SKI_HUMAN - dbPTM
SKI_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SKI_HUMAN
UniProt AC P12755
Protein Name Ski oncogene
Gene Name SKI
Organism Homo sapiens (Human).
Sequence Length 728
Subcellular Localization Nucleus.
Protein Description May play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. Functions as a repressor of TGF-beta signaling..
Protein Sequence MEAAAGGRGCFQPHPGLQKTLEQFHLSSMSSLGGPAAFSARWAQEAYKKESAKEAGAAAVPAPVPAATEPPPVLHLPAIQPPPPVLPGPFFMPSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLITKTDAERLCNALLYGGAYPPPCKKELAASLALGLELSERSVRVYHECFGKCKGLLVPELYSSPSAACIQCLDCRLMYPPHKFVVHSHKALENRTCHWGFDSANWRAYILLSQDYTGKEEQARLGRCLDDVKEKFDYGNKYKRRVPRVSSEPPASIRPKTDDTSSQSPAPSEKDKPSSWLRTLAGSSNKSLGCVHPRQRLSAFRPWSPAVSASEKELSPHLPALIRDSFYSYKSFETAVAPNVALAPPAQQKVVSSPPCAAAVSRAPEPLATCTQPRKRKLTVDTPGAPETLAPVAAPEEDKDSEAEVEVESREEFTSSLSSLSSPSFTSSSSAKDLGSPGARALPSAVPDAAAPADAPSGLEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAENEKKMKEANESRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQLWPRARPEAAGSEGAAELEP
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
103PhosphorylationRSTERCETVLEGETI
CCCCCCCCHHCCCEE
33.7322817900
119UbiquitinationCFVVGGEKRLCLPQI
EEEECCCEEECHHHH
54.6822817900
170PhosphorylationVMGILPFSAPSCGLI
HHCCCCCCCCCCCCC
37.0123403867
173PhosphorylationILPFSAPSCGLITKT
CCCCCCCCCCCCCHH
22.1223403867
214PhosphorylationLALGLELSERSVRVY
HHHCHHCHHHHHHHH
22.9123532336
227UbiquitinationVYHECFGKCKGLLVP
HHHHHHCCCCCCCCC
16.72-
245UbiquitinationSSPSAACIQCLDCRL
CCCCHHHHHHHCCCC
2.5122817900
258UbiquitinationRLMYPPHKFVVHSHK
CCCCCCCEEEEECCC
45.7029967540
294UbiquitinationLSQDYTGKEEQARLG
ECCCCCCHHHHHHHC
50.7221906983
316UbiquitinationEKFDYGNKYKRRVPR
HHCCCCCCCCCCCCC
48.0329967540
318AcetylationFDYGNKYKRRVPRVS
CCCCCCCCCCCCCCC
35.0220167786
325PhosphorylationKRRVPRVSSEPPASI
CCCCCCCCCCCCCCC
30.2023312004
326PhosphorylationRRVPRVSSEPPASIR
CCCCCCCCCCCCCCC
51.7930624053
335AcetylationPPASIRPKTDDTSSQ
CCCCCCCCCCCCCCC
55.5320167786
339PhosphorylationIRPKTDDTSSQSPAP
CCCCCCCCCCCCCCC
32.8429396449
340PhosphorylationRPKTDDTSSQSPAPS
CCCCCCCCCCCCCCC
33.1229396449
341PhosphorylationPKTDDTSSQSPAPSE
CCCCCCCCCCCCCCC
36.4525262027
343PhosphorylationTDDTSSQSPAPSEKD
CCCCCCCCCCCCCCC
25.6125627689
347PhosphorylationSSQSPAPSEKDKPSS
CCCCCCCCCCCCCCH
60.4225072903
349AcetylationQSPAPSEKDKPSSWL
CCCCCCCCCCCCHHH
75.3325953088
349UbiquitinationQSPAPSEKDKPSSWL
CCCCCCCCCCCCHHH
75.3329967540
351AcetylationPAPSEKDKPSSWLRT
CCCCCCCCCCHHHHH
58.8425953088
351UbiquitinationPAPSEKDKPSSWLRT
CCCCCCCCCCHHHHH
58.8429967540
354PhosphorylationSEKDKPSSWLRTLAG
CCCCCCCHHHHHHHC
38.3625159151
365UbiquitinationTLAGSSNKSLGCVHP
HHHCCCCCCCCCCCH
49.3532015554
366PhosphorylationLAGSSNKSLGCVHPR
HHCCCCCCCCCCCHH
33.9525159151
377PhosphorylationVHPRQRLSAFRPWSP
CCHHHHHHHCCCCCC
27.7923403867
383PhosphorylationLSAFRPWSPAVSASE
HHHCCCCCCCCCCCC
12.9823401153
387O-linked_GlycosylationRPWSPAVSASEKELS
CCCCCCCCCCCCHHC
28.3428657654
387PhosphorylationRPWSPAVSASEKELS
CCCCCCCCCCCCHHC
28.3423403867
389O-linked_GlycosylationWSPAVSASEKELSPH
CCCCCCCCCCHHCCC
41.5128657654
389PhosphorylationWSPAVSASEKELSPH
CCCCCCCCCCHHCCC
41.5123403867
394PhosphorylationSASEKELSPHLPALI
CCCCCHHCCCHHHHH
16.0328188228
404PhosphorylationLPALIRDSFYSYKSF
HHHHHHHCCCCCCCC
19.0825159151
409UbiquitinationRDSFYSYKSFETAVA
HHCCCCCCCCCCCCC
42.6121906983
431PhosphorylationPAQQKVVSSPPCAAA
HHHHCCCCCCCCHHH
39.8623401153
432PhosphorylationAQQKVVSSPPCAAAV
HHHCCCCCCCCHHHH
22.6623401153
440O-linked_GlycosylationPPCAAAVSRAPEPLA
CCCHHHHHCCCCCCC
20.2828657654
440PhosphorylationPPCAAAVSRAPEPLA
CCCHHHHHCCCCCCC
20.2829396449
448PhosphorylationRAPEPLATCTQPRKR
CCCCCCCCCCCCCCC
24.6226074081
450PhosphorylationPEPLATCTQPRKRKL
CCCCCCCCCCCCCCC
36.9326074081
458PhosphorylationQPRKRKLTVDTPGAP
CCCCCCCCCCCCCCC
21.2629978859
461PhosphorylationKRKLTVDTPGAPETL
CCCCCCCCCCCCCCC
21.2029978859
467PhosphorylationDTPGAPETLAPVAAP
CCCCCCCCCCCCCCC
27.4530108239
480PhosphorylationAPEEDKDSEAEVEVE
CCCCCCCCCCEEEEE
44.4330266825
488PhosphorylationEAEVEVESREEFTSS
CCEEEEECHHHHHHH
50.6030266825
493PhosphorylationVESREEFTSSLSSLS
EECHHHHHHHHHHHC
22.2329978859
495PhosphorylationSREEFTSSLSSLSSP
CHHHHHHHHHHHCCC
29.2529978859
497PhosphorylationEEFTSSLSSLSSPSF
HHHHHHHHHHCCCCC
31.0529978859
498PhosphorylationEFTSSLSSLSSPSFT
HHHHHHHHHCCCCCC
37.2528348404
500PhosphorylationTSSLSSLSSPSFTSS
HHHHHHHCCCCCCCC
41.9929978859
501PhosphorylationSSLSSLSSPSFTSSS
HHHHHHCCCCCCCCC
29.8328348404
503PhosphorylationLSSLSSPSFTSSSSA
HHHHCCCCCCCCCCC
43.0029978859
505PhosphorylationSLSSPSFTSSSSAKD
HHCCCCCCCCCCCHH
31.8529978859
506PhosphorylationLSSPSFTSSSSAKDL
HCCCCCCCCCCCHHH
26.6429978859
507PhosphorylationSSPSFTSSSSAKDLG
CCCCCCCCCCCHHHC
25.8429978859
508PhosphorylationSPSFTSSSSAKDLGS
CCCCCCCCCCHHHCC
33.8029978859
509PhosphorylationPSFTSSSSAKDLGSP
CCCCCCCCCHHHCCC
41.0929978859
515PhosphorylationSSAKDLGSPGARALP
CCCHHHCCCCHHCCC
27.7028102081
523PhosphorylationPGARALPSAVPDAAA
CCHHCCCCCCCCCCC
42.6326074081
584UbiquitinationLSAALQAKRSLHQEL
HHHHHHHHHHHHHHH
29.5629967540
633PhosphorylationKMKEANESRLRLKRE
HHHHHHHHHHHHHHH
36.1026074081
662UbiquitinationEAGRLRAKYSAQIED
HHHHHHHHHHHHHHH
33.0529967540
673UbiquitinationQIEDLQVKLQHAEAD
HHHHHHHHHHHHHHC
29.4829967540
720PhosphorylationARPEAAGSEGAAELE
CCHHHCCCCCCCCCC
28.2930576142

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
326SPhosphorylationKinaseAURKAO14965
GPS
383SPhosphorylationKinaseAURKAO14965
GPS
458TPhosphorylationKinaseAKT1P31749
PSP
-KUbiquitinationE3 ubiquitin ligaseRNF111Q6ZNA4
PMID:17510063

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 SKI_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HIPK2_HUMANHIPK2physical
12874272
SMAD3_HUMANSMAD3physical
12857746
SMAD4_HUMANSMAD4physical
12857746
SMAD4_HUMANSMAD4physical
12419246
SNW1_HUMANSNW1physical
11522815
NFIX_HUMANNFIXphysical
9380514
SKI_HUMANSKIphysical
9927733
SKIL_HUMANSKILphysical
9927733
SNW1_HUMANSNW1physical
9569025
MECP2_HUMANMECP2physical
11441023
HDAC3_HUMANHDAC3physical
19341714
PRD16_HUMANPRDM16physical
19049980
SMAD2_HUMANSMAD2physical
19032343
SMAD3_HUMANSMAD3physical
19032343
SMAD4_HUMANSMAD4physical
19032343
ANM5_HUMANPRMT5physical
19032343
HDAC3_HUMANHDAC3physical
19032343
TBL1R_HUMANTBL1XR1physical
19032343
NCOR1_HUMANNCOR1physical
19032343
SIX1_HUMANSIX1physical
19008232
EYA3_HUMANEYA3physical
19008232
SMAD2_HUMANSMAD2physical
12732634
SMAD4_HUMANSMAD4physical
12732634
GLI3_HUMANGLI3physical
12435627
GLI2_HUMANGLI2physical
12435627
SMAD2_HUMANSMAD2physical
10575014
SMAD3_HUMANSMAD3physical
10575014
RB_HUMANRB1physical
9988677
MYB_HUMANMYBphysical
14761981
SMAD3_HUMANSMAD3physical
14699069
SMAD4_HUMANSMAD4physical
14699069
HDAC3_HUMANHDAC3physical
17621263
SPI1_HUMANSPI1physical
17621263
SIAH2_HUMANSIAH2physical
20691163
P53_HUMANTP53physical
21149449
SMAD2_HUMANSMAD2physical
21149449
SIN3A_HUMANSIN3Aphysical
21149449
SIR1_HUMANSIRT1physical
21149449
TGFR1_HUMANTGFBR1physical
20959473
SMAD2_HUMANSMAD2physical
20959473
SMAD4_HUMANSMAD4physical
20959473
ESR1_HUMANESR1physical
22227247
NCOR1_HUMANNCOR1physical
14525983
SIN3A_HUMANSIN3Aphysical
14525983
SMAD4_HUMANSMAD4physical
14525983
SMAD3_HUMANSMAD3physical
14525983
RBCC1_HUMANRB1CC1physical
21795712
AKT1_HUMANAKT1physical
19875456
AKT2_HUMANAKT2physical
19875456
SMAD3_HUMANSMAD3physical
19875456
SMAD3_HUMANSMAD3physical
12764135
SMAD2_HUMANSMAD2physical
12764135
SMAD4_HUMANSMAD4physical
12764135
SMAD3_HUMANSMAD3physical
17469184
SMAD4_HUMANSMAD4physical
17469184
LATS2_HUMANLATS2physical
25670202
STK38_HUMANSTK38physical
25670202
ST38L_HUMANSTK38Lphysical
25670202
SMAD3_HUMANSMAD3physical
25670202
MERTK_HUMANMERTKphysical
25670202
SAV1_HUMANSAV1physical
25670202
MOB1A_HUMANMOB1Aphysical
25670202
MOB1B_HUMANMOB1Bphysical
25670202
TEAD1_HUMANTEAD1physical
25670202
SMAD4_HUMANSMAD4physical
25670202
SKI_HUMANSKIphysical
25670202
PLEC_HUMANPLECphysical
25670202
ACTB_HUMANACTBphysical
25670202
HSP7C_HUMANHSPA8physical
25670202
TBA1A_HUMANTUBA1Aphysical
25670202
TBA1B_HUMANTUBA1Bphysical
25670202
TBB6_HUMANTUBB6physical
25670202
TBB5_HUMANTUBBphysical
25670202
TBB2A_HUMANTUBB2Aphysical
25670202
GRP75_HUMANHSPA9physical
25670202
GRP78_HUMANHSPA5physical
25670202
ACTBL_HUMANACTBL2physical
25670202
ATPA_HUMANATP5A1physical
25670202
PRDX1_HUMANPRDX1physical
25670202
PYGB_HUMANPYGBphysical
25670202
TBA4A_HUMANTUBA4Aphysical
25670202
PYR1_HUMANCADphysical
25670202
RL4_HUMANRPL4physical
25670202
HS71L_HUMANHSPA1Lphysical
25670202
PRKDC_HUMANPRKDCphysical
25670202
ADT2_HUMANSLC25A5physical
25670202
ATPB_HUMANATP5Bphysical
25670202
PFKAP_HUMANPFKPphysical
25670202
HS90B_HUMANHSP90AB1physical
25670202
TCPA_HUMANTCP1physical
25670202
MVP_HUMANMVPphysical
25670202
RL18_HUMANRPL18physical
25670202
AHNK_HUMANAHNAKphysical
25670202
ADT3_HUMANSLC25A6physical
25670202
HSP76_HUMANHSPA6physical
25670202
RL12_HUMANRPL12physical
25670202
ITB4_HUMANITGB4physical
25670202
LDHA_HUMANLDHAphysical
25670202
EFTU_HUMANTUFMphysical
25670202
PPM1B_HUMANPPM1Bphysical
25670202
ADT1_HUMANSLC25A4physical
25670202
SQSTM_HUMANSQSTM1physical
25670202
WDR26_HUMANWDR26physical
25670202
RS3_HUMANRPS3physical
25670202
RACK1_HUMANGNB2L1physical
25670202
RS16_HUMANRPS16physical
25670202
PABP1_HUMANPABPC1physical
25670202
DDX5_HUMANDDX5physical
25670202
EPIPL_HUMANEPPK1physical
25670202
AT1A1_HUMANATP1A1physical
25670202
NUCL_HUMANNCLphysical
25670202
HNRPM_HUMANHNRNPMphysical
25670202
RLA0_HUMANRPLP0physical
25670202
CMC2_HUMANSLC25A13physical
25670202
SQOR_HUMANSQRDLphysical
25670202
PGBM_HUMANHSPG2physical
25670202
PABP4_HUMANPABPC4physical
25670202
AGRIN_HUMANAGRNphysical
25670202
DYHC1_HUMANDYNC1H1physical
25670202
ECHB_HUMANHADHBphysical
25670202
SMAD2_HUMANSMAD2physical
25670202
RS4X_HUMANRPS4Xphysical
25670202
RL14_HUMANRPL14physical
25670202
CH60_HUMANHSPD1physical
25670202
QCR2_HUMANUQCRC2physical
25670202
RL30_HUMANRPL30physical
25670202
TCPG_HUMANCCT3physical
25670202
COPB_HUMANCOPB1physical
25670202
DCAF7_HUMANDCAF7physical
25670202
RANB9_HUMANRANBP9physical
25670202
PCNA_HUMANPCNAphysical
25670202
AT2A2_HUMANATP2A2physical
25670202
DIAP1_HUMANDIAPH1physical
25670202
ECHA_HUMANHADHAphysical
25670202
ATPO_HUMANATP5Ophysical
25670202
SMAD4_HUMANSMAD4physical
28468752
SMAD2_HUMANSMAD2physical
28468752
SMUF2_HUMANSMURF2physical
28468752

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
182212Shprintzen-Goldberg craniosynostosis syndrome (SGS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SKI_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND MASSSPECTROMETRY.

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