LG3BP_HUMAN - dbPTM
LG3BP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LG3BP_HUMAN
UniProt AC Q08380
Protein Name Galectin-3-binding protein
Gene Name LGALS3BP
Organism Homo sapiens (Human).
Sequence Length 585
Subcellular Localization Secreted . Secreted, extracellular space, extracellular matrix .
Protein Description Promotes integrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells..
Protein Sequence MTPPRLFWVWLLVAGTQGVNDGDMRLADGGATNQGRVEIFYRGQWGTVCDNLWDLTDASVVCRALGFENATQALGRAAFGQGSGPIMLDEVQCTGTEASLADCKSLGWLKSNCRHERDAGVVCTNETRSTHTLDLSRELSEALGQIFDSQRGCDLSISVNVQGEDALGFCGHTVILTANLEAQALWKEPGSNVTMSVDAECVPMVRDLLRYFYSRRIDITLSSVKCFHKLASAYGARQLQGYCASLFAILLPQDPSFQMPLDLYAYAVATGDALLEKLCLQFLAWNFEALTQAEAWPSVPTDLLQLLLPRSDLAVPSELALLKAVDTWSWGERASHEEVEGLVEKIRFPMMLPEELFELQFNLSLYWSHEALFQKKTLQALEFHTVPFQLLARYKGLNLTEDTYKPRIYTSPTWSAFVTDSSWSARKSQLVYQSRRGPLVKYSSDYFQAPSDYRYYPYQSFQTPQHPSFLFQDKRVSWSLVYLPTIQSCWNYGFSCSSDELPVLGLTKSGGSDRTIAYENKALMLCEGLFVADVTDFEGWKAAIPSALDTNSSKSTSSFPCPAGHFNGFRTVIRPFYLTNSSGVD
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
41PhosphorylationQGRVEIFYRGQWGTV
CCEEEEEECCCCCCC
21.35-
69N-linked_GlycosylationCRALGFENATQALGR
HHHCCCCCHHHHHHH
46.1315084671
69N-linked_GlycosylationCRALGFENATQALGR
HHHCCCCCHHHHHHH
46.1315084671
110UbiquitinationCKSLGWLKSNCRHER
HHHHCHHHHHCCCCC
32.87-
125N-linked_GlycosylationDAGVVCTNETRSTHT
CCCEEECCCCCCCCC
43.4417623646
125N-linked_GlycosylationDAGVVCTNETRSTHT
CCCEEECCCCCCCCC
43.4416335952
136PhosphorylationSTHTLDLSRELSEAL
CCCCHHHHHHHHHHH
24.3129759185
192N-linked_GlycosylationLWKEPGSNVTMSVDA
HHCCCCCCEEEEECC
38.9117623646
192N-linked_GlycosylationLWKEPGSNVTMSVDA
HHCCCCCCEEEEECC
38.9116335952
220PhosphorylationYSRRIDITLSSVKCF
HHHCCCEEHHHHHHH
19.4820068231
229UbiquitinationSSVKCFHKLASAYGA
HHHHHHHHHHHHHCH
26.04-
256PhosphorylationILLPQDPSFQMPLDL
HHCCCCCCCCCCHHH
36.08-
323UbiquitinationPSELALLKAVDTWSW
CCHHHHHHHHHHCCC
47.41-
345UbiquitinationEVEGLVEKIRFPMML
HHHHHHHHHCCCCCC
31.53-
3452-HydroxyisobutyrylationEVEGLVEKIRFPMML
HHHHHHHHHCCCCCC
31.53-
362N-linked_GlycosylationELFELQFNLSLYWSH
HHHHCHHHHHHEECH
18.76UniProtKB CARBOHYD
376UbiquitinationHEALFQKKTLQALEF
HHHHHCCHHHHHHHH
43.62-
395UbiquitinationFQLLARYKGLNLTED
HHHHHHHCCCCCCCC
51.90-
398N-linked_GlycosylationLARYKGLNLTEDTYK
HHHHCCCCCCCCCCC
54.2917623646
398N-linked_GlycosylationLARYKGLNLTEDTYK
HHHHCCCCCCCCCCC
54.2917623646
405UbiquitinationNLTEDTYKPRIYTSP
CCCCCCCCCCEECCC
29.88-
411PhosphorylationYKPRIYTSPTWSAFV
CCCCEECCCCCEEEE
11.89-
413O-linked_GlycosylationPRIYTSPTWSAFVTD
CCEECCCCCEEEECC
31.64OGP
413PhosphorylationPRIYTSPTWSAFVTD
CCEECCCCCEEEECC
31.64-
415PhosphorylationIYTSPTWSAFVTDSS
EECCCCCEEEECCCC
17.82-
427UbiquitinationDSSWSARKSQLVYQS
CCCHHHCHHHHHEEE
42.12-
428PhosphorylationSSWSARKSQLVYQSR
CCHHHCHHHHHEEEC
24.1620639409
432PhosphorylationARKSQLVYQSRRGPL
HCHHHHHEEECCCCC
14.90-
434PhosphorylationKSQLVYQSRRGPLVK
HHHHHEEECCCCCEE
13.2720639409
441AcetylationSRRGPLVKYSSDYFQ
ECCCCCEECCCCCCC
47.2826051181
441UbiquitinationSRRGPLVKYSSDYFQ
ECCCCCEECCCCCCC
47.2821890473
442PhosphorylationRRGPLVKYSSDYFQA
CCCCCEECCCCCCCC
13.1120639409
443PhosphorylationRGPLVKYSSDYFQAP
CCCCEECCCCCCCCC
15.8325884760
443O-linked_GlycosylationRGPLVKYSSDYFQAP
CCCCEECCCCCCCCC
15.83OGP
444PhosphorylationGPLVKYSSDYFQAPS
CCCEECCCCCCCCCC
32.9926657352
444O-linked_GlycosylationGPLVKYSSDYFQAPS
CCCEECCCCCCCCCC
32.9955817675
446PhosphorylationLVKYSSDYFQAPSDY
CEECCCCCCCCCCCC
10.2720639409
451O-linked_GlycosylationSDYFQAPSDYRYYPY
CCCCCCCCCCCCCCC
50.74OGP
451PhosphorylationSDYFQAPSDYRYYPY
CCCCCCCCCCCCCCC
50.7420639409
453PhosphorylationYFQAPSDYRYYPYQS
CCCCCCCCCCCCCCC
12.5920639409
458PhosphorylationSDYRYYPYQSFQTPQ
CCCCCCCCCCCCCCC
10.73-
463PhosphorylationYPYQSFQTPQHPSFL
CCCCCCCCCCCCCCC
23.94-
474UbiquitinationPSFLFQDKRVSWSLV
CCCCCCCCCCEEEEE
43.8721890473
550O-linked_GlycosylationAIPSALDTNSSKSTS
HCCCCCCCCCCCCCC
37.5423301498
551N-linked_GlycosylationIPSALDTNSSKSTSS
CCCCCCCCCCCCCCC
43.9118638581
551N-linked_GlycosylationIPSALDTNSSKSTSS
CCCCCCCCCCCCCCC
43.9118780401
554UbiquitinationALDTNSSKSTSSFPC
CCCCCCCCCCCCCCC
58.54-
580N-linked_GlycosylationIRPFYLTNSSGVD--
EEEEECCCCCCCC--
31.4216740002

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 LG3BP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LG3BP_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 LG3BP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LEG1_HUMANLGALS1physical
11146440
LEG3_HUMANLGALS3physical
11146440
CD9_HUMANCD9physical
20581239
CD82_HUMANCD82physical
20581239
LEG3_HUMANLGALS3physical
16518858
LYAM2_HUMANSELEphysical
22970241
ACTB_HUMANACTBphysical
23443559
BAG2_HUMANBAG2physical
23443559
PRC2C_HUMANPRRC2Cphysical
23443559
TCPB_HUMANCCT2physical
23443559
TCPG_HUMANCCT3physical
23443559
TCPD_HUMANCCT4physical
23443559
TCPE_HUMANCCT5physical
23443559
TCPZ_HUMANCCT6Aphysical
23443559
TCPH_HUMANCCT7physical
23443559
TCPQ_HUMANCCT8physical
23443559
CEP55_HUMANCEP55physical
23443559
CRTC2_HUMANCRTC2physical
23443559
TBB5_HUMANTUBBphysical
23443559
ENAH_HUMANENAHphysical
23443559
TRAP1_HUMANTRAP1physical
23443559
RL23_HUMANRPL23physical
23443559
MOGS_HUMANMOGSphysical
23443559
GGYF2_HUMANGIGYF2physical
23443559
HNRPU_HUMANHNRNPUphysical
23443559
HS90A_HUMANHSP90AA1physical
23443559
HS90B_HUMANHSP90AB1physical
23443559
GRP78_HUMANHSPA5physical
23443559
HSP7C_HUMANHSPA8physical
23443559
CH60_HUMANHSPD1physical
23443559
IRS4_HUMANIRS4physical
23443559
MAGD2_HUMANMAGED2physical
23443559
RAVR1_HUMANRAVER1physical
23443559
RL38_HUMANRPL38physical
23443559
RS4X_HUMANRPS4Xphysical
23443559
TCPA_HUMANTCP1physical
23443559
TBA1A_HUMANTUBA1Aphysical
23443559
TBA1C_HUMANTUBA1Cphysical
23443559
TBB4B_HUMANTUBB4Bphysical
23443559
XRN2_HUMANXRN2physical
23443559
GCP3_HUMANTUBGCP3physical
23443559
LG3BP_HUMANLGALS3BPphysical
25320078
PYR1_HUMANCADphysical
26496610
NRDC_HUMANNRD1physical
26496610
SURF4_HUMANSURF4physical
26496610
TBG1_HUMANTUBG1physical
26496610
RAE1L_HUMANRAE1physical
26496610
SEP15_HUMANSEP15physical
26496610
MVP_HUMANMVPphysical
26496610
GCP3_HUMANTUBGCP3physical
26496610
GCP2_HUMANTUBGCP2physical
26496610
TEST_HUMANPRSS21physical
26496610
MYCB2_HUMANMYCBP2physical
26496610
ZC3H3_HUMANZC3H3physical
26496610
GANAB_HUMANGANABphysical
26496610
MYOF_HUMANMYOFphysical
26496610
NDK7_HUMANNME7physical
26496610
T161A_HUMANTMEM161Aphysical
26496610
NKRF_HUMANNKRFphysical
26496610
UGGG1_HUMANUGGT1physical
26496610
VCIP1_HUMANVCPIP1physical
26496610
CE290_HUMANCEP290physical
26496610
SPRY3_HUMANSPRYD3physical
26496610
GCP6_HUMANTUBGCP6physical
26496610
FBSP1_HUMANFBXO45physical
26496610
MZT2A_HUMANMZT2Aphysical
26496610
LEG3_HUMANLGALS3physical
26168351
LEG1_HUMANLGALS1physical
26168351
SPRY3_HUMANSPRYD3physical
28514442
DJC13_HUMANDNAJC13physical
28514442
HELZ2_HUMANHELZ2physical
28514442
MZT2A_HUMANMZT2Aphysical
28514442
MYCB2_HUMANMYCBP2physical
28514442
GLCNE_HUMANGNEphysical
28514442
FBSP1_HUMANFBXO45physical
28514442
FINC_HUMANFN1physical
28514442
GCP5_HUMANTUBGCP5physical
28514442
KIF7_HUMANKIF7physical
28514442
GCP6_HUMANTUBGCP6physical
28514442
FXR1_HUMANFXR1physical
28514442
KPBB_HUMANPHKBphysical
28514442
ACACA_HUMANACACAphysical
28514442
NEUL4_HUMANNEURL4physical
28514442
GCP3_HUMANTUBGCP3physical
28514442
GCP2_HUMANTUBGCP2physical
28514442
DPOE1_HUMANPOLEphysical
28514442
TPPC9_HUMANTRAPPC9physical
28514442
MIO_HUMANMIOSphysical
28514442
PPHLN_HUMANPPHLN1physical
28514442
GEPH_HUMANGPHNphysical
28514442
LENG8_HUMANLENG8physical
28514442
F120A_HUMANFAM120Aphysical
28514442
TBG1_HUMANTUBG1physical
28514442
RAE1L_HUMANRAE1physical
28514442
UBP54_HUMANUSP54physical
28514442
NKRF_HUMANNKRFphysical
28514442
N42L2_HUMANN4BP2L2physical
28514442
RGPD8_HUMANRGPD8physical
28514442
TYK2_HUMANTYK2physical
28514442
FA83H_HUMANFAM83Hphysical
28514442
CUL7_HUMANCUL7physical
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 LG3BP_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-69; ASN-125; ASN-192;ASN-398 AND ASN-551, AND MASS SPECTROMETRY.
"Identification of N-linked glycoproteins in human milk by hydrophilicinteraction liquid chromatography and mass spectrometry.";
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
Proteomics 8:3833-3847(2008).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69 AND ASN-551, AND MASSSPECTROMETRY.
"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry.";
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.;
J. Proteome Res. 5:1493-1503(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-398; ASN-551 ANDASN-580, AND MASS SPECTROMETRY.
"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-69; ASN-125; ASN-192;ASN-398; ASN-551 AND ASN-580, AND MASS SPECTROMETRY.
"A proteomic analysis of human bile.";
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
Mol. Cell. Proteomics 3:715-728(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69, AND MASS SPECTROMETRY.

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