FMOD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FMOD_HUMAN
• UniProt AC: Q06828
• Protein Name: Fibromodulin
• Gene Name: FMOD
• Organism: Homo sapiens (Human).
• Sequence Length: 376
• Subcellular Localization: Secreted, extracellular space, extracellular matrix.
• Protein Description: Affects the rate of fibrils formation. May have a primary role in collagen fibrillogenesis (By similarity)..
• Protein Sequence: MQWTSLLLLAGLFSLSQAQYEDDPHWWFHYLRSQQSTYYDPYDPYPYETYEPYPYGVDEGPAYTYGSPSPPDPRDCPQECDCPPNFPTAMYCDNRNLKYLPFVPSRMKYVYFQNNQITSIQEGVFDNATGLLWIALHGNQITSDKVGRKVFSKLRHLERLYLDHNNLTRMPGPLPRSLRELHLDHNQISRVPNNALEGLENLTALYLQHNEIQEVGSSMRGLRSLILLDLSYNHLRKVPDGLPSALEQLYMEHNNVYTVPDSYFRGAPKLLYVRLSHNSLTNNGLASNTFNSSSLLELDLSYNQLQKIPPVNTNLENLYLQGNRINEFSISSFCTVVDVVNFSKLQVLRLDGNEIKRSAMPADAPLCLRLASLIEI

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
19	Pyrrolidone_carboxylic_acid	LFSLSQAQYEDDPHW HHHHHHHHHCCCCHH	34.21	-
19	Pyrrolidone_carboxylic_acid	LFSLSQAQYEDDPHW HHHHHHHHHCCCCHH	34.21	14551184
19	Pyrrolidone_carboxylic_acid	LFSLSQAQYEDDPHW HHHHHHHHHCCCCHH	34.21	14551184
20	Sulfation	FSLSQAQYEDDPHWW HHHHHHHHCCCCHHH	25.09	-
20	Sulfation	FSLSQAQYEDDPHWW HHHHHHHHCCCCHHH	25.09	14551184
38	Sulfation	LRSQQSTYYDPYDPY HHHCCCCCCCCCCCC	15.89	-
38	Sulfation	LRSQQSTYYDPYDPY HHHCCCCCCCCCCCC	15.89	14551184
39	Sulfation	RSQQSTYYDPYDPYP HHCCCCCCCCCCCCC	15.55	-
39	Sulfation	RSQQSTYYDPYDPYP HHCCCCCCCCCCCCC	15.55	14551184
45	Sulfation	YYDPYDPYPYETYEP CCCCCCCCCCCCCCC	18.62	14551184
45	Sulfation	YYDPYDPYPYETYEP CCCCCCCCCCCCCCC	18.62	-
47	Sulfation	DPYDPYPYETYEPYP CCCCCCCCCCCCCCC	18.30	-
47	Sulfation	DPYDPYPYETYEPYP CCCCCCCCCCCCCCC	18.30	14551184
53	Sulfation	PYETYEPYPYGVDEG CCCCCCCCCCCCCCC	9.35	-
53	Sulfation	PYETYEPYPYGVDEG CCCCCCCCCCCCCCC	9.35	14551184
55	Sulfation	ETYEPYPYGVDEGPA CCCCCCCCCCCCCCC	24.76	14551184
55	Sulfation	ETYEPYPYGVDEGPA CCCCCCCCCCCCCCC	24.76	-
67	O-linked_Glycosylation	GPAYTYGSPSPPDPR CCCCCCCCCCCCCCC	16.28	OGP
105	Phosphorylation	KYLPFVPSRMKYVYF CCCCCCCCCCEEEEE	39.44	23612710
127	N-linked_Glycosylation	IQEGVFDNATGLLWI EEECCCCCHHHEEEE	28.12	UniProtKB CARBOHYD
166	N-linked_Glycosylation	RLYLDHNNLTRMPGP HHHCCCCCCCCCCCC	39.09	UniProtKB CARBOHYD
168	Phosphorylation	YLDHNNLTRMPGPLP HCCCCCCCCCCCCCC	27.35	25849741
201	N-linked_Glycosylation	NALEGLENLTALYLQ CHHHHHHHHHHHHHH	47.97	UniProtKB CARBOHYD
291	N-linked_Glycosylation	GLASNTFNSSSLLEL CCCCCCCCCCHHEEE	38.65	UniProtKB CARBOHYD
341	N-linked_Glycosylation	CTVVDVVNFSKLQVL CEEEEEECCCCCEEE	35.01	UniProtKB CARBOHYD

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FMOD_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 FMOD_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZBT32_HUMAN	ZBTB32	physical	25011449

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

Sulfation

"Identification of tyrosine sulfation in extracellular leucine-richrepeat proteins using mass spectrometry.";
Onnerfjord P., Heathfield T.F., Heinegaard D.;
J. Biol. Chem. 279:26-33(2004).
Cited for: SULFATION AT TYR-20; TYR-38; TYR-39; TYR-45; TYR-47; TYR-53 ANDTYR-55, LACK OF SULFATION AT TYR-63 AND TYR-65, PYROGLUTAMATEFORMATION AT GLN-19, AND MASS SPECTROMETRY.
PubMed: 14551184