SKIV2_HUMAN - dbPTM
SKIV2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SKIV2_HUMAN
UniProt AC Q15477
Protein Name Helicase SKI2W
Gene Name SKIV2L
Organism Homo sapiens (Human).
Sequence Length 1246
Subcellular Localization Nucleus . Cytoplasm .
Protein Description Helicase; has ATPase activity. Component of the SKI complex which is thought to be involved in exosome-mediated RNA decay and associates with transcriptionally active genes in a manner dependent on PAF1 complex (PAF1C)..
Protein Sequence MMETERLVLPPPDPLDLPLRAVELGCTGHWELLNLPGAPESSLPHGLPPCAPDLQQEAEQLFLSSPAWLPLHGVEHSARKWQRKTDPWSLLAVLGAPVPSDLQAQRHPTTGQILGYKEVLLENTNLSATTSLSLRRPPGPASQSLWGNPTQYPFWPGGMDEPTITDLNTREEAEEEIDFEKDLLTIPPGFKKGMDFAPKDCPTPAPGLLSLSCMLEPLDLGGGDEDENEAVGQPGGPRGDTVSASPCSAPLARASSLEDLVLKEASTAVSTPEAPEPPSQEQWAIPVDATSPVGDFYRLIPQPAFQWAFEPDVFQKQAILHLERHDSVFVAAHTSAGKTVVAEYAIALAQKHMTRTIYTSPIKALSNQKFRDFRNTFGDVGLLTGDVQLHPEASCLIMTTEILRSMLYSGSDVIRDLEWVIFDEVHYINDVERGVVWEEVLIMLPDHVSIILLSATVPNALEFADWIGRLKRRQIYVISTVTRPVPLEHYLFTGNSSKTQGELFLLLDSRGAFHTKGYYAAVEAKKERMSKHAQTFGAKQPTHQGGPAQDRGVYLSLLASLRTRAQLPVVVFTFSRGRCDEQASGLTSLDLTTSSEKSEIHLFLQRCLARLRGSDRQLPQVLHMSELLNRGLGVHHSGILPILKEIVEMLFSRGLVKVLFATETFAMGVNMPARTVVFDSMRKHDGSTFRDLLPGEYVQMAGRAGRRGLDPTGTVILLCKGRVPEMADLHRMMMGKPSQLQSQFRLTYTMILNLLRVDALRVEDMMKRSFSEFPSRKDSKAHEQALAELTKRLGALEEPDMTGQLVDLPEYYSWGEELTETQHMIQRRIMESVNGLKSLSAGRVVVVKNQEHHNALGVILQVSSNSTSRVFTTLVLCDKPLSQDPQDRGPATAEVPYPDDLVGFKLFLPEGPCDHTVVKLQPGDMAAITTKVLRVNGEKILEDFSKRQQPKFKKDPPLAAVTTAVQELLRLAQAHPAGPPTLDPVNDLQLKDMSVVEGGLRARKLEELIQGAQCVHSPRFPAQYLKLRERMQIQKEMERLRFLLSDQSLLLLPEYHQRVEVLRTLGYVDEAGTVKLAGRVACAMSSHELLLTELMFDNALSTLRPEEIAALLSGLVCQSPGDAGDQLPNTLKQGIERVRAVAKRIGEVQVACGLNQTVEEFVGELNFGLVEVVYEWARGMPFSELAGLSGTPEGLVVRCIQRLAEMCRSLRGAARLVGEPVLGAKMETAATLLRRDIVFAASLYTQ
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----MMETERLVLPP
----CCCCEECCCCC		25.7121406692
84UbiquitinationSARKWQRKTDPWSLL
CHHHHCCCCCCCHHH		42.03-
131PhosphorylationTNLSATTSLSLRRPP
CCCCCEEEEEECCCC		16.1722167270
133PhosphorylationLSATTSLSLRRPPGP
CCCEEEEEECCCCCC		21.4322167270
181UbiquitinationEEEIDFEKDLLTIPP
HHHCCCCHHHCCCCC		54.38-
185PhosphorylationDFEKDLLTIPPGFKK
CCCHHHCCCCCCCCC		38.44-
191UbiquitinationLTIPPGFKKGMDFAP
CCCCCCCCCCCCCCC		55.09-
192UbiquitinationTIPPGFKKGMDFAPK
CCCCCCCCCCCCCCC		58.15-
241PhosphorylationPGGPRGDTVSASPCS
CCCCCCCCCCCCCCC		21.1323927012
243PhosphorylationGPRGDTVSASPCSAP
CCCCCCCCCCCCCCC		25.7330266825
245PhosphorylationRGDTVSASPCSAPLA
CCCCCCCCCCCCCHH		20.9519664994
248PhosphorylationTVSASPCSAPLARAS
CCCCCCCCCCHHCCC		35.9830266825
255PhosphorylationSAPLARASSLEDLVL
CCCHHCCCCHHHHHH		29.8722167270
256PhosphorylationAPLARASSLEDLVLK
CCHHCCCCHHHHHHH		34.4919664994
266PhosphorylationDLVLKEASTAVSTPE
HHHHHHHCCCCCCCC		20.2828464451
267PhosphorylationLVLKEASTAVSTPEA
HHHHHHCCCCCCCCC		37.8229116813
270PhosphorylationKEASTAVSTPEAPEP
HHHCCCCCCCCCCCC		35.4629116813
271PhosphorylationEASTAVSTPEAPEPP
HHCCCCCCCCCCCCC		20.6722817900
279PhosphorylationPEAPEPPSQEQWAIP
CCCCCCCCHHCCCCC		58.0028102081
290PhosphorylationWAIPVDATSPVGDFY
CCCCCCCCCCCCCHH		29.1528102081
291PhosphorylationAIPVDATSPVGDFYR
CCCCCCCCCCCCHHH		21.2228102081
316UbiquitinationFEPDVFQKQAILHLE
CCCCHHHHHHHHHHH		30.17-
327PhosphorylationLHLERHDSVFVAAHT
HHHHHCCCEEEEEEC		16.0120873877
334PhosphorylationSVFVAAHTSAGKTVV
CEEEEEECCCCCHHH		18.6228851738
335PhosphorylationVFVAAHTSAGKTVVA
EEEEEECCCCCHHHH		25.7528851738
351UbiquitinationYAIALAQKHMTRTIY
HHHHHHHHHCCCEEE		29.72-
356PhosphorylationAQKHMTRTIYTSPIK
HHHHCCCEEECCHHH		14.7928787133
358PhosphorylationKHMTRTIYTSPIKAL
HHCCCEEECCHHHHH		10.6826074081
359PhosphorylationHMTRTIYTSPIKALS
HCCCEEECCHHHHHC		24.9526074081
360PhosphorylationMTRTIYTSPIKALSN
CCCEEECCHHHHHCC		13.9926074081
363UbiquitinationTIYTSPIKALSNQKF
EEECCHHHHHCCCCH		46.8121906983
363UbiquitinationTIYTSPIKALSNQKF
EEECCHHHHHCCCCH		46.8121890473
366PhosphorylationTSPIKALSNQKFRDF
CCHHHHHCCCCHHHH		41.9126074081
3692-HydroxyisobutyrylationIKALSNQKFRDFRNT
HHHHCCCCHHHHHHH		46.76-
369UbiquitinationIKALSNQKFRDFRNT
HHHHCCCCHHHHHHH		46.76-
405PhosphorylationMTTEILRSMLYSGSD
CCHHHHHHHHHCCCH		15.0829396449
408PhosphorylationEILRSMLYSGSDVIR
HHHHHHHHCCCHHHH		11.4429396449
409PhosphorylationILRSMLYSGSDVIRD
HHHHHHHCCCHHHHC		28.0520068231
411PhosphorylationRSMLYSGSDVIRDLE
HHHHHCCCHHHHCCE		23.8220068231
476PhosphorylationRLKRRQIYVISTVTR
HHHHCEEEEEEEECC		5.38-
493PhosphorylationPLEHYLFTGNSSKTQ
ECCEEEEECCCCCCC		32.6220860994
496PhosphorylationHYLFTGNSSKTQGEL
EEEEECCCCCCCEEE		34.2620860994
509PhosphorylationELFLLLDSRGAFHTK
EEEEEEECCCCCCCC		32.3623186163
516UbiquitinationSRGAFHTKGYYAAVE
CCCCCCCCHHHHHHH		36.0221906983
518PhosphorylationGAFHTKGYYAAVEAK
CCCCCCHHHHHHHHH		7.47-
519PhosphorylationAFHTKGYYAAVEAKK
CCCCCHHHHHHHHHH		9.21-
5252-HydroxyisobutyrylationYYAAVEAKKERMSKH
HHHHHHHHHHHHHHH		41.48-
525MalonylationYYAAVEAKKERMSKH
HHHHHHHHHHHHHHH		41.4826320211
525UbiquitinationYYAAVEAKKERMSKH
HHHHHHHHHHHHHHH		41.48-
526UbiquitinationYAAVEAKKERMSKHA
HHHHHHHHHHHHHHH		58.56-
530PhosphorylationEAKKERMSKHAQTFG
HHHHHHHHHHHHHHC		27.7520068231
531UbiquitinationAKKERMSKHAQTFGA
HHHHHHHHHHHHHCC		33.35-
535PhosphorylationRMSKHAQTFGAKQPT
HHHHHHHHHCCCCCC		25.4822210691
539AcetylationHAQTFGAKQPTHQGG
HHHHHCCCCCCCCCC		58.1325953088
539UbiquitinationHAQTFGAKQPTHQGG
HHHHHCCCCCCCCCC		58.1321906983
560PhosphorylationVYLSLLASLRTRAQL
HHHHHHHHHHHHCCC		20.5324719451
573PhosphorylationQLPVVVFTFSRGRCD
CCCEEEEEECCCCCC		14.75-
575PhosphorylationPVVVFTFSRGRCDEQ
CEEEEEECCCCCCHH		30.66-
597UbiquitinationDLTTSSEKSEIHLFL
ECCCCCCHHHHHHHH		56.17-
637PhosphorylationRGLGVHHSGILPILK
CCCCCCCCCHHHHHH		16.7925850435
697PhosphorylationRDLLPGEYVQMAGRA
HHHCCHHHHHHCCCC		11.2527642862
714PhosphorylationRGLDPTGTVILLCKG
CCCCCCCCEEEEECC		13.5728857561
720UbiquitinationGTVILLCKGRVPEMA
CCEEEEECCCCHHHH		50.12-
736UbiquitinationLHRMMMGKPSQLQSQ
HHHHHCCCHHHHHHH		24.49-
748PhosphorylationQSQFRLTYTMILNLL
HHHHHHHHHHHHHHH		10.0220068231
767UbiquitinationLRVEDMMKRSFSEFP
HHHHHHHHHCHHHCC		37.95-
769PhosphorylationVEDMMKRSFSEFPSR
HHHHHHHCHHHCCCH		27.8329209046
771PhosphorylationDMMKRSFSEFPSRKD
HHHHHCHHHCCCHHC		39.3029209046
775PhosphorylationRSFSEFPSRKDSKAH
HCHHHCCCHHCCHHH		58.2322115753
777UbiquitinationFSEFPSRKDSKAHEQ
HHHCCCHHCCHHHHH		71.36-
779PhosphorylationEFPSRKDSKAHEQAL
HCCCHHCCHHHHHHH		34.4723927012
780UbiquitinationFPSRKDSKAHEQALA
CCCHHCCHHHHHHHH		64.9921906983
791UbiquitinationQALAELTKRLGALEE
HHHHHHHHHHCCCCC		59.2421906983
802PhosphorylationALEEPDMTGQLVDLP
CCCCCCCCCCEECCH		29.2023403867
837UbiquitinationMESVNGLKSLSAGRV
HHHHCCHHHCCCCCE		51.2321906983
863PhosphorylationLGVILQVSSNSTSRV
EEEEEEEECCCCCCE		15.7320860994
864PhosphorylationGVILQVSSNSTSRVF
EEEEEEECCCCCCEE		35.6220860994
866PhosphorylationILQVSSNSTSRVFTT
EEEEECCCCCCEEEE		29.7020860994
879UbiquitinationTTLVLCDKPLSQDPQ
EEEEEECCCCCCCCC		47.03-
882PhosphorylationVLCDKPLSQDPQDRG
EEECCCCCCCCCCCC		40.8523663014
892PhosphorylationPQDRGPATAEVPYPD
CCCCCCCCCCCCCCC		26.8721406692
897PhosphorylationPATAEVPYPDDLVGF
CCCCCCCCCCCCCEE		25.1921406692
905UbiquitinationPDDLVGFKLFLPEGP
CCCCCEEEEECCCCC		32.19-
919UbiquitinationPCDHTVVKLQPGDMA
CCCCEEEECCCCCHH		36.75-
930PhosphorylationGDMAAITTKVLRVNG
CCHHHEEEEEEEECH		17.0319413330
931UbiquitinationDMAAITTKVLRVNGE
CHHHEEEEEEEECHH		30.53-
939UbiquitinationVLRVNGEKILEDFSK
EEEECHHHHHHHHHH		54.73-
945PhosphorylationEKILEDFSKRQQPKF
HHHHHHHHHHCCCCC		38.9727542207
946UbiquitinationKILEDFSKRQQPKFK
HHHHHHHHHCCCCCC		54.97-
953UbiquitinationKRQQPKFKKDPPLAA
HHCCCCCCCCCCHHH		63.49-
954UbiquitinationRQQPKFKKDPPLAAV
HCCCCCCCCCCHHHH		77.82-
991UbiquitinationPVNDLQLKDMSVVEG
CCCCCCCCCCCHHHC		38.1221906983
994PhosphorylationDLQLKDMSVVEGGLR
CCCCCCCCHHHCCHH		32.9028857561
1004UbiquitinationEGGLRARKLEELIQG
HCCHHHHHHHHHHHH		60.30-
1017PhosphorylationQGAQCVHSPRFPAQY
HHCCCCCCCCCCHHH		9.4320873877
1026UbiquitinationRFPAQYLKLRERMQI
CCCHHHHHHHHHHHH		40.33-
1035UbiquitinationRERMQIQKEMERLRF
HHHHHHHHHHHHHHH		61.73-
1075UbiquitinationVDEAGTVKLAGRVAC
CCCCCCEEECHHHHH		32.2421906983
1225UbiquitinationGEPVLGAKMETAATL
CCCCCCCCHHHHHHH		35.1621906983
1228PhosphorylationVLGAKMETAATLLRR
CCCCCHHHHHHHHHH		20.3520068231
1231PhosphorylationAKMETAATLLRRDIV
CCHHHHHHHHHHHHH		24.7020068231
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 SKIV2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SKIV2_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 SKIV2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD11A_HUMANCDK11Aphysical
15231747
TSSK2_HUMANTSSK2physical
21988832
EXOS4_HUMANEXOSC4physical
15231747
XRN1_HUMANXRN1physical
15231747
RSMB_HUMANSNRPBphysical
15231747
MPPA_HUMANPMPCAphysical
15231747
GLT13_HUMANGALNT13physical
15231747
WDR1_HUMANWDR1physical
15231747
THOC4_HUMANALYREFphysical
26344197
CBS_HUMANCBSphysical
26344197
RAN_HUMANRANphysical
26344197
TTC37_HUMANTTC37physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614602Trichohepatoenteric syndrome 2 (THES2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SKIV2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, 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-245 AND SER-256, ANDMASS 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-245, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND SER-256, ANDMASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND SER-366, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND SER-256, ANDMASS SPECTROMETRY.

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