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Protein Page:
LRSAM1 (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
LRSAM1 E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivate the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (HIV-1 viral proteins) cargos. Defects in LRSAM1 are a cause of Charcot-Marie-Tooth disease type 2P (CMT2P). CMT2P is an axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 6.3.2.19; Ubiquitin conjugating system; EC 6.3.2.-; Ligase; Ubiquitin ligase
Cellular Component: membrane; cytoplasm; extracellular region
Molecular Function: protein binding; zinc ion binding; hormone activity; ubiquitin-protein ligase activity
Biological Process: protein transport; protein autoubiquitination; protein polyubiquitination; negative regulation of endocytosis; non-lytic virus budding; protein catabolic process
Reference #:  Q6UWE0 (UniProtKB)
Alt. Names/Synonyms: E3 ubiquitin-protein ligase LRSAM1; FLJ31641; hTAL; leucine rich repeat and sterile alpha motif containing 1; Leucine-rich repeat and sterile alpha motif-containing protein 1; LRSAM1; LRSM1; RIFLE; TAL; Tsg101-associated ligase
Gene Symbols: LRSAM1
Molecular weight: 83,594 Da
Basal Isoelectric point: 5.7  Predict pI for various phosphorylation states
Select Structure to View Below

LRSAM1

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 S76 SLLPKSCSLLSLATI
0 1 K135 QLQTLNVKDNKLKEL
0 2 S234-p GIENSRDsPDGPTDR
0 24 Y256-p WQNRFSDyEKRKEQK
0 1 S337-p QTEQNISsRIQKLLQ
0 7 K491-u QLTQLELkRKSLDTE
0 28 K520-u SLLQQLLkEkQQREE
0 3 K522-u LQQLLkEkQQREEEL
0 1 T534-p EELREILtELEAKSE
0 2 K564-u NQKPLSLkLQEEGME
0 1 S601 RLSLDLLSQMsPGDL
0 3 S604-p LDLLSQMsPGDLAKV
  mouse

 
S76-p SLLPKSCsLLSLVTI
K135-u QLQTLNVkDNKLKEL
S234-p GAENTQDsPDGPASR
Y256 WQNRFSDYEKRKEQK
S337 QTEQSIASRIQRLLQ
K491-u QLTQLELkRKSLDTE
K520-u NLLQQLLkEKKQREE
K522 LQQLLkEKKQREEEL
A534 EELHGILAELEAKSE
K564 NQKPLSLKLQEEGME
S601-p RISLDMLsRMSPGDL
S604 LDMLsRMSPGDLAKV
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