GRN_HUMAN - dbPTM
GRN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRN_HUMAN
UniProt AC P28799
Protein Name Granulins
Gene Name GRN
Organism Homo sapiens (Human).
Sequence Length 593
Subcellular Localization Secreted.
Protein Description Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling.; Granulin-4 promotes proliferation of the epithelial cell line A431 in culture while granulin-3 acts as an antagonist to granulin-4, inhibiting the growth..
Protein Sequence MWTLVSWVALTAGLVAGTRCPDGQFCPVACCLDPGGASYSCCRPLLDKWPTTLSRHLGGPCQVDAHCSAGHSCIFTVSGTSSCCPFPEAVACGDGHHCCPRGFHCSADGRSCFQRSGNNSVGAIQCPDSQFECPDFSTCCVMVDGSWGCCPMPQASCCEDRVHCCPHGAFCDLVHTRCITPTGTHPLAKKLPAQRTNRAVALSSSVMCPDARSRCPDGSTCCELPSGKYGCCPMPNATCCSDHLHCCPQDTVCDLIQSKCLSKENATTDLLTKLPAHTVGDVKCDMEVSCPDGYTCCRLQSGAWGCCPFTQAVCCEDHIHCCPAGFTCDTQKGTCEQGPHQVPWMEKAPAHLSLPDPQALKRDVPCDNVSSCPSSDTCCQLTSGEWGCCPIPEAVCCSDHQHCCPQGYTCVAEGQCQRGSEIVAGLEKMPARRASLSHPRDIGCDQHTSCPVGQTCCPSLGGSWACCQLPHAVCCEDRQHCCPAGYTCNVKARSCEKEVVSAQPATFLARSPHVGVKDVECGEGHFCHDNQTCCRDNRQGWACCPYRQGVCCADRRHCCPAGFRCAARGTKCLRREAPRWDAPLRDPALRQLL
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
3Phosphorylation-----MWTLVSWVAL
-----CCCHHHHHHH		18.9120068231
6Phosphorylation--MWTLVSWVALTAG
--CCCHHHHHHHHHH		20.9520068231
11PhosphorylationLVSWVALTAGLVAGT
HHHHHHHHHHHHCCC		14.6720068231
18PhosphorylationTAGLVAGTRCPDGQF
HHHHHCCCCCCCCCE		21.2520068231
81PhosphorylationIFTVSGTSSCCPFPE
EEEECCCCCCCCCCC		25.55-
118N-linked_GlycosylationSCFQRSGNNSVGAIQ
CCEECCCCCCCCEEE		38.5620188224
180O-linked_GlycosylationLVHTRCITPTGTHPL
EEECEECCCCCCCCH		20.58OGP
180PhosphorylationLVHTRCITPTGTHPL
EEECEECCCCCCCCH		20.5821712546
182PhosphorylationHTRCITPTGTHPLAK
ECEECCCCCCCCHHH		46.1721712546
182O-linked_GlycosylationHTRCITPTGTHPLAK
ECEECCCCCCCCHHH		46.1763775991
184PhosphorylationRCITPTGTHPLAKKL
EECCCCCCCCHHHHC		23.8521712546
196PhosphorylationKKLPAQRTNRAVALS
HHCCCCCCCCHHHHH		19.5825690035
205PhosphorylationRAVALSSSVMCPDAR
CHHHHHCCCCCCCHH		15.5324670416
226PhosphorylationSTCCELPSGKYGCCP
CCEEECCCCCCCCCC		61.6224719451
236N-linked_GlycosylationYGCCPMPNATCCSDH
CCCCCCCCCCEECCC		41.45UniProtKB CARBOHYD
265N-linked_GlycosylationSKCLSKENATTDLLT
HHHCCCCCCCHHHHH		46.4520188224
273UbiquitinationATTDLLTKLPAHTVG
CCHHHHHHCCCCCCC		53.0629967540
286SulfoxidationVGDVKCDMEVSCPDG
CCCEECCEEEECCCC		8.4228465586
295PhosphorylationVSCPDGYTCCRLQSG
EECCCCCEEEEECCC		15.62-
347AcetylationHQVPWMEKAPAHLSL
CCCCCCCCCCCCCCC		43.4927452117
368N-linked_GlycosylationKRDVPCDNVSSCPSS
CCCCCCCCCCCCCCC		42.1420188224
435PhosphorylationKMPARRASLSHPRDI
HCCCHHHHCCCCCCC		28.7022985185
437PhosphorylationPARRASLSHPRDIGC
CCHHHHCCCCCCCCC		29.0228102081
497UbiquitinationVKARSCEKEVVSAQP
EECCCCCCEEEECCC		61.2029901268
501PhosphorylationSCEKEVVSAQPATFL
CCCCEEEECCCCEEE		26.7720068231
530N-linked_GlycosylationEGHFCHDNQTCCRDN
CCCEECCCCEEECCC		18.5220188224
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
81SPhosphorylationKinasePRKCBP05771
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GRN_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 GRN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
F131C_HUMANFAM131Cphysical
16189514
HXA1_HUMANHOXA1physical
16189514
CCNT1_HUMANCCNT1physical
12588988
CDK9_HUMANCDK9physical
12588988
ATTY_HUMANTATphysical
12588988
TRIB3_HUMANTRIB3physical
18276110
TGM2_HUMANTGM2physical
21988832
K1C18_HUMANKRT18physical
21988832
RAC1_HUMANRAC1physical
21988832
P85B_HUMANPIK3R2physical
21988832
AAKB2_HUMANPRKAB2physical
21988832
TYY1_HUMANYY1physical
21988832
POTE1_HUMANPOT1physical
21988832
HXK3_RATHk3physical
11068878
HXA1_HUMANHOXA1physical
25416956
OTX1_HUMANOTX1physical
25416956
SGTA_HUMANSGTAphysical
25416956
GLRX3_HUMANGLRX3physical
25416956
NLK_HUMANNLKphysical
25416956
FANCL_HUMANFANCLphysical
25416956
ARFG1_HUMANARFGAP1physical
25416956
CCD33_HUMANCCDC33physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR261_HUMANKRTAP26-1physical
25416956
PKP2_HUMANPKP2physical
26186194
GBB2_HUMANGNB2physical
26186194
FWCH2_HUMANFLYWCH2physical
26186194
F207A_HUMANFAM207Aphysical
26186194
SAHH3_HUMANAHCYL2physical
26186194
PP2AA_HUMANPPP2CAphysical
26186194
NIPA_HUMANZC3HC1physical
26186194
DCP1B_HUMANDCP1Bphysical
26186194
CX6B1_HUMANCOX6B1physical
26186194
TLE3_HUMANTLE3physical
26186194
EGFL7_HUMANEGFL7physical
26186194
OTUD5_HUMANOTUD5physical
26186194
OTUD5_HUMANOTUD5physical
28514442
NIPA_HUMANZC3HC1physical
28514442
PKP2_HUMANPKP2physical
28514442
GBB2_HUMANGNB2physical
28514442
DCP1B_HUMANDCP1Bphysical
28514442
RPGF6_HUMANRAPGEF6physical
28514442
FWCH2_HUMANFLYWCH2physical
28514442
EGFL7_HUMANEGFL7physical
28514442
EDC3_HUMANEDC3physical
28514442
SAHH3_HUMANAHCYL2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
607485Ubiquitin-positive frontotemporal dementia (UP-FTD)
614706Ceroid lipofuscinosis, neuronal, 11 (CLN11)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GRN_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-265, AND MASSSPECTROMETRY.

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