BCAM_HUMAN - dbPTM
BCAM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BCAM_HUMAN
UniProt AC P50895
Protein Name Basal cell adhesion molecule
Gene Name BCAM
Organism Homo sapiens (Human).
Sequence Length 628
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Laminin alpha-5 receptor. May mediate intracellular signaling..
Protein Sequence MEPPDAPAQARGAPRLLLLAVLLAAHPDAQAEVRLSVPPLVEVMRGKSVILDCTPTGTHDHYMLEWFLTDRSGARPRLASAEMQGSELQVTMHDTRGRSPPYQLDSQGRLVLAEAQVGDERDYVCVVRAGAAGTAEATARLNVFAKPEATEVSPNKGTLSVMEDSAQEIATCNSRNGNPAPKITWYRNGQRLEVPVEMNPEGYMTSRTVREASGLLSLTSTLYLRLRKDDRDASFHCAAHYSLPEGRHGRLDSPTFHLTLHYPTEHVQFWVGSPSTPAGWVREGDTVQLLCRGDGSPSPEYTLFRLQDEQEEVLNVNLEGNLTLEGVTRGQSGTYGCRVEDYDAADDVQLSKTLELRVAYLDPLELSEGKVLSLPLNSSAVVNCSVHGLPTPALRWTKDSTPLGDGPMLSLSSITFDSNGTYVCEASLPTVPVLSRTQNFTLLVQGSPELKTAEIEPKADGSWREGDEVTLICSARGHPDPKLSWSQLGGSPAEPIPGRQGWVSSSLTLKVTSALSRDGISCEASNPHGNKRHVFHFGTVSPQTSQAGVAVMAVAVSVGLLLLVVAVFYCVRRKGGPCCRQRREKGAPPPGEPGLSHSGSEQPEQTGLLMGGASGGARGGSGGFGDEC
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
150O-linked_GlycosylationVFAKPEATEVSPNKG
EEECCCCEEECCCCC
34.95OGP
205PhosphorylationMNPEGYMTSRTVREA
ECCCCCEEHHHHHHH
13.43-
206PhosphorylationNPEGYMTSRTVREAS
CCCCCEEHHHHHHHH
14.93-
213PhosphorylationSRTVREASGLLSLTS
HHHHHHHHHHHHHEE
25.8124719451
223PhosphorylationLSLTSTLYLRLRKDD
HHHEEEEEEEECCCC
7.0024719451
296PhosphorylationLLCRGDGSPSPEYTL
EEECCCCCCCCCEEE
27.26-
301PhosphorylationDGSPSPEYTLFRLQD
CCCCCCCEEEEECCC
16.48-
302PhosphorylationGSPSPEYTLFRLQDE
CCCCCCEEEEECCCC
20.12-
321N-linked_GlycosylationLNVNLEGNLTLEGVT
ECEECCCCEEEEEEE
22.07UniProtKB CARBOHYD
332PhosphorylationEGVTRGQSGTYGCRV
EEEECCCCCCEEEEE
35.6129978859
334PhosphorylationVTRGQSGTYGCRVED
EECCCCCCEEEEEEC
23.2229978859
335PhosphorylationTRGQSGTYGCRVEDY
ECCCCCCEEEEEECC
20.1129978859
342PhosphorylationYGCRVEDYDAADDVQ
EEEEEECCCCCCCCC
8.2529978859
351PhosphorylationAADDVQLSKTLELRV
CCCCCCCCCEEEEEE
13.4029978859
353PhosphorylationDDVQLSKTLELRVAY
CCCCCCCEEEEEEEE
23.3029978859
360PhosphorylationTLELRVAYLDPLELS
EEEEEEEECCCEECC
14.58-
367PhosphorylationYLDPLELSEGKVLSL
ECCCEECCCCEEEEE
34.62-
377N-linked_GlycosylationKVLSLPLNSSAVVNC
EEEEEECCCCCEEEE
31.79UniProtKB CARBOHYD
383N-linked_GlycosylationLNSSAVVNCSVHGLP
CCCCCEEEEEECCCC
13.02UniProtKB CARBOHYD
419N-linked_GlycosylationSSITFDSNGTYVCEA
EEEEECCCCCEEEEE
48.98UniProtKB CARBOHYD
439N-linked_GlycosylationPVLSRTQNFTLLVQG
CEEECCCCEEEEECC
31.1212754519
447PhosphorylationFTLLVQGSPELKTAE
EEEEECCCCCCEEEE
9.7124719451
458UbiquitinationKTAEIEPKADGSWRE
EEEEEECCCCCCCCC
46.44-
486PhosphorylationPDPKLSWSQLGGSPA
CCCCCCHHHCCCCCC
16.49-
491O-linked_GlycosylationSWSQLGGSPAEPIPG
CHHHCCCCCCCCCCC
21.09OGP
505PhosphorylationGRQGWVSSSLTLKVT
CCCCCCCCCEEEEHH
21.5429457462
506PhosphorylationRQGWVSSSLTLKVTS
CCCCCCCCEEEEHHH
20.1924719451
541PhosphorylationVFHFGTVSPQTSQAG
EEEEECCCCCCCHHH
15.8920886841
585UbiquitinationCCRQRREKGAPPPGE
CHHHHHHCCCCCCCC
59.57-
596PhosphorylationPPGEPGLSHSGSEQP
CCCCCCCCCCCCCCH
22.8630266825
598PhosphorylationGEPGLSHSGSEQPEQ
CCCCCCCCCCCCHHH
40.4130266825
600PhosphorylationPGLSHSGSEQPEQTG
CCCCCCCCCCHHHCC
35.7530266825
606PhosphorylationGSEQPEQTGLLMGGA
CCCCHHHCCEECCCC
28.3030266825
614PhosphorylationGLLMGGASGGARGGS
CEECCCCCCCCCCCC
40.8223090842
621PhosphorylationSGGARGGSGGFGDEC
CCCCCCCCCCCCCCC
38.2730278072

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
596SPhosphorylationKinaseGSK3BP49841
PSP
596SPhosphorylationKinaseGSK-FAMILY-GPS
596SPhosphorylationKinaseGSK3-Uniprot
598SPhosphorylationKinaseCSNK2A1P68400
GPS
598SPhosphorylationKinaseCK2-FAMILY-GPS
598SPhosphorylationKinaseCK2-Uniprot
621SPhosphorylationKinasePRKACAP17612
GPS
621SPhosphorylationKinasePKA-FAMILY-GPS
621SPhosphorylationKinasePKA-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
621SPhosphorylation

15975931

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 BCAM_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC9_HUMANUBE2Iphysical
17087659
KLHL2_HUMANKLHL2physical
25416956
LAMA4_HUMANLAMA4physical
28514442
VPP1_HUMANATP6V0A1physical
28514442
TMM11_HUMANTMEM11physical
28514442
LAMA5_HUMANLAMA5physical
28514442
VPP2_HUMANATP6V0A2physical
28514442
AT11C_HUMANATP11Cphysical
28514442
TNPO2_HUMANTNPO2physical
28514442
MTCH2_HUMANMTCH2physical
28514442
TNPO3_HUMANTNPO3physical
28514442
LAMB1_HUMANLAMB1physical
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 BCAM_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-439, AND MASSSPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-439.
Phosphorylation
ReferencePubMed
"Protein kinase A-dependent phosphorylation of Lutheran/basal celladhesion molecule glycoprotein regulates cell adhesion to lamininalpha5.";
Gauthier E., Rahuel C., Wautier M.P., El Nemer W., Gane P.,Wautier J.L., Cartron J.P., Colin Y., Le Van Kim C.;
J. Biol. Chem. 280:30055-30062(2005).
Cited for: PHOSPHORYLATION AT SER-596; SER-598 AND SER-621, AND MUTAGENESIS OFSER-621.

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