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Protein Page:
LRPAP1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
LRPAP1 Interacts with LRP1/alpha-2-macroglobulin receptor and glycoprotein 330. In complex with the alpha-2-MR or gp330, it may have some role in the pathogenesis of membrane glomerular nephritis. Belongs to the alpha-2-MRAP family. Note: This description may include information from UniProtKB.
Protein type: Receptor, misc.
Cellular Component: cell surface; endoplasmic reticulum; extracellular region; plasma membrane; integral to membrane; vesicle
Molecular Function: heparin binding; protein binding; receptor antagonist activity; low-density lipoprotein receptor binding; unfolded protein binding; asialoglycoprotein receptor activity
Biological Process: vesicle-mediated transport; receptor-mediated endocytosis; protein folding; negative regulation of protein binding
Reference #:  P30533 (UniProtKB)
Alt. Names/Synonyms: A2MRAP; A2RAP; Alpha-2-macroglobulin receptor-associated protein; alpha-2-macroglobulin receptor-associated protein 1; Alpha-2-MRAP; AMRP; HBP44; lipoprotein receptor associated protein; low density lipoprotein receptor-related protein associated protein 1; Low density lipoprotein receptor-related protein-associated protein 1; low density lipoprotein-related protein-associated protein 1 (alpha-2-macroglobulin receptor-associated protein 1); LRPAP1; MGC138272; MRAP; RAP
Gene Symbols: LRPAP1
Molecular weight: 41,466 Da
Basal Isoelectric point: 8.73  Predict pI for various phosphorylation states
Select Structure to View Below

LRPAP1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S45-p EKNQPKPsPKREsGE
0 4 S50-p KPsPKREsGEEFRME
0 1 K128 KYGLDGKKDARQVts
0 1 T134-ga KKDARQVtsNSLSGT
0 2 S135-p KDARQVtsNSLSGTQ
0 1 G166 KTSGKFSGEELDKLW
0 1 K182 EFLHHKEKVHEYNVL
0 1 S230-p ELKEKLRsINQGLDR
1 1 S242 LDRLRRVSHQGYstE
0 1 S247-p RVSHQGYstEAEFEE
0 1 T248-p VSHQGYstEAEFEEP
0 1 K287-a ELKHFEAkIEKHNHY
0 1 K323 RVSRSREKHALLEGR
0 1 T337-ga RTKELGYtVKKHLQD
0 1 S346-ga KKHLQDLsGRISRAR
  mouse

 
A48 EKNEPEMAAKREsGE
S53-p EMAAKREsGEEFRME
K131-u RYGLDGRkDAQMVHs
H137 RkDAQMVHsNALNED
S138-p kDAQMVHsNALNEDT
S169-p KTSGKFSsEELDKLW
K185-u EFLHYKEkIQEYNVL
S233 ELKDRLRSINQGLDR
S245 LDRLRKVSHQGYGST
G250 KVSHQGYGSTTEFEE
S251 VSHQGYGSTTEFEEP
K290 ELKHFEAKIEKHNHY
K326-a HISRNKEkYVLLEEK
K340 KTKELGYKVKKHLQD
S349 KKHLQDLSSRVSRAR
  rat

 
A48 EKNEPEMAAKRESGE
S53 EMAAKRESGEEFRME
K131 RYGLDGRKDTQTVHS
H137 RKDTQTVHSNALNED
S138 KDTQTVHSNALNEDT
S169 KTSGKFSSEELDKLW
K185 EFLHYKEKIHEYNVL
S233 ELKDRLRSINQGLDR
S245-p LDRLRKVsHQGYGPA
G250 KVsHQGYGPATEFEE
P251 VsHQGYGPATEFEEP
K290 ELKHFEAKIEKHNHY
K326 HISRNKEKYVLLEEK
K340 KTKELGYKVKKHLQD
S349 KKHLQDLSSRVSRAR
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