dbPTM

ECM1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ECM1_HUMAN
UniProt AC	Q16610
Protein Name	Extracellular matrix protein 1
Gene Name	ECM1
Organism	Homo sapiens (Human).
Sequence Length	540
Subcellular Localization	Secreted, extracellular space, extracellular matrix.
Protein Description	Involved in endochondral bone formation as negative regulator of bone mineralization. Stimulates the proliferation of endothelial cells and promotes angiogenesis. Inhibits MMP9 proteolytic activity..
Protein Sequence	MGTTARAALVLTYLAVASAASEGGFTATGQRQLRPEHFQEVGYAAPPSPPLSRSLPMDHPDSSQHGPPFEGQSQVQPPPSQEATPLQQEKLLPAQLPAEKEVGPPLPQEAVPLQKELPSLQHPNEQKEGTPAPFGDQSHPEPESWNAAQHCQQDRSQGGWGHRLDGFPPGRPSPDNLNQICLPNRQHVVYGPWNLPQSSYSHLTRQGETLNFLEIGYSRCCHCRSHTNRLECAKLVWEEAMSRFCEAEFSVKTRPHWCCTRQGEARFSCFQEEAPQPHYQLRACPSHQPDISSGLELPFPPGVPTLDNIKNICHLRRFRSVPRNLPATDPLQRELLALIQLEREFQRCCRQGNNHTCTWKAWEDTLDKYCDREYAVKTHHHLCCRHPPSPTRDECFARRAPYPNYDRDILTIDIGRVTPNLMGHLCGNQRVLTKHKHIPGLIHNMTARCCDLPFPEQACCAEEEKLTFINDLCGPRRNIWRDPALCCYLSPGDEQVNCFNINYLRNVALVSGDTENAKGQGEQGSTGGTNISSTSEPKEE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MGTTARAALV -----CCHHHHHHHH	18.91	-
12	Phosphorylation	ARAALVLTYLAVASA HHHHHHHHHHHHHHH	14.71	23532336
18	Phosphorylation	LTYLAVASAASEGGF HHHHHHHHHHHHCCC	20.12	24719451
43	Phosphorylation	EHFQEVGYAAPPSPP HHHHHCCCCCCCCCC	12.55	-
43	O-linked_Glycosylation	EHFQEVGYAAPPSPP HHHHHCCCCCCCCCC	12.55	30806347
48	Phosphorylation	VGYAAPPSPPLSRSL CCCCCCCCCCCCCCC	37.78	26091039
48	O-linked_Glycosylation	VGYAAPPSPPLSRSL CCCCCCCCCCCCCCC	37.78	55833179
52	Phosphorylation	APPSPPLSRSLPMDH CCCCCCCCCCCCCCC	26.12	26091039
63	O-linked_Glycosylation	PMDHPDSSQHGPPFE CCCCCCHHHCCCCCC	33.31	OGP
80	O-linked_Glycosylation	SQVQPPPSQEATPLQ CCCCCCCCCCCCCCC	46.56	OGP
80	Phosphorylation	SQVQPPPSQEATPLQ CCCCCCCCCCCCCCC	46.56	24505115
84	O-linked_Glycosylation	PPPSQEATPLQQEKL CCCCCCCCCCCHHHC	24.63	OGP
119	O-linked_Glycosylation	PLQKELPSLQHPNEQ CHHHHCCCCCCCCCC	53.97	55824565
130	O-linked_Glycosylation	PNEQKEGTPAPFGDQ CCCCCCCCCCCCCCC	19.85	OGP
138	O-linked_Glycosylation	PAPFGDQSHPEPESW CCCCCCCCCCCCCCC	45.83	OGP
354	N-linked_Glycosylation	RCCRQGNNHTCTWKA HHHHHCCCCCEEEHH	38.37	UniProtKB CARBOHYD
369	Phosphorylation	WEDTLDKYCDREYAV HHHHHHHHHCHHHHH	10.15	22468782
374	Phosphorylation	DKYCDREYAVKTHHH HHHHCHHHHHHCCCC	20.00	22468782
378	Phosphorylation	DREYAVKTHHHLCCR CHHHHHHCCCCCCCC	21.60	22468782
391	O-linked_Glycosylation	CRHPPSPTRDECFAR CCCCCCCCHHHHHHH	55.90	55829579
411	Phosphorylation	NYDRDILTIDIGRVT CCCCCEEEEECCCCC	19.55	24719451
418	Phosphorylation	TIDIGRVTPNLMGHL EEECCCCCCCHHHHH	12.71	-
433	Phosphorylation	CGNQRVLTKHKHIPG HCCCHHHCCCCCCCC	28.39	-
438	Phosphorylation	VLTKHKHIPGLIHNM HHCCCCCCCCHHHHC	3.27	24719451
444	N-linked_Glycosylation	HIPGLIHNMTARCCD CCCCHHHHCCCHHCC	23.62	17623646
444	N-linked_Glycosylation	HIPGLIHNMTARCCD CCCCHHHHCCCHHCC	23.62	16335952
530	N-linked_Glycosylation	QGSTGGTNISSTSEP CCCCCCCCCCCCCCC	35.11	UniProtKB CARBOHYD
534	O-linked_Glycosylation	GGTNISSTSEPKEE- CCCCCCCCCCCCCC-	30.25	OGP

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 ECM1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ECM1_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 ECM1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
IRAK3_HUMAN	IRAK3	physical	21988832
CPTP_HUMAN	CPTP	physical	21988832

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
247100	Lipoid proteinosis (LiP)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ECM1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-444, AND MASSSPECTROMETRY.	16335952 [Abstract]