dbPTM

LAMC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LAMC1_HUMAN
UniProt AC	P11047
Protein Name	Laminin subunit gamma-1
Gene Name	LAMC1
Organism	Homo sapiens (Human).
Sequence Length	1609
Subcellular Localization	Secreted, extracellular space, extracellular matrix, basement membrane.
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..
Protein Sequence	MRGSHRAAPALRPRGRLWPVLAVLAAAAAAGCAQAAMDECTDEGGRPQRCMPEFVNAAFNVTVVATNTCGTPPEEYCVQTGVTGVTKSCHLCDAGQPHLQHGAAFLTDYNNQADTTWWQSQTMLAGVQYPSSINLTLHLGKAFDITYVRLKFHTSRPESFAIYKRTREDGPWIPYQYYSGSCENTYSKANRGFIRTGGDEQQALCTDEFSDISPLTGGNVAFSTLEGRPSAYNFDNSPVLQEWVTATDIRVTLNRLNTFGDEVFNDPKVLKSYYYAISDFAVGGRCKCNGHASECMKNEFDKLVCNCKHNTYGVDCEKCLPFFNDRPWRRATAESASECLPCDCNGRSQECYFDPELYRSTGHGGHCTNCQDNTDGAHCERCRENFFRLGNNEACSSCHCSPVGSLSTQCDSYGRCSCKPGVMGDKCDRCQPGFHSLTEAGCRPCSCDPSGSIDECNIETGRCVCKDNVEGFNCERCKPGFFNLESSNPRGCTPCFCFGHSSVCTNAVGYSVYSISSTFQIDEDGWRAEQRDGSEASLEWSSERQDIAVISDSYFPRYFIAPAKFLGKQVLSYGQNLSFSFRVDRRDTRLSAEDLVLEGAGLRVSVPLIAQGNSYPSETTVKYVFRLHEATDYPWRPALTPFEFQKLLNNLTSIKIRGTYSERSAGYLDDVTLASARPGPGVPATWVESCTCPVGYGGQFCEMCLSGYRRETPNLGPYSPCVLCACNGHSETCDPETGVCNCRDNTAGPHCEKCSDGYYGDSTAGTSSDCQPCPCPGGSSCAVVPKTKEVVCTNCPTGTTGKRCELCDDGYFGDPLGRNGPVRLCRLCQCSDNIDPNAVGNCNRLTGECLKCIYNTAGFYCDRCKDGFFGNPLAPNPADKCKACNCNLYGTMKQQSSCNPVTGQCECLPHVTGQDCGACDPGFYNLQSGQGCERCDCHALGSTNGQCDIRTGQCECQPGITGQHCERCEVNHFGFGPEGCKPCDCHPEGSLSLQCKDDGRCECREGFVGNRCDQCEENYFYNRSWPGCQECPACYRLVKDKVADHRVKLQELESLIANLGTGDEMVTDQAFEDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNNTLSSQISRLQNIRNTIEETGNLAEQARAHVENTERLIEIASRELEKAKVAAANVSVTQPESTGDPNNMTLLAEEARKLAERHKQEADDIVRVAKTANDTSTEAYNLLLRTLAGENQTAFEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLSPLDSETLENEANNIKMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARADAAKALAEEAAKKGRDTLQEANDILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQDMMMAGMASQAAQEAEINARKAKNSVTSLLSIINDLLEQLGQLDTVDLNKLNEIEGTLNKAKDEMKVSDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLEDIRKTLPSGCFNTPSIEKP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MRGSHRAAPAL ----CCCCCCCCCCC	18.94	24719451
60	N-linked_Glycosylation	EFVNAAFNVTVVATN HHHHHHCCEEEEEEC	24.67	UniProtKB CARBOHYD
134	N-linked_Glycosylation	VQYPSSINLTLHLGK CCCCCCEEEEEEECC	28.99	UniProtKB CARBOHYD
154	Phosphorylation	YVRLKFHTSRPESFA EEEEEEECCCCHHEE	29.57	20068231
155	Phosphorylation	VRLKFHTSRPESFAI EEEEEECCCCHHEEE	36.95	20068231
159	Phosphorylation	FHTSRPESFAIYKRT EECCCCHHEEEEEEE	23.74	20068231
163	Phosphorylation	RPESFAIYKRTREDG CCHHEEEEEEECCCC	7.32	20068231
164	Ubiquitination	PESFAIYKRTREDGP CHHEEEEEEECCCCC	40.97	-
166	Phosphorylation	SFAIYKRTREDGPWI HEEEEEEECCCCCCC	33.97	20068231
175	Phosphorylation	EDGPWIPYQYYSGSC CCCCCCCCEEECCCC	10.46	20068231
177	Phosphorylation	GPWIPYQYYSGSCEN CCCCCCEEECCCCCC	8.18	20068231
178	Phosphorylation	PWIPYQYYSGSCENT CCCCCEEECCCCCCC	7.33	20068231
179	Phosphorylation	WIPYQYYSGSCENTY CCCCEEECCCCCCCC	21.21	20068231
181	Phosphorylation	PYQYYSGSCENTYSK CCEEECCCCCCCCCC	16.59	20068231
185	Phosphorylation	YSGSCENTYSKANRG ECCCCCCCCCCCCCC	13.59	20068231
186	Phosphorylation	SGSCENTYSKANRGF CCCCCCCCCCCCCCE	21.54	20068231
187	Phosphorylation	GSCENTYSKANRGFI CCCCCCCCCCCCCEE	24.21	20068231
188	Ubiquitination	SCENTYSKANRGFIR CCCCCCCCCCCCEEC	38.99	-
196	Phosphorylation	ANRGFIRTGGDEQQA CCCCEECCCCCHHHE	40.47	-
210	Phosphorylation	ALCTDEFSDISPLTG EEECCCCCCCCCCCC	31.80	-
216	Phosphorylation	FSDISPLTGGNVAFS CCCCCCCCCCCEEEE	46.56	-
258	Phosphorylation	VTLNRLNTFGDEVFN HHHHHHHCCCHHHHC	33.32	-
268	Ubiquitination	DEVFNDPKVLKSYYY HHHHCCHHHHHHEEE	64.16	-
272	Phosphorylation	NDPKVLKSYYYAISD CCHHHHHHEEEEECC	17.76	-
273	Phosphorylation	DPKVLKSYYYAISDF CHHHHHHEEEEECCC	10.02	-
274	Phosphorylation	PKVLKSYYYAISDFA HHHHHHEEEEECCCE	8.10	-
275	Phosphorylation	KVLKSYYYAISDFAV HHHHHEEEEECCCEE	6.82	-
302	Ubiquitination	CMKNEFDKLVCNCKH HHHHHCCHHHHCCCC	48.41	-
308	Ubiquitination	DKLVCNCKHNTYGVD CHHHHCCCCCCCCCC	26.37	-
351	Glutathionylation	CNGRSQECYFDPELY CCCCCCEEECCHHHH	2.96	22555962
396	Phosphorylation	LGNNEACSSCHCSPV CCCCCCCCCCCCCCC	42.94	24114839
397	Phosphorylation	GNNEACSSCHCSPVG CCCCCCCCCCCCCCC	14.04	24114839
401	Phosphorylation	ACSSCHCSPVGSLST CCCCCCCCCCCCCCC	10.04	24114839
413	Phosphorylation	LSTQCDSYGRCSCKP CCCCCCCCCCCCCCC	8.71	-
564	Ubiquitination	RYFIAPAKFLGKQVL CHHCCCHHHCCEEHH	39.81	-
572	Phosphorylation	FLGKQVLSYGQNLSF HCCEEHHHCCCCEEE	28.49	25690035
573	Phosphorylation	LGKQVLSYGQNLSFS CCEEHHHCCCCEEEE	20.69	25690035
576	N-linked_Glycosylation	QVLSYGQNLSFSFRV EHHHCCCCEEEEEEE	33.03	UniProtKB CARBOHYD
578	Phosphorylation	LSYGQNLSFSFRVDR HHCCCCEEEEEEECC	26.79	24719451
580	Phosphorylation	YGQNLSFSFRVDRRD CCCCEEEEEEECCCC	14.57	24719451
622	Ubiquitination	YPSETTVKYVFRLHE CCCCCCEEEEEEHHC	33.34	-
650	N-linked_Glycosylation	EFQKLLNNLTSIKIR HHHHHHHCCCCCEEE	44.67	12754519
650	N-linked_Glycosylation	EFQKLLNNLTSIKIR HHHHHHHCCCCCEEE	44.67	12754519
664	Phosphorylation	RGTYSERSAGYLDDV ECCCCCCCCCCCCEE	23.22	20068231
667	Phosphorylation	YSERSAGYLDDVTLA CCCCCCCCCCEEEEE	13.48	20068231
672	Phosphorylation	AGYLDDVTLASARPG CCCCCEEEEECCCCC	24.49	20068231
675	Phosphorylation	LDDVTLASARPGPGV CCEEEEECCCCCCCC	28.11	20068231
788	Ubiquitination	CAVVPKTKEVVCTNC CEEECCCCEEEEECC	55.42	-
802	Ubiquitination	CPTGTTGKRCELCDD CCCCCCCCCCCCCCC	52.35	-
1022	N-linked_Glycosylation	CEENYFYNRSWPGCQ CHHHHCCCCCCCCCC	22.93	UniProtKB CARBOHYD
1093	Ubiquitination	LREAQDVKDVDQNLM HHHHCCHHHHCHHHH	61.39	21906983
1102	Methylation	VDQNLMDRLQRVNNT HCHHHHHHHHHHHHH	20.82	115481557
1107	N-linked_Glycosylation	MDRLQRVNNTLSSQI HHHHHHHHHHHHHHH	37.65	16335952
1109	O-linked_Glycosylation	RLQRVNNTLSSQISR HHHHHHHHHHHHHHH	23.86	28657654
1127	Phosphorylation	IRNTIEETGNLAEQA HHHHHHHHCCHHHHH	20.69	19413330
1149	Phosphorylation	ERLIEIASRELEKAK HHHHHHHHHHHHHHC	31.76	26091039
1161	N-linked_Glycosylation	KAKVAAANVSVTQPE HHCHHEEEEEECCCC	23.13	16335952
1170	O-linked_Glycosylation	SVTQPESTGDPNNMT EECCCCCCCCCCHHH	43.90	OGP
1175	N-linked_Glycosylation	ESTGDPNNMTLLAEE CCCCCCCHHHHHHHH	30.15	16335952
1203	O-linked_Glycosylation	DIVRVAKTANDTSTE HHHHHHHHCCCCCHH	22.43	28657654
1205	N-linked_Glycosylation	VRVAKTANDTSTEAY HHHHHHCCCCCHHHH	59.32	UniProtKB CARBOHYD
1208	O-linked_Glycosylation	AKTANDTSTEAYNLL HHHCCCCCHHHHHHH	27.41	28657654
1218	Phosphorylation	AYNLLLRTLAGENQT HHHHHHHHHCCCCCC	22.41	26657352
1223	N-linked_Glycosylation	LRTLAGENQTAFEIE HHHHCCCCCCHHHHH	43.51	16335952
1225	Phosphorylation	TLAGENQTAFEIEEL HHCCCCCCHHHHHHH	44.91	23403867
1225	O-linked_Glycosylation	TLAGENQTAFEIEEL HHCCCCCCHHHHHHH	44.91	28657654
1241	N-linked_Glycosylation	RKYEQAKNISQDLEK HHHHHHHCCCHHHHH	42.00	19159218
1275	Phosphorylation	YASVAQLSPLDSETL HEEHHHHCCCCHHHH	16.01	-
1303	Ubiquitination	LEQLIDQKLKDYEDL HHHHHHHHCCCHHHH	54.48	21906983
1307	Phosphorylation	IDQKLKDYEDLREDM HHHHCCCHHHHHHHH	15.12	-
1329	Ubiquitination	KNLLEKGKTEQQTAD HHHHHCCCCCHHHHH	61.02	-
1371	Ubiquitination	NDILNNLKDFDRRVN HHHHHHHHHHHHHHC	59.48	21906983
1380	N-linked_Glycosylation	FDRRVNDNKTAAEEA HHHHHCCCHHHHHHH	38.07	UniProtKB CARBOHYD
1395	N-linked_Glycosylation	LRKIPAINQTITEAN HHHCHHHHHHHHHHH	34.74	16335952
1404	Acetylation	TITEANEKTREAQQA HHHHHHHHHHHHHHH	53.33	7960413
1414	Phosphorylation	EAQQALGSAAADATE HHHHHHHHHHHHHHH	18.65	23403867
1420	Phosphorylation	GSAAADATEAKNKAH HHHHHHHHHHHHHHH	36.70	23403867
1423	Ubiquitination	AADATEAKNKAHEAE HHHHHHHHHHHHHHH	53.39	-
1439	N-linked_Glycosylation	IASAVQKNATSTKAE HHHHHHHHCCCCHHH	31.21	UniProtKB CARBOHYD
1466	Ubiquitination	NEVNNMLKQLQEAEK HHHHHHHHHHHHHHH	37.89	-
1493	Phosphorylation	MMMAGMASQAAQEAE HHHHHHHHHHHHHHH	16.09	3360804
1529	Phosphorylation	EQLGQLDTVDLNKLN HHHCCCCCCCHHHHH	25.22	-
1541	Phosphorylation	KLNEIEGTLNKAKDE HHHHHCCHHHHHHHH	17.86	26074081
1544	Ubiquitination	EIEGTLNKAKDEMKV HHCCHHHHHHHHHCH	60.98	-
1552	Phosphorylation	AKDEMKVSDLDRKVS HHHHHCHHHHHHHHH	27.26	26074081
1557	Ubiquitination	KVSDLDRKVSDLENE CHHHHHHHHHHHHHH	45.84	2190698
1559	Phosphorylation	SDLDRKVSDLENEAK HHHHHHHHHHHHHHH	39.24	26074081
1566	Ubiquitination	SDLENEAKKQEAAIM HHHHHHHHHHHHHHH	49.13	-
1584	Ubiquitination	RDIEEIMKDIRNLED CCHHHHHHHHCCHHH	56.52	-
1603	Phosphorylation	LPSGCFNTPSIEKP- CCCCCCCCCCCCCC-	9.73	25627689
1603	O-linked_Glycosylation	LPSGCFNTPSIEKP- CCCCCCCCCCCCCC-	9.73	55824509
1605	Phosphorylation	SGCFNTPSIEKP--- CCCCCCCCCCCC---	41.14	28348404

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
258	T	Phosphorylation	Kinase	CHEK1	O14757	GPS
1149	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 LAMC1_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 LAMC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NID1_HUMAN	NID1	physical	9733643
NID1_MOUSE	Nid1	physical	9733643
NID2_HUMAN	NID2	physical	9733643
LAMA1_MOUSE	Lama1	physical	17517882
LAMB1_HUMAN	LAMB1	physical	17517882
A4_HUMAN	APP	physical	21832049
SNX2_HUMAN	SNX2	physical	21988832
TANK_HUMAN	TANK	physical	21988832
LAMA5_HUMAN	LAMA5	physical	26344197
PSMD5_HUMAN	PSMD5	physical	26344197

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 LAMC1_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-650; ASN-1107; ASN-1241AND ASN-1395, AND MASS SPECTROMETRY.	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-1107; ASN-1161; ASN-1175;ASN-1223 AND ASN-1395, AND MASS SPECTROMETRY.	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-650.	12754519 [Abstract]