| UniProt ID | LAMC3_HUMAN | |
|---|---|---|
| UniProt AC | Q9Y6N6 | |
| Protein Name | Laminin subunit gamma-3 | |
| Gene Name | LAMC3 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 1575 | |
| 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 | MAAAALLLGLALLAPRAAGAGMGACYDGAGRPQRCLPVFENAAFGRLAQASHTCGSPPEDFCPHVGAAGAGAHCQRCDAADPQRHHNASYLTDFHSQDESTWWQSPSMAFGVQYPTSVNITLRLGKAYEITYVRLKFHTSRPESFAIYKRSRADGPWEPYQFYSASCQKTYGRPEGQYLRPGEDERVAFCTSEFSDISPLSGGNVAFSTLEGRPSAYNFEESPGLQEWVTSTELLISLDRLNTFGDDIFKDPKVLQSYYYAVSDFSVGGRCKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFFQDRPWARGTAEAAHECLPCNCSGRSEECTFDRELFRSTGHGGRCHHCRDHTAGPHCERCQENFYHWDPRMPCQPCDCQSAGSLHLQCDDTGTCACKPTVTGWKCDRCLPGFHSLSEGGCRPCTCNPAGSLDTCDPRSGRCPCKENVEGNLCDRCRPGTFNLQPHNPAGCSSCFCYGHSKVCASTAQFQVHHILSDFHQGAEGWWARSVGGSEHPPQWSPNGVLLSPEDEEELTAPEKFLGDQRFSYGQPLILTFRVPPGDSPLPVQLRLEGTGLALSLRHSSLSGPQDAGHPREVELRFHLQETSEDVAPPLPPFHFQRLLANLTSLRLRVSPGPSPAGPVFLTEVRLTSARPGLSPPASWVEICSCPTGYTGQFCESCAPGYKREMPQGGPYASCVPCTCNQHGTCDPNTGICVCSHHTEGPSCERCLPGFYGNPFAGQADDCQPCPCPGQSACTTIPESREVVCTHCPPGQRGRRCEVCDDGFFGDPLGLFGHPQPCHQCQCSGNVDPNAVGNCDPLSGHCLRCLHNTTGDHCEHCQEGFYGSALAPRPADKCMPCSCHPQGSVSEQMPCDPVTGQCSCLPHVTARDCSRCYPGFFDLQPGRGCRSCKCHPLGSQEDQCHPKTGQCTCRPGVTGQACDRCQLGFFGFSIKGCRACRCSPLGAASAQCHENGTCVCRPGFEGYKCDRCHDNFFLTADGTHCQQCPSCYALVKEEAAKLKARLTLTEGWLQGSDCGSPWGPLDILLGEAPRGDVYQGHHLLPGAREAFLEQMMSLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEIPQEGPSQPTKWSHLATEARALARSHRDTATKIAATAWRALLASNTSYALLWNLLEGRVALETQRDLEDRYQEVQAAQKALRTAVAEVLPEAESVLATVQQVGADTAPYLALLASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTKLHQEARAALTQASSSVQAATVTVMGARTLLADLEGMKLQFPRPKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQLGSPGSLQRKLSLLEQESQQQELQIQGFESDLAEIRADKQNLEAILHSLPENCASWQ | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 87 | N-linked_Glycosylation | ADPQRHHNASYLTDF CCCCCCCCCCHHCCC | 25.18 | UniProtKB CARBOHYD | |
| 119 | N-linked_Glycosylation | VQYPTSVNITLRLGK CCCCCEEEEEEECCC | 22.69 | UniProtKB CARBOHYD | |
| 121 | Phosphorylation | YPTSVNITLRLGKAY CCCEEEEEEECCCEE | 10.71 | 24719451 | |
| 139 | Phosphorylation | YVRLKFHTSRPESFA EEEEEEECCCCCCEE | 29.57 | 20068231 | |
| 140 | Phosphorylation | VRLKFHTSRPESFAI EEEEEECCCCCCEEE | 36.95 | 20068231 | |
| 144 | Phosphorylation | FHTSRPESFAIYKRS EECCCCCCEEEEEEC | 23.74 | 20068231 | |
| 148 | Phosphorylation | RPESFAIYKRSRADG CCCCEEEEEECCCCC | 9.27 | 20068231 | |
| 149 | Ubiquitination | PESFAIYKRSRADGP CCCEEEEEECCCCCC | 37.47 | - | |
| 151 | Phosphorylation | SFAIYKRSRADGPWE CEEEEEECCCCCCCC | 27.89 | - | |
| 160 | Phosphorylation | ADGPWEPYQFYSASC CCCCCCCCEEEECCC | 10.35 | - | |
| 295 | N-linked_Glycosylation | LACRCQHNTTGTDCE HHHHCCCCCCCCCHH | 17.29 | UniProtKB CARBOHYD | |
| 328 | N-linked_Glycosylation | AHECLPCNCSGRSEE HHHHCCCCCCCCCCC | 22.50 | UniProtKB CARBOHYD | |
| 585 | Phosphorylation | EGTGLALSLRHSSLS ECCCEEEEEHHHHCC | 20.11 | 24719451 | |
| 631 | N-linked_Glycosylation | HFQRLLANLTSLRLR HHHHHHHHHHHCEEE | 43.77 | UniProtKB CARBOHYD | |
| 837 | N-linked_Glycosylation | HCLRCLHNTTGDHCE CHHHHHCCCCCCCCH | 26.79 | UniProtKB CARBOHYD | |
| 980 | N-linked_Glycosylation | ASAQCHENGTCVCRP CCCEECCCCCEEECC | 27.66 | UniProtKB CARBOHYD | |
| 1082 | Phosphorylation | AFLEQMMSLEGAVKA HHHHHHHHHHHHHHH | 20.23 | 29978859 | |
| 1185 | N-linked_Glycosylation | WRALLASNTSYALLW HHHHHHCCHHHHHHH | 27.69 | UniProtKB CARBOHYD | |
| 1278 | Phosphorylation | KAKALEKTVASWQHM HHHHHHHHHHHHHHH | 16.36 | - | |
| 1281 | Phosphorylation | ALEKTVASWQHMATE HHHHHHHHHHHHHHH | 23.96 | - | |
| 1287 | Phosphorylation | ASWQHMATEAARTLQ HHHHHHHHHHHHHHH | 20.69 | - | |
| 1300 | Phosphorylation | LQTAAQATLRQTEPL HHHHHHHHHHCCCCH | 15.47 | 22210691 | |
| 1351 | Methylation | GMKLQFPRPKDQAAL CCCCCCCCHHHHHHH | 52.79 | 115389629 | |
| 1413 | Sumoylation | KDSAKLAKALLRERK HHHHHHHHHHHHHHH | 50.43 | - | |
| 1413 | Sumoylation | KDSAKLAKALLRERK HHHHHHHHHHHHHHH | 50.43 | - | |
| 1465 | Phosphorylation | ERVGAGLSEMEQQIR HHHCCCHHHHHHHHH | 33.70 | 22468782 | |
| 1521 | Phosphorylation | RLRLQLGSPGSLQRK HHHHHHCCCHHHHHH | 34.38 | 30177828 | |
| 1524 | Phosphorylation | LQLGSPGSLQRKLSL HHHCCCHHHHHHHHH | 25.39 | 30177828 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of LAMC3_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LAMC3_HUMAN !! | ||||||
* 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 LAMC3_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RL35_HUMAN | RPL35 | physical | 21988832 | |
| S43A3_HUMAN | SLC43A3 | physical | 21988832 | |
| TRFE_HUMAN | TF | physical | 21988832 | |
| AACT_HUMAN | SERPINA3 | physical | 21988832 | |
| LGMN_HUMAN | LGMN | physical | 21988832 | |
| NR1H2_HUMAN | NR1H2 | physical | 21988832 | |
| POTE1_HUMAN | POT1 | physical | 21988832 | |
| PELI2_HUMAN | PELI2 | physical | 21988832 | |
| ZN160_HUMAN | ZNF160 | physical | 21988832 | |
| YTDC1_HUMAN | YTHDC1 | physical | 21988832 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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