PRG2_HUMAN - dbPTM
PRG2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRG2_HUMAN
UniProt AC P13727
Protein Name Bone marrow proteoglycan
Gene Name PRG2
Organism Homo sapiens (Human).
Sequence Length 222
Subcellular Localization Bone marrow proteoglycan: Secreted. The proform is secreted.
Eosinophil granule major basic protein: Cytoplasmic vesicle, secretory vesicle. The proform is secreted. The mature protein is found in the matrix of the eosinophil's large specific g
Protein Description Cytotoxin and helminthotoxin. Also induces non-cytolytic histamine release from human basophils. Involved in antiparasitic defense mechanisms and immune hypersensitivity reactions. The proform acts as a proteinase inhibitor, reducing the activity of PAPPA..
Protein Sequence MKLPLLLALLFGAVSALHLRSETSTFETPLGAKTLPEDEETPEQEMEETPCRELEEEEEWGSGSEDASKKDGAVESISVPDMVDKNLTCPEEEDTVKVVGIPGCQTCRYLLVRSLQTFSQAWFTCRRCYRGNLVSIHNFNINYRIQCSVSALNQGQVWIGGRITGSGRCRRFQWVDGSRWNFAYWAAHQPWSRGGHCVALCTRGGHWRRAHCLRRLPFICSY
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
23O-linked_GlycosylationALHLRSETSTFETPL
HHHHCCCCCCCCCCC		34.027524900
24O-linked_GlycosylationLHLRSETSTFETPLG
HHHCCCCCCCCCCCC		27.357524900
25O-linked_GlycosylationHLRSETSTFETPLGA
HHCCCCCCCCCCCCC		32.677524900
34O-linked_GlycosylationETPLGAKTLPEDEET
CCCCCCCCCCCCCCC		47.197524900
62O-linked_GlycosylationEEEEEWGSGSEDASK
HHHHHHCCCCCCHHH		39.978507662
86N-linked_GlycosylationVPDMVDKNLTCPEEE
CCCCCCCCCCCCCCC		35.808507662
109 (in isoform 2)Phosphorylation-13.4122617229
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 PRG2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRG2_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 PRG2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBM48_HUMANRBM48physical
16169070
CHD3_HUMANCHD3physical
16169070
TBB3_HUMANTUBB3physical
26186194
TBB8_HUMANTUBB8physical
26186194
TBB1_HUMANTUBB1physical
26186194
WDR26_HUMANWDR26physical
26186194
1A02_HUMANHLA-Aphysical
26186194
1A03_HUMANHLA-Aphysical
26186194
1A01_HUMANHLA-Aphysical
26186194
1A26_HUMANHLA-Aphysical
26186194
N42L2_HUMANN4BP2L2physical
26186194
ZN460_HUMANZNF460physical
26186194
GASP2_HUMANGPRASP2physical
26186194
ACTA_HUMANACTA2physical
26186194
POTEE_HUMANPOTEEphysical
26186194
PP6R2_HUMANPPP6R2physical
26186194
ARMC8_HUMANARMC8physical
26186194
PATZ1_HUMANPATZ1physical
26186194
MKLN1_HUMANMKLN1physical
26186194
ATS1_HUMANADAMTS1physical
26186194
MFR1L_HUMANMTFR1Lphysical
26186194
DICER_HUMANDICER1physical
26186194
MAEA_HUMANMAEAphysical
26186194
TBA4A_HUMANTUBA4Aphysical
26186194
TBA1A_HUMANTUBA1Aphysical
26186194
RBP10_HUMANRANBP10physical
26186194
RANB9_HUMANRANBP9physical
26186194
RMD5A_HUMANRMND5Aphysical
26186194
PASK_HUMANPASKphysical
26186194
SC65_HUMANP3H4physical
26186194
CO6A2_HUMANCOL6A2physical
26186194
FBN2_HUMANFBN2physical
26186194
PP6R1_HUMANPPP6R1physical
26186194
GID4_HUMANGID4physical
26186194
TOR3A_HUMANTOR3Aphysical
26186194
PKHG4_HUMANPLEKHG4physical
26186194
DUS11_HUMANDUSP11physical
26186194
ZMYM3_HUMANZMYM3physical
26186194
FOXF2_HUMANFOXF2physical
26186194
GID8_HUMANGID8physical
26186194
VWDE_HUMANVWDEphysical
26186194
ERGI2_HUMANERGIC2physical
26186194
ZMY19_HUMANZMYND19physical
26186194
FUT11_HUMANFUT11physical
26186194
YPEL5_HUMANYPEL5physical
26186194
TP4AP_HUMANTRPC4APphysical
26186194
MELK_HUMANMELKphysical
26186194
LDLR_HUMANLDLRphysical
26186194
DVL2_HUMANDVL2physical
26186194
PHLB3_HUMANPHLDB3physical
26186194
SELN_HUMANSEPN1physical
26186194
SI1L2_HUMANSIPA1L2physical
26186194
THUM3_HUMANTHUMPD3physical
26186194
ZSWM8_HUMANZSWIM8physical
26186194
JMJD4_HUMANJMJD4physical
26186194
ZN589_HUMANZNF589physical
26186194
ATS2_HUMANADAMTS2physical
26186194
GCP6_HUMANTUBGCP6physical
26186194
POTEE_HUMANPOTEEphysical
28514442
TBB1_HUMANTUBB1physical
28514442
FOXF2_HUMANFOXF2physical
28514442
VWDE_HUMANVWDEphysical
28514442
FUT11_HUMANFUT11physical
28514442
SI1L2_HUMANSIPA1L2physical
28514442
DVL2_HUMANDVL2physical
28514442
TOR3A_HUMANTOR3Aphysical
28514442
N42L2_HUMANN4BP2L2physical
28514442
ZMY19_HUMANZMYND19physical
28514442
ARMC8_HUMANARMC8physical
28514442
ZN460_HUMANZNF460physical
28514442
TP4AP_HUMANTRPC4APphysical
28514442
WDR26_HUMANWDR26physical
28514442
PASK_HUMANPASKphysical
28514442
ZN589_HUMANZNF589physical
28514442
RBP10_HUMANRANBP10physical
28514442
MFR1L_HUMANMTFR1Lphysical
28514442
GASP2_HUMANGPRASP2physical
28514442
ZSWM8_HUMANZSWIM8physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
MKLN1_HUMANMKLN1physical
28514442
FOXF1_HUMANFOXF1physical
28514442
DICER_HUMANDICER1physical
28514442
RMD5A_HUMANRMND5Aphysical
28514442
JMJD4_HUMANJMJD4physical
28514442
GID4_HUMANGID4physical
28514442
ATS1_HUMANADAMTS1physical
28514442
MAEA_HUMANMAEAphysical
28514442
LDLR_HUMANLDLRphysical
28514442
YPEL5_HUMANYPEL5physical
28514442
GID8_HUMANGID8physical
28514442
ALG13_HUMANALG13physical
28514442
ATS2_HUMANADAMTS2physical
28514442
SELN_HUMANSEPN1physical
28514442
RANB9_HUMANRANBP9physical
28514442
PP6R1_HUMANPPP6R1physical
28514442
GALNS_HUMANGALNSphysical
28514442
PCSK5_HUMANPCSK5physical
28514442
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 PRG2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Location and nature of carbohydrate groups in proform of human majorbasic protein isolated from pregnancy serum.";
Oxvig C., Haaning J., Hojrup P., Sottrup-Jensen L.;
Biochem. Mol. Biol. Int. 33:329-336(1994).
Cited for: GLYCOSYLATION AT THR-23; SER-24; THR-25; THR-34; SER-62 AND ASN-86.
"Pro-major basic protein has three types of sugar chains at the pro-portion.";
Shikata Y., Hayashi Y., Yoshimatsu K., Ohya Y., Seto T., Fukushima K.,Yoshida Y.;
Biochim. Biophys. Acta 1163:243-249(1993).
Cited for: PROTEIN SEQUENCE OF 17-222, AND GLYCOSYLATION AT SER-24; THR-25;SER-62 AND ASN-86.
O-linked Glycosylation
ReferencePubMed
"Location and nature of carbohydrate groups in proform of human majorbasic protein isolated from pregnancy serum.";
Oxvig C., Haaning J., Hojrup P., Sottrup-Jensen L.;
Biochem. Mol. Biol. Int. 33:329-336(1994).
Cited for: GLYCOSYLATION AT THR-23; SER-24; THR-25; THR-34; SER-62 AND ASN-86.
"Pro-major basic protein has three types of sugar chains at the pro-portion.";
Shikata Y., Hayashi Y., Yoshimatsu K., Ohya Y., Seto T., Fukushima K.,Yoshida Y.;
Biochim. Biophys. Acta 1163:243-249(1993).
Cited for: PROTEIN SEQUENCE OF 17-222, AND GLYCOSYLATION AT SER-24; THR-25;SER-62 AND ASN-86.

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