RAP1_SCHPO - dbPTM
RAP1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAP1_SCHPO
UniProt AC Q96TL7
Protein Name DNA-binding protein rap1
Gene Name rap1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 693
Subcellular Localization Nucleus . Chromosome, telomere .
Protein Description Involved in the regulation of telomere length, clustering and has a specific role in telomere position effect (TPE). Unlike yeast, exhibits no effect in transcription regulation..
Protein Sequence MSFTFTKSDGSSILFAVSKNFEHIRGFKNAIDCFKGKIEFLSFDKVDPTKHDYYLVAEDERVSDLDIPKGFFERNPEFRHKMLKIAWITQCIEQGKLLPTESFEVELNQDDVNRTHDGFRKRELFTLEDEKILIDHVHKNDINRFGTKVYEELARKYPQHSLESWRQHYKYMKKRLPPVSDSDESNYCQRIIVKPYSSQKDYTQSTHEQTLSSPISKSASVSKSENKALVNNKRYSDSYFYFSKMRRISIDVDYVDEDLNLINAYLSQFGKKRSLNELCALLSRRFSNRHTFSEWRALFMHFFPFINSEGVDPAILSDRETSAMLDETSDNEVADIDDQMIERKYLFSASEPNTVKSTNRLIFSERKAYAADDSIDNTPSKVPIVNSLSDPRTNRPFFYSNPDSMYRSISNPLHLVDSQHLSPLNRKTHFNNPIGQPQFTCLDDHEKTLRETSFRSLDDMSLRKSNSDNIFVKPGEDLEIPLLSDYSDSENISEKSSDDEEAFEKQVTSSYSSPIKVKSQGKSSKGSSGLDVREHEGSDDDAEVFVDRSPESFGATKVAHTSLEGNAASHKKVEENMQQPVTKKQKKYRMVNEEAHTGPTIIIPSDNNEKVTTLPAGHVPSEEKGKFINLAMHELQNEVSILRSSVNHREVDEAIDNILRYTNSTEQQFLEAMESTGGRVRIAIAKLLSKQTS
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
205PhosphorylationSQKDYTQSTHEQTLS
CCCCCCCCCCHHHCC		24.7521712547
210PhosphorylationTQSTHEQTLSSPISK
CCCCCHHHCCCCCCC		26.1421712547
212PhosphorylationSTHEQTLSSPISKSA
CCCHHHCCCCCCCCC		37.1421712547
213PhosphorylationTHEQTLSSPISKSAS
CCHHHCCCCCCCCCC		29.3924763107
216PhosphorylationQTLSSPISKSASVSK
HHCCCCCCCCCCCCH		24.7629996109
350PhosphorylationRKYLFSASEPNTVKS
HHHCCCCCCCCCCCC		53.0024763107
354PhosphorylationFSASEPNTVKSTNRL
CCCCCCCCCCCCCEE		39.7724763107
357PhosphorylationSEPNTVKSTNRLIFS
CCCCCCCCCCEEEEE		26.9521712547
358PhosphorylationEPNTVKSTNRLIFSE
CCCCCCCCCEEEEEC		20.7421712547
364PhosphorylationSTNRLIFSERKAYAA
CCCEEEEECCHHHCC		29.5121712547
374PhosphorylationKAYAADDSIDNTPSK
HHHCCCCCCCCCCCC		32.1824763107
378PhosphorylationADDSIDNTPSKVPIV
CCCCCCCCCCCCCCC		25.7824763107
408PhosphorylationNPDSMYRSISNPLHL
CHHHHHHHCCCCCHH		16.9325720772
410PhosphorylationDSMYRSISNPLHLVD
HHHHHHCCCCCHHCC		33.3729996109
418PhosphorylationNPLHLVDSQHLSPLN
CCCHHCCCCCCCCCC		16.4229996109
422PhosphorylationLVDSQHLSPLNRKTH
HCCCCCCCCCCCCCC		25.8025720772
509PhosphorylationAFEKQVTSSYSSPIK
HHHHHHHHCCCCCEE		28.5524763107
511PhosphorylationEKQVTSSYSSPIKVK
HHHHHHCCCCCEEEE		16.9724763107
513PhosphorylationQVTSSYSSPIKVKSQ
HHHHCCCCCEEEEEC		23.5525720772
528PhosphorylationGKSSKGSSGLDVREH
CCCCCCCCCCCCCCC		52.6321712547
538PhosphorylationDVREHEGSDDDAEVF
CCCCCCCCCCCCEEE		34.5821712547
549PhosphorylationAEVFVDRSPESFGAT
CEEEECCCHHHCCCC		28.6721712547
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 RAP1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAP1_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 RAP1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RIF1_SCHPOrif1genetic
11676925
TAZ1_SCHPOtaz1genetic
16096639
RIF1_SCHPOrif1genetic
16096639
TOP2_SCHPOtop2genetic
16096639
TAZ1_SCHPOtaz1physical
11676924
RAP1_SCHPOrap1physical
11676925
RAD57_SCHPOrad57genetic
18931302
DNLI4_SCHPOlig4genetic
17632059
TAZ1_SCHPOtaz1physical
21217703
ELOC_SCHPOSPBC1861.07genetic
18818364
ELP5_SCHPOelp5genetic
18818364
VPS71_SCHPOvps71genetic
18818364
YB33_SCHPOebs1genetic
18818364
YB3C_SCHPOcay1genetic
18818364
TMA20_SCHPOtma20genetic
18818364
HIR1_SCHPOhip1genetic
18818364
MAD1_SCHPOmad1genetic
18818364
RAD14_SCHPOrhp14genetic
18818364
TAS3_SCHPOtas3genetic
18818364
UBP3_SCHPOubp3genetic
18818364
MGDP1_SCHPOSPBP8B7.31genetic
18818364
CDS1_SCHPOcds1genetic
18818364
MSH6_SCHPOmsh6genetic
18818364
SET1_SCHPOset1genetic
18818364
SKI2_SCHPOSPCC550.03cgenetic
18818364
SWC5_SCHPOswc5genetic
18818364
JHD1_SCHPOepe1genetic
18818364
ELP2_SCHPOelp2genetic
18818364
CCQ1_SCHPOccq1genetic
22101932
ATM_SCHPOtel1genetic
22101932
RAD3_SCHPOrad3genetic
22101932
BQT2_SCHPObqt2physical
23133674
POZ1_SCHPOpoz1physical
23133674
TAZ1_SCHPOtaz1physical
23133674
BQT1_SCHPObqt1physical
23133674
DDB1_SCHPOddb1genetic
22681890
RIK1_SCHPOrik1genetic
22681890
YG58_SCHPOSPBC56F2.08cgenetic
22681890
GPD1_SCHPOgpd1genetic
22681890
RAF2_SCHPOraf2genetic
22681890
TWF1_SCHPOtwf1genetic
22681890
RAD55_SCHPOrad55genetic
22681890
CIP1_SCHPOcip1genetic
22681890
GDA1_SCHPOgda1genetic
22681890
CHP1_SCHPOchp1genetic
22681890
HRQ1_SCHPOhrq1genetic
22681890
FTA6_SCHPOfta6genetic
22681890
CSN1_SCHPOcsn1genetic
22681890
ARP42_SCHPOarp42genetic
22681890
YGL4_SCHPOmxr2genetic
22681890
ASH2_SCHPOash2genetic
22681890
RAD57_SCHPOrad57genetic
22681890
JHD1_SCHPOepe1genetic
22681890
ERS1_SCHPOers1genetic
22681890
UBP3_SCHPOubp3genetic
22681890
MST2_SCHPOmst2genetic
22681890
BCS1_SCHPOSPAC644.07genetic
22681890
YE87_SCHPOSPAC9G1.07genetic
22681890
RLA6_SCHPOrpp203genetic
22681890
YBPD_SCHPOSPBC16H5.13genetic
22681890
YK1D_SCHPOSPAPB1A10.13genetic
22681890
CGM2_SCHPOmcs2genetic
22681890
MU154_SCHPOmug154genetic
22681890
NBS1_SCHPOnbs1genetic
23188080
TAZ1_SCHPOtaz1genetic
24244195
BQT1_SCHPObqt1physical
26058898
BQT2_SCHPObqt2physical
26058898
BQT4_SCHPObqt4physical
26058898
POZ1_SCHPOpoz1physical
26058898
POZ1_SCHPOpoz1physical
26063574
POZ1_SCHPOpoz1physical
26988418
TPZ1_SCHPOtpz1physical
26988418
POT1_SCHPOpot1physical
26988418
CCQ1_SCHPOccq1physical
26988418
TAZ1_SCHPOtaz1physical
26988418
CLR4_SCHPOclr4physical
26988418
CUL4_SCHPOpcu4physical
26988418
RIK1_SCHPOrik1physical
26988418
CLR3_SCHPOclr3physical
26988418
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAP1_SCHPO

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory