PERF_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PERF_HUMAN
• UniProt AC: P14222
• Protein Name: Perforin-1
• Gene Name: PRF1
• Organism: Homo sapiens (Human).
• Sequence Length: 555
• Subcellular Localization: Cytoplasmic granule lumen. Secreted. Cell membrane; Multi-pass membrane protein. Endosome lumen. Stored in cytoplasmic granules of cytolytic T-lymphocytes and secreted into the cleft between T-lymphocyte and target cell. Inserts into the cell membran
• Protein Description: Plays a key role in secretory granule-dependent cell death, and in defense against virus-infected or neoplastic cells. Plays an important role in killing other cells that are recognized as non-self by the immune system, e.g. in transplant rejection or some forms of autoimmune disease. Can insert into the membrane of target cells in its calcium-bound form, oligomerize and form large pores. Promotes cytolysis and apoptosis of target cells by facilitating the uptake of cytotoxic granzymes..
• Protein Sequence: MAARLLLLGILLLLLPLPVPAPCHTAARSECKRSHKFVPGAWLAGEGVDVTSLRRSGSFPVDTQRFLRPDGTCTLCENALQEGTLQRLPLALTNWRAQGSGCQRHVTRAKVSSTEAVARDAARSIRNDWKVGLDVTPKPTSNVHVSVAGSHSQAANFAAQKTHQDQYSFSTDTVECRFYSFHVVHTPPLHPDFKRALGDLPHHFNASTQPAYLRLISNYGTHFIRAVELGGRISALTALRTCELALEGLTDNEVEDCLTVEAQVNIGIHGSISAEAKACEEKKKKHKMTASFHQTYRERHSEVVGGHHTSINDLLFGIQAGPEQYSAWVNSLPGSPGLVDYTLEPLHVLLDSQDPRREALRRALSQYLTDRARWRDCSRPCPPGRQKSPRDPCQCVCHGSAVTTQDCCPRQRGLAQLEVTFIQAWGLWGDWFTATDAYVKLFFGGQELRTSTVWDNNNPIWSVRLDFGDVLLATGGPLRLQVWDQDSGRDDDLLGTCDQAPKSGSHEVRCNLNHGHLKFRYHARCLPHLGGGTCLDYVPQMLLGEPPGNRSGAVW

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
112	Phosphorylation	HVTRAKVSSTEAVAR HHCCCCCCHHHHHHH	30.73	-
114	Phosphorylation	TRAKVSSTEAVARDA CCCCCCHHHHHHHHH	22.06	21815630
162	Phosphorylation	ANFAAQKTHQDQYSF HHHHHHHHCCCCCCC	16.82	24043423
167	Phosphorylation	QKTHQDQYSFSTDTV HHHCCCCCCCCCCEE	21.70	24043423
168	Phosphorylation	KTHQDQYSFSTDTVE HHCCCCCCCCCCEEE	13.69	24043423
170	Phosphorylation	HQDQYSFSTDTVECR CCCCCCCCCCEEEEE	21.31	24043423
171	Phosphorylation	QDQYSFSTDTVECRF CCCCCCCCCEEEEEE	33.41	24043423
173	Phosphorylation	QYSFSTDTVECRFYS CCCCCCCEEEEEEEE	20.49	24043423
205	N-linked_Glycosylation	GDLPHHFNASTQPAY CCCCCCCCCCCCHHH	28.73	19159218
237	Phosphorylation	GGRISALTALRTCEL CCHHHHHHHHHHHHH	24.30	24719451
533	Phosphorylation	LPHLGGGTCLDYVPQ CCCCCCCCHHHHCCH	17.11	-
549	N-linked_Glycosylation	LLGEPPGNRSGAVW- HCCCCCCCCCCCCC-	40.49	UniProtKB CARBOHYD

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PERF_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 PERF_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PERF_HUMAN	PRF1	physical	21685908

Drug and Disease Associations

• Kegg Disease
• H00109: Familial hemophagocytic lymphohistiocytosis (FHPL), including the following three diseases: Perforin
• OMIM Disease
• 603553: Familial hemophagocytic lymphohistiocytosis 2 (FHL2)
• 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

N-linked Glycosylation

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-205, AND MASSSPECTROMETRY.
PubMed: 19159218