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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
150 | O-linked_Glycosylation | VFAKPEATEVSPNKG EEECCCCEEECCCCC | 34.95 | OGP | |
205 | Phosphorylation | MNPEGYMTSRTVREA ECCCCCEEHHHHHHH | 13.43 | - | |
206 | Phosphorylation | NPEGYMTSRTVREAS CCCCCEEHHHHHHHH | 14.93 | - | |
213 | Phosphorylation | SRTVREASGLLSLTS HHHHHHHHHHHHHEE | 25.81 | 24719451 | |
223 | Phosphorylation | LSLTSTLYLRLRKDD HHHEEEEEEEECCCC | 7.00 | 24719451 | |
296 | Phosphorylation | LLCRGDGSPSPEYTL EEECCCCCCCCCEEE | 27.26 | - | |
301 | Phosphorylation | DGSPSPEYTLFRLQD CCCCCCCEEEEECCC | 16.48 | - | |
302 | Phosphorylation | GSPSPEYTLFRLQDE CCCCCCEEEEECCCC | 20.12 | - | |
321 | N-linked_Glycosylation | LNVNLEGNLTLEGVT ECEECCCCEEEEEEE | 22.07 | UniProtKB CARBOHYD | |
332 | Phosphorylation | EGVTRGQSGTYGCRV EEEECCCCCCEEEEE | 35.61 | 29978859 | |
334 | Phosphorylation | VTRGQSGTYGCRVED EECCCCCCEEEEEEC | 23.22 | 29978859 | |
335 | Phosphorylation | TRGQSGTYGCRVEDY ECCCCCCEEEEEECC | 20.11 | 29978859 | |
342 | Phosphorylation | YGCRVEDYDAADDVQ EEEEEECCCCCCCCC | 8.25 | 29978859 | |
351 | Phosphorylation | AADDVQLSKTLELRV CCCCCCCCCEEEEEE | 13.40 | 29978859 | |
353 | Phosphorylation | DDVQLSKTLELRVAY CCCCCCCEEEEEEEE | 23.30 | 29978859 | |
360 | Phosphorylation | TLELRVAYLDPLELS EEEEEEEECCCEECC | 14.58 | - | |
367 | Phosphorylation | YLDPLELSEGKVLSL ECCCEECCCCEEEEE | 34.62 | - | |
377 | N-linked_Glycosylation | KVLSLPLNSSAVVNC EEEEEECCCCCEEEE | 31.79 | UniProtKB CARBOHYD | |
383 | N-linked_Glycosylation | LNSSAVVNCSVHGLP CCCCCEEEEEECCCC | 13.02 | UniProtKB CARBOHYD | |
419 | N-linked_Glycosylation | SSITFDSNGTYVCEA EEEEECCCCCEEEEE | 48.98 | UniProtKB CARBOHYD | |
439 | N-linked_Glycosylation | PVLSRTQNFTLLVQG CEEECCCCEEEEECC | 31.12 | 12754519 | |
447 | Phosphorylation | FTLLVQGSPELKTAE EEEEECCCCCCEEEE | 9.71 | 24719451 | |
458 | Ubiquitination | KTAEIEPKADGSWRE EEEEEECCCCCCCCC | 46.44 | - | |
486 | Phosphorylation | PDPKLSWSQLGGSPA CCCCCCHHHCCCCCC | 16.49 | - | |
491 | O-linked_Glycosylation | SWSQLGGSPAEPIPG CHHHCCCCCCCCCCC | 21.09 | OGP | |
505 | Phosphorylation | GRQGWVSSSLTLKVT CCCCCCCCCEEEEHH | 21.54 | 29457462 | |
506 | Phosphorylation | RQGWVSSSLTLKVTS CCCCCCCCEEEEHHH | 20.19 | 24719451 | |
541 | Phosphorylation | VFHFGTVSPQTSQAG EEEEECCCCCCCHHH | 15.89 | 20886841 | |
585 | Ubiquitination | CCRQRREKGAPPPGE CHHHHHHCCCCCCCC | 59.57 | - | |
596 | Phosphorylation | PPGEPGLSHSGSEQP CCCCCCCCCCCCCCH | 22.86 | 30266825 | |
598 | Phosphorylation | GEPGLSHSGSEQPEQ CCCCCCCCCCCCHHH | 40.41 | 30266825 | |
600 | Phosphorylation | PGLSHSGSEQPEQTG CCCCCCCCCCHHHCC | 35.75 | 30266825 | |
606 | Phosphorylation | GSEQPEQTGLLMGGA CCCCHHHCCEECCCC | 28.30 | 30266825 | |
614 | Phosphorylation | GLLMGGASGGARGGS CEECCCCCCCCCCCC | 40.82 | 23090842 | |
621 | Phosphorylation | SGGARGGSGGFGDEC CCCCCCCCCCCCCCC | 38.27 | 30278072 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
596 | S | Phosphorylation | Kinase | GSK3B | P49841 | PSP |
596 | S | Phosphorylation | Kinase | GSK-FAMILY | - | GPS |
596 | S | Phosphorylation | Kinase | GSK3 | - | Uniprot |
598 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
598 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
598 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
621 | S | Phosphorylation | Kinase | PRKACA | P17612 | GPS |
621 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
621 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
621 | S | Phosphorylation |
| 15975931 |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
UBC9_HUMAN | UBE2I | physical | 17087659 | |
KLHL2_HUMAN | KLHL2 | physical | 25416956 | |
LAMA4_HUMAN | LAMA4 | physical | 28514442 | |
VPP1_HUMAN | ATP6V0A1 | physical | 28514442 | |
TMM11_HUMAN | TMEM11 | physical | 28514442 | |
LAMA5_HUMAN | LAMA5 | physical | 28514442 | |
VPP2_HUMAN | ATP6V0A2 | physical | 28514442 | |
AT11C_HUMAN | ATP11C | physical | 28514442 | |
TNPO2_HUMAN | TNPO2 | physical | 28514442 | |
MTCH2_HUMAN | MTCH2 | physical | 28514442 | |
TNPO3_HUMAN | TNPO3 | physical | 28514442 | |
LAMB1_HUMAN | LAMB1 | physical | 28514442 |
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. |
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N-linked Glycosylation | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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. |