MRC2_HUMAN - dbPTM
MRC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MRC2_HUMAN
UniProt AC Q9UBG0
Protein Name C-type mannose receptor 2
Gene Name MRC2
Organism Homo sapiens (Human).
Sequence Length 1479
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description May play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. Internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. May be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. May contribute to cellular uptake, remodeling and degradation of extracellular collagen matrices. May play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. May participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs)..
Protein Sequence MGPGRPAPAPWPRHLLRCVLLLGCLHLGRPGAPGDAALPEPNVFLIFSHGLQGCLEAQGGQVRVTPACNTSLPAQRWKWVSRNRLFNLGTMQCLGTGWPGTNTTASLGMYECDREALNLRWHCRTLGDQLSLLLGARTSNISKPGTLERGDQTRSGQWRIYGSEEDLCALPYHEVYTIQGNSHGKPCTIPFKYDNQWFHGCTSTGREDGHLWCATTQDYGKDERWGFCPIKSNDCETFWDKDQLTDSCYQFNFQSTLSWREAWASCEQQGADLLSITEIHEQTYINGLLTGYSSTLWIGLNDLDTSGGWQWSDNSPLKYLNWESDQPDNPSEENCGVIRTESSGGWQNRDCSIALPYVCKKKPNATAEPTPPDRWANVKVECEPSWQPFQGHCYRLQAEKRSWQESKKACLRGGGDLVSIHSMAELEFITKQIKQEVEELWIGLNDLKLQMNFEWSDGSLVSFTHWHPFEPNNFRDSLEDCVTIWGPEGRWNDSPCNQSLPSICKKAGQLSQGAAEEDHGCRKGWTWHSPSCYWLGEDQVTYSEARRLCTDHGSQLVTITNRFEQAFVSSLIYNWEGEYFWTALQDLNSTGSFFWLSGDEVMYTHWNRDQPGYSRGGCVALATGSAMGLWEVKNCTSFRARYICRQSLGTPVTPELPGPDPTPSLTGSCPQGWASDTKLRYCYKVFSSERLQDKKSWVQAQGACQELGAQLLSLASYEEEHFVANMLNKIFGESEPEIHEQHWFWIGLNRRDPRGGQSWRWSDGVGFSYHNFDRSRHDDDDIRGCAVLDLASLQWVAMQCDTQLDWICKIPRGTDVREPDDSPQGRREWLRFQEAEYKFFEHHSTWAQAQRICTWFQAELTSVHSQAELDFLSHNLQKFSRAQEQHWWIGLHTSESDGRFRWTDGSIINFISWAPGKPRPVGKDKKCVYMTASREDWGDQRCLTALPYICKRSNVTKETQPPDLPTTALGGCPSDWIQFLNKCFQVQGQEPQSRVKWSEAQFSCEQQEAQLVTITNPLEQAFITASLPNVTFDLWIGLHASQRDFQWVEQEPLMYANWAPGEPSGPSPAPSGNKPTSCAVVLHSPSAHFTGRWDDRSCTEETHGFICQKGTDPSLSPSPAALPPAPGTELSYLNGTFRLLQKPLRWHDALLLCESRNASLAYVPDPYTQAFLTQAARGLRTPLWIGLAGEEGSRRYSWVSEEPLNYVGWQDGEPQQPGGCTYVDVDGAWRTTSCDTKLQGAVCGVSSGPPPPRRISYHGSCPQGLADSAWIPFREHCYSFHMELLLGHKEARQRCQRAGGAVLSILDEMENVFVWEHLQSYEGQSRGAWLGMNFNPKGGTLVWQDNTAVNYSNWGPPGLGPSMLSHNSCYWIQSNSGLWRPGACTNITMGVVCKLPRAEQSSFSPSALPENPAALVVVLMAVLLLLALLTAALILYRRRQSIERGAFEGARYSRSSSSPTEATEKNILVSDMEMNEQQE
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
69N-linked_GlycosylationVRVTPACNTSLPAQR
EEEECCCCCCCCHHH		34.5119139490
131PhosphorylationRTLGDQLSLLLGART
CHHHHHHHHHHCCCC		16.02-
138PhosphorylationSLLLGARTSNISKPG
HHHHCCCCCCCCCCC		26.12-
139PhosphorylationLLLGARTSNISKPGT
HHHCCCCCCCCCCCC		26.98-
140N-linked_GlycosylationLLGARTSNISKPGTL
HHCCCCCCCCCCCCC		41.77UniProtKB CARBOHYD
142PhosphorylationGARTSNISKPGTLER
CCCCCCCCCCCCCCC		36.73-
146PhosphorylationSNISKPGTLERGDQT
CCCCCCCCCCCCCCC		33.69-
258PhosphorylationFNFQSTLSWREAWAS
CCCHHCCCHHHHHHH		24.9524719451
364N-linked_GlycosylationYVCKKKPNATAEPTP
EEECCCCCCCCCCCC		59.82UniProtKB CARBOHYD
370O-linked_GlycosylationPNATAEPTPPDRWAN
CCCCCCCCCCCCCCC		38.6755825519
496S-palmitoylationGRWNDSPCNQSLPSI
CCCCCCCCCCCHHHH		9.3029575903
504S-palmitoylationNQSLPSICKKAGQLS
CCCHHHHHHHHCCCC		4.3129575903
506UbiquitinationSLPSICKKAGQLSQG
CHHHHHHHHCCCCCC		54.0329967540
588N-linked_GlycosylationWTALQDLNSTGSFFW
EEEHHHHCCCCCEEE		45.90UniProtKB CARBOHYD
650O-linked_GlycosylationICRQSLGTPVTPELP
HHHHCCCCCCCCCCC		21.63OGP
662O-linked_GlycosylationELPGPDPTPSLTGSC
CCCCCCCCCCCCCCC		32.65OGP
687PhosphorylationRYCYKVFSSERLQDK
HHEEEECCCHHHCCC		33.9930631047
688PhosphorylationYCYKVFSSERLQDKK
HEEEECCCHHHCCCC		18.4430631047
944PhosphorylationWGDQRCLTALPYICK
HCCCHHHHHHHHHHH		29.7630631047
954N-linked_GlycosylationPYICKRSNVTKETQP
HHHHHHCCCCCCCCC		49.89UniProtKB CARBOHYD
957UbiquitinationCKRSNVTKETQPPDL
HHHCCCCCCCCCCCC		55.2521963094
966O-linked_GlycosylationTQPPDLPTTALGGCP
CCCCCCCCCCCCCCC		31.81OGP
1029N-linked_GlycosylationFITASLPNVTFDLWI
HHHCCCCCEEEEEEE		51.24UniProtKB CARBOHYD
1084O-linked_GlycosylationSCAVVLHSPSAHFTG
EEEEEEECCCCCCCC		19.18OGP
1097PhosphorylationTGRWDDRSCTEETHG
CCCCCCCCCCCCEEC		32.1730631047
1142UbiquitinationGTFRLLQKPLRWHDA
HHHHCCCCCCCHHHH		46.09-
1142SumoylationGTFRLLQKPLRWHDA
HHHHCCCCCCCHHHH		46.09-
1142SumoylationGTFRLLQKPLRWHDA
HHHHCCCCCCCHHHH		46.09-
1155PhosphorylationDALLLCESRNASLAY
HHEEEECCCCCCEEE		29.8229978859
1159PhosphorylationLCESRNASLAYVPDP
EECCCCCCEEECCCH		19.6529978859
1162PhosphorylationSRNASLAYVPDPYTQ
CCCCCEEECCCHHHH		20.1529978859
1167PhosphorylationLAYVPDPYTQAFLTQ
EEECCCHHHHHHHHH		20.9029978859
1168PhosphorylationAYVPDPYTQAFLTQA
EECCCHHHHHHHHHH		20.8629978859
1173PhosphorylationPYTQAFLTQAARGLR
HHHHHHHHHHHHCCC		15.0929978859
1232PhosphorylationVDGAWRTTSCDTKLQ
CCCCEEECCCCCCCC		20.84-
1233PhosphorylationDGAWRTTSCDTKLQG
CCCEEECCCCCCCCC		14.91-
1237UbiquitinationRTTSCDTKLQGAVCG
EECCCCCCCCCCCCC		26.0921963094
1350N-linked_GlycosylationWQDNTAVNYSNWGPP
EECCCCEECCCCCCC		31.86UniProtKB CARBOHYD
1394UbiquitinationITMGVVCKLPRAEQS
EEEEEEEECCCHHHC		50.3323503661
1441PhosphorylationILYRRRQSIERGAFE
HHHHHHHHHHCCCCC		25.3029449344
1452PhosphorylationGAFEGARYSRSSSSP
CCCCCCCCCCCCCCC		14.1126657352
1453PhosphorylationAFEGARYSRSSSSPT
CCCCCCCCCCCCCCC		21.8222617229
1455PhosphorylationEGARYSRSSSSPTEA
CCCCCCCCCCCCCHH		28.7325463755
1456PhosphorylationGARYSRSSSSPTEAT
CCCCCCCCCCCCHHH		33.4525463755
1457PhosphorylationARYSRSSSSPTEATE
CCCCCCCCCCCHHHH		41.4029255136
1458PhosphorylationRYSRSSSSPTEATEK
CCCCCCCCCCHHHHH		37.4829255136
1460PhosphorylationSRSSSSPTEATEKNI
CCCCCCCCHHHHHCE		39.9520363803
1463PhosphorylationSSSPTEATEKNILVS
CCCCCHHHHHCEEEE		41.0629978859
1465UbiquitinationSPTEATEKNILVSDM
CCCHHHHHCEEEEEC		44.9521906983
1470PhosphorylationTEKNILVSDMEMNEQ
HHHCEEEEECCCHHC		28.0029514088
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 MRC2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MRC2_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 MRC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MRC2_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 MRC2_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-69, AND MASS SPECTROMETRY.

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