SOSB1_HUMAN - dbPTM
SOSB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SOSB1_HUMAN
UniProt AC Q9BQ15
Protein Name SOSS complex subunit B1
Gene Name NABP2
Organism Homo sapiens (Human).
Sequence Length 211
Subcellular Localization Nucleus . Localizes to nuclear foci following DNA damage. Foci formation is not cell-cycle dependent. Partial colocalization with RAD51 after ionizing radiation treatment.
Protein Description Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. In the SOSS complex, acts as a sensor of single-stranded DNA that binds to single-stranded DNA, in particular to polypyrimidines. The SOSS complex associates with DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways..
Protein Sequence MTTETFVKDIKPGLKNLNLIFIVLETGRVTKTKDGHEVRTCKVADKTGSINISVWDDVGNLIQPGDIIRLTKGYASVFKGCLTLYTGRGGDLQKIGEFCMVYSEVPNFSEPNPEYSTQQAPNKAVQNDSNPSASQPTTGPSAASPASENQNGNGLSAPPGPGGGPHPPHTPSHPPSTRITRSQPNHTPAGPPGPSSNPVSNGKETRRSSKR
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
8UbiquitinationMTTETFVKDIKPGLK
CCHHHHHHHCCCCCC		49.93-
11UbiquitinationETFVKDIKPGLKNLN
HHHHHHCCCCCCCCC		43.07-
15AcetylationKDIKPGLKNLNLIFI
HHCCCCCCCCCEEEE		66.367965545
71PhosphorylationPGDIIRLTKGYASVF
CCHHHHCCCCHHHHH		16.7526270265
72UbiquitinationGDIIRLTKGYASVFK
CHHHHCCCCHHHHHC		55.29-
74PhosphorylationIIRLTKGYASVFKGC
HHHCCCCHHHHHCCC		9.3926270265
76PhosphorylationRLTKGYASVFKGCLT
HCCCCHHHHHCCCEE		21.4326270265
116PhosphorylationSEPNPEYSTQQAPNK
CCCCCCCCCCCCCCC		20.34-
117PhosphorylationEPNPEYSTQQAPNKA
CCCCCCCCCCCCCCC		24.6515498874
134PhosphorylationNDSNPSASQPTTGPS
CCCCCCCCCCCCCCC		40.82-
141PhosphorylationSQPTTGPSAASPASE
CCCCCCCCCCCCCCC		37.5026714015
144PhosphorylationTTGPSAASPASENQN
CCCCCCCCCCCCCCC		22.2526714015
147PhosphorylationPSAASPASENQNGNG
CCCCCCCCCCCCCCC		40.2326714015
182PhosphorylationPSTRITRSQPNHTPA
CCCCCCCCCCCCCCC		41.1428555341
187PhosphorylationTRSQPNHTPAGPPGP
CCCCCCCCCCCCCCC		22.8325159151
195PhosphorylationPAGPPGPSSNPVSNG
CCCCCCCCCCCCCCC		48.9725159151
196PhosphorylationAGPPGPSSNPVSNGK
CCCCCCCCCCCCCCC		48.5721712546
200PhosphorylationGPSSNPVSNGKETRR
CCCCCCCCCCCCCCC		40.9125159151
203AcetylationSNPVSNGKETRRSSK
CCCCCCCCCCCCCCC		61.2326051181
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
117TPhosphorylationKinaseATMQ13315
Uniprot
134SPhosphorylationKinasePRKDCP78527
GPS
-KUbiquitinationE3 ubiquitin ligaseFBXL5Q9UKA1
PMID:25249620
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SOSB1_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 SOSB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
INT3_HUMANINTS3physical
19683501
SOSSC_HUMANINIPphysical
19683501
SSBP_HUMANSSBP1physical
22939629
SRPRB_HUMANSRPRBphysical
22939629
P53_HUMANTP53physical
23184057
EP300_HUMANEP300physical
23184057
SKP1_HUMANSKP1physical
25249620
CUL1_HUMANCUL1physical
25249620
FBXL5_HUMANFBXL5physical
25249620
SOSSC_HUMANINIPphysical
26344197
INT3_HUMANINTS3physical
26344197
MTCH1_HUMANMTCH1physical
26496610
EDRF1_HUMANEDRF1physical
26496610
VPS41_HUMANVPS41physical
26496610
VPS4A_HUMANVPS4Aphysical
26496610
LC7L3_HUMANLUC7L3physical
26496610
P66A_HUMANGATAD2Aphysical
26496610
CENPJ_HUMANCENPJphysical
26496610
SOSSC_HUMANINIPphysical
26496610
INT3_HUMANINTS3physical
26496610
YIPF5_HUMANYIPF5physical
26496610
BUD13_HUMANBUD13physical
26496610
EP300_HUMANEP300physical
26170237
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 SOSB1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Single-stranded DNA-binding protein hSSB1 is critical for genomicstability.";
Richard D.J., Bolderson E., Cubeddu L., Wadsworth R.I.M., Savage K.,Sharma G.G., Nicolette M.L., Tsvetanov S., McIlwraith M.J.,Pandita R.K., Takeda S., Hay R.T., Gautier J., West S.C., Paull T.T.,Pandita T.K., White M.F., Khanna K.K.;
Nature 453:677-681(2008).
Cited for: FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, INTERACTION WITH ATM ANDRAD51, PHOSPHORYLATION AT THR-117, AND MUTAGENESIS OF THR-117.

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