STIL_HUMAN - dbPTM
STIL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STIL_HUMAN
UniProt AC Q15468
Protein Name SCL-interrupting locus protein
Gene Name STIL
Organism Homo sapiens (Human).
Sequence Length 1287
Subcellular Localization Cytoplasm, cytosol . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole .
Protein Description Immediate-early gene. Plays an important role in embryonic development as well as in cellular growth and proliferation; its long-term silencing affects cell survival and cell cycle distribution as well as decreases CDK1 activity correlated with reduced phosphorylation of CDK1. Plays a role as a positive regulator of the sonic hedgehog pathway, acting downstream of PTCH1. [PubMed: 16024801]
Protein Sequence MEPIYPFARPQMNTRFPSSRMVPFHFPPSKCALWNPTPTGDFIYLHLSYYRNPKLVVTEKTIRLAYRHAKQNKKNSSCFLLGSLTADEDEEGVTLTVDRFDPGREVPECLEITPTASLPGDFLIPCKVHTQELCSREMIVHSVDDFSSALKALQCHICSKDSLDCGKLLSLRVHITSRESLDSVEFDLHWAAVTLANNFKCTPVKPIPIIPTALARNLSSNLNISQVQGTYKYGYLTMDETRKLLLLLESDPKVYSLPLVGIWLSGITHIYSPQVWACCLRYIFNSSVQERVFSESGNFIIVLYSMTHKEPEFYECFPCDGKIPDFRFQLLTSKETLHLFKNVEPPDKNPIRCELSAESQNAETEFFSKASKNFSIKRSSQKLSSGKMPIHDHDSGVEDEDFSPRPIPSPHPVSQKISKIQPSVPELSLVLDGNFIESNPLPTPLEMVNNENPPLINHLEHLKPLQPQLYDEKHSPEVEAGEPSLRGIPNQLNQDKPALLRHCKVRQPPAYKKGNPHTRNSIKPSSHNGPSHDIFEKLQTVSAGNVQNEEYPIRPSTLNSRQSSLAPQSQPHDFVFSPHNSGRPMELQIPTPPLPSYCSTNVCRCCQHHSHIQYSPLNSWQGANTVGSIQDVQSEALQKHSLFHPSGCPALYCNAFCSSSSPIALRPQGDMGSCSPHSNIEPSPVARPPSHMDLCNPQPCTVCMHTPKTESDNGMMGLSPDAYRFLTEQDRQLRLLQAQIQRLLEAQSLMPCSPKTTAVEDTVQAGRQMELVSVEAQSSPGLHMRKGVSIAVSTGASLFWNAAGEDQEPDSQMKQDDTKISSEDMNFSVDINNEVTSLPGSASSLKAVDIPSFEESNIAVEEEFNQPLSVSNSSLVVRKEPDVPVFFPSGQLAESVSMCLQTGPTGGASNNSETSEEPKIEHVMQPLLHQPSDNQKIYQDLLGQVNHLLNSSSKETEQPSTKAVIISHECTRTQNVYHTKKKTHHSRLVDKDCVLNATLKQLRSLGVKIDSPTKVKKNAHNVDHASVLACISPEAVISGLNCMSFANVGMSGLSPNGVDLSMEANAIALKYLNENQLSQLSVTRSNQNNCDPFSLLHINTDRSTVGLSLISPNNMSFATKKYMKRYGLLQSSDNSEDEEEPPDNADSKSEYLLNQNLRSIPEQLGGQKEPSKNDHEIINCSNCESVGTNADTPVLRNITNEVLQTKAKQQLTEKPAFLVKNLKPSPAVNLRTGKAEFTQHPEKENEGDITIFPESLQPSETLKQMNSMNSVGTFLDVKRLRQLPKLF
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
1Acetylation-------MEPIYPFA
-------CCCCCCCC		53.4122814378
54UbiquitinationLSYYRNPKLVVTEKT
CEECCCCCEEEEHHH		58.42-
54 (in isoform 2)Ubiquitination-58.42-
60UbiquitinationPKLVVTEKTIRLAYR
CCEEEEHHHHHHHHH		39.63-
60 (in isoform 2)Ubiquitination-39.63-
94PhosphorylationDEDEEGVTLTVDRFD
CCCCCCCEEEEECCC		27.80-
96PhosphorylationDEEGVTLTVDRFDPG
CCCCCEEEEECCCCC		15.82-
127UbiquitinationGDFLIPCKVHTQELC
CCEEEECEECHHHHH		31.53-
127 (in isoform 2)Ubiquitination-31.53-
147PhosphorylationVHSVDDFSSALKALQ
EECHHHHHHHHHHHC		22.99-
148PhosphorylationHSVDDFSSALKALQC
ECHHHHHHHHHHHCC		37.30-
151UbiquitinationDDFSSALKALQCHIC
HHHHHHHHHHCCCCC		46.93-
151 (in isoform 2)Ubiquitination-46.93-
162PhosphorylationCHICSKDSLDCGKLL
CCCCCCCCCCHHCEE		29.82-
225PhosphorylationLSSNLNISQVQGTYK
HCCCCCHHHEEEEEE		24.1928555341
232UbiquitinationSQVQGTYKYGYLTMD
HHEEEEEECEEEECH		31.85-
233PhosphorylationQVQGTYKYGYLTMDE
HEEEEEECEEEECHH		10.6925262027
235PhosphorylationQGTYKYGYLTMDETR
EEEEECEEEECHHHH		8.9125262027
237PhosphorylationTYKYGYLTMDETRKL
EEECEEEECHHHHHH		17.6925262027
241PhosphorylationGYLTMDETRKLLLLL
EEEECHHHHHHHHHH		28.9225262027
243UbiquitinationLTMDETRKLLLLLES
EECHHHHHHHHHHHC		51.40-
272PhosphorylationSGITHIYSPQVWACC
CCCCCCCCHHHHHHH		14.30-
334UbiquitinationRFQLLTSKETLHLFK
EEEEECCHHHHHHHH		49.86-
334 (in isoform 2)Ubiquitination-49.86-
336PhosphorylationQLLTSKETLHLFKNV
EEECCHHHHHHHHCC		24.18-
341UbiquitinationKETLHLFKNVEPPDK
HHHHHHHHCCCCCCC		67.45-
341 (in isoform 2)Ubiquitination-67.45-
348UbiquitinationKNVEPPDKNPIRCEL
HCCCCCCCCCCCCEE		71.09-
348 (in isoform 2)Ubiquitination-71.09-
369UbiquitinationAETEFFSKASKNFSI
HHHHHHHHHHCCCCC		52.07-
372UbiquitinationEFFSKASKNFSIKRS
HHHHHHHCCCCCCCC		67.86-
375PhosphorylationSKASKNFSIKRSSQK
HHHHCCCCCCCCCCC		36.2723186163
379PhosphorylationKNFSIKRSSQKLSSG
CCCCCCCCCCCCCCC		31.9229052541
380PhosphorylationNFSIKRSSQKLSSGK
CCCCCCCCCCCCCCC		35.0529052541
395PhosphorylationMPIHDHDSGVEDEDF
CCCCCCCCCCCCCCC		41.1229255136
403PhosphorylationGVEDEDFSPRPIPSP
CCCCCCCCCCCCCCC		32.1126471730
409PhosphorylationFSPRPIPSPHPVSQK
CCCCCCCCCCCCHHH		36.2425159151
414PhosphorylationIPSPHPVSQKISKIQ
CCCCCCCHHHHHHCC		30.1523186163
416UbiquitinationSPHPVSQKISKIQPS
CCCCCHHHHHHCCCC		41.25-
428PhosphorylationQPSVPELSLVLDGNF
CCCCCCEEEEECCCC		18.12-
470PhosphorylationKPLQPQLYDEKHSPE
CCCCCCCCCCCCCCC		19.4625159151
475PhosphorylationQLYDEKHSPEVEAGE
CCCCCCCCCCCCCCC		33.5528985074
496UbiquitinationPNQLNQDKPALLRHC
CCCCCCCCCHHHHHC		23.56-
496 (in isoform 2)Ubiquitination-23.56-
512AcetylationVRQPPAYKKGNPHTR
ECCCCCCCCCCCCCC		57.2012431479
521PhosphorylationGNPHTRNSIKPSSHN
CCCCCCCCCCCCCCC		28.7928555341
523UbiquitinationPHTRNSIKPSSHNGP
CCCCCCCCCCCCCCC		38.37-
523 (in isoform 2)Ubiquitination-38.37-
557PhosphorylationEYPIRPSTLNSRQSS
CCCCCHHHCCCCCCC		32.4228555341
560PhosphorylationIRPSTLNSRQSSLAP
CCHHHCCCCCCCCCC		34.5128555341
591PhosphorylationPMELQIPTPPLPSYC
CCEEECCCCCCCCCC		38.89-
719PhosphorylationDNGMMGLSPDAYRFL
CCCCCCCCHHHHHHH		18.2721815630
748PhosphorylationQRLLEAQSLMPCSPK
HHHHHHHHCCCCCCC		33.4126552605
753PhosphorylationAQSLMPCSPKTTAVE
HHHCCCCCCCCCCHH		24.4625159151
755UbiquitinationSLMPCSPKTTAVEDT
HCCCCCCCCCCHHHH		42.06-
755 (in isoform 2)Ubiquitination-42.06-
778PhosphorylationLVSVEAQSSPGLHMR
EEEEEECCCCCCCCC		45.6122210691
779PhosphorylationVSVEAQSSPGLHMRK
EEEEECCCCCCCCCC		15.7725159151
811PhosphorylationGEDQEPDSQMKQDDT
CCCCCCCHHCCCCCC		42.7822210691
852PhosphorylationLKAVDIPSFEESNIA
CEEECCCCHHHCCCC		45.70-
869PhosphorylationEEFNQPLSVSNSSLV
EHHCCCCCCCCCCEE		30.13-
936UbiquitinationHQPSDNQKIYQDLLG
CCCCCCHHHHHHHHH		50.03-
938PhosphorylationPSDNQKIYQDLLGQV
CCCCHHHHHHHHHHH		11.7428796482
939PhosphorylationSDNQKIYQDLLGQVN
CCCHHHHHHHHHHHH		38.0527642862
952PhosphorylationVNHLLNSSSKETEQP
HHHHHHCCCCCCCCC		44.3425627689
953PhosphorylationNHLLNSSSKETEQPS
HHHHHCCCCCCCCCC		34.0425627689
954UbiquitinationHLLNSSSKETEQPST
HHHHCCCCCCCCCCC		71.2821906983
954 (in isoform 1)Ubiquitination-71.2821906983
955 (in isoform 2)Ubiquitination-60.5721906983
962UbiquitinationETEQPSTKAVIISHE
CCCCCCCEEEEEEEE		45.02-
963 (in isoform 2)Ubiquitination-9.60-
991UbiquitinationHHSRLVDKDCVLNAT
CCHHHCCHHHHHHHH		45.61-
992 (in isoform 2)Ubiquitination-24.24-
1000UbiquitinationCVLNATLKQLRSLGV
HHHHHHHHHHHHCCC		42.82-
1001 (in isoform 2)Ubiquitination-45.26-
1004PhosphorylationATLKQLRSLGVKIDS
HHHHHHHHCCCCCCC		37.7617924679
1008UbiquitinationQLRSLGVKIDSPTKV
HHHHCCCCCCCCCCC		38.712190698
1008 (in isoform 1)Ubiquitination-38.7121906983
1009 (in isoform 2)Ubiquitination-6.1921906983
1011PhosphorylationSLGVKIDSPTKVKKN
HCCCCCCCCCCCCCC		37.6324719451
1012PhosphorylationLGVKIDSPTKVKKNA
CCCCCCCCCCCCCCC		32.2724719451
1014UbiquitinationVKIDSPTKVKKNAHN
CCCCCCCCCCCCCCC		56.28-
1072PhosphorylationNAIALKYLNENQLSQ
HHHHHHHCCHHHCCC		6.5727642862
1079PhosphorylationLNENQLSQLSVTRSN
CCHHHCCCCCCCCCC		46.4827642862
1082PhosphorylationNQLSQLSVTRSNQNN
HHCCCCCCCCCCCCC		7.5827642862
1108PhosphorylationDRSTVGLSLISPNNM
CCCCEEEEEECCCCC		20.0928348404
1111PhosphorylationTVGLSLISPNNMSFA
CEEEEEECCCCCCHH		27.2025159151
1116PhosphorylationLISPNNMSFATKKYM
EECCCCCCHHHHHHH		17.53-
1119PhosphorylationPNNMSFATKKYMKRY
CCCCCHHHHHHHHHH		26.5121712546
1120UbiquitinationNNMSFATKKYMKRYG
CCCCHHHHHHHHHHC		38.18-
1122 (in isoform 2)Ubiquitination-14.93-
1126PhosphorylationTKKYMKRYGLLQSSD
HHHHHHHHCCCCCCC		13.4528450419
1131PhosphorylationKRYGLLQSSDNSEDE
HHHCCCCCCCCCCCC		39.3628450419
1132PhosphorylationRYGLLQSSDNSEDEE
HHCCCCCCCCCCCCC		28.0528102081
1135PhosphorylationLLQSSDNSEDEEEPP
CCCCCCCCCCCCCCC		51.9525159151
1136PhosphorylationLQSSDNSEDEEEPPD
CCCCCCCCCCCCCCC		75.5727251275
1147PhosphorylationEPPDNADSKSEYLLN
CCCCCCCCHHHHHHH		35.3523186163
1152PhosphorylationADSKSEYLLNQNLRS
CCCHHHHHHHHHHHC		2.9627642862
1168UbiquitinationPEQLGGQKEPSKNDH
HHHHCCCCCCCCCCC		74.90-
1206UbiquitinationTNEVLQTKAKQQLTE
HHHHHHHHHHHHHHC		40.40-
1207 (in isoform 2)Ubiquitination-20.48-
1209 (in isoform 2)Ubiquitination-48.66-
1214UbiquitinationAKQQLTEKPAFLVKN
HHHHHHCCCCEEECC		36.09-
1215 (in isoform 2)Ubiquitination-23.24-
1223UbiquitinationAFLVKNLKPSPAVNL
CEEECCCCCCCCEEC		53.49-
1224 (in isoform 2)Ubiquitination-49.03-
1225PhosphorylationLVKNLKPSPAVNLRT
EECCCCCCCCEECCC		24.7325159151
1234UbiquitinationAVNLRTGKAEFTQHP
CEECCCCCEEECCCC		44.10-
1235 (in isoform 2)Ubiquitination-20.62-
1243UbiquitinationEFTQHPEKENEGDIT
EECCCCCCCCCCCEE		71.00-
1244 (in isoform 2)Ubiquitination-59.87-
1270PhosphorylationKQMNSMNSVGTFLDV
HHHHCCCCCCHHHCH		17.1824260401
1273PhosphorylationNSMNSVGTFLDVKRL
HCCCCCCHHHCHHHH		20.9024260401
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
1108SPhosphorylationKinasePLK1P53350
PSP
1116SPhosphorylationKinasePLK1P53350
PSP
1116SPhosphorylationKinasePLK4O00444
PSP
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:24485834
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STIL_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 STIL_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SAS6_HUMANSASS6physical
22349698
ADPPT_HUMANAASDHPPTphysical
26638075
ABLM1_HUMANABLIM1physical
26638075
ARP2_HUMANACTR2physical
26638075
AP3M1_HUMANAP3M1physical
26638075
ARI1B_HUMANARID1Bphysical
26638075
BAG2_HUMANBAG2physical
26638075
BAG3_HUMANBAG3physical
26638075
BTF3_HUMANBTF3physical
26638075
FBW1A_HUMANBTRCphysical
26638075
C2D1A_HUMANCC2D1Aphysical
26638075
CDC37_HUMANCDC37physical
26638075
CEP85_HUMANCEP85physical
26638075
CNOT3_HUMANCNOT3physical
26638075
CUL1_HUMANCUL1physical
26638075
NB5R3_HUMANCYB5R3physical
26638075
DCP1B_HUMANDCP1Bphysical
26638075
DNJA1_HUMANDNAJA1physical
26638075
DVL3_HUMANDVL3physical
26638075
EDC3_HUMANEDC3physical
26638075
FBW1B_HUMANFBXW11physical
26638075
FKBP4_HUMANFKBP4physical
26638075
GLMN_HUMANGLMNphysical
26638075
GPTC1_HUMANGPATCH1physical
26638075
GTPB1_HUMANGTPBP1physical
26638075
HAUS7_HUMANHAUS7physical
26638075
HINT1_HUMANHINT1physical
26638075
HS105_HUMANHSPH1physical
26638075
IRAK1_HUMANIRAK1physical
26638075
LIMD1_HUMANLIMD1physical
26638075
LRC49_HUMANLRRC49physical
26638075
MAGD1_HUMANMAGED1physical
26638075
MK09_HUMANMAPK9physical
26638075
M21D2_HUMANMB21D2physical
26638075
MTMR6_HUMANMTMR6physical
26638075
NAA15_HUMANNAA15physical
26638075
NEDD1_HUMANNEDD1physical
26638075
NDK7_HUMANNME7physical
26638075
NMT1_HUMANNMT1physical
26638075
NUDC2_HUMANNUDCD2physical
26638075
OFD1_HUMANOFD1physical
26638075
PCM1_HUMANPCM1physical
26638075
PEA15_HUMANPEA15physical
26638075
PFD4_HUMANPFDN4physical
26638075
PRPS1_HUMANPRPS1physical
26638075
RPAP3_HUMANRPAP3physical
26638075
RIR2_HUMANRRM2physical
26638075
SAS6_HUMANSASS6physical
26638075
SDCG3_HUMANSDCCAG3physical
26638075
SC23B_HUMANSEC23Bphysical
26638075
SC24C_HUMANSEC24Cphysical
26638075
SMG7_HUMANSMG7physical
26638075
SMG9_HUMANSMG9physical
26638075
ADIP_HUMANSSX2IPphysical
26638075
CHIP_HUMANSTUB1physical
26638075
SGT1_HUMANSUGT1physical
26638075
SP16H_HUMANSUPT16Hphysical
26638075
TBK1_HUMANTBK1physical
26638075
TCHP_HUMANTCHPphysical
26638075
TNPO1_HUMANTNPO1physical
26638075
TNR6B_HUMANTNRC6Bphysical
26638075
TPGS1_HUMANTPGS1physical
26638075
TRIP6_HUMANTRIP6physical
26638075
TXND9_HUMANTXNDC9physical
26638075
UN45A_HUMANUNC45Aphysical
26638075
RENT1_HUMANUPF1physical
26638075
VCIP1_HUMANVCPIP1physical
26638075
WDR83_HUMANWDR83physical
26638075
XRN1_HUMANXRN1physical
26638075
YTHD3_HUMANYTHDF3physical
26638075
CENPJ_HUMANCENPJphysical
26638075
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
Note=A chromosomal aberration involving STIL may be a cause of some T-cell acute lymphoblastic leukemias (T-ALL). A deletion at 1p32 between STIL and TAL1 genes leads to STIL/TAL1 fusion mRNA with STIL exon 1 slicing to TAL1 exon 3. As both STIL exon 1 and TAL1 exon 3 are 5'-untranslated exons, STIL/TAL1 fusion mRNA predicts a full length TAL1 protein under the control of the STIL promoter, leading to inappropriate TAL1 expression. In childhood T-cell malignancies (T-ALL), a type of defect such as STIL/TAL1 fusion is associated with a good prognosis. In cultured lymphocytes from healthy adults, STIL/TAL1 fusion mRNA may be detected after 7 days of culture.
612703
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STIL_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-1135, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-753, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1004, AND MASSSPECTROMETRY.

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