F219A_HUMAN - dbPTM
F219A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F219A_HUMAN
UniProt AC Q8IW50
Protein Name Protein FAM219A
Gene Name FAM219A
Organism Homo sapiens (Human).
Sequence Length 185
Subcellular Localization
Protein Description
Protein Sequence MMEEIDRFQVPTAHSEMQPLDPAAASISDGDCDAREGESVAMNYKPSPLQVKLEKQRELARKGSLKNGSMGSPVNQQPKKNNVMARTRLVVPNKGYSSLDQSPDEKPLVALDTDSDDDFDMSRYSSSGYSSAEQINQDLNIQLLKDGYRLDEIPDDEDLDLIPPKSVNPTCMCCQATSSTACHIQ
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-------MMEEIDRF
-------CCCCCCCC		7.4222814378
15 (in isoform 4)Phosphorylation-32.0927732954
15 (in isoform 3)Phosphorylation-32.0927732954
15 (in isoform 2)Phosphorylation-32.0927732954
17 (in isoform 4)Phosphorylation-5.8027732954
17 (in isoform 3)Phosphorylation-5.8027732954
17 (in isoform 2)Phosphorylation-5.8027732954
26 (in isoform 5)Phosphorylation-20.2129507054
26 (in isoform 6)Phosphorylation-20.2129507054
26PhosphorylationPLDPAAASISDGDCD
CCCHHHHCCCCCCCC		20.2123663014
28 (in isoform 5)Phosphorylation-32.8028348404
28 (in isoform 6)Phosphorylation-32.8028348404
28PhosphorylationDPAAASISDGDCDAR
CHHHHCCCCCCCCCC		32.8023663014
36 (in isoform 2)Phosphorylation-69.8725849741
36 (in isoform 3)Phosphorylation-69.8725849741
38UbiquitinationDCDAREGESVAMNYK
CCCCCCCCEECCCCC		36.9732015554
39PhosphorylationCDAREGESVAMNYKP
CCCCCCCEECCCCCC		26.4930266825
44PhosphorylationGESVAMNYKPSPLQV
CCEECCCCCCCCCHH		15.9330266825
47PhosphorylationVAMNYKPSPLQVKLE
ECCCCCCCCCHHHHH		33.8130266825
47 (in isoform 6)Phosphorylation-33.8125849741
47 (in isoform 5)Phosphorylation-33.8125849741
49UbiquitinationMNYKPSPLQVKLEKQ
CCCCCCCCHHHHHHH		12.2632015554
53PhosphorylationPSPLQVKLEKQRELA
CCCCHHHHHHHHHHH		11.9033259812
55UbiquitinationPLQVKLEKQRELARK
CCHHHHHHHHHHHHH		66.1632015554
55PhosphorylationPLQVKLEKQRELARK
CCHHHHHHHHHHHHH		66.1632142685
61PhosphorylationEKQRELARKGSLKNG
HHHHHHHHHCCCCCC		57.3932142685
64PhosphorylationRELARKGSLKNGSMG
HHHHHHCCCCCCCCC		38.9230266825
66UbiquitinationLARKGSLKNGSMGSP
HHHHCCCCCCCCCCC		62.0432015554
69PhosphorylationKGSLKNGSMGSPVNQ
HCCCCCCCCCCCCCC		29.3930266825
72PhosphorylationLKNGSMGSPVNQQPK
CCCCCCCCCCCCCCC		19.6230266825
87PhosphorylationKNNVMARTRLVVPNK
CCCCCCEEEEECCCC		20.8632142685
96PhosphorylationLVVPNKGYSSLDQSP
EECCCCCCCCCCCCC		9.1923403867
97PhosphorylationVVPNKGYSSLDQSPD
ECCCCCCCCCCCCCC		32.8523927012
98PhosphorylationVPNKGYSSLDQSPDE
CCCCCCCCCCCCCCC		27.7323927012
102PhosphorylationGYSSLDQSPDEKPLV
CCCCCCCCCCCCCCE		33.7022167270
104PhosphorylationSSLDQSPDEKPLVAL
CCCCCCCCCCCCEEE		80.1232142685
113PhosphorylationKPLVALDTDSDDDFD
CCCEEECCCCCCCCC		37.9522167270
115PhosphorylationLVALDTDSDDDFDMS
CEEECCCCCCCCCHH		45.0622167270
122PhosphorylationSDDDFDMSRYSSSGY
CCCCCCHHHHCCCCC		29.8823927012
128UbiquitinationMSRYSSSGYSSAEQI
HHHHCCCCCCCHHHH		28.4332015554
129PhosphorylationSRYSSSGYSSAEQIN
HHHCCCCCCCHHHHC		11.0327642862
130PhosphorylationRYSSSGYSSAEQINQ
HHCCCCCCCHHHHCH		26.9724719451
131PhosphorylationYSSSGYSSAEQINQD
HCCCCCCCHHHHCHH		27.6028348404
131 (in isoform 7)Phosphorylation-27.6024043423
132 (in isoform 7)Phosphorylation-13.5324043423
133 (in isoform 7)Phosphorylation-54.6724043423
134 (in isoform 7)Phosphorylation-39.3824043423
137 (in isoform 7)Phosphorylation-59.1924043423
145UbiquitinationDLNIQLLKDGYRLDE
HHCCEECCCCCCCCC		58.6732015554
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 F219A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F219A_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 F219A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDE6D_HUMANPDE6Dphysical
16169070
DPOA2_HUMANPOLA2physical
16169070
P66A_HUMANGATAD2Aphysical
26186194
MBD3_HUMANMBD3physical
26186194
FBX10_HUMANFBXO10physical
26186194
MTA2_HUMANMTA2physical
26186194
MTA3_HUMANMTA3physical
26186194
MTA1_HUMANMTA1physical
26186194
UBR3_HUMANUBR3physical
26186194
ATE1_HUMANATE1physical
26186194
MRE11_HUMANMRE11Aphysical
26186194
OBSL1_HUMANOBSL1physical
26186194
RAD50_HUMANRAD50physical
26186194
NBN_HUMANNBNphysical
26186194
WDFY1_HUMANWDFY1physical
26186194
SYMM_HUMANMARS2physical
26186194
FBW1A_HUMANBTRCphysical
26186194
FBW1B_HUMANFBXW11physical
26186194
KLH24_HUMANKLHL24physical
26186194
SHPK_HUMANSHPKphysical
26186194
FBX21_HUMANFBXO21physical
26186194
CTU2_HUMANCTU2physical
26186194
NBN_HUMANNBNphysical
28514442
RAD50_HUMANRAD50physical
28514442
FBX10_HUMANFBXO10physical
28514442
FBW1A_HUMANBTRCphysical
28514442
MRE11_HUMANMRE11Aphysical
28514442
MTA3_HUMANMTA3physical
28514442
FBW1B_HUMANFBXW11physical
28514442
MTA1_HUMANMTA1physical
28514442
MTA2_HUMANMTA2physical
28514442
SYMM_HUMANMARS2physical
28514442
UBR3_HUMANUBR3physical
28514442
MBD3_HUMANMBD3physical
28514442
P66B_HUMANGATAD2Bphysical
28514442
WDFY1_HUMANWDFY1physical
28514442
P66A_HUMANGATAD2Aphysical
28514442
OBSL1_HUMANOBSL1physical
28514442
ATE1_HUMANATE1physical
28514442
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 F219A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113 AND SER-115, ANDMASS SPECTROMETRY.
"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-64; SER-72 AND SER-102,AND MASS SPECTROMETRY.
"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-102; THR-113 ANDSER-115, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113 AND SER-115, ANDMASS SPECTROMETRY.

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