AMRP_HUMAN - dbPTM
AMRP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMRP_HUMAN
UniProt AC P30533
Protein Name Alpha-2-macroglobulin receptor-associated protein
Gene Name LRPAP1
Organism Homo sapiens (Human).
Sequence Length 357
Subcellular Localization Rough endoplasmic reticulum lumen . Endoplasmic reticulum-Golgi intermediate compartment lumen . Golgi apparatus, cis-Golgi network . Golgi apparatus lumen . Endosome lumen . Cell surface . May be associated with receptors at the cell surface.
Protein Description Molecular chaperone for LDL receptor-related proteins that may regulate their ligand binding activity along the secretory pathway..
Protein Sequence MAPRRVRSFLRGLPALLLLLLFLGPWPAASHGGKYSREKNQPKPSPKRESGEEFRMEKLNQLWEKAQRLHLPPVRLAELHADLKIQERDELAWKKLKLDGLDEDGEKEARLIRNLNVILAKYGLDGKKDARQVTSNSLSGTQEDGLDDPRLEKLWHKAKTSGKFSGEELDKLWREFLHHKEKVHEYNVLLETLSRTEEIHENVISPSDLSDIKGSVLHSRHTELKEKLRSINQGLDRLRRVSHQGYSTEAEFEEPRVIDLWDLAQSANLTDKELEAFREELKHFEAKIEKHNHYQKQLEIAHEKLRHAESVGDGERVSRSREKHALLEGRTKELGYTVKKHLQDLSGRISRARHNEL
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
35PhosphorylationAASHGGKYSREKNQP
CHHCCHHCCCCCCCC		19.0826437602
36PhosphorylationASHGGKYSREKNQPK
HHCCHHCCCCCCCCC		37.1326437602
43UbiquitinationSREKNQPKPSPKRES
CCCCCCCCCCCCCCC		48.6524816145
45PhosphorylationEKNQPKPSPKRESGE
CCCCCCCCCCCCCCH		49.5320068231
50PhosphorylationKPSPKRESGEEFRME
CCCCCCCCCHHHHHH		56.3829255136
652-HydroxyisobutyrylationKLNQLWEKAQRLHLP
HHHHHHHHHHHCCCC		37.93-
84UbiquitinationAELHADLKIQERDEL
HHHHCCCCCHHHHHH		42.7833845483
97SumoylationELAWKKLKLDGLDED
HHHHHHHHCCCCCCC		54.11-
972-HydroxyisobutyrylationELAWKKLKLDGLDED
HHHHHHHHCCCCCCC		54.11-
97SumoylationELAWKKLKLDGLDED
HHHHHHHHCCCCCCC		54.1117000644
122PhosphorylationLNVILAKYGLDGKKD
HHHHHHHHCCCCCCC		19.8128985074
1272-HydroxyisobutyrylationAKYGLDGKKDARQVT
HHHCCCCCCCHHHHH		47.34-
134O-linked_GlycosylationKKDARQVTSNSLSGT
CCCHHHHHHCCCCCC		17.5355828577
134PhosphorylationKKDARQVTSNSLSGT
CCCHHHHHHCCCCCC		17.53-
135PhosphorylationKDARQVTSNSLSGTQ
CCHHHHHHCCCCCCC		26.09-
137PhosphorylationARQVTSNSLSGTQED
HHHHHHCCCCCCCCC		24.5525159151
139PhosphorylationQVTSNSLSGTQEDGL
HHHHCCCCCCCCCCC		39.3525627689
141PhosphorylationTSNSLSGTQEDGLDD
HHCCCCCCCCCCCCC		25.9625159151
153UbiquitinationLDDPRLEKLWHKAKT
CCCHHHHHHHHHHHH		62.5629967540
161PhosphorylationLWHKAKTSGKFSGEE
HHHHHHHCCCCCHHH		39.0024719451
163AcetylationHKAKTSGKFSGEELD
HHHHHCCCCCHHHHH		35.8027452117
165PhosphorylationAKTSGKFSGEELDKL
HHHCCCCCHHHHHHH		49.1022798277
1802-HydroxyisobutyrylationWREFLHHKEKVHEYN
HHHHHHHHHHHHHHH		48.78-
186PhosphorylationHKEKVHEYNVLLETL
HHHHHHHHHHHHHHH		8.83-
2252-HydroxyisobutyrylationHSRHTELKEKLRSIN
HHCHHHHHHHHHHHH		46.71-
227UbiquitinationRHTELKEKLRSINQG
CHHHHHHHHHHHHHH		47.8424816145
230PhosphorylationELKEKLRSINQGLDR
HHHHHHHHHHHHHHH		36.0120068231
242PhosphorylationLDRLRRVSHQGYSTE
HHHHHHHHCCCCCCC		14.3129255136
246PhosphorylationRRVSHQGYSTEAEFE
HHHHCCCCCCCCCCC		13.0729255136
247PhosphorylationRVSHQGYSTEAEFEE
HHHCCCCCCCCCCCC		26.9629255136
248PhosphorylationVSHQGYSTEAEFEEP
HHCCCCCCCCCCCCC		30.6329255136
268N-linked_GlycosylationWDLAQSANLTDKELE
HHHHHHCCCCHHHHH		49.0419159218
287AcetylationELKHFEAKIEKHNHY
HHHHHHHHHHHCCHH		44.1719608861
304UbiquitinationQLEIAHEKLRHAESV
HHHHHHHHHHHCHHH		40.7429967540
3042-HydroxyisobutyrylationQLEIAHEKLRHAESV
HHHHHHHHHHHCHHH		40.74-
310PhosphorylationEKLRHAESVGDGERV
HHHHHCHHHCCCCCC		31.9828355574
323AcetylationRVSRSREKHALLEGR
CCCHHHHHHHHHHCC		32.8227452117
323UbiquitinationRVSRSREKHALLEGR
CCCHHHHHHHHHHCC		32.8233845483
331O-linked_GlycosylationHALLEGRTKELGYTV
HHHHHCCHHHHCHHH		39.46OGP
332UbiquitinationALLEGRTKELGYTVK
HHHHCCHHHHCHHHH		49.9723000965
3322-HydroxyisobutyrylationALLEGRTKELGYTVK
HHHHCCHHHHCHHHH		49.97-
336PhosphorylationGRTKELGYTVKKHLQ
CCHHHHCHHHHHHHH		22.4528152594
337O-linked_GlycosylationRTKELGYTVKKHLQD
CHHHHCHHHHHHHHH		24.8555831075
337PhosphorylationRTKELGYTVKKHLQD
CHHHHCHHHHHHHHH		24.8528152594
3392-HydroxyisobutyrylationKELGYTVKKHLQDLS
HHHCHHHHHHHHHHC		27.03-
340AcetylationELGYTVKKHLQDLSG
HHCHHHHHHHHHHCH		45.2527452117
346O-linked_GlycosylationKKHLQDLSGRISRAR
HHHHHHHCHHHHHHH		34.0255828359
346PhosphorylationKKHLQDLSGRISRAR
HHHHHHHCHHHHHHH		34.0227251275
348MethylationHLQDLSGRISRARHN
HHHHHCHHHHHHHHC		21.97115482273
350PhosphorylationQDLSGRISRARHNEL
HHHCHHHHHHHHCCC		20.6627251275
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 AMRP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMRP_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 AMRP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LRP8_HUMANLRP8physical
12899622
VLDLR_HUMANVLDLRphysical
12899622
DPOA2_HUMANPOLA2physical
16169070
RTN4_HUMANRTN4physical
16169070
VLDLR_HUMANVLDLRphysical
10571241
RAF1_HUMANRAF1physical
10783161
GNDS_HUMANRALGDSphysical
10783161
SORL_HUMANSORL1physical
8940146
SORL_HUMANSORL1physical
11557679
4EBP1_HUMANEIF4EBP1physical
16798736
MTOR_HUMANMTORphysical
16798736
LRP2_HUMANLRP2physical
7512726
VLDLR_HUMANVLDLRphysical
28514442
LRP1B_HUMANLRP1Bphysical
28514442
LRP4_HUMANLRP4physical
28514442
SORL_HUMANSORL1physical
28514442
ROCK2_HUMANROCK2physical
28514442
LDLR_HUMANLDLRphysical
28514442
LRP8_HUMANLRP8physical
28514442
LRP1_HUMANLRP1physical
28514442
LRP2_HUMANLRP2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615431Myopia 23, autosomal recessive (MYP23)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AMRP_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-287, AND MASS SPECTROMETRY.
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-268, AND MASSSPECTROMETRY.

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