dbPTM

LAMB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LAMB1_HUMAN
UniProt AC	P07942
Protein Name	Laminin subunit beta-1
Gene Name	LAMB1
Organism	Homo sapiens (Human).
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 cerebral cortex. 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. 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..
Protein Sequence	MGLLQLLAFSFLALCRARVRAQEPEFSYGCAEGSCYPATGDLLIGRAQKLSVTSTCGLHKPEPYCIVSHLQEDKKCFICNSQDPYHETLNPDSHLIENVVTTFAPNRLKIWWQSENGVENVTIQLDLEAEFHFTHLIMTFKTFRPAAMLIERSSDFGKTWGVYRYFAYDCEASFPGISTGPMKKVDDIICDSRYSDIEPSTEGEVIFRALDPAFKIEDPYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIREKYYYAVYDMVVRGNCFCYGHASECAPVDGFNEEVEGMVHGHCMCRHNTKGLNCELCMDFYHDLPWRPAEGRNSNACKKCNCNEHSISCHFDMAVYLATGNVSGGVCDDCQHNTMGRNCEQCKPFYYQHPERDIRDPNFCERCTCDPAGSQNEGICDSYTDFSTGLIAGQCRCKLNVEGEHCDVCKEGFYDLSSEDPFGCKSCACNPLGTIPGGNPCDSETGHCYCKRLVTGQHCDQCLPEHWGLSNDLDGCRPCDCDLGGALNNSCFAESGQCSCRPHMIGRQCNEVEPGYYFATLDHYLYEAEEANLGPGVSIVERQYIQDRIPSWTGAGFVRVPEGAYLEFFIDNIPYSMEYDILIRYEPQLPDHWEKAVITVQRPGRIPTSSRCGNTIPDDDNQVVSLSPGSRYVVLPRPVCFEKGTNYTVRLELPQYTSSDSDVESPYTLIDSLVLMPYCKSLDIFTVGGSGDGVVTNSAWETFQRYRCLENSRSVVKTPMTDVCRNIIFSISALLHQTGLACECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGFGPSGCKPCECHLQGSVNAFCNPVTGQCHCFQGVYARQCDRCLPGHWGFPSCQPCQCNGHADDCDPVTGECLNCQDYTMGHNCERCLAGYYGDPIIGSGDHCRPCPCPDGPDSGRQFARSCYQDPVTLQLACVCDPGYIGSRCDDCASGYFGNPSEVGGSCQPCQCHNNIDTTDPEACDKETGRCLKCLYHTEGEHCQFCRFGYYGDALQQDCRKCVCNYLGTVQEHCNGSDCQCDKATGQCLCLPNVIGQNCDRCAPNTWQLASGTGCDPCNCNAAHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPDVECRACDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSGVFPDCTPCHQCFALWDVIIAELTNRTHRFLEKAKALKISGVIGPYRETVDSVERKVSEIKDILAQSPAAEPLKNIGNLFEEAEKLIKDVTEMMAQVEVKLSDTTSQSNSTAKELDSLQTEAESLDNTVKELAEQLEFIKNSDIRGALDSITKYFQMSLEAEERVNASTTEPNSTVEQSALMRDRVEDVMMERESQFKEKQEEQARLLDELAGKLQSLDLSAAAEMTCGTPPGASCSETECGGPNCRTDEGERKCGGPGCGGLVTVAHNAWQKAMDLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIEAVANEVLKMEMPSTPQQLQNLTEDIRERVESLSQVEVILQHSAADIARAEMLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEYIEKVVYTVKQSAEDVKKTLDGELDEKYKKVENLIAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQKVAVYSTCL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	LLQLLAFSFLALCRA HHHHHHHHHHHHHHH	17.47	24043423
120	N-linked_Glycosylation	QSENGVENVTIQLDL ECCCCEEEEEEEEEE	33.55	UniProtKB CARBOHYD
154	Phosphorylation	AMLIERSSDFGKTWG HHHHHCCCCHHHCCC	43.08	20058876
158	Ubiquitination	ERSSDFGKTWGVYRY HCCCCHHHCCCEEEE	40.89	-
184	Ubiquitination	ISTGPMKKVDDIICD CCCCCCCCCCEEEEC	44.65	-
192	Phosphorylation	VDDIICDSRYSDIEP CCEEEECCCCCCCCC	28.80	23532336
195	Phosphorylation	IICDSRYSDIEPSTE EEECCCCCCCCCCCC	30.88	-
215	Ubiquitination	RALDPAFKIEDPYSP EECCCCCCCCCCCCH	47.49	21906983
215	Sumoylation	RALDPAFKIEDPYSP EECCCCCCCCCCCCH	47.49	-
215	Sumoylation	RALDPAFKIEDPYSP EECCCCCCCCCCCCH	47.49	-
220	Phosphorylation	AFKIEDPYSPRIQNL CCCCCCCCCHHHHHH	43.56	21659604
221	Phosphorylation	FKIEDPYSPRIQNLL CCCCCCCCHHHHHHH	17.06	22617229
229	Ubiquitination	PRIQNLLKITNLRIK HHHHHHHHHHCCEEE	51.13	21906983
231	Phosphorylation	IQNLLKITNLRIKFV HHHHHHHHCCEEEEE	26.98	21659604
239	Ubiquitination	NLRIKFVKLHTLGDN CCEEEEEEEEECCCC	37.37	-
242	Phosphorylation	IKFVKLHTLGDNLLD EEEEEEEECCCCHHH	42.76	19562805
250	Phosphorylation	LGDNLLDSRMEIREK CCCCHHHCCHHHHHH	33.23	-
356	N-linked_Glycosylation	AVYLATGNVSGGVCD EEEEHHCCCCCCCCC	22.04	UniProtKB CARBOHYD
369	Phosphorylation	CDDCQHNTMGRNCEQ CCCCCCCCCCCCHHH	20.91	-
399	Phosphorylation	PNFCERCTCDPAGSQ CCCHHCCCCCCCCCC	26.60	23532336
414	Phosphorylation	NEGICDSYTDFSTGL CCCCCCCCCCCCCCC	9.33	23532336
482	2-Hydroxyisobutyrylation	ETGHCYCKRLVTGQH CCCCEEECCCCCCCC	23.46	-
519	N-linked_Glycosylation	CDLGGALNNSCFAES CCCCHHCCCCCHHCC	37.52	UniProtKB CARBOHYD
677	N-linked_Glycosylation	VCFEKGTNYTVRLEL EEECCCCCEEEEEEC	38.86	UniProtKB CARBOHYD
687	Phosphorylation	VRLELPQYTSSDSDV EEEECCCCCCCCCCC	13.47	28857561
688	Phosphorylation	RLELPQYTSSDSDVE EEECCCCCCCCCCCC	19.26	28857561
689	Phosphorylation	LELPQYTSSDSDVES EECCCCCCCCCCCCC	27.49	27251275
690	Phosphorylation	ELPQYTSSDSDVESP ECCCCCCCCCCCCCC	33.08	27251275
692	Phosphorylation	PQYTSSDSDVESPYT CCCCCCCCCCCCCCC	45.57	28857561
696	Phosphorylation	SSDSDVESPYTLIDS CCCCCCCCCCCHHHH	24.05	24719451
939	Phosphorylation	SCYQDPVTLQLACVC HHHCCCEEEEEEEEE	17.74	18767875
950	Phosphorylation	ACVCDPGYIGSRCDD EEEECCCCCCCCCCC	13.90	18767875
953	Phosphorylation	CDPGYIGSRCDDCAS ECCCCCCCCCCCCCC	21.85	18767875
1041	N-linked_Glycosylation	GTVQEHCNGSDCQCD HHHHHHCCCCCCCCC	55.71	UniProtKB CARBOHYD
1195	N-linked_Glycosylation	VIIAELTNRTHRFLE HHHHHHHHCHHHHHH	60.52	UniProtKB CARBOHYD
1219	Phosphorylation	VIGPYRETVDSVERK EECCCHHHHHHHHHH	22.18	30242111
1222	Phosphorylation	PYRETVDSVERKVSE CCHHHHHHHHHHHHH	22.88	30242111
1231	Ubiquitination	ERKVSEIKDILAQSP HHHHHHHHHHHHCCC	34.36	-
1244	Ubiquitination	SPAAEPLKNIGNLFE CCCCHHHCCHHHHHH	58.18	-
1255	Ubiquitination	NLFEEAEKLIKDVTE HHHHHHHHHHHHHHH	63.66	-
1279	N-linked_Glycosylation	SDTTSQSNSTAKELD CCCCCCCCHHHHHHH	35.42	16335952
1279	N-linked_Glycosylation	SDTTSQSNSTAKELD CCCCCCCCHHHHHHH	35.42	19159218
1280	Phosphorylation	DTTSQSNSTAKELDS CCCCCCCHHHHHHHH	34.68	19413330
1280	O-linked_Glycosylation	DTTSQSNSTAKELDS CCCCCCCHHHHHHHH	34.68	30059200
1281	Phosphorylation	TTSQSNSTAKELDSL CCCCCCHHHHHHHHH	46.10	19413330
1287	Phosphorylation	STAKELDSLQTEAES HHHHHHHHHHHHHHH	34.69	25338102
1290	Phosphorylation	KELDSLQTEAESLDN HHHHHHHHHHHHHHH	42.32	-
1310	Ubiquitination	AEQLEFIKNSDIRGA HHHHHHHHCCCHHHH	56.57	21906983
1315	Methylation	FIKNSDIRGALDSIT HHHCCCHHHHHHHHH	29.35	115481541
1320	Phosphorylation	DIRGALDSITKYFQM CHHHHHHHHHHHHHH	32.76	21406692
1322	Phosphorylation	RGALDSITKYFQMSL HHHHHHHHHHHHHHH	24.52	21406692
1324	Phosphorylation	ALDSITKYFQMSLEA HHHHHHHHHHHHHHH	7.15	21406692
1328	Phosphorylation	ITKYFQMSLEAEERV HHHHHHHHHHHHHHH	16.57	21406692
1336	N-linked_Glycosylation	LEAEERVNASTTEPN HHHHHHHCCCCCCCC	34.10	UniProtKB CARBOHYD
1338	Phosphorylation	AEERVNASTTEPNST HHHHHCCCCCCCCCH	30.56	21406692
1339	Phosphorylation	EERVNASTTEPNSTV HHHHCCCCCCCCCHH	32.54	21406692
1340	Phosphorylation	ERVNASTTEPNSTVE HHHCCCCCCCCCHHH	47.12	21406692
1343	N-linked_Glycosylation	NASTTEPNSTVEQSA CCCCCCCCCHHHHHH	44.04	UniProtKB CARBOHYD
1344	Phosphorylation	ASTTEPNSTVEQSAL CCCCCCCCHHHHHHH	44.54	21406692
1345	Phosphorylation	STTEPNSTVEQSALM CCCCCCCHHHHHHHH	34.40	21406692
1349	Phosphorylation	PNSTVEQSALMRDRV CCCHHHHHHHHHHHH	15.18	21406692
1365	Phosphorylation	DVMMERESQFKEKQE HHHHHCHHHHHHHHH	47.33	-
1435	O-linked_Glycosylation	PGCGGLVTVAHNAWQ CCCCCHHHHHHHHHH	19.61	55825123
1445	Sulfoxidation	HNAWQKAMDLDQDVL HHHHHHHCCCCHHHH	7.28	30846556
1453	Phosphorylation	DLDQDVLSALAEVEQ CCCHHHHHHHHHHHH	22.53	21406692
1462	Phosphorylation	LAEVEQLSKMVSEAK HHHHHHHHHHHHHHH	20.57	21406692
1476	Ubiquitination	KLRADEAKQSAEDIL HHCHHHHHHHHHHHH	42.62	-
1478	Phosphorylation	RADEAKQSAEDILLK CHHHHHHHHHHHHHH	32.68	26091039
1487	N-linked_Glycosylation	EDILLKTNATKEKMD HHHHHHCHHCHHHHH	43.98	UniProtKB CARBOHYD
1496	Phosphorylation	TKEKMDKSNEELRNL CHHHHHCCHHHHHHH	45.25	29802988
1520	Phosphorylation	QDSADLDSIEAVANE CCCCCHHHHHHHHHH	29.62	27251275
1542	N-linked_Glycosylation	STPQQLQNLTEDIRE CCHHHHHHHHHHHHH	58.48	UniProtKB CARBOHYD
1579	2-Hydroxyisobutyrylation	EMLLEEAKRASKSAT HHHHHHHHHHCCCCC	52.34	-
1611	Ubiquitination	KAQVAAEKAIKQADE HHHHHHHHHHHHHHH	51.16	-
1659	2-Hydroxyisobutyrylation	ERNVEELKRKAAQNS HHHHHHHHHHHHHCC	55.95	-
1666	Phosphorylation	KRKAAQNSGEAEYIE HHHHHHCCCCHHHHH	26.40	25850435
1671	Phosphorylation	QNSGEAEYIEKVVYT HCCCCHHHHHHHHHH	22.79	24719451
1678	Phosphorylation	YIEKVVYTVKQSAED HHHHHHHHHHHCHHH	15.04	24719451
1682	Phosphorylation	VVYTVKQSAEDVKKT HHHHHHHCHHHHHHH	28.10	3611077
1689	Phosphorylation	SAEDVKKTLDGELDE CHHHHHHHHCCHHHH	25.10	28258704
1697	2-Hydroxyisobutyrylation	LDGELDEKYKKVENL HCCHHHHHHHHHHHH	63.14	-
1728	Phosphorylation	MLQNEAKTLLAQANS HHHHHHHHHHHHHHH	33.77	21406692
1735	Phosphorylation	TLLAQANSKLQLLKD HHHHHHHHHHHHHHH	37.45	20068231
1741	Ubiquitination	NSKLQLLKDLERKYE HHHHHHHHHHHHHHH	69.71	-
1757	Ubiquitination	NQRYLEDKAQELARL HHHHHHHHHHHHHHH	42.46	-
1757	2-Hydroxyisobutyrylation	NQRYLEDKAQELARL HHHHHHHHHHHHHHH	42.46	-
1770	Phosphorylation	RLEGEVRSLLKDISQ HHHHHHHHHHHHHHH	43.14	24719451
1773	Ubiquitination	GEVRSLLKDISQKVA HHHHHHHHHHHHHHH	59.31	-

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
1478	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
1496	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
1666	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
1682	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LAMB1_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 LAMB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LAMA1_MOUSE	Lama1	physical	17517882
LAMC1_HUMAN	LAMC1	physical	17517882
NQO1_HUMAN	NQO1	physical	22939629
WASC4_HUMAN	KIAA1033	physical	22863883
RPAB1_HUMAN	POLR2E	physical	22863883

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615191	Lissencephaly 5 (LIS5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of LAMB1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-1279, AND MASSSPECTROMETRY.	19159218 [Abstract]
"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-1279, AND MASSSPECTROMETRY.	16335952 [Abstract]