dbPTM

TRY1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TRY1_HUMAN
UniProt AC	P07477
Protein Name	Trypsin-1
Gene Name	PRSS1
Organism	Homo sapiens (Human).
Sequence Length	247
Subcellular Localization	Secreted, extracellular space.
Protein Description	Has activity against the synthetic substrates Boc-Phe-Ser-Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val-Pro-Arg-Mec. The single-chain form is more active than the two-chain form against all of these substrates..
Protein Sequence	MNPLLILTFVAAALAAPFDDDDKIVGGYNCEENSVPYQVSLNSGYHFCGGSLINEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPQYDRKTLNNDIMLIKLSSRAVINARVSTISLPTAPPATGTKCLISGWGNTASSGADYPDELQCLDAPVLSQAKCEASYPGKITSNMFCVGFLEGGKDSCQGDSGGPVVCNGQLQGVVSWGDGCAQKNKPGVYTKVYNYVKWIKNTIAANS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MNPLLILTFVAAALA CCHHHHHHHHHHHHH	14.74	21406692
92	Ubiquitination	EQFINAAKIIRHPQY HHHHHHHHHHHCCCC	35.93	22817900
99	Phosphorylation	KIIRHPQYDRKTLNN HHHHCCCCCCCCCCC	23.36	26330541
103	Phosphorylation	HPQYDRKTLNNDIML CCCCCCCCCCCCEEE	35.30	26330541
112	Acetylation	NNDIMLIKLSSRAVI CCCEEEEEECCHHEE	38.05	12652799
154	Phosphorylation	TASSGADYPDELQCL CCCCCCCCCCHHCCC	16.43	8683601
154	Sulfation	TASSGADYPDELQCL CCCCCCCCCCHHCCC	16.43	-
154	Sulfation	TASSGADYPDELQCL CCCCCCCCCCHHCCC	16.43	17087724
195	Phosphorylation	FLEGGKDSCQGDSGG EEECCCCCCCCCCCC	16.30	-
215	Phosphorylation	GQLQGVVSWGDGCAQ CEEEEEEEECCCCCC	23.96	25247763
225	Ubiquitination	DGCAQKNKPGVYTKV CCCCCCCCCCEEEHH	50.62	25015289
229	Phosphorylation	QKNKPGVYTKVYNYV CCCCCCEEEHHHHHH	13.52	26267517
231	Ubiquitination	NKPGVYTKVYNYVKW CCCCEEEHHHHHHHH	25.65	25015289
317	Ubiquitination	----------------------------------------------------------------------------- -----------------------------------------------------------------------------		22817900
450	Ubiquitination	------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		25015289
456	Ubiquitination	------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		25015289

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 TRY1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TRY1_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 TRY1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SPB8_HUMAN	SERPINB8	physical	9402754
A2AP_HUMAN	SERPINF2	physical	2437112

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
167800	Pancreatitis, hereditary (PCTT)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TRY1_HUMAN

Related Literatures of Post-Translational Modification

Sulfation
Reference	PubMed
"Human cationic trypsinogen is sulfated on Tyr154."; Sahin-Toth M., Kukor Z., Nemoda Z.; FEBS J. 273:5044-5050(2006). Cited for: SULFATION AT TYR-154, AND MUTAGENESIS OF TYR-154.	17087724 [Abstract]