Q3U9G9 (LBR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lamin-B receptor

Alternative name(s):
Integral nuclear envelope inner membrane protein

Gene names

Name:

Lbr

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	626 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Anchors the lamina and the heterochromatin to the inner nuclear membrane By similarity.
Subunit structure	Interacts directly with CBX5. Can interact with chromodomain proteins. Interacts directly with DNA. Interaction with DNA is sequence independent with higher affinity for supercoiled and relaxed circular DNA than linear DNA By similarity.
Subcellular location	Nucleus inner membrane; Multi-pass membrane protein By similarity.
Domain	The Tudor domain may not recognize methylation marks, but rather bind unassembled free histone H3 By similarity.
Post-translational modification	Phosphorylated by CDK1 in mitosis when the inner nuclear membrane breaks down into vesicles that dissociate from the lamina and the chromatin. It is phosphorylated by different protein kinases in interphase when the membrane is associated with these structures. Phosphorylation of LBR and HP1 proteins may be responsible for some of the alterations in chromatin organization and nuclear structure which occur at various times during the cell cycle. Phosphorylated by SRPK1. In late anaphase LBR is dephosphorylated, probably by PP1 and/or PP2A, allowing reassociation with chromatin By similarity.
Sequence similarities	Belongs to the ERG4/ERG24 family. Contains 1 Tudor domain.

Ontologies

Keywords
Cellular component	Membrane Nucleus
Domain	Transmembrane Transmembrane helix
Ligand	DNA-binding
Molecular function	Receptor
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	integral to membrane Inferred from sequence orthology PubMed 10671519. Source: MGI mitochondrion Inferred from electronic annotation. Source: Compara nuclear inner membrane Traceable author statement PubMed 11591818. Source: MGI nuclear lamina Traceable author statement PubMed 11591818. Source: MGI
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 626	626	Lamin-B receptor		PRO_0000227909
Regions
	Topological domain	1 – 221	221	Nuclear Potential
	Transmembrane	222 – 242	21	Helical; Potential
	Transmembrane	269 – 289	21	Helical; Potential
	Transmembrane	310 – 330	21	Helical; Potential
	Transmembrane	337 – 357	21	Helical; Potential
	Transmembrane	427 – 447	21	Helical; Potential
	Transmembrane	458 – 478	21	Helical; Potential
	Transmembrane	492 – 512	21	Helical; Potential
	Transmembrane	572 – 592	21	Helical; Potential
	Domain	1 – 62	62	Tudor
Amino acid modifications
	Modified residue	55	1	N6-acetyllysine By similarity
	Modified residue	71	1	Phosphoserine; by CDK1 By similarity
	Modified residue	86	1	Phosphoserine; by CDK1 By similarity
	Modified residue	90	1	Phosphoserine By similarity
	Modified residue	101	1	Phosphoserine Ref.4
	Modified residue	103	1	Phosphoserine Ref.4
	Modified residue	128	1	Phosphothreonine By similarity
	Modified residue	605	1	N6-acetyllysine By similarity
	Modified residue	612	1	N6-acetyllysine By similarity
	Glycosylation	98	1	O-linked (GlcNAc) By similarity
Experimental info
	Sequence conflict	174	1	T → A in AAH42522. Ref.2
	Sequence conflict	174	1	T → A in AAH21516. Ref.2
	Sequence conflict	263	1	E → G in BAE30698. Ref.1
	Sequence conflict	525	1	N → S in BAE30698. Ref.1
	Sequence conflict	585	1	I → T in AAH14835. Ref.2
	Sequence conflict	600	1	H → N in BAE36563. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q3U9G9 [UniParc]. Last modified March 21, 2006. Version 2. Checksum: 559CAAFFF73836F4	FASTA	626	71,440
	10 20 30 40 50 60 MPSRKFVEGE VVRGRWPGSS LYYEVEILSH DNKSQLYTVK YKDGTELELK ESDIKPLKSF 70 80 90 100 110 120 KQRKSGSISS SPSRRRGSRS RSRSRSRSRS PGRAPKGSRR SVSASHEGDV KEKKEKEMRR 130 140 150 160 170 180 EILQVKLTPL VLKPFGNSVS VYNGEPEHME KNATPYKDKQ ERIILSTEDR YIVTQYSLRP 190 200 210 220 230 240 RREEVKAKEI ESEEQNLVTK GPAPLGTFQV TTPQRKDLEF GGVPGAVLIM LGLPACVLLL 250 260 270 280 290 300 LLQCRQKDPG LLHFPPPLPA LHELWEPRVC GVYLLWFFVQ ALFHLLPVGK VAEGTPLVDG 310 320 330 340 350 360 RRLQYRLNGL YAFILTSAAL GAAVFWGVEL CYLYTHFLQL ALAATGFSVL LSAYLYVRSL 370 380 390 400 410 420 RAPREELSPA SSGNAVYDFF IGRELNPRLG AFDLKFFCEL RPGLIGWVVI NLVMLLMEMK 430 440 450 460 470 480 IQERAAPSLA MILVNSFQLL YVVDALWNEE ALLTSMDIMH DGFGFMLAFG DLVWVPFTYS 490 500 510 520 530 540 LQAFYLVSHP HDLSWPLASV IIALKLCGYV IFRCANSQKN AFRKNPTDPK LAHLKTIHTS 550 560 570 580 590 600 TGKSLLVSGW WGFVRHPNYL GDLIMALAWS LPCGFNHLLP YFYIIYFTAL LIHREARDEH 610 620 QCRRKYGLAW EKYCQRVPYR IFPYIY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone marrow, Colon, Liver, Pituitary and Thymus.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary gland.
[3]	"Mutations at the mouse ichthyosis locus are within the lamin B receptor gene: a single gene model for human Pelger-Huet anomaly." Shultz L.D., Lyons B.L., Burzenski L.M., Gott B., Samuels R., Schweitzer P.A., Dreger C., Herrmann H., Kalscheuer V., Olins A.L., Olins D.E., Sperling K., Hoffmann K. Hum. Mol. Genet. 12:61-69(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-308 AND 324-584.
[4]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-103, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK030606 mRNA. Translation: BAC27042.1. AK028426 mRNA. Translation: BAE20442.1. AK033459 mRNA. Translation: BAE20487.1. AK151798 mRNA. Translation: BAE30698.1. AK161762 mRNA. Translation: BAE36563.1. AK166850 mRNA. Translation: BAE39069.1. AK167157 mRNA. Translation: BAE39298.1. BC010261 mRNA. Translation: AAH10261.1. BC014835 mRNA. Translation: AAH14835.1. BC021516 mRNA. Translation: AAH21516.1. BC029171 mRNA. Translation: AAH29171.1. BC042522 mRNA. Translation: AAH42522.1. AY148158 Genomic DNA. Translation: AAN76314.1. AY148158 Genomic DNA. Translation: AAN76315.1.
IPI	IPI00331173.
RefSeq	NP_598576.2. NM_133815.2.
UniGene	Mm.4538.
3D structure databases
ProteinModelPortal	Q3U9G9.
SMR	Q3U9G9. Positions 1-55.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4112231.
PTM databases
PhosphoSite	Q3U9G9.
Proteomic databases
PaxDb	Q3U9G9.
PRIDE	Q3U9G9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000005003; ENSMUSP00000005003; ENSMUSG00000004880.
GeneID	98386.
KEGG	mmu:98386.
UCSC	uc007dxo.2. mouse.
Organism-specific databases
CTD	3930.
MGI	MGI:2138281. Lbr.
Phylogenomic databases
eggNOG	NOG72042.
GeneTree	ENSGT00390000000417.
HOVERGEN	HBG007825.
InParanoid	Q3U9G9.
OMA	ANSQKNA.
OrthoDB	EOG4FBHT3.
Gene expression databases
ArrayExpress	Q3U9G9.
Bgee	Q3U9G9.
CleanEx	MM_LBR.
Genevestigator	Q3U9G9.
GermOnline	ENSMUSG00000004880. Mus musculus.
Family and domain databases
InterPro	IPR001171. Ergosterol_biosynth_ERG4_ERG24. IPR019023. Lamin-B_rcpt_of_tudor. IPR018083. Sterol_reductase_CS. IPR002999. Tudor. [Graphical view]
Pfam	PF01222. ERG4_ERG24. 1 hit. PF09465. LBR_tudor. 1 hit. [Graphical view]
SMART	SM00333. TUDOR. 1 hit. [Graphical view]
PROSITE	PS01017. STEROL_REDUCT_1. 1 hit. PS01018. STEROL_REDUCT_2. 1 hit. PS50304. TUDOR. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	353440.
SOURCE	Search...

Entry information

Entry name

LBR_MOUSE

Accession

Primary (citable) accession number: Q3U9G9
Secondary accession number(s): Q3TSW2 , Q811V8, Q811V9, Q8BST3, Q8K2Y8, Q8VDM0, Q91YS5, Q91Z27

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	March 21, 2006
Last modified:	April 3, 2013
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program