SOSSC_HUMAN - dbPTM
SOSSC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SOSSC_HUMAN
UniProt AC Q9NRY2
Protein Name SOSS complex subunit C
Gene Name INIP
Organism Homo sapiens (Human).
Sequence Length 104
Subcellular Localization Nucleus . Localizes to nuclear foci following DNA damage.
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. The SOSS complex associates with single-stranded DNA at 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 MAANSSGQGFQNKNRVAILAELDKEKRKLLMQNQSSTNHPGASIALSRPSLNKDFRDHAEQQHIAAQQKAALQHAHAHSSGYFITQDSAFGNLILPVLPRLDPE
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
2Acetylation------MAANSSGQG
------CCCCCCCCC
18.4919413330
5Phosphorylation---MAANSSGQGFQN
---CCCCCCCCCCCC
30.9922210691
6Phosphorylation--MAANSSGQGFQNK
--CCCCCCCCCCCCC
34.6422210691
24AcetylationAILAELDKEKRKLLM
EHHHCCHHHHHHHHH
77.1826051181
28UbiquitinationELDKEKRKLLMQNQS
CCHHHHHHHHHCCCC
57.9721890473
28 (in isoform 1)Ubiquitination-57.9721890473
35PhosphorylationKLLMQNQSSTNHPGA
HHHHCCCCCCCCCCC
46.8326074081
36PhosphorylationLLMQNQSSTNHPGAS
HHHCCCCCCCCCCCC
24.3826074081
37PhosphorylationLMQNQSSTNHPGASI
HHCCCCCCCCCCCCH
42.6726074081
43PhosphorylationSTNHPGASIALSRPS
CCCCCCCCHHCCCCC
17.8226074081
47PhosphorylationPGASIALSRPSLNKD
CCCCHHCCCCCCCHH
32.8826074081
50PhosphorylationSIALSRPSLNKDFRD
CHHCCCCCCCHHHHH
43.3925159151
53UbiquitinationLSRPSLNKDFRDHAE
CCCCCCCHHHHHHHH
64.63-

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 SOSSC_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SOSSC_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 SOSSC_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SOSB1_HUMANNABP2physical
19683501
SOSB2_HUMANNABP1physical
19683501
INT3_HUMANINTS3physical
19683501
A4_HUMANAPPphysical
21832049
TF3C6_HUMANGTF3C6physical
22939629

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 SOSSC_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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