SKA3_HUMAN - dbPTM
SKA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SKA3_HUMAN
UniProt AC Q8IX90
Protein Name Spindle and kinetochore-associated protein 3
Gene Name SKA3
Organism Homo sapiens (Human).
Sequence Length 412
Subcellular Localization Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore . Localizes to the outer kinetochore and spindle microtubules during mitosis in a NDC80 complex-dependent manner.
Protein Description Component of the SKA1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. [PubMed: 19289083]
Protein Sequence MDPIRSFCGKLRSLASTLDCETARLQRALDGEESDFEDYPMRILYDLHSEVQTLKDDVNILLDKARLENQEGIDFIKATKVLMEKNSMDIMKIREYFQKYGYSPRVKKNSVHEQEAINSDPELSNCENFQKTDVKDDLSDPPVASSCISEKSPRSPQLSDFGLERYIVSQVLPNPPQAVNNYKEEPVIVTPPTKQSLVKVLKTPKCALKMDDFECVTPKLEHFGISEYTMCLNEDYTMGLKNARNNKSEEAIDTESRLNDNVFATPSPIIQQLEKSDAEYTNSPLVPTFCTPGLKIPSTKNSIALVSTNYPLSKTNSSSNDLEVEDRTSLVLNSDTCFENLTDPSSPTISSYENLLRTPTPPEVTKIPEDILQLLSKYNSNLATPIAIKAVPPSKRFLKHGQNIRDVSNKEN
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
10AcetylationPIRSFCGKLRSLAST
HHHHHHHHHHHHHHH		41.7425953088
10UbiquitinationPIRSFCGKLRSLAST
HHHHHHHHHHHHHHH		41.74-
17UbiquitinationKLRSLASTLDCETAR
HHHHHHHHCCHHHHH		22.4727667366
34PhosphorylationRALDGEESDFEDYPM
HHHCCCCCCCCCCCH		43.2121712546
39PhosphorylationEESDFEDYPMRILYD
CCCCCCCCCHHHHHH		7.5429396449
45PhosphorylationDYPMRILYDLHSEVQ
CCCHHHHHHHHHHHH		17.68-
59UbiquitinationQTLKDDVNILLDKAR
HHHHHHHHHHHHHHH		26.6127667366
64AcetylationDVNILLDKARLENQE
HHHHHHHHHHHHCCC		35.067428227
64UbiquitinationDVNILLDKARLENQE
HHHHHHHHHHHHCCC		35.0629967540
77UbiquitinationQEGIDFIKATKVLME
CCCCCHHHHHHHHHH		50.42-
87PhosphorylationKVLMEKNSMDIMKIR
HHHHHHCCCCHHHHH		28.9720068231
99UbiquitinationKIREYFQKYGYSPRV
HHHHHHHHHCCCCCC		30.6432015554
100PhosphorylationIREYFQKYGYSPRVK
HHHHHHHHCCCCCCC		15.5426074081
102PhosphorylationEYFQKYGYSPRVKKN
HHHHHHCCCCCCCCC		16.6528985074
103PhosphorylationYFQKYGYSPRVKKNS
HHHHHCCCCCCCCCC		11.2323911959
108UbiquitinationGYSPRVKKNSVHEQE
CCCCCCCCCCCCHHH		52.1529967540
110PhosphorylationSPRVKKNSVHEQEAI
CCCCCCCCCCHHHHH		33.4623401153
112UbiquitinationRVKKNSVHEQEAINS
CCCCCCCCHHHHHHC		30.7327667366
119PhosphorylationHEQEAINSDPELSNC
CHHHHHHCCCCHHCC		48.7229255136
120UbiquitinationEQEAINSDPELSNCE
HHHHHHCCCCHHCCC		35.8827667366
124PhosphorylationINSDPELSNCENFQK
HHCCCCHHCCCCCCC		37.4629255136
131UbiquitinationSNCENFQKTDVKDDL
HCCCCCCCCCCCCCC		42.4229967540
132PhosphorylationNCENFQKTDVKDDLS
CCCCCCCCCCCCCCC		34.93-
139PhosphorylationTDVKDDLSDPPVASS
CCCCCCCCCCCCHHH		55.8825159151
145PhosphorylationLSDPPVASSCISEKS
CCCCCCHHHHHCCCC		26.4423663014
146PhosphorylationSDPPVASSCISEKSP
CCCCCHHHHHCCCCC		13.0123663014
149PhosphorylationPVASSCISEKSPRSP
CCHHHHHCCCCCCCC		43.2123663014
151UbiquitinationASSCISEKSPRSPQL
HHHHHCCCCCCCCCH		59.9929967540
152PhosphorylationSSCISEKSPRSPQLS
HHHHCCCCCCCCCHH		22.8425159151
154UbiquitinationCISEKSPRSPQLSDF
HHCCCCCCCCCHHHH		68.9727667366
155PhosphorylationISEKSPRSPQLSDFG
HCCCCCCCCCHHHHC		22.0019664994
159PhosphorylationSPRSPQLSDFGLERY
CCCCCCHHHHCCCHH		26.1625159151
162UbiquitinationSPQLSDFGLERYIVS
CCCHHHHCCCHHHHH		31.4527667366
165UbiquitinationLSDFGLERYIVSQVL
HHHHCCCHHHHHHCC		31.3624816145
166PhosphorylationSDFGLERYIVSQVLP
HHHCCCHHHHHHCCC		9.0423879269
182PhosphorylationPPQAVNNYKEEPVIV
CCCHHHCCCCCCEEE		17.9928450419
183UbiquitinationPQAVNNYKEEPVIVT
CCHHHCCCCCCEEEC		58.69-
190PhosphorylationKEEPVIVTPPTKQSL
CCCCEEECCCCHHHH		16.6619664994
193PhosphorylationPVIVTPPTKQSLVKV
CEEECCCCHHHHHHH		42.8130266825
194UbiquitinationVIVTPPTKQSLVKVL
EEECCCCHHHHHHHH		43.6027667366
196PhosphorylationVTPPTKQSLVKVLKT
ECCCCHHHHHHHHCC		36.3620068231
199UbiquitinationPTKQSLVKVLKTPKC
CCHHHHHHHHCCCCC		47.33-
202UbiquitinationQSLVKVLKTPKCALK
HHHHHHHCCCCCCCC		66.8127667366
203PhosphorylationSLVKVLKTPKCALKM
HHHHHHCCCCCCCCC		24.6624719451
207UbiquitinationVLKTPKCALKMDDFE
HHCCCCCCCCCCCCE		19.1524816145
209UbiquitinationKTPKCALKMDDFECV
CCCCCCCCCCCCEEC		23.04-
217PhosphorylationMDDFECVTPKLEHFG
CCCCEECCCCCHHCC		26.7725159151
228PhosphorylationEHFGISEYTMCLNED
HHCCCCCEEEECCCC		7.93-
229PhosphorylationHFGISEYTMCLNEDY
HCCCCCEEEECCCCC		9.4327642862
236PhosphorylationTMCLNEDYTMGLKNA
EEECCCCCHHHCCCC		7.7627642862
247UbiquitinationLKNARNNKSEEAIDT
CCCCCCCCCHHHCCC		63.8924816145
248PhosphorylationKNARNNKSEEAIDTE
CCCCCCCCHHHCCCH		42.6729255136
254PhosphorylationKSEEAIDTESRLNDN
CCHHHCCCHHHHCCC		29.7328985074
265PhosphorylationLNDNVFATPSPIIQQ
HCCCCCCCCCHHHHH		16.9125159151
267PhosphorylationDNVFATPSPIIQQLE
CCCCCCCCHHHHHHH		25.1125159151
275UbiquitinationPIIQQLEKSDAEYTN
HHHHHHHHCCCCCCC		63.3329967540
276PhosphorylationIIQQLEKSDAEYTNS
HHHHHHHCCCCCCCC		32.4528796482
280PhosphorylationLEKSDAEYTNSPLVP
HHHCCCCCCCCCCCC		16.9728796482
281PhosphorylationEKSDAEYTNSPLVPT
HHCCCCCCCCCCCCC		22.2630576142
283PhosphorylationSDAEYTNSPLVPTFC
CCCCCCCCCCCCCCC		16.2925159151
288PhosphorylationTNSPLVPTFCTPGLK
CCCCCCCCCCCCCCC		24.7027732954
291PhosphorylationPLVPTFCTPGLKIPS
CCCCCCCCCCCCCCC		19.0525159151
295UbiquitinationTFCTPGLKIPSTKNS
CCCCCCCCCCCCCCE		59.4929967540
300UbiquitinationGLKIPSTKNSIALVS
CCCCCCCCCEEEEEE		53.7029967540
302PhosphorylationKIPSTKNSIALVSTN
CCCCCCCEEEEEECC		15.7018452278
307PhosphorylationKNSIALVSTNYPLSK
CCEEEEEECCCCCCC		16.2828442448
308PhosphorylationNSIALVSTNYPLSKT
CEEEEEECCCCCCCC		31.1528442448
310PhosphorylationIALVSTNYPLSKTNS
EEEEECCCCCCCCCC		12.9730576142
313PhosphorylationVSTNYPLSKTNSSSN
EECCCCCCCCCCCCC		32.6930576142
314UbiquitinationSTNYPLSKTNSSSND
ECCCCCCCCCCCCCC		60.4529967540
315PhosphorylationTNYPLSKTNSSSNDL
CCCCCCCCCCCCCCC		36.6419690332
317PhosphorylationYPLSKTNSSSNDLEV
CCCCCCCCCCCCCEE		40.1325159151
318PhosphorylationPLSKTNSSSNDLEVE
CCCCCCCCCCCCEEC		34.9225159151
319PhosphorylationLSKTNSSSNDLEVED
CCCCCCCCCCCEECC		33.9019690332
329PhosphorylationLEVEDRTSLVLNSDT
CEECCHHEEECCCCC		19.8528464451
334PhosphorylationRTSLVLNSDTCFENL
HHEEECCCCCHHHCC		30.0926074081
336PhosphorylationSLVLNSDTCFENLTD
EEECCCCCHHHCCCC		20.9326074081
342PhosphorylationDTCFENLTDPSSPTI
CCHHHCCCCCCCCCC		58.4026074081
345PhosphorylationFENLTDPSSPTISSY
HHCCCCCCCCCCCCH		52.3226074081
346PhosphorylationENLTDPSSPTISSYE
HCCCCCCCCCCCCHH		31.3028464451
348PhosphorylationLTDPSSPTISSYENL
CCCCCCCCCCCHHHH		35.1226074081
350PhosphorylationDPSSPTISSYENLLR
CCCCCCCCCHHHHHC		29.3726074081
351PhosphorylationPSSPTISSYENLLRT
CCCCCCCCHHHHHCC		32.3926074081
352PhosphorylationSSPTISSYENLLRTP
CCCCCCCHHHHHCCC		11.3126074081
358PhosphorylationSYENLLRTPTPPEVT
CHHHHHCCCCCCHHH		31.3325159151
360PhosphorylationENLLRTPTPPEVTKI
HHHHCCCCCCHHHCC		51.3625159151
365PhosphorylationTPTPPEVTKIPEDIL
CCCCCHHHCCCHHHH		22.9227174698
366 (in isoform 3)Ubiquitination-62.5321906983
366UbiquitinationPTPPEVTKIPEDILQ
CCCCHHHCCCHHHHH		62.5329967540
376PhosphorylationEDILQLLSKYNSNLA
HHHHHHHHHHCCCCC		41.5124719451
377UbiquitinationDILQLLSKYNSNLAT
HHHHHHHHHCCCCCC		48.7132015554
378PhosphorylationILQLLSKYNSNLATP
HHHHHHHHCCCCCCC		22.0520068231
380PhosphorylationQLLSKYNSNLATPIA
HHHHHHCCCCCCCEE		30.0820068231
384PhosphorylationKYNSNLATPIAIKAV
HHCCCCCCCEEEECC		20.5625159151
389AcetylationLATPIAIKAVPPSKR
CCCCEEEECCCCHHH		34.0225953088
394PhosphorylationAIKAVPPSKRFLKHG
EEECCCCHHHHHHCC		30.3220068231
399UbiquitinationPPSKRFLKHGQNIRD
CCHHHHHHCCCCHHH		42.8729967540
399AcetylationPPSKRFLKHGQNIRD
CCHHHHHHCCCCHHH		42.8725953088
408PhosphorylationGQNIRDVSNKEN---
CCCHHHCCCCCC---		46.61-
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
203TPhosphorylationKinaseCDK1P06493
PSP
217TPhosphorylationKinaseCDK1P06493
PSP
283SPhosphorylationKinaseCDK1P06493
PSP
291TPhosphorylationKinaseCDK1P06493
PSP
358TPhosphorylationKinaseCDK1P06493
PSP
360TPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SKA3_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 SKA3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CREST_HUMANSS18L1physical
22371557
SPC24_HUMANSPC24physical
22371557
A4_HUMANAPPphysical
21832049
ECT2_HUMANECT2physical
26496610
GDIB_HUMANGDI2physical
26496610
K2C3_HUMANKRT3physical
26496610
MYO5B_HUMANMYO5Bphysical
26496610
IKBE_HUMANNFKBIEphysical
26496610
MP2K1_HUMANMAP2K1physical
26496610
MRCKA_HUMANCDC42BPAphysical
26496610
AP3B1_HUMANAP3B1physical
26496610
RTL8C_HUMANFAM127Aphysical
26496610
PALLD_HUMANPALLDphysical
26496610
ANKH1_HUMANANKHD1physical
26496610
HMCES_HUMANHMCESphysical
26496610
INT5_HUMANINTS5physical
26496610
K2013_HUMANKIAA2013physical
26496610
SKA1_HUMANSKA1physical
26496610
PGM2L_HUMANPGM2L1physical
26496610
SKA2_HUMANSKA2physical
26496610
PHLB3_HUMANPHLDB3physical
26496610
SKA1_HUMANSKA1physical
28514442
SKA2_HUMANSKA2physical
28514442
NOL4_HUMANNOL4physical
28514442
NOL4L_HUMANNOL4Lphysical
28514442
CC85B_HUMANCCDC85Bphysical
28514442
LRCC1_HUMANLRRCC1physical
28514442
CC85C_HUMANCCDC85Cphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SKA3_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-155; SER-318 ANDTHR-358, AND MASS SPECTROMETRY.
"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-34; SER-119; SER-155;THR-217; THR-265; SER-267 AND THR-384, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; THR-190; THR-217;SER-276; THR-315; SER-318 AND THR-384, AND MASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-155; THR-265;THR-291 AND THR-358, AND MASS SPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-280, AND MASSSPECTROMETRY.

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