SAS10_HUMAN - dbPTM
SAS10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAS10_HUMAN
UniProt AC Q9NQZ2
Protein Name Something about silencing protein 10
Gene Name UTP3
Organism Homo sapiens (Human).
Sequence Length 479
Subcellular Localization Nucleus.
Protein Description Essential for gene silencing: has a role in the structure of silenced chromatin. Plays a role in the developing brain (By similarity)..
Protein Sequence MVGRSRRRGAAKWAAVRAKAGPTLTDENGDDLGLPPSPGDTSYYQDQVDDFHEARSRAALAKGWNEVQSGDEEDGEEEEEEVLALDMDDEDDEDGGNAGEEEEEENADDDGGSSVQSEAEASVDPSLSWGQRKKLYYDTDYGSKSRGRQSQQEAEEEEREEEEEAQIIQRRLAQALQEDDFGVAWVEAFAKPVPQVDEAETRVVKDLAKVSVKEKLKMLRKESPELLELIEDLKVKLTEVKDELEPLLELVEQGIIPPGKGSQYLRTKYNLYLNYCSNISFYLILKARRVPAHGHPVIERLVTYRNLINKLSVVDQKLSSEIRHLLTLKDDAVKKELIPKAKSTKPKPKSVSKTSAAACAVTDLSDDSDFDEKAKLKYYKEIEDRQKLKRKKEENSTEEQALEDQNAKRAITYQIAKNRGLTPRRKKIDRNPRVKHREKFRRAKIRRRGQVREVRKEEQRYSGELSGIRAGVKKSIKLK
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
8MethylationMVGRSRRRGAAKWAA
CCCCCCHHHHHHHHH		37.68-
12AcetylationSRRRGAAKWAAVRAK
CCHHHHHHHHHHHHH		36.5125953088
23PhosphorylationVRAKAGPTLTDENGD
HHHHCCCCCCCCCCC		41.1823927012
25PhosphorylationAKAGPTLTDENGDDL
HHCCCCCCCCCCCCC		43.6923927012
37PhosphorylationDDLGLPPSPGDTSYY
CCCCCCCCCCCCCCC		39.3125159151
41PhosphorylationLPPSPGDTSYYQDQV
CCCCCCCCCCCHHHC		25.2530266825
42PhosphorylationPPSPGDTSYYQDQVD
CCCCCCCCCCHHHCC		26.9530266825
43PhosphorylationPSPGDTSYYQDQVDD
CCCCCCCCCHHHCCC		13.7730266825
44PhosphorylationSPGDTSYYQDQVDDF
CCCCCCCCHHHCCCH		12.8423927012
56PhosphorylationDDFHEARSRAALAKG
CCHHHHHHHHHHHCC		33.0626074081
69PhosphorylationKGWNEVQSGDEEDGE
CCCCCCCCCCCCCCC		54.0826074081
134SumoylationLSWGQRKKLYYDTDY
CCCHHCCCCEEECCC		43.86-
134UbiquitinationLSWGQRKKLYYDTDY
CCCHHCCCCEEECCC		43.8629967540
134SumoylationLSWGQRKKLYYDTDY
CCCHHCCCCEEECCC		43.86-
136PhosphorylationWGQRKKLYYDTDYGS
CHHCCCCEEECCCCC		14.2627642862
137PhosphorylationGQRKKLYYDTDYGSK
HHCCCCEEECCCCCC		23.8527642862
139PhosphorylationRKKLYYDTDYGSKSR
CCCCEEECCCCCCCC		18.26-
143PhosphorylationYYDTDYGSKSRGRQS
EEECCCCCCCCCHHH		22.6421815630
144SumoylationYDTDYGSKSRGRQSQ
EECCCCCCCCCHHHH		39.5528112733
144UbiquitinationYDTDYGSKSRGRQSQ
EECCCCCCCCCHHHH		39.5533845483
144AcetylationYDTDYGSKSRGRQSQ
EECCCCCCCCCHHHH		39.5525953088
150PhosphorylationSKSRGRQSQQEAEEE
CCCCCHHHHHHHHHH		32.2517525332
191UbiquitinationAWVEAFAKPVPQVDE
HHHHHHCCCCCCCCH		39.8421906983
205AcetylationEAETRVVKDLAKVSV
HHHHHHHHHHHHCCH		44.1426051181
217UbiquitinationVSVKEKLKMLRKESP
CCHHHHHHHHHHCCH		47.1322817900
221UbiquitinationEKLKMLRKESPELLE
HHHHHHHHCCHHHHH		59.5921906983
260UbiquitinationQGIIPPGKGSQYLRT
CCCCCCCCCHHHHHH		62.2523503661
310AcetylationTYRNLINKLSVVDQK
HHHHHHHHHHHHCHH		34.8426051181
310UbiquitinationTYRNLINKLSVVDQK
HHHHHHHHHHHHCHH		34.8423000965
3102-HydroxyisobutyrylationTYRNLINKLSVVDQK
HHHHHHHHHHHHCHH		34.84-
317UbiquitinationKLSVVDQKLSSEIRH
HHHHHCHHHHHHHHH		45.9623000965
319PhosphorylationSVVDQKLSSEIRHLL
HHHCHHHHHHHHHHH		32.7224719451
327PhosphorylationSEIRHLLTLKDDAVK
HHHHHHHHCCCHHHH		37.8120860994
329UbiquitinationIRHLLTLKDDAVKKE
HHHHHHCCCHHHHHH		48.6129967540
3292-HydroxyisobutyrylationIRHLLTLKDDAVKKE
HHHHHHCCCHHHHHH		48.61-
329AcetylationIRHLLTLKDDAVKKE
HHHHHHCCCHHHHHH		48.6126051181
334AcetylationTLKDDAVKKELIPKA
HCCCHHHHHHHCCCC		42.1026051181
343PhosphorylationELIPKAKSTKPKPKS
HHCCCCCCCCCCCCC		46.6626657352
344PhosphorylationLIPKAKSTKPKPKSV
HCCCCCCCCCCCCCC		51.1426657352
354PhosphorylationKPKSVSKTSAAACAV
CCCCCCHHHHHHHHH		18.9823927012
355PhosphorylationPKSVSKTSAAACAVT
CCCCCHHHHHHHHHH		21.4624732914
362PhosphorylationSAAACAVTDLSDDSD
HHHHHHHHCCCCCCC		16.8226503892
365PhosphorylationACAVTDLSDDSDFDE
HHHHHCCCCCCCCCH		42.0323927012
368PhosphorylationVTDLSDDSDFDEKAK
HHCCCCCCCCCHHHH		45.2123927012
385CitrullinationYYKEIEDRQKLKRKK
HHHHHHHHHHHHHHH		23.81-
385CitrullinationYYKEIEDRQKLKRKK
HHHHHHHHHHHHHHH		23.81-
392UbiquitinationRQKLKRKKEENSTEE
HHHHHHHHHCCCHHH		74.4324816145
396PhosphorylationKRKKEENSTEEQALE
HHHHHCCCHHHHHHH		40.2429255136
397PhosphorylationRKKEENSTEEQALED
HHHHCCCHHHHHHHH		55.9421815630
408SumoylationALEDQNAKRAITYQI
HHHHHHHHHHHHHHH		50.33-
408UbiquitinationALEDQNAKRAITYQI
HHHHHHHHHHHHHHH		50.3332015554
408MethylationALEDQNAKRAITYQI
HHHHHHHHHHHHHHH		50.33110876137
408SumoylationALEDQNAKRAITYQI
HHHHHHHHHHHHHHH		50.33-
413PhosphorylationNAKRAITYQIAKNRG
HHHHHHHHHHHHHCC		7.5727642862
417AcetylationAITYQIAKNRGLTPR
HHHHHHHHHCCCCCC		49.1325953088
422PhosphorylationIAKNRGLTPRRKKID
HHHHCCCCCCHHCCC		19.9924719451
461PhosphorylationVRKEEQRYSGELSGI
HHHHHHHHHHCCCCH		22.2619691289
462PhosphorylationRKEEQRYSGELSGIR
HHHHHHHHHCCCCHH		28.1625159151
466PhosphorylationQRYSGELSGIRAGVK
HHHHHCCCCHHCCCC		28.0719691289
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
462SPhosphorylationKinaseAURKBQ96GD4
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAS10_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
191Ubiquitination194 (3)P ⇒ Srs111485612
  • Glucagon levels in response to oral glucose tolerance test (120 minutes)
29093273
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HAP1_HUMANHAP1physical
16169070
PTN_HUMANPTNphysical
16169070
ZHX1_HUMANZHX1physical
16169070
TRFE_HUMANTFphysical
26186194
TBA3C_HUMANTUBA3Cphysical
26186194
CTNA2_HUMANCTNNA2physical
26186194
IMP3_HUMANIMP3physical
26344197
IMP4_HUMANIMP4physical
26344197
MPP10_HUMANMPHOSPH10physical
26344197
TRFE_HUMANTFphysical
28514442
TBA3C_HUMANTUBA3Cphysical
28514442
HNRPQ_HUMANSYNCRIPphysical
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 SAS10_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-37; SER-365 AND SER-368,AND MASS SPECTROMETRY.
"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-365 AND SER-368, 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-37; SER-150; THR-362;SER-365 AND SER-368, AND MASS SPECTROMETRY.
"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-365; SER-368; SER-462AND SER-466, AND MASS SPECTROMETRY.
"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 SER-150, AND MASSSPECTROMETRY.
"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-37, 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-37; SER-365 AND SER-368,AND MASS SPECTROMETRY.

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