SFTA1_HUMAN - dbPTM
SFTA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SFTA1_HUMAN
UniProt AC Q8IWL2
Protein Name Pulmonary surfactant-associated protein A1
Gene Name SFTPA1
Organism Homo sapiens (Human).
Sequence Length 248
Subcellular Localization Secreted, extracellular space, extracellular matrix. Secreted, extracellular space, surface film.
Protein Description In presence of calcium ions, it binds to surfactant phospholipids and contributes to lower the surface tension at the air-liquid interface in the alveoli of the mammalian lung and is essential for normal respiration. Enhances the expression of MYO18A/SP-R210 on alveolar macrophages (By similarity).; (Microbial infection) Recognition of M.tuberculosis by dendritic cells may occur partially via this molecule. [PubMed: 17158455]
Protein Sequence MWLCPLALNLILMAASGAVCEVKDVCVGSPGIPGTPGSHGLPGRDGRDGLKGDPGPPGPMGPPGEMPCPPGNDGLPGAPGIPGECGEKGEPGERGPPGLPAHLDEELQATLHDFRHQILQTRGALSLQGSIMTVGEKVFSSNGQSITFDAIQEACARAGGRIAVPRNPEENEAIASFVKKYNTYAYVGLTEGPSPGDFRYSDGTPVNYTNWYRGEPAGRGKEQCVEMYTDGQWNDRNCLYSRLTICEF
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 Orthologous
Protein Cluster
21AcetylationAASGAVCEVKDVCVG
HHCCCEEEEEEEECC
46.10-
30HydroxylationKDVCVGSPGIPGTPG
EEEECCCCCCCCCCC
38.51-
33HydroxylationCVGSPGIPGTPGSHG
ECCCCCCCCCCCCCC
46.66-
36HydroxylationSPGIPGTPGSHGLPG
CCCCCCCCCCCCCCC
48.48-
42HydroxylationTPGSHGLPGRDGRDG
CCCCCCCCCCCCCCC
40.12-
51UbiquitinationRDGRDGLKGDPGPPG
CCCCCCCCCCCCCCC
67.79-
54HydroxylationRDGLKGDPGPPGPMG
CCCCCCCCCCCCCCC
66.90-
57HydroxylationLKGDPGPPGPMGPPG
CCCCCCCCCCCCCCC
66.49-
63HydroxylationPPGPMGPPGEMPCPP
CCCCCCCCCCCCCCC
45.72-
67HydroxylationMGPPGEMPCPPGNDG
CCCCCCCCCCCCCCC
24.14-
70HydroxylationPGEMPCPPGNDGLPG
CCCCCCCCCCCCCCC
62.02-
121PhosphorylationFRHQILQTRGALSLQ
HHHHHHHHCCCHHCC
27.8529888752
126PhosphorylationLQTRGALSLQGSIMT
HHHCCCHHCCCCEEE
20.3629888752
130PhosphorylationGALSLQGSIMTVGEK
CCHHCCCCEEEECCE
9.0229396449
181NitrationIASFVKKYNTYAYVG
HHHHHHHHCCEEEEE
13.66-
184NitrationFVKKYNTYAYVGLTE
HHHHHCCEEEEECCC
7.72-
184PhosphorylationFVKKYNTYAYVGLTE
HHHHHCCEEEEECCC
7.72-
186NitrationKKYNTYAYVGLTEGP
HHHCCEEEEECCCCC
5.66-
207N-linked_GlycosylationYSDGTPVNYTNWYRG
CCCCCCCCCCCCCCC
38.83UniProtKB CARBOHYD
240NitrationWNDRNCLYSRLTICE
CCCCCCHHCCEEEEE
8.24-
241PhosphorylationNDRNCLYSRLTICEF
CCCCCHHCCEEEEEC
14.0924719451

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 SFTA1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SFTA1_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 SFTA1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SFTPD_HUMANSFTPDphysical
10101009
DMBT1_HUMANDMBT1physical
10101009
SFTA1_HUMANSFTPA1physical
16330552
PRDX6_HUMANPRDX6physical
16330552

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
178500Pulmonary fibrosis, idiopathic (IPF)
267450Respiratory distress syndrome in premature infants (RDS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SFTA1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Isolation and characterization of cDNA clones for the 35-kDapulmonary surfactant-associated protein.";
Floros J., Steinbrink R., Jacobs K., Phelps D., Kriz R., Recny M.,Sultzman L., Jones S., Taeusch H.W., Frank H.A., Fritsch E.F.;
J. Biol. Chem. 261:9029-9033(1986).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-19, AND ACETYLATION AT GLU-21.

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