F168A_HUMAN - dbPTM
F168A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F168A_HUMAN
UniProt AC Q92567
Protein Name Protein FAM168A
Gene Name FAM168A
Organism Homo sapiens (Human).
Sequence Length 244
Subcellular Localization
Protein Description In cancer context, protects cells from induced-DNA damage and apoptosis. Acts, at least in part, through PI3K/AKT/NFKB signaling pathway and by preventing POLB degradation. Decreases POLB ubiquitation and stabilizes its protein levels..
Protein Sequence MNPVYSPVQPGAPYGNPKNMAYTGYPTAYPAAAPAYNPSLYPTNSPSYAPEFQFLHSAYATLLMKQAWPQNSSSCGTEGTFHLPVDTGTENRTYQASSAAFRYTAGTPYKVPPTQSNTAPPPYSPSPNPYQTAMYPIRSAYPQQNLYAQGAYYTQPVYAAQPHVIHHTTVVQPNSIPSAIYPAPVAAPRTNGVAMGMVAGTTMAMSAGTLLTTPQHTAIGAHPVSMPTYRAQGTPAYSYVPPHW
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
1Acetylation-------MNPVYSPV
-------CCCCCCCC		13.2719413330
5Phosphorylation---MNPVYSPVQPGA
---CCCCCCCCCCCC		14.4427259358
6Phosphorylation--MNPVYSPVQPGAP
--CCCCCCCCCCCCC		20.8728355574
14PhosphorylationPVQPGAPYGNPKNMA
CCCCCCCCCCCCCCC		29.0626074081
39 (in isoform 3)Phosphorylation-36.5828348404
39 (in isoform 2)Phosphorylation-36.5828348404
41 (in isoform 3)Phosphorylation-16.6128348404
41 (in isoform 2)Phosphorylation-16.6128348404
43 (in isoform 3)Phosphorylation-34.4728348404
43 (in isoform 2)Phosphorylation-34.4728348404
45 (in isoform 3)Phosphorylation-20.0828348404
45 (in isoform 2)Phosphorylation-20.0828348404
45PhosphorylationPSLYPTNSPSYAPEF
CCCCCCCCCCCCCHH		20.0827251275
89 (in isoform 3)Phosphorylation-31.9822210691
94PhosphorylationTGTENRTYQASSAAF
CCCCCCEEEECCEEE		9.9922817900
98 (in isoform 3)Phosphorylation-26.9922210691
102Asymmetric dimethylarginineQASSAAFRYTAGTPY
EECCEEEEECCCCCC		24.14-
102MethylationQASSAAFRYTAGTPY
EECCEEEEECCCCCC		24.14-
107PhosphorylationAFRYTAGTPYKVPPT
EEEECCCCCCCCCCC		22.4529396449
113 (in isoform 3)Phosphorylation-46.1622210691
138MethylationQTAMYPIRSAYPQQN
CCCCCCCHHHCCCCC		15.66-
189MethylationPAPVAAPRTNGVAMG
CCCCCCCCCCCCCCC		35.78-
190PhosphorylationAPVAAPRTNGVAMGM
CCCCCCCCCCCCCCC		34.9524043423
201PhosphorylationAMGMVAGTTMAMSAG
CCCCCCHHHEEECCC		12.0324043423
202PhosphorylationMGMVAGTTMAMSAGT
CCCCCHHHEEECCCC		11.3024043423
206PhosphorylationAGTTMAMSAGTLLTT
CHHHEEECCCCCCCC		17.6324043423
209PhosphorylationTMAMSAGTLLTTPQH
HEEECCCCCCCCCCC		20.5024043423
212PhosphorylationMSAGTLLTTPQHTAI
ECCCCCCCCCCCCCC		39.2724043423
213PhosphorylationSAGTLLTTPQHTAIG
CCCCCCCCCCCCCCC		22.4124043423
217PhosphorylationLLTTPQHTAIGAHPV
CCCCCCCCCCCCCCC		18.0924043423
225PhosphorylationAIGAHPVSMPTYRAQ
CCCCCCCCCCCCCCC		24.4024043423
228PhosphorylationAHPVSMPTYRAQGTP
CCCCCCCCCCCCCCC		19.5924043423
229PhosphorylationHPVSMPTYRAQGTPA
CCCCCCCCCCCCCCC		9.7024043423
234PhosphorylationPTYRAQGTPAYSYVP
CCCCCCCCCCCCCCC		7.83-
237PhosphorylationRAQGTPAYSYVPPHW
CCCCCCCCCCCCCCC		11.1827642862
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 F168A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F168A_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 F168A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
F168A_HUMANFAM168Aphysical
25416956
CREST_HUMANSS18L1physical
25416956
VP37C_HUMANVPS37Cphysical
25416956
KLH42_HUMANKLHL42physical
25416956
SMAP2_HUMANSMAP2physical
25416956
OTUB2_HUMANOTUB2physical
25416956
UBS3B_HUMANUBASH3Bphysical
25416956
CA094_HUMANC1orf94physical
25416956
OTUL_HUMANOTULINphysical
25416956
NAF1_HUMANNAF1physical
25416956
DTX2_HUMANDTX2physical
25416956
PR20E_HUMANPRR20Aphysical
25416956
PR20C_HUMANPRR20Aphysical
25416956
PR20D_HUMANPRR20Aphysical
25416956
PR20B_HUMANPRR20Aphysical
25416956
PR20A_HUMANPRR20Aphysical
25416956
CREST_HUMANSS18L1physical
21516116
FBXW5_HUMANFBXW5physical
21516116
OTUB2_HUMANOTUB2physical
21516116
UBS3B_HUMANUBASH3Bphysical
21516116
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 F168A_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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-6, AND MASS SPECTROMETRY.
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-6, AND MASS SPECTROMETRY.

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