dbPTM

TPA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TPA_HUMAN
UniProt AC	P00750
Protein Name	Tissue-type plasminogen activator
Gene Name	PLAT
Organism	Homo sapiens (Human).
Sequence Length	562
Subcellular Localization	Secreted, extracellular space.
Protein Description	Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. Plays a direct role in facilitating neuronal migration..
Protein Sequence	MDAMKRGLCCVLLLCGAVFVSPSQEIHARFRRGARSYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGTWSTAESGAECTNWNSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
96	O-linked_Glycosylation	PRCFNGGTCQQALYF CCCCCCCCCCEEEEC	14.45	1900431
96	O-linked_Glycosylation	PRCFNGGTCQQALYF CCCCCCCCCCEEEEC	14.45	1900431
118	S-nitrosocysteine	PEGFAGKCCEIDTRA CCCCCCCCCEEECCC	2.17	-
118	S-nitrosylation	PEGFAGKCCEIDTRA CCCCCCCCCEEECCC	2.17	22178444
152	N-linked_Glycosylation	GAECTNWNSSALAQK CCCCCCCCHHHHCCC	28.32	2513186
152	N-linked_Glycosylation	GAECTNWNSSALAQK CCCCCCCCHHHHCCC	28.32	6433976
219	N-linked_Glycosylation	NSDCYFGNGSAYRGT CCCCCCCCCCCCCCC	31.20	2513186
219	N-linked_Glycosylation	NSDCYFGNGSAYRGT CCCCCCCCCCCCCCC	31.20	6433976
290	Phosphorylation	NRRLTWEYCDVPSCS CCCCCEEECCCCCCC	5.87	26091039
456	Phosphorylation	YGKHEALSPFYSERL CCCCCCCCHHHHHHH	21.73	26091039
473	Phosphorylation	AHVRLYPSSRCTSQH HCEEEECCCCCCHHH	19.50	-
474	Phosphorylation	HVRLYPSSRCTSQHL CEEEECCCCCCHHHH	27.20	-
477	Phosphorylation	LYPSSRCTSQHLLNR EECCCCCCHHHHHCC	30.25	-
478	Phosphorylation	YPSSRCTSQHLLNRT ECCCCCCHHHHHCCC	21.16	-
483	N-linked_Glycosylation	CTSQHLLNRTVTDNM CCHHHHHCCCCCCCE	43.89	6433976
483	N-linked_Glycosylation	CTSQHLLNRTVTDNM CCHHHHHCCCCCCCE	43.89	2513186
487	O-linked_Glycosylation	HLLNRTVTDNMLCAG HHHCCCCCCCEEECC	22.50	55835159

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 TPA_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
152	N	Glycosylation	27613864
N-glycosylation of Asn-152; the bound oligomannosidic glycan is involved in the interaction with the mannose receptor.
219	N	Glycosylation	1900431
Differential cell-specific N-linked glycosylation gives rise to two glycoforms, type I (glycosylated at Asn-219) and type II (not glycosylated at Asn-219).

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 TPA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UROK_HUMAN	PLAU	physical	7721771
NEUS_HUMAN	SERPINI1	physical	12354288
THRB_HUMAN	F2	physical	10543954
LRP1_HUMAN	LRP1	physical	10632583
LRP1_HUMAN	LRP1	physical	1502153
FIBA_HUMAN	FGA	physical	3088041
PDGFC_HUMAN	PDGFC	physical	22035541

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 TPA_HUMAN

Related Literatures of Post-Translational Modification

O-linked Glycosylation
Reference	PubMed
"Tissue plasminogen activator has an O-linked fucose attached tothreonine-61 in the epidermal growth factor domain."; Harris R.J., Leonard C.K., Guzzetta A.W., Spellman M.W.; Biochemistry 30:2311-2314(1991). Cited for: GLYCOSYLATION AT THR-96.	1900431 [Abstract]