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Protein

Lamin-B1

Gene

Lmnb1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: RGD
  • cellular response to corticosterone stimulus Source: RGD
  • cellular response to monosodium L-glutamate Source: RGD
  • cellular response to organic cyclic compound Source: RGD
  • neurogenesis Source: RGD
  • response to antibiotic Source: RGD
  • response to drug Source: RGD
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Lamin-B1
Gene namesi
Name:Lmnb1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620522. Lmnb1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • lamin filament Source: InterPro
  • nuclear envelope Source: RGD
  • nuclear inner membrane Source: UniProtKB-SubCell
  • nuclear lamina Source: RGD
  • nuclear matrix Source: RGD
  • nuclear membrane Source: RGD
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 584583Lamin-B1PRO_0000063818Add
BLAST
Propeptidei585 – 5873Removed in mature formBy similarityPRO_0000403468

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei3 – 31PhosphothreonineBy similarity
Modified residuei5 – 51PhosphothreonineBy similarity
Modified residuei16 – 161PhosphoserineBy similarity
Modified residuei20 – 201PhosphothreonineBy similarity
Modified residuei23 – 231PhosphoserineBy similarity
Modified residuei25 – 251PhosphothreonineBy similarity
Modified residuei28 – 281PhosphoserineBy similarity
Cross-linki102 – 102Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei111 – 1111N6-acetyllysineBy similarity
Modified residuei126 – 1261PhosphoserineCombined sources
Cross-linki145 – 145Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei157 – 1571N6-acetyllysineBy similarity
Modified residuei158 – 1581PhosphoserineCombined sources
Modified residuei200 – 2001PhosphoserineBy similarity
Modified residuei232 – 2321PhosphoserineBy similarity
Cross-linki241 – 241Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki261 – 261Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei271 – 2711N6-acetyllysineBy similarity
Modified residuei278 – 2781PhosphoserineBy similarity
Modified residuei302 – 3021PhosphoserineBy similarity
Disulfide bondi317 – 317InterchainBy similarity
Modified residuei330 – 3301N6-acetyllysineBy similarity
Modified residuei375 – 3751PhosphoserineBy similarity
Modified residuei483 – 4831N6-acetyllysineBy similarity
Modified residuei534 – 5341PhosphoserineBy similarity
Modified residuei576 – 5761PhosphothreonineCombined sources
Modified residuei584 – 5841Cysteine methyl esterBy similarity
Lipidationi584 – 5841S-farnesyl cysteineBy similarity

Post-translational modificationi

B-type lamins undergo a series of modifications, such as farnesylation and phosphorylation. Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations (By similarity).By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Isopeptide bond, Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

Proteomic databases

PaxDbiP70615.
PRIDEiP70615.

2D gel databases

World-2DPAGE0004:P70615.

PTM databases

iPTMnetiP70615.
PhosphoSiteiP70615.

Interactioni

Subunit structurei

Homodimer. Interacts with lamin-associated polypeptides IA, IB and 2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi250568. 11 interactions.
STRINGi10116.ENSRNOP00000019351.

Structurei

3D structure databases

ProteinModelPortaliP70615.
SMRiP70615. Positions 30-65, 320-387, 435-545.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini434 – 546113LTDAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 3433HeadAdd
BLAST
Regioni35 – 386352RodAdd
BLAST
Regioni35 – 6935Coil 1AAdd
BLAST
Regioni70 – 8112Linker 1Add
BLAST
Regioni82 – 215134Coil 1BAdd
BLAST
Regioni216 – 24328Linker 2Add
BLAST
Regioni244 – 386143Coil 2Add
BLAST
Regioni387 – 587201TailAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi415 – 4206Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi552 – 5609Glu-rich (highly acidic; could be involved in chromatin binding)

Sequence similaritiesi

Belongs to the intermediate filament family.Curated
Contains 1 LTD domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0977. Eukaryota.
ENOG410Y2H6. LUCA.
HOGENOMiHOG000007711.
HOVERGENiHBG013015.
InParanoidiP70615.
KOiK07611.
PhylomeDBiP70615.

Family and domain databases

Gene3Di2.60.40.1260. 1 hit.
InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR027696. Lamin_B.
IPR001322. Lamin_tail_dom.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF157. PTHR23239:SF157. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF00932. LTD. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF74853. SSF74853. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P70615-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATATPVQQR AGSRASAPAT PFSPTRLSRL QEKEELRELN DRLAVYIDKV
60 70 80 90 100
RSLETENSAL QLQVTEREEV RGRELTGLKA LYETELADAR RALDDTARER
110 120 130 140 150
AKLQIELGKF KAEHDQLLLN YAKKESDLSG AQIKLREYEA ALNSKDAALA
160 170 180 190 200
TALGDKKSLE GDLEDLKDQI AQLEASLSAA KKQLADETLL KVDLENRCQS
210 220 230 240 250
LTEDLEFRKN MYEEEINETR RKHETRLVEV DSGRQIEYEY KLAQALHEMR
260 270 280 290 300
EQHDAQVRLY KEELEQTYHA KLENARLSSE MNTSTVNSAR GGMMESRMRI
310 320 330 340 350
ESLSSQLSNL QKDSRACLER IQELEDMLAK ERDNSRRMLS DKEREMAEIR
360 370 380 390 400
DQMQQQLNDY EQLLDVKLAL DMEISAYRKL LEGEEERLKL SPSPSSRVTV
410 420 430 440 450
SRASSSRSVR TTRGKRKRVD VEESEASSSV SISHSASATG NVCIEEIDVD
460 470 480 490 500
GKFIRLKNTS EQDQPMGGWE MIRKIGDTSV SYKYTSRYVL KAGQTVTVWA
510 520 530 540 550
ANAGVTASPP TDLIWKNQNS WGTGEDVKVV LKNSQGEEVA QRSTVFKTTI
560 570 580
PEEEEEEEEE PIGVPLEEER FHQQGTPRAS NKSCAIM
Length:587
Mass (Da):66,606
Last modified:January 23, 2007 - v3
Checksum:i8187CA32728CC012
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72353 mRNA. Translation: AAB09600.1.
RefSeqiNP_446357.1. NM_053905.1.
UniGeneiRn.11362.

Genome annotation databases

GeneIDi116685.
KEGGirno:116685.
UCSCiRGD:620522. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72353 mRNA. Translation: AAB09600.1.
RefSeqiNP_446357.1. NM_053905.1.
UniGeneiRn.11362.

3D structure databases

ProteinModelPortaliP70615.
SMRiP70615. Positions 30-65, 320-387, 435-545.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250568. 11 interactions.
STRINGi10116.ENSRNOP00000019351.

PTM databases

iPTMnetiP70615.
PhosphoSiteiP70615.

2D gel databases

World-2DPAGE0004:P70615.

Proteomic databases

PaxDbiP70615.
PRIDEiP70615.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi116685.
KEGGirno:116685.
UCSCiRGD:620522. rat.

Organism-specific databases

CTDi4001.
RGDi620522. Lmnb1.

Phylogenomic databases

eggNOGiKOG0977. Eukaryota.
ENOG410Y2H6. LUCA.
HOGENOMiHOG000007711.
HOVERGENiHBG013015.
InParanoidiP70615.
KOiK07611.
PhylomeDBiP70615.

Miscellaneous databases

PROiP70615.

Family and domain databases

Gene3Di2.60.40.1260. 1 hit.
InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR027696. Lamin_B.
IPR001322. Lamin_tail_dom.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF157. PTHR23239:SF157. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF00932. LTD. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF74853. SSF74853. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLMNB1_RAT
AccessioniPrimary (citable) accession number: P70615
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively.By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.