CCCCCCCCCCCCCCC
36.3621712547
600PhosphorylationRSSSDQFSNETKTEI
CCCCCCCCCCCCCCC
28.2921712547
619PhosphorylationQQQSKKDSVTQETQL
HHHHHHCCCHHHHHH
35.6225720772

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 TEA2_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TEA2_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 TEA2_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAL3_SCHPOmal3physical
12894167
TIP1_SCHPOtip1physical
15177031
MAL3_SCHPOmal3physical
15177031
TEA2_SCHPOtea2physical
15665379
RES2_SCHPOres2genetic
18931302
VPS8_SCHPOvps8genetic
18931302
FLP1_SCHPOclp1genetic
18931302
CDC16_SCHPOcdc16genetic
20498706
MAD2_SCHPOmad2genetic
20498706
PP2B_SCHPOppb1physical
21336311
RSC4_SCHPOrsc4genetic
18818364
SWD2_SCHPOswd2genetic
18818364
SGF29_SCHPOsgf29genetic
18818364
BDC1_SCHPObdc1genetic
18818364
COPE_SCHPOsec28genetic
18818364
ASK1_SCHPOask1genetic
18818364
NGG1_SCHPOngg1genetic
18818364
YB3C_SCHPOcay1genetic
18818364
SWD3_SCHPOswd3genetic
18818364
ELP6_SCHPOelp6genetic
18818364
CLR4_SCHPOclr4genetic
18818364
SUM2_SCHPOsum2genetic
18818364
HPC2_SCHPOhip4genetic
18818364
AIR1_SCHPOair1genetic
18818364
RIK1_SCHPOrik1genetic
18818364
RPA12_SCHPOrpa12genetic
18818364
2AD1_SCHPOpar1genetic
18818364
SET1_SCHPOset1genetic
18818364
SPP1_SCHPOspf1genetic
18818364
ASF1_SCHPOcia1genetic
18818364
DCN1_SCHPOSPBC839.03cgenetic
18818364
TIP1_SCHPOtip1physical
22144913
SFT1_SCHPOsft1genetic
22681890
HRP3_SCHPOhrp3genetic
22681890
VTS1_SCHPOSPBC13E7.03cgenetic
22681890
ILVB_SCHPOilv1genetic
22681890
BDC1_SCHPObdc1genetic
22681890
PAC2_SCHPOpac2genetic
22681890
EIF2A_SCHPOSPBC4B4.04genetic
22681890
RTF2_SCHPOrtf2genetic
22681890
COQ5_SCHPOcoq5genetic
22681890
ERFB_SCHPOerf2genetic
22681890
YIPL_SCHPOSPAPJ691.02genetic
22681890
YFY2_SCHPOSPAC9.02cgenetic
22681890
ERG28_SCHPOerg28genetic
22681890
YN8E_SCHPOSPBP35G2.14genetic
22681890
DBR1_SCHPOdbr1genetic
22681890
YKTB_SCHPOSPAPB1E7.11cgenetic
22681890
RPA12_SCHPOrpa12genetic
22681890
BST1_SCHPObst1genetic
22681890
CLR4_SCHPOclr4genetic
22681890
NEM1_SCHPOnem1genetic
22681890
SPP1_SCHPOspf1genetic
22681890
MBO1_SCHPOmto1genetic
22681890
CG121_SCHPOcgi121genetic
22681890
MOD5P_SCHPOmod5genetic
22681890
GCN5_SCHPOgcn5genetic
22681890
SWD1_SCHPOswd1genetic
22681890
HOB3_SCHPOhob3genetic
22681890
MAL3_SCHPOmal3genetic
22681890
FT105_SCHPOftp105genetic
22681890
RSC4_SCHPOrsc4genetic
22681890
HMT2_SCHPOhmt2genetic
22681890
YF19_SCHPOatd1genetic
22681890
HIBCH_SCHPOsnr1genetic
22681890
MUG20_SCHPOmug20genetic
22681890
YF75_SCHPOspa2genetic
22681890
YIDH_SCHPOSPAC227.17cgenetic
22681890
VPS3_SCHPOvps3genetic
22681890
YJ53_SCHPOSPCC4F11.03cgenetic
22681890
YE87_SCHPOSPAC9G1.07genetic
22681890
SET1_SCHPOset1genetic
22681890
CTK3_SCHPOlsg1genetic
22681890
EME1_SCHPOeme1genetic
22681890
ASK1_SCHPOask1genetic
22681890
YBPD_SCHPOSPBC16H5.13genetic
22681890
SHR3_SCHPOpsh3genetic
22681890
TOM70_SCHPOtom70genetic
22681890
YB33_SCHPOebs1genetic
22681890
SUM2_SCHPOsum2genetic
22681890
DAD2_SCHPOdad2genetic
22681890
YHZ3_SCHPOath1genetic
22681890
TBA2_SCHPOatb2genetic
22681890
TIP1_SCHPOtip1genetic
22681890
AKR1_SCHPOakr1genetic
22681890
YJC7_SCHPOSPCC736.07cgenetic
22681890
PUR4_SCHPOade3genetic
22681890
RL21B_SCHPOrpl2102genetic
22681890
ARC1_SCHPOSPAC30C2.04genetic
22681890
YKEE_SCHPOSPAC1805.14genetic
22681890
YOX1_SCHPOyox1genetic
22681890
SGF29_SCHPOsgf29genetic
22681890
TEA2_SCHPOtea2physical
23615447
TIP1_SCHPOtip1physical
23615447

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TEA2_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-82, AND MASSSPECTROMETRY.

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