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Protein Page:
LRSAM1 (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
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: Ubiquitin conjugating system; EC 6.3.2.-; Ligase; EC 6.3.2.19; Ubiquitin ligase
Chromosomal Location of Human Ortholog: 9q33.3
Cellular Component: cytoplasm; membrane
Molecular Function: ligase activity; protein binding; ubiquitin-protein ligase activity; zinc ion binding
Biological Process: autophagy; negative regulation of endocytosis; non-lytic virus budding; protein autoubiquitination; protein catabolic process; protein polyubiquitination
Disease: Charcot-marie-tooth Disease, Axonal, Type 2p
Reference #:  Q6UWE0 (UniProtKB)
Gene Symbols: LRSAM1
Molecular weight: 83,594 Da
Basal Isoelectric point: 5.7  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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


 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

► Hide Isoforms
 
0 1 S76 SLLPKSCSLLsLATI
0 1 S79‑p PKSCSLLsLATIKVL
0 1 K135 QLQTLNVKDNKLKEL
0 1 S179‑p VRTLEMLsLDASAMV
0 1 Y187‑p LDASAMVyPPREVCG
0 1 Y218‑p EYYPPSQyLLPILEQ
0 3 S234‑p GIENSRDsPDGPTDR
0 26 Y256‑p WQNRFSDyEKRKEQK
0 2 T282‑p ELGQREHtQLLQQSs
0 1 S289‑p tQLLQQSssQKDEIL
0 2 S290‑p QLLQQSssQKDEILQ
0 1 T298‑p QKDEILQtVKEEQSR
0 1 S337‑p QTEQNISsRIQKLLQ
0 8 K491‑ub QLTQLELkRKSLDTE
0 1 S494 QLELkRKSLDTESLQ
0 1 T497 LkRKSLDTESLQEMI
0 1 S499 RKSLDTESLQEMISE
0 28 K520‑ub SLLQQLLkEkQQREE
0 3 K522‑ub LQQLLkEkQQREEEL
0 1 T534‑p EELREILtELEAKSE
0 2 K564‑ub NQKPLSLkLQEEGME
0 1 S596‑p IFAHHRLsLDLLSQM
0 1 S601 RLsLDLLSQMsPGDL
0 6 S604‑p LDLLSQMsPGDLAKV
0 1 K610 MsPGDLAKVGVSEAG
  LRSAM1 iso2  
S76 SLLPKSCSLLSLATI
S79 PKSCSLLSLATIKVL
K135 QLQTLNVKDNKLKEL
S179 VRTLEMLSLDASAMV
Y187 LDASAMVYPPREVCG
Y218 EYYPPSQYLLPILEQ
S234 GIENSRDSPDGPTDR
Y256 WQNRFSDYEKRKEQK
T282 ELGQREHTQLLQQSS
S289 TQLLQQSSSQKDEIL
S290 QLLQQSSSQKDEILQ
T298 QKDEILQTVKEEQSR
S337 QTEQNISSRIQKLLQ
- gap
- gap
- gap
- gap
K493 SLLQQLLKEKQQREE
K495 LQQLLKEKQQREEEL
T507 EELREILTELEAKSE
K537 NQKPLSLKLQEEGME
S569 IFAHHRLSLDLLSQM
S574 RLSLDLLSQMSPGDL
S577 LDLLSQMSPGDLAKV
K583 MSPGDLAKVGVSEAG
  LRSAM1 iso3  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
K71 QLTQLELKRKSLDTE
S74 QLELKRKSLDTESLQ
T77 LKRKSLDTESLQEMI
S79 RKSLDTESLQEMISE
K100 SLLQQLLKEKQQREE
K102 LQQLLKEKQQREEEL
T114 EELREILTELEAKSE
K144 NQKPLSLKLQEEGME
S176 IFAHHRLSLDLLSQM
S181 RLSLDLLSQMSPGDL
S184 LDLLSQMSPGDLAKV
K190 MSPGDLAKVGVSEAG
  mouse

 
S76‑p SLLPKSCsLLSLVTI
S79 PKSCsLLSLVTIKVL
K135‑ub QLQTLNVkDNKLKEL
S179 VRTLETLSLNALAMV
Y187 LNALAMVYPPPEVCG
Y218 DYYPPSQYLLPVLEQ
S234‑p GAENTQDsPDGPASR
Y256 WQNRFSDYEKRKEQK
A282 DLGQREHAELLQQSH
H289 AELLQQSHsHKDEIL
S290‑p ELLQQSHsHKDEILQ
T298 HKDEILQTVKQEQTR
S337 QTEQSIASRIQRLLQ
K491‑ub QLTQLELkRKsLDtE
S494‑p QLELkRKsLDtEtLQ
T497‑p LkRKsLDtEtLQEMV
T499‑p RKsLDtEtLQEMVSE
K520‑ub NLLQQLLkEKKQREE
K522 LQQLLkEKKQREEEL
A534 EELHGILAELEAKSE
K564 NQKPLSLKLQEEGME
S596 LFAHHRISLDMLsRM
S601‑p RISLDMLsRMSPGDL
S604 LDMLsRMSPGDLAkV
K610‑ac MSPGDLAkVGVSEAG
  rat

 
L77 CFLPTACLIYSVSSR
S80 PTACLIYSVSSRQVL
K136 QLQTLNVKDNKLKEL
S180 VRTLETLSLDALSMV
Y188 LDALSMVYPPPEVCG
Y219 DYYPPSQYLLPVLEQ
S235 GAENSQDSPDGPTRR
Y257 WQNRFSDYEKRKEQK
A283 DLGQREHAELLQQSH
H290 AELLQQSHSHKDEIL
S291 ELLQQSHSHKDEILQ
T299 HKDEILQTVKQEQTR
S338 QSEQSIASRIQRLLQ
K492 QLTQLELKRKSLDTE
S495 QLELKRKSLDTETLQ
T498 LKRKSLDTETLQEMV
T500 RKSLDTETLQEMVSE
K521 NLLQQLLKEKKQREE
K523 LQQLLKEKKQREEEL
A535 EELHGILAELEAKSE
K565 NQKPLSLKLQEEGME
T597 LFAHHRITLDMLSRM
S602 RITLDMLSRMGPGDL
G605 LDMLSRMGPGDLAKV
K611 MGPGDLAKVGVSEAG
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