F124B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: F124B_HUMAN
• UniProt AC: Q9H5Z6
• Protein Name: Protein FAM124B
• Gene Name: FAM124B
• Organism: Homo sapiens (Human).
• Sequence Length: 455
• Subcellular Localization: Nucleus .
• Protein Sequence: MDETQGPLAMTVHLLANSGHGSLLQRTLDQLLDCICPEVRLFQVSERASPVKYCEKSHSKRSRFPGMSVLLFLHESPGEDRLFRVLDSLQHSPWQCYPTQDTRGRLCPYFFANQEFYSLDSQLPIWGVRQVHCGSEILRVTLYCSFDNYEDAIRLYEMILQREATLQKSNFCFFVLYASKSFALQLSLKQLPPGMSVDPKESSVLQFKVQEIGQLVPLLPNPCMPISSTRWQTQDYDGNKILLQVQLNPELGVKNGILGAGMLPLGSRLTSVSAKRTSEPRSQRNQGKRSQGHSLELPEPSGSPTSDRCAGTSWKSPGRSFQVSSPAMGAHLHLSSHHLESGARMKVLNRENSFQKLEAETNVDTGLTIINSEPRQTYFGGFPRDLQTSQPPFCLPASSLGVATSKNNSVLKERVSPLPLAGQRDLGTRKTISECLLHLQVQGEEKEEDEEEFFI

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	Phosphorylation	TQGPLAMTVHLLANS CCCCCHHHHHHHHHC	10.12	24719451
18	Phosphorylation	TVHLLANSGHGSLLQ HHHHHHHCCCHHHHH	26.93	24719451
22	Phosphorylation	LANSGHGSLLQRTLD HHHCCCHHHHHHHHH	21.89	24719451
49	Phosphorylation	FQVSERASPVKYCEK EECCCCCCCCCCCCC	36.13	14702039
53	Phosphorylation	ERASPVKYCEKSHSK CCCCCCCCCCCCCCC	13.18	-
196	Phosphorylation	KQLPPGMSVDPKESS CCCCCCCCCCCCCCC	29.32	29396449
200	Acetylation	PGMSVDPKESSVLQF CCCCCCCCCCCEEEE	66.81	19608861
273	Phosphorylation	GSRLTSVSAKRTSEP CCCCCHHCCCCCCCC	28.04	-
290	Phosphorylation	QRNQGKRSQGHSLEL HCCCCCCCCCCCCCC	43.96	18767875
294	Phosphorylation	GKRSQGHSLELPEPS CCCCCCCCCCCCCCC	30.29	23403867
301	Phosphorylation	SLELPEPSGSPTSDR CCCCCCCCCCCCCCC	50.68	23532336
303	Phosphorylation	ELPEPSGSPTSDRCA CCCCCCCCCCCCCCC	29.37	23403867
305	Phosphorylation	PEPSGSPTSDRCAGT CCCCCCCCCCCCCCC	44.98	23403867
306	Phosphorylation	EPSGSPTSDRCAGTS CCCCCCCCCCCCCCC	26.83	23403867
353	Phosphorylation	KVLNRENSFQKLEAE EEECCCCCCHHHHEE	25.05	23403867
416	Phosphorylation	SVLKERVSPLPLAGQ HHHHHCCCCCCCCCC	27.26	23403867

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

Oops, there are no upstream regulatory protein records of F124B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of F124B_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 F124B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MDFI_HUMAN	MDFI	physical	19447967
TRI37_HUMAN	TRIM37	physical	19447967
MDFI_HUMAN	MDFI	physical	19060904
USBP1_HUMAN	USHBP1	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
ADIP_HUMAN	SSX2IP	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
K1958_HUMAN	KIAA1958	physical	25416956
KCTD6_HUMAN	KCTD6	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
KR109_HUMAN	KRTAP10-9	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
NT2NL_HUMAN	NOTCH2NL	physical	25416956

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

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-200, AND MASS SPECTROMETRY.
PubMed: 19608861