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Protein Page:
LRPAP1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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.
Chromosomal Location of Human Ortholog: 4p16.3
Cellular Component: cell surface; endoplasmic reticulum; plasma membrane; integral to membrane; extracellular region; vesicle
Molecular Function: heparin binding; receptor antagonist activity; protein binding; 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
Disease: Myopia 23, Autosomal Recessive
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


 LTP 

LTP: 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.


 HTP 

HTP: 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 7 S50-p KPsPKREsGEEFRME
0 1 K65 KLNQLWEKAQRLHLP
0 1 K94 ERDELAWKKLKLDGL
0 1 K97 ELAWKKLKLDGLDED
0 1 K107 GLDEDGEKEARLIRN
0 1 K128 KYGLDGKKDARQVts
0 1 T134-ga KKDARQVtsNsLSGt
0 4 S135-p KDARQVtsNsLSGtQ
0 1 S137-p ARQVtsNsLSGtQED
0 1 T141-p tsNsLSGtQEDGLDD
0 1 K153 LDDPRLEKLWHKAKT
0 1 K163 HKAKTSGKFSGEELD
0 2 G166 KTSGKFSGEELDKLW
0 1 K182 EFLHHKEKVHEYNVL
0 1 K182 EFLHHKEKVHEYNVL
0 1 S207 HENVISPSDLSDIKG
0 1 K225 HSRHTELKEKLRsIN
0 1 S230-p ELKEKLRsINQGLDR
1 3 S242-p LDRLRRVsHQGYstE
0 2 S247-p RVsHQGYstEAEFEE
0 2 T248-p VsHQGYstEAEFEEP
0 1 K282 EAFREELKHFEAkIE
0 2 K287-ac ELKHFEAkIEKHNHY
0 1 K296 EKHNHYQKQLEIAHE
0 1 K304 QLEIAHEKLRHAEsV
0 1 R306 EIAHEKLRHAEsVGD
0 1 S310-p EKLRHAEsVGDGERV
0 2 K323 RVSRSREKHALLEGR
0 1 R330 KHALLEGRTkELGyt
0 1 K332-ub ALLEGRTkELGytVK
0 1 Y336-p GRTkELGytVKKHLQ
0 1 T337-ga RTkELGytVKKHLQD
0 1 S346-ga KKHLQDLsGRISRAR
  mouse

 
A48 EKNEPEMAAKREsGE
S53-p EMAAKREsGEEFRME
K68 KLNQLWEKAKRLHLS
K97 ERDELNWKKLKVEGL
K100 ELNWKKLKVEGLDKD
K110 GLDKDGEKEAKLIHN
K131-ub RYGLDGRkDAQMVHs
H137 RkDAQMVHsNALNED
S138-p kDAQMVHsNALNEDT
A140 AQMVHsNALNEDTQD
D144 HsNALNEDTQDELGD
K156 LGDPRLEKLWHKAKT
K166 HKAKTSGKFSsEELD
S169-p KTSGKFSsEELDKLW
K185 EFLHYKEKIQEYNVL
K185-ub EFLHYKEkIQEYNVL
S210-p YENLLSPsDMAHIKS
K228 ISKHSELKDRLRSIN
S233 ELKDRLRSINQGLDR
S245-p LDRLRKVsHQGYGST
G250 KVsHQGYGSTTEFEE
S251 VsHQGYGSTTEFEEP
K285 ESFREELKHFEAKIE
K290 ELKHFEAKIEKHNHY
K299 EKHNHYQKQLEISHQ
K307 QLEISHQKLKHVESI
K309 EISHQKLKHVESIGD
S313 QKLKHVESIGDPEHI
K326-ac HISRNKEkYVLLEEK
K333 kYVLLEEKTKELGYK
K335 VLLEEKTKELGYKVK
Y339 EKTKELGYKVKKHLQ
K340 KTKELGYKVKKHLQD
S349 KKHLQDLSSRVSRAR
  rat

 
A48 EKNEPEMAAKREsGE
S53-p EMAAKREsGEEFRME
K68-ac KLNQLWEkAKRLHLS
K97-ac ERDELNWkKLkVEGL
K100-ac ELNWkKLkVEGLDGD
K110-ac GLDGDGEkEAKLVHN
K131 RYGLDGRKDTQTVHS
H137 RKDTQTVHSNALNED
S138 KDTQTVHSNALNEDT
A140 TQTVHSNALNEDTQD
D144 HSNALNEDTQDELGD
K156-ac LGDPRLEkLWHKAKT
K166-ac HKAKTSGkFSsEELD
S169-p KTSGkFSsEELDKLW
K185-ac EFLHYKEkIHEYNVL
K185 EFLHYKEKIHEYNVL
S210 YENLLSPSDMTHIKS
K228-ac ASKHSELkDRLRSIN
S233 ELkDRLRSINQGLDR
S245-p LDRLRKVsHQGYGPA
G250 KVsHQGYGPATEFEE
P251 VsHQGYGPATEFEEP
K285-ac ESFREELkHFEAkIE
K290-ac ELkHFEAkIEKHNHY
K299-ac EKHNHYQkQLEISHQ
K307-ac QLEISHQkLkHVESI
K309-ac EISHQkLkHVESIGD
S313 QkLkHVESIGDPEHI
K326-ac HISRNKEkYVLLEEk
K333-ac kYVLLEEkTKELGYK
K335 VLLEEkTKELGYKVK
Y339 EkTKELGYKVKKHLQ
K340 kTKELGYKVKKHLQD
S349 KKHLQDLSSRVSRAR
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