LAMA4_HUMAN - dbPTM
LAMA4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LAMA4_HUMAN
UniProt AC Q16363
Protein Name Laminin subunit alpha-4
Gene Name LAMA4
Organism Homo sapiens (Human).
Sequence Length 1823
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..
Protein Sequence MALSSAWRSVLPLWLLWSAACSRAASGDDNAFPFDIEGSSAVGRQDPPETSEPRVALGRLPPAAEKCNAGFFHTLSGECVPCDCNGNSNECLDGSGYCVHCQRNTTGEHCEKCLDGYIGDSIRGAPQFCQPCPCPLPHLANFAESCYRKNGAVRCICNENYAGPNCERCAPGYYGNPLLIGSTCKKCDCSGNSDPNLIFEDCDEVTGQCRNCLRNTTGFKCERCAPGYYGDARIAKNCAVCNCGGGPCDSVTGECLEEGFEPPTGMDCPTISCDKCVWDLTDALRLAALSIEEGKSGVLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEEIRSRQPFFTQRELVDEEADEAYELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLGQSRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRPASNVSASIQRIRELIAQTRSVASKIQVSMMFDGQSAVEVHSRTSMDDLKAFTSLSLYMKPPVKRPELTETADQFILYLGSKNAKKEYMGLAIKNDNLVYVYNLGTKDVEIPLDSKPVSSWPAYFSIVKIERVGKHGKVFLTVPSLSSTAEEKFIKKGEFSGDDSLLDLDPEDTVFYVGGVPSNFKLPTSLNLPGFVGCLELATLNNDVISLYNFKHIYNMDPSTSVPCARDKLAFTQSRAASYFFDGSGYAVVRDITRRGKFGQVTRFDIEVRTPADNGLILLMVNGSMFFRLEMRNGYLHVFYDFGFSGGPVHLEDTLKKAQINDAKYHEISIIYHNDKKMILVVDRRHVKSMDNEKMKIPFTDIYIGGAPPEILQSRALRAHLPLDINFRGCMKGFQFQKKDFNLLEQTETLGVGYGCPEDSLISRRAYFNGQSFIASIQKISFFDGFEGGFNFRTLQPNGLLFYYASGSDVFSISLDNGTVIMDVKGIKVQSVDKQYNDGLSHFVISSVSPTRYELIVDKSRVGSKNPTKGKIEQTQASEKKFYFGGSPISAQYANFTGCISNAYFTRVDRDVEVEDFQRYTEKVHTSLYECPIESSPLFLLHKKGKNLSKPKASQNKKGGKSKDAPSWDPVALKLPERNTPRNSHCHLSNSPRAIEHAYQYGGTANSRQEFEHLKGDFGAKSQFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVIFIRERSSGRLVIDGLRVLEESLPPTEATWKIKGPIYLGGVAPGKAVKNVQINSIYSFSGCLSNLQLNGASITSASQTFSVTPCFEGPMETGTYFSTEGGYVVLDESFNIGLKFEIAFEVRPRSSSGTLVHGHSVNGEYLNVHMKNGQVIVKVNNGIRDFSTSVTPKQSLCDGRWHRITVIRDSNVVQLDVDSEVNHVVGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGHPVSFSKAALVSGAVSINSCPAA
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 Orthologous
Protein Cluster
104N-linked_GlycosylationYCVHCQRNTTGEHCE
EEEECCCCCCCCHHH		19.00UniProtKB CARBOHYD
117 (in isoform 3)Phosphorylation-11.0326503514
215N-linked_GlycosylationQCRNCLRNTTGFKCE
HHHHHHHHCCCCCCE		29.10UniProtKB CARBOHYD
264O-linked_GlycosylationEEGFEPPTGMDCPTI
HCCCCCCCCCCCCCC		56.72OGP
290PhosphorylationALRLAALSIEEGKSG
HHHHHHHHHHCCCCC		24.1927499020
296PhosphorylationLSIEEGKSGVLSVSS
HHHHCCCCCEEEECC		45.02-
300PhosphorylationEGKSGVLSVSSGAAA
CCCCCEEEECCHHHH		19.97-
303PhosphorylationSGVLSVSSGAAAHRH
CCEEEECCHHHHHHH		30.23-
315N-linked_GlycosylationHRHVNEINATIYLLK
HHHHHHHHHHEEHHH		25.50UniProtKB CARBOHYD
317PhosphorylationHVNEINATIYLLKTK
HHHHHHHHEEHHHHC		12.98-
319PhosphorylationNEINATIYLLKTKLS
HHHHHHEEHHHHCCC		11.1322817900
323PhosphorylationATIYLLKTKLSEREN
HHEEHHHHCCCHHHH		36.87-
332PhosphorylationLSERENQYALRKIQI
CCHHHHHHHHHHHHC		21.1322817900
351PhosphorylationNTMKSLLSDVEELVE
HHHHHHHHHHHHHHH		44.92-
412PhosphorylationYGEEHELSPKEISEK
CCCCCCCCHHHHHHH		30.8228111955
465N-linked_GlycosylationESWQRLHNETRTLFP
HHHHHHHHHHHHHHH		57.85UniProtKB CARBOHYD
531N-linked_GlycosylationREQMEVVNMSLSTSA
HHHHHHHHHHHCCCC		21.36UniProtKB CARBOHYD
542PhosphorylationSTSADSLTTPRLTLS
CCCCCCCCCCCCCHH		38.4124719451
557N-linked_GlycosylationELDDIIKNASGIYAE
HHHHHHHHCCCEEEE		29.0019159218
578N-linked_GlycosylationELQVKLSNLSNLSHD
HHHHHHHHHHCCCHH		58.9019159218
581N-linked_GlycosylationVKLSNLSNLSHDLVQ
HHHHHHHCCCHHHHH		49.0519159218
610PhosphorylationELSRKLHSSDMNGLV
HHHHHHHHCCHHHHH		38.1729083192
611PhosphorylationLSRKLHSSDMNGLVQ
HHHHHHHCCHHHHHH		30.0829083192
638N-linked_GlycosylationVNYVSEANETAEFAL
HHHHHHCCHHHHHHH		43.00UniProtKB CARBOHYD
646N-linked_GlycosylationETAEFALNTTDRIYD
HHHHHHHCCCCHHHH		37.19UniProtKB CARBOHYD
734PhosphorylationAQQRLGQSRLITEEA
HHHHHHHHHHHHHHH		27.5326074081
742N-linked_GlycosylationRLITEEANRTTMEVQ
HHHHHHHHHHHHHHH		45.1519159218
744PhosphorylationITEEANRTTMEVQQA
HHHHHHHHHHHHHHH		30.2422210691
758N-linked_GlycosylationATAPMANNLTNWSQN
HHHCCCCCCCCHHHH		38.41UniProtKB CARBOHYD
760PhosphorylationAPMANNLTNWSQNLQ
HCCCCCCCCHHHHHH		36.4422210691
761N-linked_GlycosylationPMANNLTNWSQNLQH
CCCCCCCCHHHHHHH		39.30UniProtKB CARBOHYD
780PhosphorylationAYNTAVNSARDAVRN
HHHHHHHHHHHHHHH		20.3422210691
787N-linked_GlycosylationSARDAVRNLTEVVPQ
HHHHHHHHHHHHHHH		44.7219159218
810N-linked_GlycosylationEQKRPASNVSASIQR
HHHCCCCCCHHHHHH		33.5919159218
851PhosphorylationVEVHSRTSMDDLKAF
EEEECCCCHHHHHHH		21.0724719451
859PhosphorylationMDDLKAFTSLSLYMK
HHHHHHHHEEHHCCC		33.3524719451
862PhosphorylationLKAFTSLSLYMKPPV
HHHHHEEHHCCCCCC		19.7424719451
894PhosphorylationSKNAKKEYMGLAIKN
CCCCCCCEEEEEEEC		12.8322817900
925PhosphorylationPLDSKPVSSWPAYFS
CCCCCCCCCCCEEEE		34.9023909892
926PhosphorylationLDSKPVSSWPAYFSI
CCCCCCCCCCEEEEE		36.9923909892
930PhosphorylationPVSSWPAYFSIVKIE
CCCCCCEEEEEEEEE		8.1923909892
932PhosphorylationSSWPAYFSIVKIERV
CCCCEEEEEEEEEEE		17.5023909892
951PhosphorylationKVFLTVPSLSSTAEE
EEEEECCCCCCCHHH		36.2328857561
953PhosphorylationFLTVPSLSSTAEEKF
EEECCCCCCCHHHHH		29.9429691806
954PhosphorylationLTVPSLSSTAEEKFI
EECCCCCCCHHHHHH		36.6126657352
955PhosphorylationTVPSLSSTAEEKFIK
ECCCCCCCHHHHHHH		34.4128857561
1045PhosphorylationDKLAFTQSRAASYFF
HCCEECCHHHHHHHC		22.3422210691
1050PhosphorylationTQSRAASYFFDGSGY
CCHHHHHHHCCCCCE		11.9822210691
1081PhosphorylationRFDIEVRTPADNGLI
EEEEEEECCCCCCEE		28.18-
1093N-linked_GlycosylationGLILLMVNGSMFFRL
CEEEEEECCEEEEEE		23.90UniProtKB CARBOHYD
1143PhosphorylationYHEISIIYHNDKKMI
CEEEEEEEECCCEEE		7.9027642862
1171PhosphorylationEKMKIPFTDIYIGGA
CCCCCCCCEEEECCC		19.01-
1231PhosphorylationGYGCPEDSLISRRAY
CCCCCCCCCCCCEEE		26.4124719451
1234PhosphorylationCPEDSLISRRAYFNG
CCCCCCCCCEEECCC		22.4724719451
1288N-linked_GlycosylationVFSISLDNGTVIMDV
EEEEECCCCEEEEEE		54.02UniProtKB CARBOHYD
1307PhosphorylationVQSVDKQYNDGLSHF
EEEECCCCCCCCCCE		22.4422817900
1312PhosphorylationKQYNDGLSHFVISSV
CCCCCCCCCEEEECC		22.0222817900
1317PhosphorylationGLSHFVISSVSPTRY
CCCCEEEECCCCCEE		21.2722817900
1324PhosphorylationSSVSPTRYELIVDKS
ECCCCCEEEEEEEHH		19.9822817900
1366N-linked_GlycosylationPISAQYANFTGCISN
CCCHHHCCCCCCCCC		30.03UniProtKB CARBOHYD
1418N-linked_GlycosylationLLHKKGKNLSKPKAS
EEECCCCCCCCCCHH		59.21UniProtKB CARBOHYD
1420PhosphorylationHKKGKNLSKPKASQN
ECCCCCCCCCCHHCC		57.2024719451
1563PhosphorylationVIFIRERSSGRLVID
EEEEEECCCCCEEEE		32.18-
1578PhosphorylationGLRVLEESLPPTEAT
EEEHHHHCCCCCCCC		36.4826330541
1582PhosphorylationLEESLPPTEATWKIK
HHHCCCCCCCCEEEE		35.9926330541
1585PhosphorylationSLPPTEATWKIKGPI
CCCCCCCCEEEECCE		22.5126330541
1593PhosphorylationWKIKGPIYLGGVAPG
EEEECCEEECCCCCC		11.4817924679
1719PhosphorylationGIRDFSTSVTPKQSL
CCCCCCCCCCCCCHH		23.8524719451
1725PhosphorylationTSVTPKQSLCDGRWH
CCCCCCCHHCCCCCE		36.7724719451
1749PhosphorylationVVQLDVDSEVNHVVG
EEEEECCCCCCEECC		43.2022210691
1804PhosphorylationVIDGHPVSFSKAALV
EECCCCCCCCHHHHH		28.4024719451
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

Oops, there are no upstream regulatory protein records of LAMA4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LAMA4_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 LAMA4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSN6_HUMANCOPS6physical
16169070
PTN_HUMANPTNphysical
16169070
UBR1_HUMANUBR1physical
16169070
ZHX1_HUMANZHX1physical
16169070
BRD7_HUMANBRD7physical
16169070
MED31_HUMANMED31physical
16169070
G3P_HUMANGAPDHphysical
16169070
LRIF1_HUMANLRIF1physical
16169070
P53_HUMANTP53physical
16169070
TBB2A_HUMANTUBB2Aphysical
16169070
U119A_HUMANUNC119physical
16169070
EF1A1_HUMANEEF1A1physical
16169070
RTN4_HUMANRTN4physical
21988832
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615235Cardiomyopathy, dilated 1JJ (CMD1JJ)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LAMA4_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-557; ASN-578; ASN-581;ASN-742; ASN-787 AND ASN-810, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1593, AND MASSSPECTROMETRY.

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