LAMB3_HUMAN - dbPTM
LAMB3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LAMB3_HUMAN
UniProt AC Q13751
Protein Name Laminin subunit beta-3
Gene Name LAMB3
Organism Homo sapiens (Human).
Sequence Length 1172
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 MRPFFLLCFALPGLLHAQQACSRGACYPPVGDLLVGRTRFLRASSTCGLTKPETYCTQYGEWQMKCCKCDSRQPHNYYSHRVENVASSSGPMRWWQSQNDVNPVSLQLDLDRRFQLQEVMMEFQGPMPAGMLIERSSDFGKTWRVYQYLAADCTSTFPRVRQGRPQSWQDVRCQSLPQRPNARLNGGKVQLNLMDLVSGIPATQSQKIQEVGEITNLRVNFTRLAPVPQRGYHPPSAYYAVSQLRLQGSCFCHGHADRCAPKPGASAGPSTAVQVHDVCVCQHNTAGPNCERCAPFYNNRPWRPAEGQDAHECQRCDCNGHSETCHFDPAVFAASQGAYGGVCDNCRDHTEGKNCERCQLHYFRNRRPGASIQETCISCECDPDGAVPGAPCDPVTGQCVCKEHVQGERCDLCKPGFTGLTYANPQGCHRCDCNILGSRRDMPCDEESGRCLCLPNVVGPKCDQCAPYHWKLASGQGCEPCACDPHNSLSPQCNQFTGQCPCREGFGGLMCSAAAIRQCPDRTYGDVATGCRACDCDFRGTEGPGCDKASGRCLCRPGLTGPRCDQCQRGYCNRYPVCVACHPCFQTYDADLREQALRFGRLRNATASLWSGPGLEDRGLASRILDAKSKIEQIRAVLSSPAVTEQEVAQVASAILSLRRTLQGLQLDLPLEEETLSLPRDLESLDRSFNGLLTMYQRKREQFEKISSADPSGAFRMLSTAYEQSAQAAQQVSDSSRLLDQLRDSRREAERLVRQAGGGGGTGSPKLVALRLEMSSLPDLTPTFNKLCGNSRQMACTPISCPGELCPQDNGTACGSRCRGVLPRAGGAFLMAGQVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEDVRRTRLLIQQVRDFLTDPDTDAATIQEVSEAVLALWLPTDSATVLQKMNEIQAIAARLPNVDLVLSQTKQDIARARRLQAEAEEARSRAHAVEGQVEDVVGNLRQGTVALQEAQDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQQGAEAVQAQQLAEGASEQALSAQEGFERIKQKYAELKDRLGQSSMLGEQGARIQSVKTEAEELFGETMEMMDRMKDMELELLRGSQAIMLRSADLTGLEKRVEQIRDHINGRVLYYATCK
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
44PhosphorylationRTRFLRASSTCGLTK
CCCCHHHHCCCCCCC		21.5327282143
51UbiquitinationSSTCGLTKPETYCTQ
HCCCCCCCCCCEECH		45.99-
65UbiquitinationQYGEWQMKCCKCDSR
HHCCEEEEEECCCCC		22.75-
136PhosphorylationAGMLIERSSDFGKTW
CCCEEEECCCCCCHH		22.8228270605
137PhosphorylationGMLIERSSDFGKTWR
CCEEEECCCCCCHHH		43.0828270605
141UbiquitinationERSSDFGKTWRVYQY
EECCCCCCHHHHHHH		44.9321906983
142PhosphorylationRSSDFGKTWRVYQYL
ECCCCCCHHHHHHHH		20.9128270605
188UbiquitinationNARLNGGKVQLNLMD
CCCCCCCEEEEEHHH		28.3621906983
207UbiquitinationIPATQSQKIQEVGEI
CCCCCCHHHHHHHCE		52.16-
220N-linked_GlycosylationEITNLRVNFTRLAPV
CEEEEEEEEEEEECC		26.58UniProtKB CARBOHYD
402UbiquitinationVTGQCVCKEHVQGER
CCCCEEECHHHCCCC		30.38-
414UbiquitinationGERCDLCKPGFTGLT
CCCCCCCCCCCCCCC		56.31-
604N-linked_GlycosylationLRFGRLRNATASLWS
HHHCHHHHHCHHCCC		46.35UniProtKB CARBOHYD
677PhosphorylationPLEEETLSLPRDLES
CCCCCCCCCCCCHHH		43.6924719451
705SumoylationRKREQFEKISSADPS
HHHHHHHHHHCCCCC		49.53-
705SumoylationRKREQFEKISSADPS
HHHHHHHHHHCCCCC		49.53-
705UbiquitinationRKREQFEKISSADPS
HHHHHHHHHHCCCCC		49.5321906983
712O-linked_GlycosylationKISSADPSGAFRMLS
HHHCCCCCHHHHHHH		43.2155832779
766UbiquitinationGGGTGSPKLVALRLE
CCCCCCHHHHHHHHH		58.2421906983
786UbiquitinationDLTPTFNKLCGNSRQ
CCCHHHHHHHCCCCC		40.75-
791PhosphorylationFNKLCGNSRQMACTP
HHHHHCCCCCCEECC		14.79-
810N-linked_GlycosylationGELCPQDNGTACGSR
CCCCCCCCCCCCCHH		44.46UniProtKB CARBOHYD
812PhosphorylationLCPQDNGTACGSRCR
CCCCCCCCCCCHHCC		25.65-
816PhosphorylationDNGTACGSRCRGVLP
CCCCCCCHHCCCCCC		28.26-
831SulfoxidationRAGGAFLMAGQVAEQ
CCCCCCHHHHHHHHH		2.9628465586
866PhosphorylationSASQIQSSAQRLETQ
HHHHHHHHHHHHHHH		16.4330576142
950PhosphorylationPNVDLVLSQTKQDIA
CCHHEEEECCHHHHH		28.4625599653
953UbiquitinationDLVLSQTKQDIARAR
HEEEECCHHHHHHHH		38.0321906983
971PhosphorylationAEAEEARSRAHAVEG
HHHHHHHHHHHHHHC		40.65-
1004PhosphorylationAQDTMQGTSRSLRLI
HHHHHCCCHHHHHHH		12.2228842319
1027UbiquitinationQVLRPAEKLVTSMTK
HHHHHHHHHHHHHHH		50.82-
1034UbiquitinationKLVTSMTKQLGDFWT
HHHHHHHHHHHHHHH		34.58-
1084UbiquitinationGFERIKQKYAELKDR
HHHHHHHHHHHHHHH		41.23-
1089UbiquitinationKQKYAELKDRLGQSS
HHHHHHHHHHHCCCH		32.10-
1096PhosphorylationKDRLGQSSMLGEQGA
HHHHCCCHHHHHHCH		15.3320068231
1109SumoylationGARIQSVKTEAEELF
CHHHHHHHHHHHHHH		45.99-
1109UbiquitinationGARIQSVKTEAEELF
CHHHHHHHHHHHHHH		45.99-
1109SumoylationGARIQSVKTEAEELF
CHHHHHHHHHHHHHH		45.99-
1127MethylationMEMMDRMKDMELELL
HHHHHHHHHHHHHHH		55.61-
1127TrimethylationMEMMDRMKDMELELL
HHHHHHHHHHHHHHH		55.61-
1152UbiquitinationADLTGLEKRVEQIRD
CCCCCHHHHHHHHHH		67.7821906983
1167PhosphorylationHINGRVLYYATCK--
HHCCEEEEEEECC--		6.5421406692
1168PhosphorylationINGRVLYYATCK---
HCCEEEEEEECC---		7.4121406692
1170PhosphorylationGRVLYYATCK-----
CEEEEEEECC-----		12.5220068231
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 LAMB3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LAMB3_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 LAMB3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ABCA2_HUMANABCA2physical
26496610
CH60_HUMANHSPD1physical
26496610
ICT1_HUMANICT1physical
26496610
LG3BP_HUMANLGALS3BPphysical
26496610
STX3_HUMANSTX3physical
26496610
TOP1_HUMANTOP1physical
26496610
MED14_HUMANMED14physical
26496610
BAG2_HUMANBAG2physical
26496610
SNR27_HUMANSNRNP27physical
26496610
U2AF2_HUMANU2AF2physical
26496610
ATX10_HUMANATXN10physical
26496610
TIDC1_HUMANTIMMDC1physical
26496610
SFXN3_HUMANSFXN3physical
26496610
SCMC2_HUMANSLC25A25physical
26496610
TMTC3_HUMANTMTC3physical
26496610
LAMA1_HUMANLAMA1physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
226700Epidermolysis bullosa, junctional, Herlitz type (H-JEB)
226650Generalized atrophic benign epidermolysis bullosa (GABEB)
104530Amelogenesis imperfecta 1A (AI1A)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LAMB3_HUMAN

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Related Literatures of Post-Translational Modification

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