SGTB_HUMAN - dbPTM
SGTB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SGTB_HUMAN
UniProt AC Q96EQ0
Protein Name Small glutamine-rich tetratricopeptide repeat-containing protein beta
Gene Name SGTB
Organism Homo sapiens (Human).
Sequence Length 304
Subcellular Localization
Protein Description Co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity..
Protein Sequence MSSIKHLVYAVIRFLREQSQMDTYTSDEQESLEVAIQCLETVFKISPEDTHLAVSQPLTEMFTSSFCKNDVLPLSNSVPEDVGKADQLKDEGNNHMKEENYAAAVDCYTQAIELDPNNAVYYCNRAAAQSKLGHYTDAIKDCEKAIAIDSKYSKAYGRMGLALTALNKFEEAVTSYQKALDLDPENDSYKSNLKIAEQKLREVSSPTGTGLSFDMASLINNPAFISMAASLMQNPQVQQLMSGMMTNAIGGPAAGVGGLTDLSSLIQAGQQFAQQIQQQNPELIEQLRNHIRSRSFSSSAEEHS
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
3Phosphorylation-----MSSIKHLVYA
-----CCHHHHHHHH		34.0724719451
5Ubiquitination---MSSIKHLVYAVI
---CCHHHHHHHHHH		32.6023000965
9PhosphorylationSSIKHLVYAVIRFLR
CHHHHHHHHHHHHHH		11.0824719451
75PhosphorylationKNDVLPLSNSVPEDV
CCCCCCCCCCCCCCC		25.7228122231
77PhosphorylationDVLPLSNSVPEDVGK
CCCCCCCCCCCCCCC		35.3625159151
84UbiquitinationSVPEDVGKADQLKDE
CCCCCCCCHHHHCCC		48.9532015554
86UbiquitinationPEDVGKADQLKDEGN
CCCCCCHHHHCCCCC		58.8121890473
89UbiquitinationVGKADQLKDEGNNHM
CCCHHHHCCCCCCCC		48.3722817900
103UbiquitinationMKEENYAAAVDCYTQ
CCHHHHHHHHHCHHH		9.5423503661
113UbiquitinationDCYTQAIELDPNNAV
HCHHHHEECCCCCHH		50.5723503661
125UbiquitinationNAVYYCNRAAAQSKL
CHHHHCCHHHHHHHH		23.2622817900
129UbiquitinationYCNRAAAQSKLGHYT
HCCHHHHHHHHCCHH		36.0522817900
131MalonylationNRAAAQSKLGHYTDA
CHHHHHHHHCCHHHH		46.5426320211
131AcetylationNRAAAQSKLGHYTDA
CHHHHHHHHCCHHHH		46.5425953088
134UbiquitinationAAQSKLGHYTDAIKD
HHHHHHCCHHHHHHH		32.5222817900
151UbiquitinationKAIAIDSKYSKAYGR
HHHHHCCCCHHHHHC		50.2021906983
154UbiquitinationAIDSKYSKAYGRMGL
HHCCCCHHHHHCHHH		42.4022817900
168UbiquitinationLALTALNKFEEAVTS
HHHHHHHHHHHHHHH		55.8123503661
176PhosphorylationFEEAVTSYQKALDLD
HHHHHHHHHHHHCCC		12.5029759185
178UbiquitinationEAVTSYQKALDLDPE
HHHHHHHHHHCCCCC		42.5632015554
190UbiquitinationDPENDSYKSNLKIAE
CCCCCCHHHHHHHHH		36.5032015554
194UbiquitinationDSYKSNLKIAEQKLR
CCHHHHHHHHHHHHH		44.0922817900
199UbiquitinationNLKIAEQKLREVSSP
HHHHHHHHHHHCCCC		40.8022817900
293PhosphorylationQLRNHIRSRSFSSSA
HHHHHHHHCCCCCCC		31.5022617229
295PhosphorylationRNHIRSRSFSSSAEE
HHHHHHCCCCCCCCC		30.6323401153
297PhosphorylationHIRSRSFSSSAEEHS
HHHHCCCCCCCCCCC		25.3222167270
298PhosphorylationIRSRSFSSSAEEHS-
HHHCCCCCCCCCCC-		31.4022167270
299PhosphorylationRSRSFSSSAEEHS--
HHCCCCCCCCCCC--		38.2022167270
304PhosphorylationSSSAEEHS-------
CCCCCCCC-------		45.2420363803
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 SGTB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SGTB_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 SGTB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PPIB_HUMANPPIBphysical
21516116
ASSY_HUMANASS1physical
26496610
BLMH_HUMANBLMHphysical
26496610
MCAT_HUMANSLC25A20physical
26496610
EI2BA_HUMANEIF2B1physical
26496610
IF4G1_HUMANEIF4G1physical
26496610
ERF_HUMANERFphysical
26496610
ERF1_HUMANETF1physical
26496610
ETFA_HUMANETFAphysical
26496610
FLOT2_HUMANFLOT2physical
26496610
MTOR_HUMANMTORphysical
26496610
HEXA_HUMANHEXAphysical
26496610
HSP76_HUMANHSPA6physical
26496610
ITB4_HUMANITGB4physical
26496610
MA2C1_HUMANMAN2C1physical
26496610
M3K4_HUMANMAP3K4physical
26496610
MSH5_HUMANMSH5physical
26496610
NHS_HUMANNHSphysical
26496610
FURIN_HUMANFURINphysical
26496610
PHLP_HUMANPDCLphysical
26496610
PLXB1_HUMANPLXNB1physical
26496610
RET_HUMANRETphysical
26496610
UAP1_HUMANUAP1physical
26496610
SPTN2_HUMANSPTBN2physical
26496610
TLN1_HUMANTLN1physical
26496610
UBP1_HUMANUSP1physical
26496610
BAG6_HUMANBAG6physical
26496610
UBL4A_HUMANUBL4Aphysical
26496610
RAD54_HUMANRAD54Lphysical
26496610
MTA1_HUMANMTA1physical
26496610
RABE1_HUMANRABEP1physical
26496610
VATG1_HUMANATP6V1G1physical
26496610
GT2D1_HUMANGTF2IRD1physical
26496610
AKA12_HUMANAKAP12physical
26496610
ESPL1_HUMANESPL1physical
26496610
RHG32_HUMANARHGAP32physical
26496610
RBCC1_HUMANRB1CC1physical
26496610
C2CD5_HUMANC2CD5physical
26496610
OSBL2_HUMANOSBPL2physical
26496610
UBP15_HUMANUSP15physical
26496610
FLOT1_HUMANFLOT1physical
26496610
ABCA7_HUMANABCA7physical
26496610
RACK1_HUMANGNB2L1physical
26496610
HYOU1_HUMANHYOU1physical
26496610
LTOR5_HUMANLAMTOR5physical
26496610
SRS10_HUMANSRSF10physical
26496610
MORC2_HUMANMORC2physical
26496610
ACINU_HUMANACIN1physical
26496610
WDFY3_HUMANWDFY3physical
26496610
MD13L_HUMANMED13Lphysical
26496610
ECM29_HUMANKIAA0368physical
26496610
DICER_HUMANDICER1physical
26496610
SIR5_HUMANSIRT5physical
26496610
KLDC2_HUMANKLHDC2physical
26496610
ZN318_HUMANZNF318physical
26496610
DNJC2_HUMANDNAJC2physical
26496610
PLPL8_HUMANPNPLA8physical
26496610
RRP15_HUMANRRP15physical
26496610
CHMP5_HUMANCHMP5physical
26496610
GET4_HUMANGET4physical
26496610
PPIL3_HUMANPPIL3physical
26496610
URFB1_HUMANUHRF1BP1physical
26496610
PINX1_HUMANPINX1physical
26496610
HEAT3_HUMANHEATR3physical
26496610
BRX1_HUMANBRIX1physical
26496610
DNJA4_HUMANDNAJA4physical
26496610
PLXA3_HUMANPLXNA3physical
26496610
BI2L1_HUMANBAIAP2L1physical
26496610
DDX24_HUMANDDX24physical
26496610
Z286A_HUMANZNF286Aphysical
26496610
K1143_HUMANKIAA1143physical
26496610
WDR35_HUMANWDR35physical
26496610
NCEH1_HUMANNCEH1physical
26496610
DEFM_HUMANPDFphysical
26496610
ZN668_HUMANZNF668physical
26496610
TLN2_HUMANTLN2physical
26496610
ARP8_HUMANACTR8physical
26496610
PDE12_HUMANPDE12physical
26496610
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 SGTB_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-297, 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-295 AND SER-297, ANDMASS SPECTROMETRY.

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