TMPS2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TMPS2_HUMAN
• UniProt AC: O15393
• Protein Name: Transmembrane protease serine 2
• Gene Name: TMPRSS2
• Organism: Homo sapiens (Human).
• Sequence Length: 492
• Subcellular Localization: Cell membrane ; Single-pass type II membrane protein .; Transmembrane protease serine 2 catalytic chain: Secreted . Activated by cleavage and secreted.
• Protein Description: Serine protease that proteolytically cleaves and activates the viral spike glycoproteins which facilitate virus-cell membrane fusions; spike proteins are synthesized and maintained in precursor intermediate folding states and proteolysis permits the refolding and energy release required to create stable virus-cell linkages and membrane coalescence. Facilitates human SARS coronavirus (SARS-CoV) infection via two independent mechanisms, proteolytic cleavage of ACE2, which might promote viral uptake, and cleavage of coronavirus spike glycoprotein which activates the glycoprotein for cathepsin L-independent host cell entry. Proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9); involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity..
• Protein Sequence: MALNSGSPPAIGPYYENHGYQPENPYPAQPTVVPTVYEVHPAQYYPSPVPQYAPRVLTQASNPVVCTQPKSPSGTVCTSKTKKALCITLTLGTFLVGAALAAGLLWKFMGSKCSNSGIECDSSGTCINPSNWCDGVSHCPGGEDENRCVRLYGPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSGSTSFMKLNTSAGNVDIYKKLYHSDACSSKAVVSLRCIACGVNLNSSRQSRIVGGESALPGAWPWQVSLHVQNVHVCGGSIITPEWIVTAAHCVEKPLNNPWHWTAFAGILRQSFMFYGAGYQVEKVISHPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSRYVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQMRADG

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
26	Phosphorylation	GYQPENPYPAQPTVV CCCCCCCCCCCCCEE	23.84	27642862
44	Phosphorylation	YEVHPAQYYPSPVPQ EEECHHHCCCCCCCC	21.32	-
45	Phosphorylation	EVHPAQYYPSPVPQY EECHHHCCCCCCCCC	5.78	-
52	Phosphorylation	YPSPVPQYAPRVLTQ CCCCCCCCCCCCCCC	16.71	21253578
58	Phosphorylation	QYAPRVLTQASNPVV CCCCCCCCCCCCCEE	21.16	27499020
61	Phosphorylation	PRVLTQASNPVVCTQ CCCCCCCCCCEEECC	31.67	27251275
95	Phosphorylation	TLTLGTFLVGAALAA ECCHHHHHHHHHHHH	3.31	27251275
98	Phosphorylation	LGTFLVGAALAAGLL HHHHHHHHHHHHHHH	7.57	27251275
195	Phosphorylation	MGYKNNFYSSQGIVD HCCCCCCCCCCCEEC	14.99	30576142
206	Phosphorylation	GIVDDSGSTSFMKLN CEECCCCCCCEEEEC	25.48	30576142
208	Phosphorylation	VDDSGSTSFMKLNTS ECCCCCCCEEEECCC	25.66	30576142
213	N-linked_Glycosylation	STSFMKLNTSAGNVD CCCEEEECCCCCCCC	26.86	UniProtKB CARBOHYD
222	Phosphorylation	SAGNVDIYKKLYHSD CCCCCCHHHHHHCCC	9.52	28509920
249	N-linked_Glycosylation	IACGVNLNSSRQSRI EECCCCCCCCCCCEE	32.51	UniProtKB CARBOHYD
341	Phosphorylation	HPNYDSKTKNNDIAL CCCCCCCCCCCCEEE	42.85	-

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

Oops, there are no upstream regulatory protein records of TMPS2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TMPS2_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 TMPS2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of TMPS2_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• H00024: Prostate cancer
• 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.