Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00862
Entry Name
UniProt Accession
Theoretical PI
5.4
Molecular Weight
67318.05
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Lamin-B2
Protein Synonyms/Alias
Gene Name
Lmnb2
Gene Synonyms/Alias
Created Date
01-MAY-1991
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
593
Canonical
PRTTSRGCRLM****
[1]
S-Farnesylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Jung HJ, Nobumori C, Goulbourne CN, Tu Y, Lee JM, Tatar A, Wu D, Yoshinaga Y, de Jong PJ, Coffinier C, Fong LG, Young SG. Farnesylation of lamin B1 isimportant for retention of nuclear chromatin during neuronal migration. Proc NatlAcad Sci U S A. 2013 May 21;110(21):E1923-32. doi: 10.1073/pnas.1303916110. Epub 2013 May 6.[PMID:23650370]
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: 442 550 LTD.
Region: 1 26 Head.
Region: 27 378 Rod.
Region: 27 61 Coil 1A.
Region: 62 73 Linker 1.
Region: 74 207 Coil 1B.
Region: 208 234 Linker 2.
Region: 235 378 Coil 2.
Region: 379 596 Tail.
Motif: 415 420 Nuclear localization signal.
Modified residue: 12 12 Phosphothreonine.
Modified residue: 15 15 Phosphoserine.
Modified residue: 59 59 N6-acetyllysine.
Modified residue: 398 398 Phosphoserine.
Modified residue: 400 400 Phosphoserine.
Modified residue: 402 402 Phosphoserine.
Modified residue: 593 593 Cysteine methyl ester.
Protein Length
596 AA.
Protein Sequence
(Canonical)
MASLPPHAGP ATPLSPTRLS RLQEKEELRE LNDRLAHYID RVRALELEND RLLLRISEKE  60
EVTTREVSGI KTLYESELAD ARRVLDETAR ERARLQIEIG KVQAELEEAR KSAKKREGEL  120
TVAQGRVKDL ESLFHRSEAE LATALSDKQG LETEVAELRA QLAKAEDGHA VAKKQLEKET  180
LMRVDLENRC QSLQEELAFS KSVFEEEVRE TRRRHERRLV EVDSSRQQEY DFKMAQALED  240
LRSQHDEQVR LYRVELEQTY QAKLDNAKLL SDQNDKAAHA AREELKEARM RVESLSYQLL  300
GLQKQASAAE NHIHELEEAL AGERDKFRKM LDAKEQEMTE VRDAMQQQLA EYQELLDIKL  360
ALDMEISAYR KLLEGEEERL KLSPSPSSRI TISRATSSSS SSSGVGMSVG QGRGKRRRLE  420
TEDTSGSPSR ASRVSSGSRL AQQTVATGVV NIDEVDPEGR FVRLKNSSDK DQSLGNWRIK  480
RQVLEGEDIA YKFTPKYVLR AGQTVTVWAA GAGATHSPPS TLVWKSQTNW GPGESFRTAL  540
VSADGEEVAV KAAKHSSVQG RENGEEEEEE EAEFGEEDLF HQQGDPRTTS RGCRLM      596
FASTA
(Canonical)
>LipidDB-10090-00862|P21619
MASLPPHAGPATPLSPTRLSRLQEKEELRELNDRLAHYIDRVRALELENDRLLLRISEKE
EVTTREVSGIKTLYESELADARRVLDETARERARLQIEIGKVQAELEEARKSAKKREGEL
TVAQGRVKDLESLFHRSEAELATALSDKQGLETEVAELRAQLAKAEDGHAVAKKQLEKET
LMRVDLENRCQSLQEELAFSKSVFEEEVRETRRRHERRLVEVDSSRQQEYDFKMAQALED
LRSQHDEQVRLYRVELEQTYQAKLDNAKLLSDQNDKAAHAAREELKEARMRVESLSYQLL
GLQKQASAAENHIHELEEALAGERDKFRKMLDAKEQEMTEVRDAMQQQLAEYQELLDIKL
ALDMEISAYRKLLEGEEERLKLSPSPSSRITISRATSSSSSSSGVGMSVGQGRGKRRRLE
TEDTSGSPSRASRVSSGSRLAQQTVATGVVNIDEVDPEGRFVRLKNSSDKDQSLGNWRIK
RQVLEGEDIAYKFTPKYVLRAGQTVTVWAAGAGATHSPPSTLVWKSQTNWGPGESFRTAL
VSADGEEVAVKAAKHSSVQGRENGEEEEEEEAEFGEEDLFHQQGDPRTTSRGCRLM
Gene Ontology
GO:0005638; C:lamin filament; IDA:MGI
GO:0005635; C:nuclear envelope; IDA:MGI
GO:0005637; C:nuclear inner membrane; IEA:InterPro
GO:0005634; C:nucleus; IDA:MGI
GO:0005198; F:structural molecule activity; IEA:InterPro
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