dbPTM

TIMP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TIMP1_HUMAN
UniProt AC	P01033
Protein Name	Metalloproteinase inhibitor 1
Gene Name	TIMP1
Organism	Homo sapiens (Human).
Sequence Length	207
Subcellular Localization	Secreted .
Protein Description	Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Mediates erythropoiesis in vitro; but, unlike IL3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors..
Protein Sequence	MAPFEPLASGILLLLWLIAPSRACTCVPPHPQTAFCNSDLVIRAKFVGTPEVNQTTLYQRYEIKMTKMYKGFQALGDAADIRFVYTPAMESVCGYFHRSHNRSEEFLIAGKLQDGLLHITTCSFVAPWNSLSLAQRRGFTKTYTVGCEECTVFPCLSIPCKLQSGTHCLWTDQLLQGSEKGFQSRHLACLPREPGLCTWQSLRSQIA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
25	Phosphorylation	IAPSRACTCVPPHPQ HCCCCCCCCCCCCCC	18.62	26091039
45	Ubiquitination	SDLVIRAKFVGTPEV CCEEEEEEECCCCCC	30.63	21906983
49	Phosphorylation	IRAKFVGTPEVNQTT EEEEECCCCCCCCCC	15.80	27174698
53	N-linked_Glycosylation	FVGTPEVNQTTLYQR ECCCCCCCCCCCHHE	31.64	16263699
53	N-linked_Glycosylation	FVGTPEVNQTTLYQR ECCCCCCCCCCCHHE	31.64	16263699
55	Phosphorylation	GTPEVNQTTLYQRYE CCCCCCCCCCHHEEE	17.36	27174698
56	Phosphorylation	TPEVNQTTLYQRYEI CCCCCCCCCHHEEEE	17.44	27174698
58	Phosphorylation	EVNQTTLYQRYEIKM CCCCCCCHHEEEEEE	6.72	27174698
58	Nitration	EVNQTTLYQRYEIKM CCCCCCCHHEEEEEE	6.72	-
61	Phosphorylation	QTTLYQRYEIKMTKM CCCCHHEEEEEEHHH	13.38	27174698
66	Phosphorylation	QRYEIKMTKMYKGFQ HEEEEEEHHHCHHHH	13.99	29083192
69	Phosphorylation	EIKMTKMYKGFQALG EEEEHHHCHHHHHHH	14.98	29083192
70	Ubiquitination	IKMTKMYKGFQALGD EEEHHHCHHHHHHHC	50.15	2190698
101	N-linked_Glycosylation	GYFHRSHNRSEEFLI HHHHCCCCCCCEEEE	50.88	16740002
141	Ubiquitination	AQRRGFTKTYTVGCE HHHCCCCEEEEECCC	36.95	-
143	Nitration	RRGFTKTYTVGCEEC HCCCCEEEEECCCCC	10.86	-
178	Phosphorylation	TDQLLQGSEKGFQSR EHHHHCCCCCCCCCC	24.15	22427646
180	Ubiquitination	QLLQGSEKGFQSRHL HHHCCCCCCCCCCEE	67.72	-

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
178	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TIMP1_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 TIMP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RECQ5_HUMAN	RECQL5	physical	16169070
ECH1_HUMAN	ECH1	physical	16169070
EF1B_HUMAN	EEF1B2	physical	16169070
MMP3_HUMAN	MMP3	physical	9288970
MMP1_HUMAN	MMP1	physical	9063449
ZBT16_HUMAN	ZBTB16	physical	17340613
PCSK5_MOUSE	Pcsk5	physical	16135528

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.

Regulatory Network of TIMP1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach."; Lewandrowski U., Moebius J., Walter U., Sickmann A.; Mol. Cell. Proteomics 5:226-233(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53, AND MASS SPECTROMETRY.	16263699 [Abstract]
"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry."; Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.; J. Proteome Res. 5:1493-1503(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53 AND ASN-101, AND MASSSPECTROMETRY.	16740002 [Abstract]
"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-53, AND MASS SPECTROMETRY.	16335952 [Abstract]