ANFB_HUMAN - dbPTM
ANFB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANFB_HUMAN
UniProt AC P16860
Protein Name Natriuretic peptides B
Gene Name NPPB
Organism Homo sapiens (Human).
Sequence Length 134
Subcellular Localization Secreted.
Protein Description Cardiac hormone which may function as a paracrine antifibrotic factor in the heart. Also plays a key role in cardiovascular homeostasis through natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. Specifically binds and stimulates the cGMP production of the NPR1 receptor. Binds the clearance receptor NPR3..
Protein Sequence MDPQTAPSRALLLLLFLHLAFLGGRSHPLGSPGSASDLETSGLQEQRNHLQGKLSELQVEQTSLEPLQESPRPTGVWKSREVATEGIRGHRKMVLYTLRAPRSPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH
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
36PhosphorylationLGSPGSASDLETSGL
CCCCCCHHHHHHCHH
44.41-
62O-linked_GlycosylationSELQVEQTSLEPLQE
HHHHHCCCCCCCCCC
23.0516750161
63O-linked_GlycosylationELQVEQTSLEPLQES
HHHHCCCCCCCCCCC
30.3516750161
70O-linked_GlycosylationSLEPLQESPRPTGVW
CCCCCCCCCCCCCCE
17.1616750161
74O-linked_GlycosylationLQESPRPTGVWKSRE
CCCCCCCCCCEECHH
45.7216750161
79O-linked_GlycosylationRPTGVWKSREVATEG
CCCCCEECHHHHCCC
20.2616750161
84O-linked_GlycosylationWKSREVATEGIRGHR
EECHHHHCCCCCCCC
39.6616750161
84PhosphorylationWKSREVATEGIRGHR
EECHHHHCCCCCCCC
39.66-
96PhosphorylationGHRKMVLYTLRAPRS
CCCEEEEEEEECCCC
7.7228258704
97O-linked_GlycosylationHRKMVLYTLRAPRSP
CCEEEEEEEECCCCC
12.9516750161
97PhosphorylationHRKMVLYTLRAPRSP
CCEEEEEEEECCCCC
12.9524719451
103PhosphorylationYTLRAPRSPKMVQGS
EEEECCCCCCCCCCC
28.01-

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 ANFB_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
97TGlycosylation

16750161
97TGlycosylation

16750161
97TGlycosylation

16750161

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
62O-linked Glycosylation72 (10)RH;Prs61761991
  • B-type natriuretic peptide to N-terminal pro B-type natriuretic peptide ratio
29237677
63O-linked Glycosylation72 (9)RH;Prs61761991
  • B-type natriuretic peptide to N-terminal pro B-type natriuretic peptide ratio
29237677
70O-linked Glycosylation72 (2)RH;Prs61761991
  • B-type natriuretic peptide to N-terminal pro B-type natriuretic peptide ratio
29237677
74O-linked Glycosylation72 (2)RH;Prs61761991
  • B-type natriuretic peptide to N-terminal pro B-type natriuretic peptide ratio
29237677
79O-linked Glycosylation72 (7)RH;Prs61761991
  • B-type natriuretic peptide to N-terminal pro B-type natriuretic peptide ratio
29237677

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HDAC4_HUMANHDAC4physical
21464227
ANPRC_HUMANNPR3physical
16870210
PSA3_HUMANPSMA3physical
25416956
K1C40_HUMANKRT40physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956

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.
Regulatory Network of ANFB_HUMAN

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Related Literatures of Post-Translational Modification
O-linked Glycosylation
ReferencePubMed
"The precursor to B-type natriuretic peptide is an O-linkedglycoprotein.";
Schellenberger U., O'Rear J., Guzzetta A., Jue R.A., Protter A.A.,Pollitt N.S.;
Arch. Biochem. Biophys. 451:160-166(2006).
Cited for: GLYCOSYLATION AT THR-62; SER-63; SER-70; THR-74; SER-79; THR-84 ANDTHR-97.

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