SBDS_HUMAN - dbPTM
SBDS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SBDS_HUMAN
UniProt AC Q9Y3A5
Protein Name Ribosome maturation protein SBDS
Gene Name SBDS
Organism Homo sapiens (Human).
Sequence Length 250
Subcellular Localization Cytoplasm. Nucleus, nucleolus. Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, spindle. Primarily detected in the cytoplasm, and at low levels in nucleus and nucleolus (PubMed:19602484 and PubMed:17475909). Detected in the nucleolus during G1 and G2 p
Protein Description Required for the assembly of mature ribosomes and ribosome biogenesis. Together with EFL1, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Required for normal levels of protein synthesis. May play a role in cellular stress resistance. May play a role in cellular response to DNA damage. May play a role in cell proliferation..
Protein Sequence MSIFTPTNQIRLTNVAVVRMKRAGKRFEIACYKNKVVGWRSGVEKDLDEVLQTHSVFVNVSKGQVAKKEDLISAFGTDDQTEICKQILTKGEVQVSDKERHTQLEQMFRDIATIVADKCVNPETKRPYTVILIERAMKDIHYSVKTNKSTKQQALEVIKQLKEKMKIERAHMRLRFILPVNEGKKLKEKLKPLIKVIESEDYGQQLEIVCLIDPGCFREIDELIKKETKGKGSLEVLNLKDVEEGDEKFE
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
2Phosphorylation------MSIFTPTNQ
------CCCCCCCCC		26.8125850435
2Acetylation------MSIFTPTNQ
------CCCCCCCCC		26.8122223895
5Phosphorylation---MSIFTPTNQIRL
---CCCCCCCCCEEE		27.7729255136
7Phosphorylation-MSIFTPTNQIRLTN
-CCCCCCCCCEEEEE		36.3820068231
11MethylationFTPTNQIRLTNVAVV
CCCCCCEEEEEEEEE		26.20115389501
13PhosphorylationPTNQIRLTNVAVVRM
CCCCEEEEEEEEEEE		20.1424043423
33AcetylationRFEIACYKNKVVGWR
CEEEEEECCCCEEEC		50.6126051181
33UbiquitinationRFEIACYKNKVVGWR
CEEEEEECCCCEEEC		50.61-
35UbiquitinationEIACYKNKVVGWRSG
EEEEECCCCEEECCC		33.86-
45AcetylationGWRSGVEKDLDEVLQ
EECCCCCCCHHHHHH		62.2726051181
45UbiquitinationGWRSGVEKDLDEVLQ
EECCCCCCCHHHHHH		62.27-
61PhosphorylationHSVFVNVSKGQVAKK
CEEEEECCCCCEECH		26.3530622161
62UbiquitinationSVFVNVSKGQVAKKE
EEEEECCCCCEECHH		49.4321890473
67AcetylationVSKGQVAKKEDLISA
CCCCCEECHHHHHHH		58.817428269
68AcetylationSKGQVAKKEDLISAF
CCCCEECHHHHHHHH		46.8826051181
68UbiquitinationSKGQVAKKEDLISAF
CCCCEECHHHHHHHH		46.88-
73PhosphorylationAKKEDLISAFGTDDQ
ECHHHHHHHHCCCCH		25.5029214152
77PhosphorylationDLISAFGTDDQTEIC
HHHHHHCCCCHHHHH		29.9225159151
84GlutathionylationTDDQTEICKQILTKG
CCCHHHHHHHHHHCC		1.8522555962
85UbiquitinationDDQTEICKQILTKGE
CCHHHHHHHHHHCCC		46.14-
90AcetylationICKQILTKGEVQVSD
HHHHHHHCCCCCCCC		50.0226051181
90UbiquitinationICKQILTKGEVQVSD
HHHHHHHCCCCCCCC		50.0221890473
96PhosphorylationTKGEVQVSDKERHTQ
HCCCCCCCCHHHHHH		26.3528348404
98UbiquitinationGEVQVSDKERHTQLE
CCCCCCCHHHHHHHH		49.4921890473
98AcetylationGEVQVSDKERHTQLE
CCCCCCCHHHHHHHH		49.4923236377
102PhosphorylationVSDKERHTQLEQMFR
CCCHHHHHHHHHHHH		40.8628555341
118AcetylationIATIVADKCVNPETK
HHHHHHHCCCCCCCC		30.2826051181
118UbiquitinationIATIVADKCVNPETK
HHHHHHHCCCCCCCC		30.28-
1182-HydroxyisobutyrylationIATIVADKCVNPETK
HHHHHHHCCCCCCCC		30.28-
124PhosphorylationDKCVNPETKRPYTVI
HCCCCCCCCCCEEEE		33.3417924679
125AcetylationKCVNPETKRPYTVIL
CCCCCCCCCCEEEEE		50.1126051181
125UbiquitinationKCVNPETKRPYTVIL
CCCCCCCCCCEEEEE		50.11-
128PhosphorylationNPETKRPYTVILIER
CCCCCCCEEEEEEEC		20.0617924679
129PhosphorylationPETKRPYTVILIERA
CCCCCCEEEEEEECH		12.0723312004
135MethylationYTVILIERAMKDIHY
EEEEEEECHHCCCCH		32.75115493383
138UbiquitinationILIERAMKDIHYSVK
EEEECHHCCCCHHHH		53.17-
142PhosphorylationRAMKDIHYSVKTNKS
CHHCCCCHHHHCCCC		18.5928060719
143PhosphorylationAMKDIHYSVKTNKST
HHCCCCHHHHCCCCH		11.7220068231
145UbiquitinationKDIHYSVKTNKSTKQ
CCCCHHHHCCCCHHH		40.20-
151MalonylationVKTNKSTKQQALEVI
HHCCCCHHHHHHHHH		47.7226320211
151UbiquitinationVKTNKSTKQQALEVI
HHCCCCHHHHHHHHH		47.72-
159UbiquitinationQQALEVIKQLKEKMK
HHHHHHHHHHHHHHC		55.5421890473
1842-HydroxyisobutyrylationILPVNEGKKLKEKLK
EEECCCCHHHHHHHH		49.07-
184MalonylationILPVNEGKKLKEKLK
EEECCCCHHHHHHHH		49.0726320211
184UbiquitinationILPVNEGKKLKEKLK
EEECCCCHHHHHHHH		49.07-
184AcetylationILPVNEGKKLKEKLK
EEECCCCHHHHHHHH		49.0725953088
210GlutathionylationGQQLEIVCLIDPGCF
CCEEEEEEEECCCHH		3.1922555962
2252-HydroxyisobutyrylationREIDELIKKETKGKG
HHHHHHHHHHHCCCC		58.12-
225AcetylationREIDELIKKETKGKG
HHHHHHHHHHHCCCC		58.1223236377
225UbiquitinationREIDELIKKETKGKG
HHHHHHHHHHHCCCC		58.12-
233PhosphorylationKETKGKGSLEVLNLK
HHHCCCCCEEEEECC		25.5025849741
240UbiquitinationSLEVLNLKDVEEGDE
CEEEEECCCHHCCCC		59.67-
248UbiquitinationDVEEGDEKFE-----
CHHCCCCCCC-----		60.5821890473
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 SBDS_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SBDS_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 SBDS_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRPRB_HUMANSRPRBphysical
22939629
SLIRP_HUMANSLIRPphysical
22939629
SNX3_HUMANSNX3physical
22939629
CHAP1_HUMANCHAMP1physical
22939629
SRRM2_HUMANSRRM2physical
22939629
STOM_HUMANSTOMphysical
22939629
MPLKI_HUMANMPLKIPphysical
22939629
TOM40_HUMANTOMM40physical
22939629
TIAR_HUMANTIAL1physical
22939629
UBE4B_HUMANUBE4Bphysical
22939629
SF01_HUMANSF1physical
22939629
STX7_HUMANSTX7physical
22939629
THIK_HUMANACAA1physical
22939629
SCO2_HUMANSCO2physical
22939629
VDAC3_HUMANVDAC3physical
22939629
TIM44_HUMANTIMM44physical
22939629
SPRE_HUMANSPRphysical
22939629
IDHC_HUMANIDH1physical
22863883
PNPH_HUMANPNPphysical
22863883
TYSY_HUMANTYMSphysical
22863883
SYCC_HUMANCARSphysical
26344197
DDX17_HUMANDDX17physical
26344197
DDX5_HUMANDDX5physical
26344197
EFL1_HUMANEFTUD1physical
26344197
GORS2_HUMANGORASP2physical
26344197
PLPHP_HUMANPROSCphysical
26344197
RUSD2_HUMANRPUSD2physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
260400Shwachman-Diamond syndrome (SDS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SBDS_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-124 AND TYR-128, ANDMASS SPECTROMETRY.

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