LMBD2_HUMAN - dbPTM
LMBD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LMBD2_HUMAN
UniProt AC Q68DH5
Protein Name LMBR1 domain-containing protein 2
Gene Name LMBRD2
Organism Homo sapiens (Human).
Sequence Length 695
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MSGAALGLEIVFVFFLALFLLHRYGDFKKQHRLVIIGTLLAWYLCFLIVFILPLDVSTTIYNRCKHAAANSSPPENSNITGLYATANPVPSQHPCFKPWSYIPDGIMPIFWRVVYWTSQFLTWILLPFMQSYARSGGFSITGKIKTALIENAIYYGTYLLIFGAFLIYVAVNPHLHLEWNQLQTIGIAAANTWGLFLLVLLLGYGLVEIPRSYWNGAKRGYLLMKTYFKAAKLMTEKADAEENLEDAMEEVRKVNESIKYNHPLRKCVDTILKKCPTEYQEKMGRNMDDYEDFDEKHSIYPSEKSLVKLHKQVIYSVQRHRRTQVQWQILLEQAFYLEDVAKNETSATHQFVHTFQSPEPENRFIQYFYNPTFEWYWECLLRPWFYKILAVVLSIFSVIVVWSECTFFSTTPVLSLFAVFIQLAEKTYNYIYIEIACFLSIFFLSICVYSTVFRIRVFNYYYLASHHQTDAYSLLFSGMLFCRLTPPLCLNFLGLTHMDSSISHKNTQPTAYTSIMGSMKVLSFIADGFYIYYPMLVVILCIATYFSLGTRCLNLLGFQQFMGDDDMTSDLVNEGKELIRKEKRKRQRQEEGENRRREWKERYGHNREDSTRNRNIHTDPKESNFSDVNTNRSAFKYTRANNRTERDRIELLQDAEPLDFNAETFTDDPLESESGRYQPGGRYLSMSRSDIFNDV
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
61UbiquitinationLDVSTTIYNRCKHAA
CCHHHHHHHHHHHHH		8.4121987572
77PhosphorylationNSSPPENSNITGLYA
CCCCCCCCCCCCEEE		28.1323879269
78N-linked_GlycosylationSSPPENSNITGLYAT
CCCCCCCCCCCEEEC		47.63UniProtKB CARBOHYD
80PhosphorylationPPENSNITGLYATAN
CCCCCCCCCEEECCC		25.9423879269
83PhosphorylationNSNITGLYATANPVP
CCCCCCEEECCCCCC		11.8423879269
85O-linked_GlycosylationNITGLYATANPVPSQ
CCCCEEECCCCCCCC		17.2655835125
154PhosphorylationALIENAIYYGTYLLI
HHHHCHHHHHHHHHH		8.07-
155PhosphorylationLIENAIYYGTYLLIF
HHHCHHHHHHHHHHH		9.25-
253UbiquitinationDAMEEVRKVNESIKY
HHHHHHHHHHHHHCC		55.3729967540
259UbiquitinationRKVNESIKYNHPLRK
HHHHHHHCCCCHHHH		49.6429967540
266UbiquitinationKYNHPLRKCVDTILK
CCCCHHHHHHHHHHH		46.4229967540
273UbiquitinationKCVDTILKKCPTEYQ
HHHHHHHHHCCHHHH		48.7832015554
282UbiquitinationCPTEYQEKMGRNMDD
CCHHHHHHHCCCCCC		31.0033845483
290PhosphorylationMGRNMDDYEDFDEKH
HCCCCCCCCCCHHHC		17.0921945579
296UbiquitinationDYEDFDEKHSIYPSE
CCCCCHHHCCCCCCH		44.4932015554
308UbiquitinationPSEKSLVKLHKQVIY
CCHHHHHHHHHHHHH		50.6029967540
451PhosphorylationLSICVYSTVFRIRVF
HHHHHHHHHHHHHHH		13.1324719451
552S-palmitoylationYFSLGTRCLNLLGFQ
HHHHHHHHHHHHCHH		2.7229575903
603PhosphorylationRREWKERYGHNREDS
HHHHHHHHCCCCCCC		24.67-
610PhosphorylationYGHNREDSTRNRNIH
HCCCCCCCCCCCCCC		25.2322817900
611PhosphorylationGHNREDSTRNRNIHT
CCCCCCCCCCCCCCC		44.2629449344
618PhosphorylationTRNRNIHTDPKESNF
CCCCCCCCCCCCCCC		50.6417192257
621UbiquitinationRNIHTDPKESNFSDV
CCCCCCCCCCCCCCC		76.2829967540
626PhosphorylationDPKESNFSDVNTNRS
CCCCCCCCCCCCCCH		44.9223186163
630PhosphorylationSNFSDVNTNRSAFKY
CCCCCCCCCCHHHHH		31.6825159151
633PhosphorylationSDVNTNRSAFKYTRA
CCCCCCCHHHHHHHC		39.8825159151
636UbiquitinationNTNRSAFKYTRANNR
CCCCHHHHHHHCCCC		45.4929967540
637PhosphorylationTNRSAFKYTRANNRT
CCCHHHHHHHCCCCC		8.59-
672PhosphorylationFTDDPLESESGRYQP
CCCCCCCCCCCCCCC		44.75-
677PhosphorylationLESESGRYQPGGRYL
CCCCCCCCCCCCCEE		23.68-
683PhosphorylationRYQPGGRYLSMSRSD
CCCCCCCEECCCHHH		13.3523403867
685PhosphorylationQPGGRYLSMSRSDIF
CCCCCEECCCHHHHC		13.0422617229
687PhosphorylationGGRYLSMSRSDIFND
CCCEECCCHHHHCCC		25.8422617229
689PhosphorylationRYLSMSRSDIFNDV-
CEECCCHHHHCCCC-		27.9622617229
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 LMBD2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LMBD2_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 LMBD2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LMBD2_HUMAN !!
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 LMBD2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-618, AND MASSSPECTROMETRY.

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