LAMB1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LAMB1_MOUSE
• UniProt AC: P02469
• Protein Name: Laminin subunit beta-1
• Gene Name: Lamb1
• Organism: Mus musculus (Mouse).
• Sequence Length: 1786
• Subcellular Localization: Secreted, extracellular space, extracellular matrix, basement membrane. Major component.
• Protein Description: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Involved in the organization of the laminar architecture of the cerebral cortex (By similarity). It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons (By similarity). Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface (By similarity)..
• Protein Sequence: MGLLQVFAFGVLALWGTRVCAQEPEFSYGCAEGSCYPATGDLLIGRAQKLSVTSTCGLHKPEPYCIVSHLQEDKKCFICDSRDPYHETLNPDSHLIENVVTTFAPNRLKIWWQSENGVENVTIQLDLEAEFHFTHLIMTFKTFRPAAMLIERSSDFGKAWGVYRYFAYDCESSFPGISTGPMKKVDDIICDSRYSDIEPSTEGEVIFRALDPAFKIEDPYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIREKYYYAVYDMVVRGNCFCYGHASECAPVDGVNEEVEGMVHGHCMCRHNTKGLNCELCMDFYHDLPWRPAEGRNSNACKKCNCNEHSSSCHFDMAVFLATGNVSGGVCDNCQHNTMGRNCEQCKPFYFQHPERDIRDPNLCEPCTCDPAGSENGGICDGYTDFSVGLIAGQCRCKLHVEGERCDVCKEGFYDLSAEDPYGCKSCACNPLGTIPGGNPCDSETGYCYCKRLVTGQRCDQCLPQHWGLSNDLDGCRPCDCDLGGALNNSCSEDSGQCSCLPHMIGRQCNEVESGYYFTTLDHYIYEAEEANLGPGVIVVERQYIQDRIPSWTGPGFVRVPEGAYLEFFIDNIPYSMEYEILIRYEPQLPDHWEKAVITVQRPGKIPASSRCGNTVPDDDNQVVSLSPGSRYVVLPRPVCFEKGMNYTVRLELPQYTASGSDVESPYTFIDSLVLMPYCKSLDIFTVGGSGDGEVTNSAWETFQRYRCLENSRSVVKTPMTDVCRNIIFSISALIHQTGLACECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGFGPNGCKPCDCHLQGSASAFCDAITGQCHCFQGIYARQCDRCLPGYWGFPSCQPCQCNGHALDCDTVTGECLSCQDYTTGHNCERCLAGYYGDPIIGSGDHCRPCPCPDGPDSGRQFARSCYQDPVTLQLACVCDPGYIGSRCDDCASGFFGNPSDFGGSCQPCQCHHNIDTTDPEACDKETGRCLKCLYHTEGDHCQLCQYGYYGDALRQDCRKCVCNYLGTVKEHCNGSDCHCDKATGQCSCLPNVIGQNCDRCAPNTWQLASGTGCGPCNCNAAHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPDVECRACDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSGVFPDCTPCHQCFALWDAIIGELTNRTHKFLEKAKALKISGVIGPYRETVDSVEKKVNEIKDILAQSPAAEPLKNIGILFEEAEKLTKDVTEKMAQVEVKLTDTASQSNSTAGELGALQAEAESLDKTVKELAEQLEFIKNSDIQGALDSITKYFQMSLEAEKRVNASTTDPNSTVEQSALTRDRVEDLMLERESPFKEQQEEQARLLDELAGKLQSLDLSAVAQMTCGTPPGADCSESECGGPNCRTDEGEKKCGGPGCGGLVTVAHSAWQKAMDFDRDVLSALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRNFLTEDSADLDSIEAVANEVLKMEMPSTPQQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEYIEKVVYSVKQNADDVKKTLDGELDEKYKKVESLIAQKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVAVYSTCL

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
120	N-linked_Glycosylation	QSENGVENVTIQLDL ECCCCEEEEEEEEEE	33.55	-
250	Phosphorylation	LGDNLLDSRMEIREK CCCCHHHCCHHHHHH	33.23	22817900
356	N-linked_Glycosylation	AVFLATGNVSGGVCD EEEECCCCCCCCCCC	22.04	-
519	N-linked_Glycosylation	CDLGGALNNSCSEDS CCCCCCCCCCCCCCC	37.52	-
677	N-linked_Glycosylation	VCFEKGMNYTVRLEL EEECCCCCEEEEEEC	37.68	-
687	Phosphorylation	VRLELPQYTASGSDV EEEECCEEECCCCCC	11.44	25293948
688	Phosphorylation	RLELPQYTASGSDVE EEECCEEECCCCCCC	14.75	25293948
690	Phosphorylation	ELPQYTASGSDVESP ECCEEECCCCCCCCC	30.91	25293948
692	Phosphorylation	PQYTASGSDVESPYT CEEECCCCCCCCCCC	35.67	25293948
696	Phosphorylation	ASGSDVESPYTFIDS CCCCCCCCCCCHHHH	24.05	25293948
698	Phosphorylation	GSDVESPYTFIDSLV CCCCCCCCCHHHHHC	24.46	25293948
699	Phosphorylation	SDVESPYTFIDSLVL CCCCCCCCHHHHHCH	19.94	25293948
703	Phosphorylation	SPYTFIDSLVLMPYC CCCCHHHHHCHHCCC	18.63	25293948
709	Phosphorylation	DSLVLMPYCKSLDIF HHHCHHCCCCCCEEE	9.88	25293948
1041	N-linked_Glycosylation	GTVKEHCNGSDCHCD HHHHHHCCCCCCCCC	55.71	-
1195	N-linked_Glycosylation	AIIGELTNRTHKFLE HHHHHHHHHHHHHHH	60.52	-
1222	Phosphorylation	PYRETVDSVEKKVNE CCHHHHHHHHHHHHH	28.04	-
1279	N-linked_Glycosylation	TDTASQSNSTAGELG ECCCCCCCCCHHHHH	35.42	19349973
1310	Ubiquitination	AEQLEFIKNSDIQGA HHHHHHHHCCCHHHH	56.57	-
1336	N-linked_Glycosylation	LEAEKRVNASTTDPN HHHHHHHCCCCCCCC	32.01	19349973
1343	N-linked_Glycosylation	NASTTDPNSTVEQSA CCCCCCCCCHHHHHH	53.79	19349973
1453	Phosphorylation	DFDRDVLSALAEVEQ CCCHHHHHHHHHHHH	22.53	19367708
1487	N-linked_Glycosylation	QDVLLKTNATKEKVD HHHHHHCCCCHHHHC	43.98	-
1496	Phosphorylation	TKEKVDKSNEDLRNL CHHHHCCCHHHHHHH	40.77	-
1542	N-linked_Glycosylation	STPQQLQNLTEDIRE CCHHHHHHHHHHHHH	58.48	-
1643	N-linked_Glycosylation	ASEETLTNASQRISK CCHHHHHHHHHHHHH	40.48	-
1666	Phosphorylation	KRKAAQNSGEAEYIE HHHHHHCCCCHHHHH	26.40	27180971
1697	Acetylation	LDGELDEKYKKVESL HCCHHHHHHHHHHHH	63.14	21728379
1708	Ubiquitination	VESLIAQKTEESADA HHHHHHHHHHHHHHH	49.21	-
1736	Acetylation	LLAQANSKLQLLEDL HHHHHHHHHHHHHHH	39.81	21728379
1770	Phosphorylation	RLEGEVRSLLKDISE HHHHHHHHHHHHHHH	43.14	23737553
1776	Phosphorylation	RSLLKDISEKVAVYS HHHHHHHHHHHHHEE	41.31	23737553

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of LAMB1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LAMB1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of LAMB1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of LAMB1_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1279; ASN-1336 ANDASN-1343, AND MASS SPECTROMETRY.
PubMed: 19349973