FBLI1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FBLI1_HUMAN
• UniProt AC: Q8WUP2
• Protein Name: Filamin-binding LIM protein 1
• Gene Name: FBLIM1
• Organism: Homo sapiens (Human).
• Sequence Length: 373
• Subcellular Localization: Cytoplasm, cell cortex. Cell junction, focal adhesion. Cytoplasm, cytoskeleton. Associated with actin stress fiber at cell-ECM focal adhesion sites. Isoform 1 and isoform 3 are recruited and localized at actin stress fibers and clustered at cell-EMC
• Protein Description: Serves as an anchoring site for cell-ECM adhesion proteins and filamin-containing actin filaments. Is implicated in cell shape modulation (spreading) and motility. May participate in the regulation of filamin-mediated cross-linking and stabilization of actin filaments. May also regulate the assembly of filamin-containing signaling complexes that control actin assembly. Promotes dissociation of FLNA from ITGB3 and ITGB7. Promotes activation of integrins and regulates integrin-mediated cell-cell adhesion..
• Protein Sequence: MASKPEKRVASSVFITLAPPRRDVAVAEEVRQAVCEARRGRPWEAPAPMKTPEAGLAGRPSPWTTPGRAAATVPAAPMQLFNGGCPPPPPVLDGEDVLPDLDLLPPPPPPPPVLLPSEEEAPAPMGASLIADLEQLHLSPPPPPPQAPAEGPSVQPGPLRPMEEELPPPPAEPVEKGASTDICAFCHKTVSPRELAVEAMKRQYHAQCFTCRTCRRQLAGQSFYQKDGRPLCEPCYQDTLERCGKCGEVVRDHIIRALGQAFHPSCFTCVTCARCIGDESFALGSQNEVYCLDDFYRKFAPVCSICENPIIPRDGKDAFKIECMGRNFHENCYRCEDCRILLSVEPTDQGCYPLNNHLFCKPCHVKRSAAGCC

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	KPEKRVASSVFITLA CCCHHHCCEEEEEEC	24.95	28857561
12	Phosphorylation	PEKRVASSVFITLAP CCHHHCCEEEEEECC	16.00	28857561
49	Sulfoxidation	PWEAPAPMKTPEAGL CCCCCCCCCCCCCCC	9.07	30846556
51	Phosphorylation	EAPAPMKTPEAGLAG CCCCCCCCCCCCCCC	21.80	26657352
61	Phosphorylation	AGLAGRPSPWTTPGR CCCCCCCCCCCCCCC	31.54	23403867
64	Phosphorylation	AGRPSPWTTPGRAAA CCCCCCCCCCCCCCC	26.88	23403867
65	Phosphorylation	GRPSPWTTPGRAAAT CCCCCCCCCCCCCCC	21.63	23403867
179	Phosphorylation	EPVEKGASTDICAFC CCCCCCCCCCHHHHC	34.97	28348404
180	Phosphorylation	PVEKGASTDICAFCH CCCCCCCCCHHHHCC	28.93	28348404
189	Phosphorylation	ICAFCHKTVSPRELA HHHHCCCCCCHHHHH	11.53	22199227
191	Phosphorylation	AFCHKTVSPRELAVE HHCCCCCCHHHHHHH	24.38	22199227
201	Acetylation	ELAVEAMKRQYHAQC HHHHHHHHHHHHHHH	43.32	7710473
222	Phosphorylation	RRQLAGQSFYQKDGR HHHHCCCCCCCCCCC	25.63	23403867
224	Phosphorylation	QLAGQSFYQKDGRPL HHCCCCCCCCCCCCC	21.65	23403867
285	Phosphorylation	DESFALGSQNEVYCL CCCEECCCCCEEEEC	30.59	26657352
333	Phosphorylation	RNFHENCYRCEDCRI CCCCCCCEECCCCEE	29.85	-
365	Phosphorylation	LFCKPCHVKRSAAGC EEECCCCCCCCCCCC	7.59	27251275
365 (in isoform 2)	Phosphorylation	-	7.59	27251275
367	Phosphorylation	CKPCHVKRSAAGCC- ECCCCCCCCCCCCC-	30.36	27251275
367 (in isoform 2)	Phosphorylation	-	30.36	27251275

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

Oops, there are no upstream regulatory protein records of FBLI1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FBLI1_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 FBLI1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FERM2_HUMAN	FERMT2	physical	12679033
FLNA_HUMAN	FLNA	physical	12679033
FLNB_HUMAN	FLNB	physical	12496242
LMO3_HUMAN	LMO3	physical	25416956

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.