SFTPD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SFTPD_HUMAN
• UniProt AC: P35247
• Protein Name: Pulmonary surfactant-associated protein D
• Gene Name: SFTPD
• Organism: Homo sapiens (Human).
• Sequence Length: 375
• Subcellular Localization: Secreted, extracellular space, extracellular matrix. Secreted, extracellular space, surface film.
• Protein Description: Contributes to the lung's defense against inhaled microorganisms, organic antigens and toxins. Interacts with compounds such as bacterial lipopolysaccharides, oligosaccharides and fatty acids and modulates leukocyte action in immune response. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties..
• Protein Sequence: MLLFLLSALVLLTQPLGYLEAEMKTYSHRTMPSACTLVMCSSVESGLPGRDGRDGREGPRGEKGDPGLPGAAGQAGMPGQAGPVGPKGDNGSVGEPGPKGDTGPSGPPGPPGVPGPAGREGPLGKQGNIGPQGKPGPKGEAGPKGEVGAPGMQGSAGARGLAGPKGERGVPGERGVPGNTGAAGSAGAMGPQGSPGARGPPGLKGDKGIPGDKGAKGESGLPDVASLRQQVEALQGQVQHLQAAFSQYKKVELFPNGQSVGEKIFKTAGFVKPFTEAQLLCTQAGGQLASPRSAAENAALQQLVVAKNEAAFLSMTDSKTEGKFTYPTGESLVYSNWAPGEPNDDGGSEDCVEIFTNGKWNDRACGEKRLVVCEF

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
30	Phosphorylation	MKTYSHRTMPSACTL HHHCCCCCCCCCCEE	28.19	-
33	Phosphorylation	YSHRTMPSACTLVMC CCCCCCCCCCEEEEC	25.75	-
35	S-nitrosylation	HRTMPSACTLVMCSS CCCCCCCCEEEECCC	3.38	22178444
35	S-nitrosocysteine	HRTMPSACTLVMCSS CCCCCCCCEEEECCC	3.38	-
40	S-nitrosocysteine	SACTLVMCSSVESGL CCCEEEECCCCCCCC	1.82	-
40	S-nitrosylation	SACTLVMCSSVESGL CCCEEEECCCCCCCC	1.82	22178444
78	Hydroxylation	AAGQAGMPGQAGPVG CCCCCCCCCCCCCCC	30.72	-
87	Hydroxylation	QAGPVGPKGDNGSVG CCCCCCCCCCCCCCC	73.33	-
90	N-linked_Glycosylation	PVGPKGDNGSVGEPG CCCCCCCCCCCCCCC	53.99	8006040
90	N-linked_Glycosylation	PVGPKGDNGSVGEPG CCCCCCCCCCCCCCC	53.99	8006040
96	Hydroxylation	DNGSVGEPGPKGDTG CCCCCCCCCCCCCCC	59.46	-
99	Hydroxylation	SVGEPGPKGDTGPSG CCCCCCCCCCCCCCC	75.28	-
171	Hydroxylation	PKGERGVPGERGVPG CCCCCCCCCCCCCCC	41.57	-
177	Hydroxylation	VPGERGVPGNTGAAG CCCCCCCCCCCCCCC	32.89	-
180	Phosphorylation	ERGVPGNTGAAGSAG CCCCCCCCCCCCCCC	33.83	22210691
185	Phosphorylation	GNTGAAGSAGAMGPQ CCCCCCCCCCCCCCC	20.85	22210691
248	Nitration	LQAAFSQYKKVELFP HHHHHHHCCEEEECC	16.16	-
326	Nitration	KTEGKFTYPTGESLV CCCCEEEECCCCCEE	11.26	-
334	Nitration	PTGESLVYSNWAPGE CCCCCEEEECCCCCC	11.11	-

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

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
35	C	S-nitrosylation	S-nitrosylation at Cys-35 and Cys-40 alters the quaternary structure which results in a pro-inflammatory chemoattractive signaling activity with macrophages.	-
40	C	S-nitrosylation	S-nitrosylation at Cys-35 and Cys-40 alters the quaternary structure which results in a pro-inflammatory chemoattractive signaling activity with macrophages.	-

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
30	Phosphorylation	31 (1)	M ⇒ T	rs721917	Chronic obstructive pulmonary disease	28166215
33	Phosphorylation	31 (2)	M ⇒ T	rs721917	Chronic obstructive pulmonary disease	28166215
35	S-nitrosylation	31 (4)	M ⇒ T	rs721917	Chronic obstructive pulmonary disease	28166215
40	S-nitrosylation	31 (9)	M ⇒ T	rs721917	Chronic obstructive pulmonary disease	28166215

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PGS2_HUMAN	DCN	physical	12730206
DNJC2_HUMAN	DNAJC2	physical	26344197

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.