POSTN_HUMAN - dbPTM
POSTN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID POSTN_HUMAN
UniProt AC Q15063
Protein Name Periostin
Gene Name POSTN
Organism Homo sapiens (Human).
Sequence Length 836
Subcellular Localization Golgi apparatus . Secreted . Secreted, extracellular space, extracellular matrix . Colocalizes with BMP1 in the Golgi.
Protein Description Induces cell attachment and spreading and plays a role in cell adhesion. [PubMed: 12235007 Enhances incorporation of BMP1 in the fibronectin matrix of connective tissues, and subsequent proteolytic activation of lysyl oxidase LOX (By similarity]
Protein Sequence MIPFLPMFSLLLLLIVNPINANNHYDKILAHSRIRGRDQGPNVCALQQILGTKKKYFSTCKNWYKKSICGQKTTVLYECCPGYMRMEGMKGCPAVLPIDHVYGTLGIVGATTTQRYSDASKLREEIEGKGSFTYFAPSNEAWDNLDSDIRRGLESNVNVELLNALHSHMINKRMLTKDLKNGMIIPSMYNNLGLFINHYPNGVVTVNCARIIHGNQIATNGVVHVIDRVLTQIGTSIQDFIEAEDDLSSFRAAAITSDILEALGRDGHFTLFAPTNEAFEKLPRGVLERIMGDKVASEALMKYHILNTLQCSESIMGGAVFETLEGNTIEIGCDGDSITVNGIKMVNKKDIVTNNGVIHLIDQVLIPDSAKQVIELAGKQQTTFTDLVAQLGLASALRPDGEYTLLAPVNNAFSDDTLSMDQRLLKLILQNHILKVKVGLNELYNGQILETIGGKQLRVFVYRTAVCIENSCMEKGSKQGRNGAIHIFREIIKPAEKSLHEKLKQDKRFSTFLSLLEAADLKELLTQPGDWTLFVPTNDAFKGMTSEEKEILIRDKNALQNIILYHLTPGVFIGKGFEPGVTNILKTTQGSKIFLKEVNDTLLVNELKSKESDIMTTNGVIHVVDKLLYPADTPVGNDQLLEILNKLIKYIQIKFVRGSTFKEIPVTVYTTKIITKVVEPKIKVIEGSLQPIIKTEGPTLTKVKIEGEPEFRLIKEGETITEVIHGEPIIKKYTKIIDGVPVEITEKETREERIITGPEIKYTRISTGGGETEETLKKLLQEEVTKVTKFIEGGDGHLFEDEEIKRLLQGDTPVRKLQANKKVQGSRRRLREGRSQ
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
25PhosphorylationPINANNHYDKILAHS
CCCCCCCHHHHHHHC
22.5125348772
56PhosphorylationILGTKKKYFSTCKNW
HHCCCHHHHHHCCHH
16.1929083192
58PhosphorylationGTKKKYFSTCKNWYK
CCCHHHHHHCCHHHH
29.7929083192
59PhosphorylationTKKKYFSTCKNWYKK
CCHHHHHHCCHHHHH
20.0129083192
83PhosphorylationLYECCPGYMRMEGMK
EEEECCCCHHCCCCC
2.69-
189PhosphorylationGMIIPSMYNNLGLFI
CCCCCHHCCCCCCEE
12.7722817900
256O-linked_GlycosylationSFRAAAITSDILEAL
HHHHHHHHHHHHHHH
18.67OGP
353PhosphorylationVNKKDIVTNNGVIHL
ECHHHHCCCCCCEEE
24.2522210691
369PhosphorylationDQVLIPDSAKQVIEL
EEEECCCCHHHHHHH
31.8222210691
498PhosphorylationIIKPAEKSLHEKLKQ
HHHHHHHHHHHHHHH
26.85-
510PhosphorylationLKQDKRFSTFLSLLE
HHHHHHHHHHHHHHH
23.4527251275
511PhosphorylationKQDKRFSTFLSLLEA
HHHHHHHHHHHHHHH
26.3627251275
545PhosphorylationNDAFKGMTSEEKEIL
CCHHCCCCHHHHEEE
41.47-
546PhosphorylationDAFKGMTSEEKEILI
CHHCCCCHHHHEEEE
34.56-
556AcetylationKEILIRDKNALQNII
HEEEECCCHHHHHHH
33.987826023
582PhosphorylationKGFEPGVTNILKTTQ
CCCCCCCCEEEHHCC
23.5827251275
599N-linked_GlycosylationKIFLKEVNDTLLVNE
EEEEEECCCEEEHHC
37.3316335952
616PhosphorylationSKESDIMTTNGVIHV
CCCCCCEECCCCEEE
19.90-
660PhosphorylationIKFVRGSTFKEIPVT
EEECCCCCCCCCCEE
41.36-
670PhosphorylationEIPVTVYTTKIITKV
CCCEEEEECCEEEHH
19.78-
675PhosphorylationVYTTKIITKVVEPKI
EEECCEEEHHHCCCE
22.66-
766PhosphorylationEIKYTRISTGGGETE
CEEEEEECCCCCCHH
20.0822985185
767PhosphorylationIKYTRISTGGGETEE
EEEEEECCCCCCHHH
37.1622985185
772PhosphorylationISTGGGETEETLKKL
ECCCCCCHHHHHHHH
42.2528857561
775PhosphorylationGGGETEETLKKLLQE
CCCCHHHHHHHHHHH
37.3328857561

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 POSTN_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of POSTN_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 POSTN_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MKS1_HUMANMKS1physical
27173435
B9D1_HUMANB9D1physical
27173435

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 POSTN_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-599, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-599, AND MASSSPECTROMETRY.
"Osteoblast-specific factor 2: cloning of a putative bone adhesionprotein with homology with the insect protein fasciclin I.";
Takeshita S., Kikuno R., Tezuka K., Amann E.;
Biochem. J. 294:271-278(1993).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).

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