LRP12_HUMAN - dbPTM
LRP12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRP12_HUMAN
UniProt AC Q9Y561
Protein Name Low-density lipoprotein receptor-related protein 12
Gene Name LRP12
Organism Homo sapiens (Human).
Sequence Length 859
Subcellular Localization Membrane
Single-pass type I membrane protein . Membrane, coated pit .
Protein Description Probable receptor, which may be involved in the internalization of lipophilic molecules and/or signal transduction. May act as a tumor suppressor..
Protein Sequence MACRWSTKESPRWRSALLLLFLAGVYGNGALAEHSENVHISGVSTACGETPEQIRAPSGIITSPGWPSEYPAKINCSWFIRANPGEIITISFQDFDIQGSRRCNLDWLTIETYKNIESYRACGSTIPPPYISSQDHIWIRFHSDDNISRKGFRLAYFSGKSEEPNCACDQFRCGNGKCIPEAWKCNNMDECGDSSDEEICAKEANPPTAAAFQPCAYNQFQCLSRFTKVYTCLPESLKCDGNIDCLDLGDEIDCDVPTCGQWLKYFYGTFNSPNYPDFYPPGSNCTWLIDTGDHRKVILRFTDFKLDGTGYGDYVKIYDGLEENPHKLLRVLTAFDSHAPLTVVSSSGQIRVHFCADKVNAARGFNATYQVDGFCLPWEIPCGGNWGCYTEQQRCDGYWHCPNGRDETNCTMCQKEEFPCSRNGVCYPRSDRCNYQNHCPNGSDEKNCFFCQPGNFHCKNNRCVFESWVCDSQDDCGDGSDEENCPVIVPTRVITAAVIGSLICGLLLVIALGCTCKLYSLRMFERRSFETQLSRVEAELLRREAPPSYGQLIAQGLIPPVEDFPVCSPNQASVLENLRLAVRSQLGFTSVRLPMAGRSSNIWNRIFNFARSRHSGSLALVSADGDEVVPSQSTSREPERNHTHRSLFSVESDDTDTENERRDMAGASGGVAAPLPQKVPPTTAVEATVGACASSSTQSTRGGHADNGRDVTSVEPPSVSPARHQLTSALSRMTQGLRWVRFTLGRSSSLSQNQSPLRQLDNGVSGREDDDDVEMLIPISDGSSDFDVNDCSRPLLDLASDQGQGLRQPYNATNPGVRPSNRDGPCERCGIVHTAQIPDTCLEVTLKNETSDDEALLLC
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
6Phosphorylation--MACRWSTKESPRW
--CCCCCCCCCCHHH		15.3924719451
7Phosphorylation-MACRWSTKESPRWR
-CCCCCCCCCCHHHH		31.6924719451
75N-linked_GlycosylationSEYPAKINCSWFIRA
CCCCCEEEEEEEEEC		17.05UniProtKB CARBOHYD
146N-linked_GlycosylationIRFHSDDNISRKGFR
EEEECCCCCCCCCEE		38.84UniProtKB CARBOHYD
160UbiquitinationRLAYFSGKSEEPNCA
EEEEECCCCCCCCCC		54.20-
208O-linked_GlycosylationAKEANPPTAAAFQPC
HHHCCCCCHHHCCCC		30.13OGP
228UbiquitinationQCLSRFTKVYTCLPE
HHHHHCCEEEECCCH		30.45-
284N-linked_GlycosylationDFYPPGSNCTWLIDT
CCCCCCCCCEEEEEC		32.90UniProtKB CARBOHYD
291PhosphorylationNCTWLIDTGDHRKVI
CCEEEEECCCCCEEE		37.2023879269
305UbiquitinationILRFTDFKLDGTGYG
EEEEECEEECCCCCC		48.77-
316UbiquitinationTGYGDYVKIYDGLEE
CCCCCEEEEECCCCC		29.35-
327UbiquitinationGLEENPHKLLRVLTA
CCCCCHHHHHHHHHH		50.93-
358UbiquitinationRVHFCADKVNAARGF
EEEEECCCCCCCCCC		20.90-
366N-linked_GlycosylationVNAARGFNATYQVDG
CCCCCCCCCEEEECC		33.91UniProtKB CARBOHYD
409N-linked_GlycosylationPNGRDETNCTMCQKE
CCCCCCCCCCCCCCC		19.74UniProtKB CARBOHYD
415UbiquitinationTNCTMCQKEEFPCSR
CCCCCCCCCCCCCCC		55.04-
430PhosphorylationNGVCYPRSDRCNYQN
CCEEECCCCCCCCCC		25.54-
432MethylationVCYPRSDRCNYQNHC
EEECCCCCCCCCCCC		16.30115389571
435PhosphorylationPRSDRCNYQNHCPNG
CCCCCCCCCCCCCCC		17.83-
441N-linked_GlycosylationNYQNHCPNGSDEKNC
CCCCCCCCCCCCCCC		68.91UniProtKB CARBOHYD
495PhosphorylationIVPTRVITAAVIGSL
ECCCHHHHHHHHHHH		13.0020166139
501PhosphorylationITAAVIGSLICGLLL
HHHHHHHHHHHHHHH		11.9320166139
515PhosphorylationLVIALGCTCKLYSLR
HHHHHHHHHHHHHHH		15.7520166139
520PhosphorylationGCTCKLYSLRMFERR
HHHHHHHHHHHHHHC		21.6724719451
531PhosphorylationFERRSFETQLSRVEA
HHHCCHHHHHHHHHH		32.5724719451
584PhosphorylationNLRLAVRSQLGFTSV
HHHHHHHHHCCCCEE		24.13-
589PhosphorylationVRSQLGFTSVRLPMA
HHHHCCCCEEECCCC		25.23-
599PhosphorylationRLPMAGRSSNIWNRI
ECCCCCCCCHHHHHH		27.1528634120
600PhosphorylationLPMAGRSSNIWNRIF
CCCCCCCCHHHHHHH		30.8628634120
615PhosphorylationNFARSRHSGSLALVS
HHHHHCCCCCEEEEE		29.0328348404
617PhosphorylationARSRHSGSLALVSAD
HHHCCCCCEEEEECC		17.3030576142
631PhosphorylationDGDEVVPSQSTSREP
CCCCCCCCCCCCCCC		25.75-
646PhosphorylationERNHTHRSLFSVESD
CCCCCCCCCEEEECC		26.6028102081
649PhosphorylationHTHRSLFSVESDDTD
CCCCCCEEEECCCCC		30.2129523821
652PhosphorylationRSLFSVESDDTDTEN
CCCEEEECCCCCCHH		38.3324114839
655PhosphorylationFSVESDDTDTENERR
EEEECCCCCCHHHHH		50.2230266825
657PhosphorylationVESDDTDTENERRDM
EECCCCCCHHHHHHH		42.6829523821
668PhosphorylationRRDMAGASGGVAAPL
HHHHCCCCCCCCCCC		34.8528555341
678UbiquitinationVAAPLPQKVPPTTAV
CCCCCCCCCCCCCCE		55.56-
718PhosphorylationVTSVEPPSVSPARHQ
CCCCCCCCCCHHHHH		46.0429255136
720PhosphorylationSVEPPSVSPARHQLT
CCCCCCCCHHHHHHH		19.7229255136
747PhosphorylationVRFTLGRSSSLSQNQ
HHHHCCCCCCCCCCC		23.6021712546
749PhosphorylationFTLGRSSSLSQNQSP
HHCCCCCCCCCCCCH		33.0321712546
751PhosphorylationLGRSSSLSQNQSPLR
CCCCCCCCCCCCHHH		29.0927251275
755PhosphorylationSSLSQNQSPLRQLDN
CCCCCCCCHHHHCCC		33.1921712546
850PhosphorylationEVTLKNETSDDEALL
EEEECCCCCCCCEEE		47.0129507054
851PhosphorylationVTLKNETSDDEALLL
EEECCCCCCCCEEEC		36.5630576142
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 LRP12_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRP12_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 LRP12_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LRP12_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 LRP12_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory