dbPTM

BCAM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
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

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
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

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
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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
621	S	Phosphorylation		15975931
Epinephrine-stimulated phosphorylation of Ser-621 by PKA enhances adhesion to laminin.

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
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

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

Related Literatures of Post-Translational Modification

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.	16335952 [Abstract]
"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.	12754519 [Abstract]
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.	15975931 [Abstract]

show