ARH_HUMAN - dbPTM
ARH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARH_HUMAN
UniProt AC Q5SW96
Protein Name Low density lipoprotein receptor adapter protein 1 {ECO:0000305}
Gene Name LDLRAP1 {ECO:0000312|HGNC:HGNC:18640}
Organism Homo sapiens (Human).
Sequence Length 308
Subcellular Localization Cytoplasm .
Protein Description Adapter protein (clathrin-associated sorting protein (CLASP)) required for efficient endocytosis of the LDL receptor (LDLR) in polarized cells such as hepatocytes and lymphocytes, but not in non-polarized cells (fibroblasts). May be required for LDL binding and internalization but not for receptor clustering in coated pits. May facilitate the endocytocis of LDLR and LDLR-LDL complexes from coated pits by stabilizing the interaction between the receptor and the structural components of the pits. May also be involved in the internalization of other LDLR family members. Binds to phosphoinositides, which regulate clathrin bud assembly at the cell surface. Required for trafficking of LRP2 to the endocytic recycling compartment which is necessary for LRP2 proteolysis, releasing a tail fragment which translocates to the nucleus and mediates transcriptional repression (By similarity)..
Protein Sequence MDALKSAGRALIRSPSLAKQSWGGGGRHRKLPENWTDTRETLLEGMLFSLKYLGMTLVEQPKGEELSAAAIKRIVATAKASGKKLQKVTLKVSPRGIILTDNLTNQLIENVSIYRISYCTADKMHDKVFAYIAQSQHNQSLECHAFLCTKRKMAQAVTLTVAQAFKVAFEFWQVSKEEKEKRDKASQEGGDVLGARQDCTPSLKSLVATGNLLDLEETAKAPLSTVSANTTNMDEVPRPQALSGSSVVWELDDGLDEAFSRLAQSRTNPQVLDTGLTAQDMHYAQCLSPVDWDKPDSSGTEQDDLFSF
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
1Acetylation-------MDALKSAG
-------CHHHHHHH
6.4922814378
5Methylation---MDALKSAGRALI
---CHHHHHHHHHHH
39.72115972471
5Ubiquitination---MDALKSAGRALI
---CHHHHHHHHHHH
39.72-
14PhosphorylationAGRALIRSPSLAKQS
HHHHHHCCHHHHCCC
16.3129255136
16PhosphorylationRALIRSPSLAKQSWG
HHHHCCHHHHCCCCC
42.0529255136
19UbiquitinationIRSPSLAKQSWGGGG
HCCHHHHCCCCCCCC
50.59-
49PhosphorylationLLEGMLFSLKYLGMT
HHHHHHHHHHHHCCE
21.7124719451
67PhosphorylationQPKGEELSAAAIKRI
CCCCHHCCHHHHHHH
21.09-
72UbiquitinationELSAAAIKRIVATAK
HCCHHHHHHHHHHHH
31.20-
79UbiquitinationKRIVATAKASGKKLQ
HHHHHHHHHCCCCEE
38.44-
81PhosphorylationIVATAKASGKKLQKV
HHHHHHHCCCCEEEE
50.9030576142
93PhosphorylationQKVTLKVSPRGIILT
EEEEEEECCCEEEEE
13.8023917254
184UbiquitinationEEKEKRDKASQEGGD
HHHHHHHHHHHHCCC
54.7121906983
186PhosphorylationKEKRDKASQEGGDVL
HHHHHHHHHHCCCCC
34.2117525332
202PhosphorylationARQDCTPSLKSLVAT
CCCCCCHHHHHHHHH
30.21-
205PhosphorylationDCTPSLKSLVATGNL
CCCHHHHHHHHHCCC
33.1128348404
274PhosphorylationTNPQVLDTGLTAQDM
CCCCHHCCCCCHHHC
29.90-
277PhosphorylationQVLDTGLTAQDMHYA
CHHCCCCCHHHCCHH
24.5027251275
283PhosphorylationLTAQDMHYAQCLSPV
CCHHHCCHHHHCCCC
7.5427642862
288PhosphorylationMHYAQCLSPVDWDKP
CCHHHHCCCCCCCCC
30.4226074081
297PhosphorylationVDWDKPDSSGTEQDD
CCCCCCCCCCCCCCC
38.9122210691

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 ARH_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARH_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 ARH_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LRP2_HUMANLRP2physical
14528014
CLH1_HUMANCLTCphysical
12221107
AP2B1_HUMANAP2B1physical
12221107
LDLR_HUMANLDLRphysical
12221107
KLC1_HUMANKLC1physical
21915095
STN1_HUMANOBFC1physical
25416956
NEUL_HUMANNLNphysical
26186194
CHK1_HUMANCHEK1physical
26186194
CC85C_HUMANCCDC85Cphysical
26186194
DCA16_HUMANDCAF16physical
26186194
NEUL_HUMANNLNphysical
28514442
CC85C_HUMANCCDC85Cphysical
28514442
CHK1_HUMANCHEK1physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
603813Hypercholesterolemia, autosomal recessive (ARH)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARH_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASSSPECTROMETRY.

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