Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00805
Entry Name
UniProt Accession
Theoretical PI
5.11
Molecular Weight
66408.34
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Lamin-B1
Protein Synonyms/Alias
Gene Name
LMNB1
Gene Synonyms/Alias
LMN2; LMNB;
Created Date
01-FEB-1991
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
583
Canonical
PRASNRSCAIM****
[1]
S-Farnesylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Farnsworth CC, Wolda SL, Gelb MH, Glomset JA. Human lamin B contains afarnesylated cysteine residue. J Biol Chem. 1989 Dec 5;264(34):20422-9. PubMedPMID: 2684976; PubMed Central PMCID: PMC3443689.[PMID:2684976]
Functional Description
Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.
Sequence Annotation
Domain: 434 546 LTD.
Region: 2 34 Head.
Region: 35 386 Rod.
Region: 35 69 Coil 1A.
Region: 70 81 Linker 1.
Region: 82 215 Coil 1B.
Region: 216 243 Linker 2.
Region: 244 386 Coil 2.
Region: 387 586 Tail.
Motif: 415 420 Nuclear localization signal.
Modified residue: 2 2 N-acetylalanine.
Modified residue: 3 3 Phosphothreonine.
Modified residue: 5 5 Phosphothreonine.
Modified residue: 20 20 Phosphothreonine.
Modified residue: 23 23 Phosphoserine.
Modified residue: 111 111 N6-acetyllysine.
Modified residue: 157 157 N6-acetyllysine.
Modified residue: 210 210 Phosphoserine.
Modified residue: 271 271 N6-acetyllysine.
Modified residue: 330 330 N6-acetyllysine.
Modified residue: 375 375 Phosphoserine.
Modified residue: 483 483 N6-acetyllysine.
Modified residue: 575 575 Phosphothreonine.
Modified residue: 583 583 Cysteine methyl ester.
Protein Length
586 AA.
Protein Sequence
(Canonical)
MATATPVPPR MGSRAGGPTT PLSPTRLSRL QEKEELRELN DRLAVYIDKV RSLETENSAL  60
QLQVTEREEV RGRELTGLKA LYETELADAR RALDDTARER AKLQIELGKC KAEHDQLLLN  120
YAKKESDLNG AQIKLREYEA ALNSKDAALA TALGDKKSLE GDLEDLKDQI AQLEASLAAA  180
KKQLADETLL KVDLENRCQS LTEDLEFRKS MYEEEINETR RKHETRLVEV DSGRQIEYEY  240
KLAQALHEMR EQHDAQVRLY KEELEQTYHA KLENARLSSE MNTSTVNSAR EELMESRMRI  300
ESLSSQLSNL QKESRACLER IQELEDLLAK EKDNSRRMLT DKEREMAEIR DQMQQQLNDY  360
EQLLDVKLAL DMEISAYRKL LEGEEERLKL SPSPSSRVTV SRASSSRSVR TTRGKRKRVD  420
VEESEASSSV SISHSASATG NVCIEEIDVD GKFIRLKNTS EQDQPMGGWE MIRKIGDTSV  480
SYKYTSRYVL KAGQTVTIWA ANAGVTASPP TDLIWKNQNS WGTGEDVKVI LKNSQGEEVA  540
QRSTVFKTTI PEEEEEEEEA AGVVVEEELF HQQGTPRASN RSCAIM                 586
FASTA
(Canonical)
>LipidDB-9606-00805|P20700
MATATPVPPRMGSRAGGPTTPLSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSAL
QLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKCKAEHDQLLLN
YAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAA
KKQLADETLLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSGRQIEYEY
KLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRI
ESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDY
EQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSRVTVSRASSSRSVRTTRGKRKRVD
VEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSV
SYKYTSRYVLKAGQTVTIWAANAGVTASPPTDLIWKNQNSWGTGEDVKVILKNSQGEEVA
QRSTVFKTTIPEEEEEEEEAAGVVVEEELFHQQGTPRASNRSCAIM
Gene Ontology
GO:0005638; C:lamin filament; TAS:ProtInc
GO:0016020; C:membrane; IDA:UniProtKB
GO:0005635; C:nuclear envelope; TAS:Reactome
GO:0005637; C:nuclear inner membrane; IEA:InterPro
GO:0031965; C:nuclear membrane; IDA:HPA
GO:0005654; C:nucleoplasm; TAS:Reactome
GO:0005198; F:structural molecule activity; TAS:ProtInc
GO:0006915; P:apoptotic process; TAS:Reactome
GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome
Interpro
InterPro; IPR001664; IF
InterPro; IPR018039; Intermediate_filament_CS
InterPro; IPR027696; Lamin
InterPro; IPR001322; Lamin_tail_dom
Pfam
Pfam; PF00038; Filament;
Pfam; PF00932; LTD;
SMART
PROSITE
PROSITE; PS00226; IF;
PRINTS