MSRE_HUMAN - dbPTM
MSRE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MSRE_HUMAN
UniProt AC P21757
Protein Name Macrophage scavenger receptor types I and II
Gene Name MSR1
Organism Homo sapiens (Human).
Sequence Length 451
Subcellular Localization Membrane
Single-pass type II membrane protein.
Protein Description Membrane glycoproteins implicated in the pathologic deposition of cholesterol in arterial walls during atherogenesis. Two types of receptor subunits exist. These receptors mediate the endocytosis of a diverse group of macromolecules, including modified low density lipoproteins (LDL). [PubMed: 2251254 Isoform III does not internalize acetylated LDL]
Protein Sequence MEQWDHFHNQQEDTDSCSESVKFDARSMTALLPPNPKNSPSLQEKLKSFKAALIALYLLVFAVLIPLIGIVAAQLLKWETKNCSVSSTNANDITQSLTGKGNDSEEEMRFQEVFMEHMSNMEKRIQHILDMEANLMDTEHFQNFSMTTDQRFNDILLQLSTLFSSVQGHGNAIDEISKSLISLNTTLLDLQLNIENLNGKIQENTFKQQEEISKLEERVYNVSAEIMAMKEEQVHLEQEIKGEVKVLNNITNDLRLKDWEHSQTLRNITLIQGPPGPPGEKGDRGPTGESGPRGFPGPIGPPGLKGDRGAIGFPGSRGLPGYAGRPGNSGPKGQKGEKGSGNTLTPFTKVRLVGGSGPHEGRVEILHSGQWGTICDDRWEVRVGQVVCRSLGYPGVQAVHKAAHFGQGTGPIWLNEVFCFGRESSIEECKIRQWGTRACSHSEDAGVTCTL
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
14PhosphorylationFHNQQEDTDSCSESV
CCCCCCCCCCCCHHH
29.1227486199
16PhosphorylationNQQEDTDSCSESVKF
CCCCCCCCCCHHHEE
22.9527486199
18PhosphorylationQEDTDSCSESVKFDA
CCCCCCCCHHHEEEC
36.5428857561
20PhosphorylationDTDSCSESVKFDARS
CCCCCCHHHEEECHH
17.8327486199
27PhosphorylationSVKFDARSMTALLPP
HHEEECHHCCCCCCC
23.3926657352
29PhosphorylationKFDARSMTALLPPNP
EEECHHCCCCCCCCC
18.5228857561
48PhosphorylationSLQEKLKSFKAALIA
HHHHHHHHHHHHHHH
42.2724719451
82N-linked_GlycosylationLLKWETKNCSVSSTN
HHHHHHCCCCCCCCC
30.62UniProtKB CARBOHYD
102N-linked_GlycosylationQSLTGKGNDSEEEMR
HHHCCCCCCCHHHHH
53.79UniProtKB CARBOHYD
104PhosphorylationLTGKGNDSEEEMRFQ
HCCCCCCCHHHHHHH
51.4028857561
143N-linked_GlycosylationMDTEHFQNFSMTTDQ
CCCHHHHHCCCCCHH
29.98UniProtKB CARBOHYD
184N-linked_GlycosylationSKSLISLNTTLLDLQ
HHHHHHHCHHHHHHH
24.99UniProtKB CARBOHYD
221N-linked_GlycosylationKLEERVYNVSAEIMA
HHHHHHHHHCHHHHH
20.5719159218
245MethylationQEIKGEVKVLNNITN
HHHHHHHEHHHHCCC
36.3823644510
249N-linked_GlycosylationGEVKVLNNITNDLRL
HHHEHHHHCCCCCCC
38.00UniProtKB CARBOHYD
251PhosphorylationVKVLNNITNDLRLKD
HEHHHHCCCCCCCCC
25.46-
267N-linked_GlycosylationEHSQTLRNITLIQGP
CCCHHCCCEEEEECC
34.41UniProtKB CARBOHYD
424PhosphorylationVFCFGRESSIEECKI
EEEECCCCCHHHHHH
34.9429396449
425PhosphorylationFCFGRESSIEECKIR
EEECCCCCHHHHHHH
29.3029396449

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 MSRE_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MSRE_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 MSRE_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRAF6_HUMANTRAF6physical
21460221
NKG7_HUMANNKG7physical
25416956
MALL_HUMANMALLphysical
25416956
LERL1_HUMANLEPROTL1physical
25416956
SC22A_HUMANSEC22Aphysical
25416956
IKIP_HUMANIKBIPphysical
28514442
CO4A2_HUMANCOL4A2physical
28514442
GT252_HUMANCOLGALT2physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
176807Prostate cancer (PC)
614266Barrett esophagus (BE)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MSRE_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-221, AND MASSSPECTROMETRY.

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