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Protein Page:
LBR (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
LBR Anchors the lamina and the heterochromatin to the inner nuclear membrane. Defects in LBR are a cause of Pelger-Huet anomaly (PHA). PHA is an autosomal dominant inherited abnormality of neutrophils, characterized by reduced nuclear segmentation and an apparently looser chromatin structure. Heterozygotes show hypolobulated neutrophil nuclei with coarse chromatin. Presumed homozygous individuals have ovoid neutrophil nuclei, as well as varying degrees of developmental delay, epilepsy, and skeletal abnormalities. Defects in LBR are the cause of hydrops-ectopic calcification-moth-eaten skeletal dysplasia (HEM); also known as Greenberg skeletal dysplasia. HEM is a rare autosomal recessive chondrodystrophy characterized by early in utero lethality and, therefore, considered to be nonviable. Affected fetuses typically present with fetal hydrops, short- limbed dwarfism, and a marked disorganization of chondro-osseous calcification and may present with polydactyly and additional nonskeletal malformations. Defects in LBR may be a cause of Reynolds syndrome (REYNS). It is a syndrome specifically associating limited cutaneous systemic sclerosis and primary biliray cirrhosis. It is characterized by liver disease, telangiectasia, abrupt onset of digital paleness or cyanosis in response to cold exposure or stress (Raynaud phenomenon), and variable features of scleroderma. The liver disease is characterized by pruritis, jaundice, hepatomegaly, increased serum alkaline phosphatase and positive serum mitochondrial autoantibodies, all consistent with primary biliary cirrhosis. Belongs to the ERG4/ERG24 family. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, integral; DNA binding protein; Membrane protein, multi-pass
Cellular Component: nuclear membrane; mitochondrion; integral to membrane; nuclear envelope; integral to nuclear inner membrane
Molecular Function: protein binding; DNA binding; oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; lamin binding
Biological Process: cholesterol biosynthetic process
Reference #:  Q14739 (UniProtKB)
Alt. Names/Synonyms: DHCR14B; FLJ43126; Integral nuclear envelope inner membrane protein; lamin B receptor; Lamin-B receptor; LBR; LMN2R; MGC9041; PHA
Gene Symbols: LBR
Molecular weight: 70,703 Da
Basal Isoelectric point: 9.41  Predict pI for various phosphorylation states
Select Structure to View Below

LBR

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 2 K5 ___MPSRKFADGEVV
0 2 S20-p RGRWPGSsLyyEVEI
0 9 Y22-p RWPGSsLyyEVEILS
0 10 Y23-p WPGSsLyyEVEILSH
0 6 K42-u QLYTVKYkDGTELEL
0 1 T45 TVKYkDGTELELKEN
0 2 K50 DGTELELKENDIkPL
0 1 K55-a ELKENDIkPLtsFRQ
0 1 T58-p ENDIkPLtsFRQRKG
0 4 S59-p NDIkPLtsFRQRKGG
0 1 G65 tsFRQRKGGsTSSsP
0 9 S67-p FRQRKGGsTSSsPSR
0 4 S69 QRKGGsTSSsPSRRR
0 4 S70 RKGGsTSSsPSRRRG
1 7 S71-p KGGsTSSsPSRRRGS
0 1 S73 GsTSSsPSRRRGSRS
1 0 S80 SRRRGSRSRSRsRsP
1 0 S82 RRGSRSRSRsRsPGR
1 1 S84-p GSRSRSRsRsPGRPP
1 1 - gap
0 4 S86-p RSRSRsRsPGRPPKS
0 3 - gap
1 0 A94 PGRPPKSARRsAsAS
0 15 S97-p PPKSARRsAsASHQA
0 23 S99-p KSARRsAsASHQADI
0 6 K107-u ASHQADIkEARREVE
0 1 K116-u ARREVEVkLtPLILk
0 9 T118-p REVEVkLtPLILkPF
0 2 K123-a kLtPLILkPFGNsIs
0 22 K123-u kLtPLILkPFGNsIs
0 5 S128-p ILkPFGNsIsRyNGE
0 3 S130-p kPFGNsIsRyNGEPE
0 2 Y132-p FGNsIsRyNGEPEHI
0 1 R141 GEPEHIERNDAPHKN
0 3 A144 EHIERNDAPHKNTQE
0 2 K147 ERNDAPHKNTQEKFS
0 6 Y161-p SLSQESSyIATQysL
0 5 Y166-p SSyIATQysLRPRRE
0 6 S167-p SyIATQysLRPRREE
0 3 K178 RREEVKLKEIDSKEE
0 1 K190-a KEEKYVAkELAVRTF
0 15 K190-u KEEKYVAkELAVRTF
0 4 T200-p AVRTFEVtPIRAKDL
0 5 K594-a DEYHCKKkYGVAWEk
0 12 K601-a kYGVAWEkYCQRVPY
0 14 K601-u kYGVAWEkYCQRVPY
  mouse

 
K5-u ___MPSRkFVEGEVV
S20 RGRWPGSSLYYEVEI
Y22 RWPGSSLYYEVEILS
Y23 WPGSSLYYEVEILSH
K42-u QLYTVKYkDGtELEL
T45-p TVKYkDGtELELkES
K50-u DGtELELkESDIKPL
K55 ELkESDIKPLKsFKQ
K58 ESDIKPLKsFKQRKs
S59-p SDIKPLKsFKQRKsG
S65-p KsFKQRKsGsIsssP
S67-p FKQRKsGsIsssPsR
S69-p QRKsGsIsssPsRRR
S70-p RKsGsIsssPsRRRG
S71-p KsGsIsssPsRRRGS
S73-p GsIsssPsRRRGSRS
S80 sRRRGSRSRSRSRsR
S82 RRGSRSRSRSRsRsR
S84 GSRSRSRSRsRsRsP
S86-p RSRSRSRsRsRsPGR
S88-p RSRSRsRsRsPGRAP
S90-p RSRsRsRsPGRAPKG
S98 PGRAPKGSRRsVsAS
S101-p APKGSRRsVsASHEG
S103-p KGSRRsVsASHEGDV
K111-u ASHEGDVkEKKEKEM
K126 RREILQVKLtPLVLk
T128-p EILQVKLtPLVLkPF
K133 KLtPLVLKPFGNSVs
K133-u KLtPLVLkPFGNSVs
S138 VLkPFGNSVsVYNGE
S140-p kPFGNSVsVYNGEPE
Y142 FGNSVsVYNGEPEHM
K151-u GEPEHMEkNAtPYkD
T154-p EHMEkNAtPYkDKQE
K157-u EkNAtPYkDKQERII
Y171 ILSTEDRYIVTQYsL
Y176 DRYIVTQYsLRPRRE
S177-p RYIVTQYsLRPRREE
K188-u RREEVKAkEIESEEQ
K200 EEQNLVTKGPAPLGT
K200-u EEQNLVTkGPAPLGT
T211 PLGTFQVTTPQRKDL
K605 DEHQCRRKYGLAWEk
K612 KYGLAWEKYCQRVPY
K612-u KYGLAWEkYCQRVPY
  rat

 
K5 ___MPGRKFADGEVV
S20 RGRWPGSSLYYEVEI
Y22 RWPGSSLYYEVEILS
Y23 WPGSSLYYEVEILSH
K42 QLYTVKYKDGTELEL
T45 TVKYKDGTELELKES
K50 DGTELELKESDIKPL
K55 ELKESDIKPLKSFKQ
K58 ESDIKPLKSFKQRKS
S59 SDIKPLKSFKQRKSG
S65 KSFKQRKSGSTSSSP
S67 FKQRKSGSTSSSPSR
S69 QRKSGSTSSSPSRRR
S70 RKSGSTSSSPSRRRS
S71 KSGSTSSSPSRRRSS
S73 GSTSSSPSRRRSSRS
S80 SRRRSSRSRSRSRSR
S82 RRSSRSRSRSRSRSP
S84 SSRSRSRSRSRSPGR
S86 RSRSRSRSRSPGRAP
S88 RSRSRSRSPGRAPKG
- gap
S96-gl PGRAPKGsRRSVsAS
S99 APKGsRRSVsASYQA
S101-p KGsRRSVsASYQADA
K109 ASYQADAKEKEMRRE
K121 RREILQVKLTPLVLK
T123 EILQVKLTPLVLKPF
K128 KLTPLVLKPFANSVS
K128 KLTPLVLKPFANSVS
S133 VLKPFANSVSVYNGE
S135 KPFANSVSVYNGEPE
Y137 FANSVSVYNGEPEHM
K146 GEPEHMEKSATPPKN
T149 EHMEKSATPPKNKQE
K152 EKSATPPKNKQERVI
Y166 ILSTEDSYIATQYSL
Y171 DSYIATQYSLRPRRE
S172 SYIATQYSLRPRREE
K183 RREEVKPKHRVRGTN
R194 RGTNLVTRGPVPLGT
R194 RGTNLVTRGPVPLGT
T205 PLGTFQVTTPQRRDL
K599 DEHQCRRKYGLAWEK
K606 KYGLAWEKYCQRVPY
K606 KYGLAWEKYCQRVPY
  turkey

 
K5 ___MPNRKYADGEVV
V20 MGRWPGSVLYYEVQV
Y22 RWPGSVLYYEVQVTS
Y23 WPGSVLYYEVQVTSY
K42 HLYTVKYKDGTELAL
T45 TVKYKDGTELALKES
K50 DGTELALKESDIRSQ
R55 ALKESDIRSQSSFKQ
- under review  
S59 SDIRSQSSFKQRKSQ
S65 SSFKQRKSQSSSSSP
S67 FKQRKSQSSSSSPSR
S69 QRKSQSSSSSPSRRS
S70 RKSQSSSSSPSRRSR
S71 KSQSSSSSPSRRSRs
S73 QSSSSSPSRRSRsRs
S78-p SPSRRSRsRsRsRsP
S80-p SRRSRsRsRsRsPGR
S82-p RSRsRsRsRsPGRPA
S84-p RsRsRsRsPGRPAKG
- gap
- gap
R92 PGRPAKGRRRSSSHS
S95 PAKGRRRSSSHSREH
S97 KGRRRSSSHSREHKD
K103 SSHSREHKDDKKKII
- gap
T114 KKIIQETTLALPKPS
K119 ETTLALPKPSENNTR
K119 ETTLALPKPSENNTR
- gap
- gap
Y128 SENNTRRYNGEPDST
R137 GEPDSTERNDTSSKL
T140 DSTERNDTSSKLLEQ
K143 ERNDTSSKLLEQQKL
- gap
Y163 VERVLDQYSLRSRRE
S164 ERVLDQYSLRSRREE
- gap
- gap
- gap
- gap
- gap
- gap
- gap
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