F207A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: F207A_HUMAN
• UniProt AC: Q9NSI2
• Protein Name: Protein FAM207A
• Gene Name: FAM207A
• Organism: Homo sapiens (Human).
• Sequence Length: 230
• Protein Sequence: MGKVRGLRARVHQAAVRPKGEAAPGPAPPAPEATPPPASAAGKDWAFINTNIFARTKIDPSALVQKLELDVRSVTSVRRGEAGSSARSVPSIRRGAEAKTVLPKKEKMKLRREQWLQKIEAIKLAEQKHREERRRRATVVVGDLHPLRDALPELLGLEAGSRRQARSRESNKPRPSELSRMSAAQRQQLLEEERTRFQELLASPAYRASPLVAIGQTLARQMQLEDGGQL

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
11	Ubiquitination	VRGLRARVHQAAVRP CCHHHHHHHEEECCC	3.71	22817900
16	Ubiquitination	ARVHQAAVRPKGEAA HHHHEEECCCCCCCC	13.93	22817900
19	Sumoylation	HQAAVRPKGEAAPGP HEEECCCCCCCCCCC	59.84	-
19	Ubiquitination	HQAAVRPKGEAAPGP HEEECCCCCCCCCCC	59.84	29967540
19	Sumoylation	HQAAVRPKGEAAPGP HEEECCCCCCCCCCC	59.84	-
19	Acetylation	HQAAVRPKGEAAPGP HEEECCCCCCCCCCC	59.84	26051181
21	Ubiquitination	AAVRPKGEAAPGPAP EECCCCCCCCCCCCC	48.02	22817900
34	Phosphorylation	APPAPEATPPPASAA CCCCCCCCCCCCHHC	34.37	29255136
39	Phosphorylation	EATPPPASAAGKDWA CCCCCCCHHCCCCCE	25.15	30266825
43	Ubiquitination	PPASAAGKDWAFINT CCCHHCCCCCEEECC	45.42	-
50	Phosphorylation	KDWAFINTNIFARTK CCCEEECCCCCCCCC	25.52	22210691
57	Ubiquitination	TNIFARTKIDPSALV CCCCCCCCCCHHHHH	39.29	-
66	Ubiquitination	DPSALVQKLELDVRS CHHHHHHHHCCCEEC	36.13	-
72	Methylation	QKLELDVRSVTSVRR HHHCCCEECCEEEEC	25.69	-
73	Phosphorylation	KLELDVRSVTSVRRG HHCCCEECCEEEECC	29.60	30576142
75	Phosphorylation	ELDVRSVTSVRRGEA CCCEECCEEEECCCC	23.81	23312004
76	Phosphorylation	LDVRSVTSVRRGEAG CCEECCEEEECCCCC	16.09	30576142
84	Phosphorylation	VRRGEAGSSARSVPS EECCCCCCCCCCCHH	28.07	-
85	Phosphorylation	RRGEAGSSARSVPSI ECCCCCCCCCCCHHH	27.12	-
88	Phosphorylation	EAGSSARSVPSIRRG CCCCCCCCCHHHHCC	37.79	21406692
90	Ubiquitination	GSSARSVPSIRRGAE CCCCCCCHHHHCCCH	25.86	24816145
91	Phosphorylation	SSARSVPSIRRGAEA CCCCCCHHHHCCCHH	26.94	26074081
99	Ubiquitination	IRRGAEAKTVLPKKE HHCCCHHCCCCCHHH	30.58	-
103	Ubiquitination	AEAKTVLPKKEKMKL CHHCCCCCHHHHHHH	41.14	22817900
103 (in isoform 2)	Ubiquitination	-	41.14	21906983
105	Ubiquitination	AKTVLPKKEKMKLRR HCCCCCHHHHHHHHH	61.70	24816145
108	Ubiquitination	VLPKKEKMKLRREQW CCCHHHHHHHHHHHH	5.32	22817900
108 (in isoform 2)	Ubiquitination	-	5.32	21906983
113	Ubiquitination	EKMKLRREQWLQKIE HHHHHHHHHHHHHHH	39.41	22817900
118	Sumoylation	RREQWLQKIEAIKLA HHHHHHHHHHHHHHH	40.10	-
118	Acetylation	RREQWLQKIEAIKLA HHHHHHHHHHHHHHH	40.10	26051181
118 (in isoform 1)	Ubiquitination	-	40.10	21906983
118	Sumoylation	RREQWLQKIEAIKLA HHHHHHHHHHHHHHH	40.10	-
118	Ubiquitination	RREQWLQKIEAIKLA HHHHHHHHHHHHHHH	40.10	21906983
123 (in isoform 1)	Ubiquitination	-	49.01	21906983
123	Ubiquitination	LQKIEAIKLAEQKHR HHHHHHHHHHHHHHH	49.01	22817900
128	Ubiquitination	AIKLAEQKHREERRR HHHHHHHHHHHHHHH	35.81	22817900
138	Phosphorylation	EERRRRATVVVGDLH HHHHHHCEEEECCCH	16.42	29978859
161	Phosphorylation	LLGLEAGSRRQARSR HHCCCCCCHHHHHHH	31.19	23917254
170	Phosphorylation	RQARSRESNKPRPSE HHHHHHHCCCCCHHH	49.39	25954137
172	Ubiquitination	ARSRESNKPRPSELS HHHHHCCCCCHHHHH	52.24	-
176	Phosphorylation	ESNKPRPSELSRMSA HCCCCCHHHHHHCCH	53.07	29214152
179	Phosphorylation	KPRPSELSRMSAAQR CCCHHHHHHCCHHHH	23.14	25954137
203	Phosphorylation	RFQELLASPAYRASP HHHHHHHCCHHHCCH	15.27	30266825
206	Phosphorylation	ELLASPAYRASPLVA HHHHCCHHHCCHHHH	15.31	30266825
209	Phosphorylation	ASPAYRASPLVAIGQ HCCHHHCCHHHHHHH	15.12	21815630

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of F207A_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of F207A_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of F207A_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of F207A_HUMAN !!

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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 SER-203, AND MASSSPECTROMETRY.
PubMed: 19690332

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34 AND SER-203, AND MASSSPECTROMETRY.
PubMed: 18691976

"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34 AND SER-203, AND MASSSPECTROMETRY.
PubMed: 16964243

"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 THR-34, AND MASSSPECTROMETRY.
PubMed: 19413330

"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 THR-34, AND MASSSPECTROMETRY.
PubMed: 18669648