SCAF8_HUMAN - dbPTM
SCAF8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCAF8_HUMAN
UniProt AC Q9UPN6
Protein Name Protein SCAF8
Gene Name SCAF8
Organism Homo sapiens (Human).
Sequence Length 1271
Subcellular Localization Nucleus. Nucleus matrix. Detected in granular nuclear foci which correspond to sites of active transcription..
Protein Description May play a role in mRNA processing..
Protein Sequence MEAVKTFNSELYSLNDYKPPISKAKMTQITKAAIKAIKFYKHVVQSVEKFIQKCKPEYKVPGLYVIDSIVRQSRHQFGQEKDVFAPRFSNNIISTFQNLYRCPGDDKSKIVRVLNLWQKNNVFKSEIIQPLLDMAAGIPPPVVTPVLASTTTAMSNTPGTPVTPVTPANVVQGLPDPWVSQITNTDTLAAVAQILQSPQGQQLQQLIQTLQIQQQKPQPSILQALDAGLVVQLQALTAQLTAAAAAANTLTPLEQGVSFNKKLMDRFDFGEDSEHSEEPKKEIPASQLSHVSESVNNSIFHQIAEQLQQQNLEHLRQQLLEQQQPQKATPQDSQEGTFGSEHSASPSQGSSQQHFLEPEVNLDDSIDIQQQDMDIDEGQDGVEEEVFEQEAKKVAVRSRSRTHSRSRSRSPRKRRSRSRSGSRKRKHRKRSRSRSRERKRKSSRSYSSERRAREREKERQKKGLPPIRSKTLSVCSTTLWVGQVDKKATQQDLTNLFEEFGQIESINMIPPRGCAYVCMVHRQDAFRALQKLSSGSYKIGSKVIKIAWALNKGVKTEYKQFWDVDLGVTYIPWEKVKVDDLEGFAEGGMIDQETVNTEWETVKSSEPVKETVQTTQSPTPVEKETVVTTQAEVFPPPVAMLQIPVAPAVPTVSLVPPAFPVSMPVPPPGFSPIPPPPFLRASFNPSQPPPGFMPPPVPPPVVPPPTIPPVVPTSLVQPSLSMTPETVKDVGFGSLVIPGGSVASNLATSALPAGNVFNAPTKQAEPEEKVPHLIDHQISSGENTRSVIPNDISSNAAILGGQPPNVTSNSGILGVQRPNVSSNSEILGVRPSNVSSSSGIIAAQPPNILNNSGILGIQPPSVSNSSGLLGVLPPNIPNNSGLVGVQPPNVPNTPGLLGTQPPAGPQNLPPLSIPNQRMPTMPMLDIRPGLIPQAPGPRFPLIQPGIPPQRGIPPPSVLDSALHPPPRGPFPPGDIFSQPERPFLAPGRQSVDNVTNPEKRIPLGNDNIQQEGDRDYRFPPIETRESISRPPPVDVRDVVGRPIDPREGPGRPPLDGRDHFGRPPVDIRENLVRPGIDHLGRRDHFGFNPEKPWGHRGDFDEREHRVLPVYGGPKGLHEERGRFRSGNYRFDPRSGPWNRGFGQEVHRDFDDRRRPWERQRDRDDRDFDFCREMNGNRLGRDRIQNTWVPPPHARVFDYFEGATSQRKGDNVPQVNGENTERHAQPPPIPVQNDPELYEKLTSSNEINKEKSDTVADIESEPVVESTETEGT
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
6Phosphorylation--MEAVKTFNSELYS
--CCHHHHHCHHHHH
22.8120388717
12PhosphorylationKTFNSELYSLNDYKP
HHHCHHHHHCCCCCC
13.6828152594
13PhosphorylationTFNSELYSLNDYKPP
HHCHHHHHCCCCCCC
33.0628152594
17PhosphorylationELYSLNDYKPPISKA
HHHHCCCCCCCCCHH
25.0727273156
18SumoylationLYSLNDYKPPISKAK
HHHCCCCCCCCCHHH
47.37-
18SumoylationLYSLNDYKPPISKAK
HHHCCCCCCCCCHHH
47.37-
18UbiquitinationLYSLNDYKPPISKAK
HHHCCCCCCCCCHHH
47.37-
22PhosphorylationNDYKPPISKAKMTQI
CCCCCCCCHHHHHHH
32.1328152594
31UbiquitinationAKMTQITKAAIKAIK
HHHHHHHHHHHHHHH
37.13-
53UbiquitinationSVEKFIQKCKPEYKV
HHHHHHHHCCCCCCC
39.13-
81UbiquitinationRHQFGQEKDVFAPRF
HHHHCCCCCCCCCCC
51.83-
89O-linked_GlycosylationDVFAPRFSNNIISTF
CCCCCCCCCCHHHHH
30.1920068230
95O-linked_GlycosylationFSNNIISTFQNLYRC
CCCCHHHHHHHHHCC
20.8720068230
119UbiquitinationRVLNLWQKNNVFKSE
HHHHHHHHCCCCHHH
38.6221890473
119UbiquitinationRVLNLWQKNNVFKSE
HHHHHHHHCCCCHHH
38.6221890473
124UbiquitinationWQKNNVFKSEIIQPL
HHHCCCCHHHHHHHH
42.78-
185UbiquitinationWVSQITNTDTLAAVA
HHHHCCCHHHHHHHH
23.01-
197UbiquitinationAVAQILQSPQGQQLQ
HHHHHHHCCCHHHHH
18.7521890473
273PhosphorylationRFDFGEDSEHSEEPK
CCCCCCCCCCCCCCC
32.6723401153
276PhosphorylationFGEDSEHSEEPKKEI
CCCCCCCCCCCCCCC
39.3329255136
281UbiquitinationEHSEEPKKEIPASQL
CCCCCCCCCCCHHHH
72.15-
333PhosphorylationQKATPQDSQEGTFGS
CCCCCCCCCCCCCCC
25.5326074081
337PhosphorylationPQDSQEGTFGSEHSA
CCCCCCCCCCCCCCC
24.8726074081
340PhosphorylationSQEGTFGSEHSASPS
CCCCCCCCCCCCCCC
28.1326074081
343PhosphorylationGTFGSEHSASPSQGS
CCCCCCCCCCCCCCC
26.7926074081
345PhosphorylationFGSEHSASPSQGSSQ
CCCCCCCCCCCCCCC
28.2626074081
347PhosphorylationSEHSASPSQGSSQQH
CCCCCCCCCCCCCCC
44.6826074081
350PhosphorylationSASPSQGSSQQHFLE
CCCCCCCCCCCCCCC
19.8226074081
351PhosphorylationASPSQGSSQQHFLEP
CCCCCCCCCCCCCCC
40.4626074081
402PhosphorylationAVRSRSRTHSRSRSR
HHHHHCCCCCCCCCC
26.0023828894
404PhosphorylationRSRSRTHSRSRSRSP
HHHCCCCCCCCCCCC
31.1923828894
406PhosphorylationRSRTHSRSRSRSPRK
HCCCCCCCCCCCCCH
37.3122468782
408PhosphorylationRTHSRSRSRSPRKRR
CCCCCCCCCCCCHHH
38.0520068231
410PhosphorylationHSRSRSRSPRKRRSR
CCCCCCCCCCHHHHC
30.2420068231
433PhosphorylationKHRKRSRSRSRERKR
HHHHHHHHHHHHHHH
35.5420068231
435PhosphorylationRKRSRSRSRERKRKS
HHHHHHHHHHHHHHH
39.4820068231
442PhosphorylationSRERKRKSSRSYSSE
HHHHHHHHHHHHHHH
34.7129449344
443PhosphorylationRERKRKSSRSYSSER
HHHHHHHHHHHHHHH
28.4222817900
445PhosphorylationRKRKSSRSYSSERRA
HHHHHHHHHHHHHHH
31.1730576142
446PhosphorylationKRKSSRSYSSERRAR
HHHHHHHHHHHHHHH
18.3329449344
447PhosphorylationRKSSRSYSSERRARE
HHHHHHHHHHHHHHH
27.2830576142
448PhosphorylationKSSRSYSSERRARER
HHHHHHHHHHHHHHH
27.2130576142
461AcetylationEREKERQKKGLPPIR
HHHHHHHHCCCCCCC
55.847266349
533PhosphorylationFRALQKLSSGSYKIG
HHHHHHHHCCCCCCC
39.4221712546
534PhosphorylationRALQKLSSGSYKIGS
HHHHHHHCCCCCCCH
42.0421712546
536PhosphorylationLQKLSSGSYKIGSKV
HHHHHCCCCCCCHHH
25.7921712546
542UbiquitinationGSYKIGSKVIKIAWA
CCCCCCHHHHHHHHH
42.65-
604PhosphorylationTEWETVKSSEPVKET
CCEEEECCCCCCCHH
35.2823927012
605PhosphorylationEWETVKSSEPVKETV
CEEEECCCCCCCHHH
39.9523927012
605O-linked_GlycosylationEWETVKSSEPVKETV
CEEEECCCCCCCHHH
39.9520068230
609AcetylationVKSSEPVKETVQTTQ
ECCCCCCCHHHCCCC
59.3812654625
611PhosphorylationSSEPVKETVQTTQSP
CCCCCCHHHCCCCCC
16.5229255136
611O-linked_GlycosylationSSEPVKETVQTTQSP
CCCCCCHHHCCCCCC
16.5220068230
614O-linked_GlycosylationPVKETVQTTQSPTPV
CCCHHHCCCCCCCCC
23.5930059200
614PhosphorylationPVKETVQTTQSPTPV
CCCHHHCCCCCCCCC
23.5930266825
615O-linked_GlycosylationVKETVQTTQSPTPVE
CCHHHCCCCCCCCCC
15.2320068230
615PhosphorylationVKETVQTTQSPTPVE
CCHHHCCCCCCCCCC
15.2329255136
617PhosphorylationETVQTTQSPTPVEKE
HHHCCCCCCCCCCCC
28.7519664994
619PhosphorylationVQTTQSPTPVEKETV
HCCCCCCCCCCCCEE
45.2529255136
686O-linked_GlycosylationLRASFNPSQPPPGFM
CCCCCCCCCCCCCCC
57.3220068230
779PhosphorylationHLIDHQISSGENTRS
CCHHCCCCCCCCCCC
26.2228348404
780PhosphorylationLIDHQISSGENTRSV
CHHCCCCCCCCCCCC
52.3228450419
784PhosphorylationQISSGENTRSVIPND
CCCCCCCCCCCCCCC
21.7328450419
807PhosphorylationGGQPPNVTSNSGILG
CCCCCCCCCCCCCCC
28.9122210691
810PhosphorylationPPNVTSNSGILGVQR
CCCCCCCCCCCCCCC
27.2922210691
821O-linked_GlycosylationGVQRPNVSSNSEILG
CCCCCCCCCCCEEEC
30.3720068230
822O-linked_GlycosylationVQRPNVSSNSEILGV
CCCCCCCCCCEEECC
39.8420068230
824O-linked_GlycosylationRPNVSSNSEILGVRP
CCCCCCCCEEECCCC
28.1420068230
861O-linked_GlycosylationILGIQPPSVSNSSGL
CCCCCCCCCCCCCCC
44.8820068230
917Asymmetric dimethylargininePLSIPNQRMPTMPML
CCCCCCCCCCCCCCC
39.42-
917MethylationPLSIPNQRMPTMPML
CCCCCCCCCCCCCCC
39.4224129315
927Asymmetric dimethylarginineTMPMLDIRPGLIPQA
CCCCCCCCCCCCCCC
20.92-
927MethylationTMPMLDIRPGLIPQA
CCCCCCCCCCCCCCC
20.9224129315
938MethylationIPQAPGPRFPLIQPG
CCCCCCCCCCCCCCC
52.2924129315
938Asymmetric dimethylarginineIPQAPGPRFPLIQPG
CCCCCCCCCCCCCCC
52.29-
967MethylationSALHPPPRGPFPPGD
HCCCCCCCCCCCCCC
71.8080702875
981MethylationDIFSQPERPFLAPGR
CCCCCCCCCCCCCCC
33.6780702883
988MethylationRPFLAPGRQSVDNVT
CCCCCCCCCCCCCCC
25.2580702891
990PhosphorylationFLAPGRQSVDNVTNP
CCCCCCCCCCCCCCH
30.0321815630
999AcetylationDNVTNPEKRIPLGND
CCCCCHHHCCCCCCC
57.8125953088
1026PhosphorylationPPIETRESISRPPPV
CCCCCCCCCCCCCCC
23.6728555341
1062MethylationDGRDHFGRPPVDIRE
CCCCCCCCCCCCHHH
31.26-
1073Asymmetric dimethylarginineDIRENLVRPGIDHLG
CHHHHCCCCCCCCCC
27.22-
1073MethylationDIRENLVRPGIDHLG
CHHHHCCCCCCCCCC
27.2254549787
1091UbiquitinationHFGFNPEKPWGHRGD
CCCCCCCCCCCCCCC
47.53-
1120MethylationPKGLHEERGRFRSGN
CCCHHCCCCCCCCCC
38.3118601187
1122MethylationGLHEERGRFRSGNYR
CHHCCCCCCCCCCCC
29.99-
1124MethylationHEERGRFRSGNYRFD
HCCCCCCCCCCCCCC
42.15-
1129MethylationRFRSGNYRFDPRSGP
CCCCCCCCCCCCCCC
33.23-
1133MethylationGNYRFDPRSGPWNRG
CCCCCCCCCCCCCCC
56.97-
1139MethylationPRSGPWNRGFGQEVH
CCCCCCCCCCCCHHC
37.6430760801
1198PhosphorylationPHARVFDYFEGATSQ
CCCCHHCCCCCCCCC
7.65-
1237PhosphorylationVQNDPELYEKLTSSN
CCCCHHHHHHHHCCC
14.8928796482
1241PhosphorylationPELYEKLTSSNEINK
HHHHHHHHCCCCCCH
40.9722468782
1251PhosphorylationNEINKEKSDTVADIE
CCCCHHHCCCCCCCC
39.3422468782

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 SCAF8_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCAF8_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 SCAF8_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SCAF8_HUMAN !!

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 SCAF8_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-617 AND THR-619, 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-617, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-615 AND SER-617, ANDMASS SPECTROMETRY.
"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-617, AND MASSSPECTROMETRY.
"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-617, AND MASSSPECTROMETRY.

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