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Q14739 (LBR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lamin-B receptor
Alternative name(s):
Integral nuclear envelope inner membrane protein
LMN2R
Gene names
Name:LBR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length615 AA.
Sequence statusComplete.
Protein existenceEvidence 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.23

Greenberg dysplasia (GRBGD) [MIM:215140]: A rare autosomal recessive chondrodystrophy characterized by early in utero lethality. Affected fetuses typically present with fetal hydrops, short-limbed dwarfism, and a marked disorganization of chondro-osseous calcification, and ectopic ossification centers.
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.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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 615615Lamin-B receptor
PRO_0000207510

Regions

Topological domain1 – 211211Nuclear Potential
Transmembrane212 – 23221Helical; Potential
Transmembrane258 – 27821Helical; Potential
Transmembrane299 – 31921Helical; Potential
Transmembrane326 – 34621Helical; Potential
Transmembrane386 – 40621Helical; Potential
Transmembrane447 – 46721Helical; Potential
Transmembrane481 – 50121Helical; Potential
Transmembrane561 – 58121Helical; Potential
Domain1 – 6262Tudor

Amino acid modifications

Modified residue551N6-acetyllysine Ref.16
Modified residue671Phosphoserine By similarity
Modified residue711Phosphoserine; by CDK1 Ref.19
Modified residue861Phosphoserine; by CDK1 Ref.19
Modified residue971Phosphoserine Ref.17
Modified residue991Phosphoserine Ref.20
Modified residue1181Phosphothreonine Ref.15 Ref.17
Modified residue5941N6-acetyllysine Ref.16
Modified residue6011N6-acetyllysine Ref.16

Natural variations

Natural variant1191P → L in PHA. Ref.23
VAR_017841
Natural variant1541S → N. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6
Corresponds to variant rs2230419 [ dbSNP | Ensembl ].
VAR_024318
Natural variant1691R → C.
Corresponds to variant rs2230420 [ dbSNP | Ensembl ].
VAR_052155
Natural variant3111T → A.
Corresponds to variant rs2275601 [ dbSNP | Ensembl ].
VAR_020209
Natural variant3721R → C in REYNS. Ref.24
VAR_063811
Natural variant5691P → R in PHA. Ref.23
VAR_017842

Experimental info

Sequence conflict3011A → P in AAA59494. Ref.1
Sequence conflict4521F → L in BAD96554. Ref.5
Sequence conflict5301T → S in AAA59494. Ref.1

Secondary structure

............ 615
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14739 [UniParc].

Last modified January 31, 2002. Version 2.
Checksum: 5A7388776F43C66D

FASTA61570,703
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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: INVOLVEMENT IN GRBGD.
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L25931 mRNA. Translation: AAA59494.1.
L25941 expand/collapse EMBL AC list , 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.
CCDSCCDS1545.1.
PIRA53616.
RefSeqNP_002287.2. NM_002296.3.
NP_919424.1. NM_194442.2.
UniGeneHs.435166.
Hs.735694.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DIGNMR-A1-55[»]
ProteinModelPortalQ14739.
SMRQ14739. Positions 1-55.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110122. 27 interactions.
DIPDIP-5987N.
IntActQ14739. 8 interactions.
MINTMINT-1631069.
STRING9606.ENSP00000272163.

PTM databases

PhosphoSiteQ14739.

Polymorphism databases

DMDM20141468.

Proteomic databases

MaxQBQ14739.
PaxDbQ14739.
PeptideAtlasQ14739.
PRIDEQ14739.

Protocols and materials databases

DNASU3930.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000272163; ENSP00000272163; ENSG00000143815.
ENST00000338179; ENSP00000339883; ENSG00000143815.
GeneID3930.
KEGGhsa:3930.
UCSCuc001hoy.3. human.

Organism-specific databases

CTD3930.
GeneCardsGC01M225589.
HGNCHGNC:6518. LBR.
HPAHPA049840.
MIM169400. phenotype.
215140. phenotype.
600024. gene.
613471. phenotype.
neXtProtNX_Q14739.
Orphanet1426. Greenberg dysplasia.
779. Reynolds syndrome.
PharmGKBPA30304.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72042.
HOGENOMHOG000193296.
HOVERGENHBG007825.
InParanoidQ14739.
OMAVYSHFLQ.
OrthoDBEOG75B85C.
PhylomeDBQ14739.
TreeFamTF101179.

Enzyme and pathway databases

BioCycMetaCyc:HS07110-MONOMER.
BRENDA1.3.1.70. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ14739.
BgeeQ14739.
CleanExHS_LBR.
GenevestigatorQ14739.

Family and domain databases

InterProIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR019023. Lamin-B_rcpt_of_tudor.
IPR018083. Sterol_reductase_CS.
IPR002999. Tudor.
[Graphical view]
PfamPF01222. ERG4_ERG24. 1 hit.
PF09465. LBR_tudor. 1 hit.
[Graphical view]
SMARTSM00333. TUDOR. 1 hit.
[Graphical view]
PROSITEPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLBR. human.
EvolutionaryTraceQ14739.
GeneWikiLamin_B_receptor.
GenomeRNAi3930.
NextBio15431.
PROQ14739.
SOURCESearch...

Entry information

Entry nameLBR_HUMAN
AccessionPrimary (citable) accession number: Q14739
Secondary accession number(s): B2R5P3 expand/collapse secondary AC list , Q14740, Q53GU7, Q59FE6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 31, 2002
Last modified: July 9, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM