Q14739 (LBR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lamin-B receptor

Alternative name(s):
Integral nuclear envelope inner membrane protein
LMN2R

Gene names

Name:

LBR

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	615 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. Ref.10
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. Ref.1 Ref.8 Ref.13
Subcellular location	Nucleus inner membrane; Multi-pass membrane protein.
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. Ref.9 Ref.19
Involvement in disease	Pelger-Huet anomaly (PHA) [MIM:169400]: An autosomal dominant inherited abnormality of granulocytes, characterized by abnormal ovoid shape, reduced nuclear segmentation and an apparently looser chromatin structure. Some individuals occasionally have skeletal anomalies, developmental delay, and seizures. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12 Ref.23 Hydrops-ectopic calcification-moth-eaten skeletal dysplasia (HEM) [MIM:215140]: 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12 Reynolds syndrome (REYNS) [MIM:613471]: A syndrome specifically associating limited cutaneous systemic sclerosis and primary biliary 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. Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12 Ref.24
Sequence similarities	Belongs to the ERG4/ERG24 family. Contains 1 Tudor domain.
Sequence caution	The sequence BAD92751.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Membrane Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Transmembrane Transmembrane helix
Ligand	DNA-binding
Molecular function	Receptor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cholesterol biosynthetic process Traceable author statement. Source: Reactome
Cellular_component	integral to nuclear inner membrane Traceable author statement Ref.1. Source: ProtInc mitochondrion Inferred from direct assay. Source: HPA
Molecular_function	DNA binding Traceable author statement Ref.1. Source: ProtInc lamin binding Traceable author statement Ref.1. Source: ProtInc oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CBX3	Q13185	4	EBI-1055147,EBI-78176
CBX5	P45973	4	EBI-1055147,EBI-78219

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 615

615

Lamin-B receptor

PRO_0000207510

Regions

Topological domain

1 – 211

211

Nuclear Potential

Transmembrane

212 – 232

21

Helical; Potential

Transmembrane

258 – 278

21

Helical; Potential

Transmembrane

299 – 319

21

Helical; Potential

Transmembrane

326 – 346

21

Helical; Potential

Transmembrane

386 – 406

21

Helical; Potential

Transmembrane

447 – 467

21

Helical; Potential

Transmembrane

481 – 501

21

Helical; Potential

Transmembrane

561 – 581

21

Helical; Potential

Domain

1 – 62

62

Tudor

Amino acid modifications

Modified residue

55

1

N6-acetyllysine Ref.16

Modified residue

71

1

Phosphoserine; by CDK1 Ref.19

Modified residue

86

1

Phosphoserine; by CDK1 Ref.19

Modified residue

97

1

Phosphoserine Ref.17

Modified residue

99

1

Phosphoserine Ref.20

Modified residue

118

1

Phosphothreonine Ref.15 Ref.17

Modified residue

594

1

N6-acetyllysine Ref.16

Modified residue

601

1

N6-acetyllysine Ref.16

Natural variations

Natural variant

119

1

P → L in PHA. Ref.23

VAR_017841

Natural variant

154

1

S → N. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6
Corresponds to variant rs2230419 [ dbSNP | Ensembl ].

VAR_024318

Natural variant

169

1

R → C.
Corresponds to variant rs2230420 [ dbSNP | Ensembl ].

VAR_052155

Natural variant

311

1

T → A.
Corresponds to variant rs2275601 [ dbSNP | Ensembl ].

VAR_020209

Natural variant

372

1

R → C in REYNS. Ref.24

VAR_063811

Natural variant

569

1

P → R in PHA. Ref.23

VAR_017842

Experimental info

Sequence conflict

301

1

A → P in AAA59494. Ref.1

Sequence conflict

452

1

F → L in BAD96554. Ref.5

Sequence conflict

530

1

T → S in AAA59494. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

615

Helix Strand Turn

Details...

Beta strand

11 – 15

5

Turn

17 – 19

3

Beta strand

22 – 31

10

Turn

32 – 35

4

Beta strand

36 – 40

5

Beta strand

46 – 50

5

Turn

51 – 53

3

Sequences

	Sequence		Length	Mass (Da)
	Q14739 [UniParc]. Last modified January 31, 2002. Version 2. Checksum: 5A7388776F43C66D	FASTA	615	70,703
	10 20 30 40 50 60 MPSRKFADGE VVRGRWPGSS LYYEVEILSH DSTSQLYTVK YKDGTELELK ENDIKPLTSF 70 80 90 100 110 120 RQRKGGSTSS SPSRRRGSRS RSRSRSPGRP PKSARRSASA SHQADIKEAR REVEVKLTPL 130 140 150 160 170 180 ILKPFGNSIS RYNGEPEHIE RNDAPHKNTQ EKFSLSQESS YIATQYSLRP RREEVKLKEI 190 200 210 220 230 240 DSKEEKYVAK ELAVRTFEVT PIRAKDLEFG GVPGVFLIMF GLPVFLFLLL LMCKQKDPSL 250 260 270 280 290 300 LNFPPPLPAL YELWETRVFG VYLLWFLIQV LFYLLPIGKV VEGTPLIDGR RLKYRLNGFY 310 320 330 340 350 360 AFILTSAVIG TSLFQGVEFH YVYSHFLQFA LAATVFCVVL SVYLYMRSLK APRNDLSPAS 370 380 390 400 410 420 SGNAVYDFFI GRELNPRIGT FDLKYFCELR PGLIGWVVIN LVMLLAEMKI QDRAVPSLAM 430 440 450 460 470 480 ILVNSFQLLY VVDALWNEEA LLTTMDIIHD GFGFMLAFGD LVWVPFIYSF QAFYLVSHPN 490 500 510 520 530 540 EVSWPMASLI IVLKLCGYVI FRGANSQKNA FRKNPSDPKL AHLKTIHTST GKNLLVSGWW 550 560 570 580 590 600 GFVRHPNYLG DLIMALAWSL PCGFNHILPY FYIIYFTMLL VHREARDEYH CKKKYGVAWE 610 KYCQRVPYRI FPYIY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure analysis and lamin B and DNA binding of human LBR, an integral protein of the nuclear envelope inner membrane." Ye Q., Worman H.J. J. Biol. Chem. 269:11306-11311(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DNA; LMNB1 AND LMNB2.
[2]	"Characterization of the human gene encoding LBR, an integral protein of the nuclear envelope inner membrane." Schuler E., Lin F., Worman H.J. J. Biol. Chem. 269:11312-11317(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASN-154.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-154.
[4]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-154. Tissue: Brain.
[5]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-154. Tissue: Liver.
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-154.
[7]	"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]. Tissue: Skin.
[8]	"Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR." Ye Q., Callebaut I., Pezhman A., Courvalin J.-C., Worman H.J. J. Biol. Chem. 272:14983-14989(1997) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, INTERACTION WITH CBX5.
[9]	"SRPK1 and LBR protein kinases show identical substrate specificities." Papoutsopoulou S., Nikolakaki E., Giannakouros T. Biochem. Biophys. Res. Commun. 255:602-607(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY SRPK1.
[10]	"Inner nuclear membrane protein LBR preferentially interacts with DNA secondary structures and nucleosomal linker." Duband-Goulet I., Courvalin J.-C. Biochemistry 39:6483-6488(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huet anomaly)." Hoffmann K., Dreger C.K., Olins A.L., Olins D.E., Shultz L.D., Lucke B., Karl H., Kaps R., Mueller D., Vaya A., Aznar J., Ware R.E., Sotelo Cruz N., Lindner T.H., Herrmann H., Reis A., Sperling K. Nat. Genet. 31:410-414(2002) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE.
[12]	"Autosomal recessive HEM/Greenberg skeletal dysplasia is caused by 3 beta-hydroxysterol delta 14-reductase deficiency due to mutations in the lamin B receptor gene." Waterham H.R., Koster J., Mooyer P., van Noort G., Kelley R.I., Wilcox W.R., Wanders R.J., Hennekam R.C.M., Oosterwijk J.C. Am. J. Hum. Genet. 72:1013-1017(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE.
[13]	"The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain." Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III Biochem. Biophys. Res. Commun. 331:929-937(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, INTERACTION WITH CBX5.
[14]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55; LYS-594 AND LYS-601, MASS SPECTROMETRY.
[17]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND THR-118, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"Temporal control of nuclear envelope assembly by phosphorylation of lamin B receptor." Tseng L.C., Chen R.H. Mol. Biol. Cell 22:3306-3317(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-71 AND SER-86 BY CDK1.
[20]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, MASS SPECTROMETRY.
[21]	"Solution structure of the Tudor domain of human lamin-B receptor." RIKEN structural genomics initiative (RSGI) Submitted (SEP-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1-55.
[22]	"Solution structure of the Tudor domain of human lamin-B receptor." RIKEN structural genomics initiative (RSGI) Submitted (FEB-2009) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1-55.
[23]	"Lamin B-receptor mutations in Pelger-Huet anomaly." Best S., Salvati F., Kallo J., Garner C., Height S., Thein S.L., Rees D.C. Br. J. Haematol. 123:542-544(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PHA LEU-119 AND ARG-569.
[24]	"LBR mutation and nuclear envelope defects in a patient affected with Reynolds syndrome." Gaudy-Marqueste C., Roll P., Esteves-Vieira V., Weiller P.J., Grob J.J., Cau P., Levy N., De Sandre-Giovannoli A. J. Med. Genet. 47:361-370(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT REYNS CYS-372.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L25931 mRNA. Translation: AAA59494.1.
L25941 , L25932, L25933, L25934, L25935, L25936, L25937, L25938, L25939, L25940 Genomic DNA. Translation: AAA59495.1.
AB209514 mRNA. Translation: BAD92751.1. Different initiation.
AK222834 mRNA. Translation: BAD96554.1.
AK312258 mRNA. Translation: BAG35190.1.
CH471098 Genomic DNA. Translation: EAW69741.1.
BC020079 mRNA. Translation: AAH20079.1.

IPI

IPI00292135.

PIR

A53616.

RefSeq

NP_002287.2. NM_002296.3.
NP_919424.1. NM_194442.2.

UniGene

Hs.435166.
Hs.735694.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DIG	NMR	-	A	1-55	[»]

ProteinModelPortal

Q14739.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5987N.

IntAct

Q14739. 3 interactions.

MINT

MINT-1631069.

STRING

9606.ENSP00000272163.

PTM databases

PhosphoSite

Q14739.

Polymorphism databases

DMDM

20141468.

Proteomic databases

PaxDb

Q14739.

PeptideAtlas

Q14739.

PRIDE

Q14739.

Protocols and materials databases

DNASU

3930.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000272163; ENSP00000272163; ENSG00000143815.
ENST00000338179; ENSP00000339883; ENSG00000143815.

GeneID

3930.

KEGG

hsa:3930.

UCSC

uc001hoy.3. human.

Organism-specific databases

CTD

3930.

GeneCards

GC01M225589.

HGNC

HGNC:6518. LBR.

HPA

HPA049840.

MIM

169400. phenotype.
215140. phenotype.
600024. gene.
613471. phenotype.

neXtProt

NX_Q14739.

Orphanet

1426. Greenberg dysplasia.
779. Reynolds syndrome.

PharmGKB

PA30304.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG72042.

HOGENOM

HOG000193296.

HOVERGEN

HBG007825.

InParanoid

Q14739.

OMA

ANSQKNA.

OrthoDB

EOG4FBHT3.

PhylomeDB

Q14739.

Enzyme and pathway databases

BioCyc

MetaCyc:HS07110-MONOMER.

BRENDA

1.3.1.70. 2681.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

Q14739.

Bgee

Q14739.

CleanEx

HS_LBR.

Genevestigator

Q14739.

GermOnline

ENSG00000143815. Homo sapiens.

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

ChiTaRS

LBR. human.

EvolutionaryTrace

Q14739.

GenomeRNAi

3930.

NextBio

15431.

SOURCE

Search...

Entry information

Entry name

LBR_HUMAN

Accession

Primary (citable) accession number: Q14739
Secondary accession number(s): B2R5P3 , Q14740, Q53GU7, Q59FE6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 31, 2002
Last modified:	May 1, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.