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Lamin-B2

 LMNB2_HUMAN             Reviewed;         620 AA.
Q03252; O75292; Q14734; Q96DF6;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
11-NOV-2015, sequence version 4.
02-JUN-2021, entry version 210.
RecName: Full=Lamin-B2;
Flags: Precursor;
Name=LMNB2; Synonyms=LMN2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 94-104; 131-150; 152-161; 192-202; 236-244; 294-306;
345-372; 486-496 AND 530-555, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 105-620, AND NUCLEOTIDE SEQUENCE [GENOMIC
DNA] OF 531-620.
PubMed=1630457; DOI=10.1128/mcb.12.8.3499;
Biamonti G., Giacca M., Perini G., Contreas G., Zentilin L., Weighardt F.,
Guerra M., Valle G.D., Saccone S., Riva S., Falaschi A.;
"The gene for a novel human lamin maps at a highly transcribed locus of
chromosome 19 which replicates at the onset of S-phase.";
Mol. Cell. Biol. 12:3499-3506(1992).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling
networks.";
Cell 127:635-648(2006).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using sequential
IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34; SER-37; SER-422; SER-424
AND SER-426, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420; SER-422; SER-424 AND
SER-426, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-23; THR-34; SER-37; SER-316
AND SER-497, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-77; LYS-81 AND LYS-195, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.o114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to replication
stress reveals novel small ubiquitin-like modified target proteins and
acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-77; LYS-81; LYS-195; LYS-255 AND
LYS-489, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[22]
VARIANT APLD THR-427, AND VARIANT GLN-235.
PubMed=16826530; DOI=10.1086/505885;
Hegele R.A., Cao H., Liu D.M., Costain G.A., Charlton-Menys V.,
Rodger N.W., Durrington P.N.;
"Sequencing of the reannotated LMNB2 gene reveals novel mutations in
patients with acquired partial lipodystrophy.";
Am. J. Hum. Genet. 79:383-389(2006).
[23]
VARIANT [LARGE SCALE ANALYSIS] TRP-236.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
[24]
VARIANT APLD HIS-252.
PubMed=22768673; DOI=10.1515/jpem-2012-0007;
Gao J., Li Y., Fu X., Luo X.;
"A Chinese patient with acquired partial lipodystrophy caused by a novel
mutation with LMNB2 gene.";
J. Pediatr. Endocrinol. Metab. 25:375-377(2012).
[25]
VARIANT EPM9 TYR-157, AND CHARACTERIZATION OF VARIANT EPM9 TYR-157.
PubMed=25954030; DOI=10.1093/hmg/ddv171;
Damiano J.A., Afawi Z., Bahlo M., Mauermann M., Misk A., Arsov T.,
Oliver K.L., Dahl H.H., Shearer A.E., Smith R.J., Hall N.E., Mahmood K.,
Leventer R.J., Scheffer I.E., Muona M., Lehesjoki A.E., Korczyn A.D.,
Herrmann H., Berkovic S.F., Hildebrand M.S.;
"Mutation of the nuclear lamin gene LMNB2 in progressive myoclonus epilepsy
with early ataxia.";
Hum. Mol. Genet. 24:4483-4490(2015).
[26]
VARIANT GLN-235.
PubMed=27535533; DOI=10.1038/nature19057;
Exome Aggregation Consortium;
Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E., Fennell T.,
O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B., Tukiainen T.,
Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K., Zhao F., Zou J.,
Pierce-Hoffman E., Berghout J., Cooper D.N., Deflaux N., DePristo M.,
Do R., Flannick J., Fromer M., Gauthier L., Goldstein J., Gupta N.,
Howrigan D., Kiezun A., Kurki M.I., Moonshine A.L., Natarajan P.,
Orozco L., Peloso G.M., Poplin R., Rivas M.A., Ruano-Rubio V., Rose S.A.,
Ruderfer D.M., Shakir K., Stenson P.D., Stevens C., Thomas B.P., Tiao G.,
Tusie-Luna M.T., Weisburd B., Won H.H., Yu D., Altshuler D.M.,
Ardissino D., Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S., Laakso M.,
McCarroll S., McCarthy M.I., McGovern D., McPherson R., Neale B.M.,
Palotie A., Purcell S.M., Saleheen D., Scharf J.M., Sklar P.,
Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C., Wilson J.G.,
Daly M.J., MacArthur D.G.;
"Analysis of protein-coding genetic variation in 60,706 humans.";
Nature 536:285-291(2016).
-!- FUNCTION: 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.
-!- SUBUNIT: Interacts with TMEM43. {ECO:0000250}.
-!- INTERACTION:
Q03252; A2BDD9: AMOT; NbExp=3; IntAct=EBI-2830427, EBI-17286414;
Q03252; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-2830427, EBI-746752;
Q03252; P35219: CA8; NbExp=3; IntAct=EBI-2830427, EBI-718700;
Q03252; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-2830427, EBI-744556;
Q03252; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-2830427, EBI-347573;
Q03252; Q16543: CDC37; NbExp=3; IntAct=EBI-2830427, EBI-295634;
Q03252; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-2830427, EBI-2349927;
Q03252; P07954: FH; NbExp=3; IntAct=EBI-2830427, EBI-1050358;
Q03252; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2830427, EBI-618309;
Q03252; P02545: LMNA; NbExp=6; IntAct=EBI-2830427, EBI-351935;
Q03252; P20700: LMNB1; NbExp=5; IntAct=EBI-2830427, EBI-968218;
Q03252; Q03252: LMNB2; NbExp=3; IntAct=EBI-2830427, EBI-2830427;
Q03252; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-2830427, EBI-1216080;
Q03252; P55081: MFAP1; NbExp=3; IntAct=EBI-2830427, EBI-1048159;
Q03252; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-2830427, EBI-10172526;
Q03252; O14753: OVOL1; NbExp=3; IntAct=EBI-2830427, EBI-3917713;
Q03252; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-2830427, EBI-14066006;
Q03252; P78424: POU6F2; NbExp=3; IntAct=EBI-2830427, EBI-12029004;
Q03252; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-2830427, EBI-1105153;
Q03252; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-2830427, EBI-1105213;
Q03252; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-2830427, EBI-741515;
Q03252; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-2830427, EBI-11952721;
Q03252; P14373: TRIM27; NbExp=3; IntAct=EBI-2830427, EBI-719493;
Q03252; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-2830427, EBI-10241197;
Q03252; O75604: USP2; NbExp=3; IntAct=EBI-2830427, EBI-743272;
Q03252; Q9Y3C0: WASHC3; NbExp=3; IntAct=EBI-2830427, EBI-712969;
Q03252; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-2830427, EBI-14104088;
Q03252; Q15911-2: ZFHX3; NbExp=3; IntAct=EBI-2830427, EBI-10237226;
-!- SUBCELLULAR LOCATION: Nucleus inner membrane; Lipid-anchor;
Nucleoplasmic side.
-!- PTM: 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.
-!- DISEASE: Partial acquired lipodystrophy (APLD) [MIM:608709]: A rare
childhood disease characterized by loss of subcutaneous fat from the
face and trunk. Fat deposition on the pelvic girdle and lower limbs is
normal or excessive. Most frequently, onset between 5 and 15 years of
age. Most affected subjects are females and some show no other
abnormality, but many develop glomerulonephritis, diabetes mellitus,
hyperlipidemia, and complement deficiency. Mental retardation in some
cases. APLD is a sporadic disorder of unknown etiology.
{ECO:0000269|PubMed:16826530, ECO:0000269|PubMed:22768673}. Note=The
disease is caused by variants affecting the gene represented in this
entry.
-!- DISEASE: Epilepsy, progressive myoclonic 9 (EPM9) [MIM:616540]: A form
of progressive myoclonic epilepsy, a clinically and genetically
heterogeneous group of disorders defined by the combination of action
and reflex myoclonus, other types of epileptic seizures, and
progressive neurodegeneration and neurocognitive impairment. EPM9 is an
autosomal recessive form characterized by myoclonus, tonic-clonic
seizures, ataxia, and delayed psychomotor development.
{ECO:0000269|PubMed:25954030}. Note=The disease may be caused by
variants affecting the gene represented in this entry.
-!- 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.
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
-!- SEQUENCE CAUTION:
Sequence=AAH06551.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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EMBL; BT007441; AAP36109.1; -; mRNA.
EMBL; AC011522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005624; AAC34573.1; -; Genomic_DNA.
EMBL; BC006551; AAH06551.1; ALT_INIT; mRNA.
EMBL; M94362; AAA80979.1; -; mRNA.
EMBL; M94363; AAB00873.1; ALT_SEQ; Genomic_DNA.
CCDS; CCDS12090.2; -.
RefSeq; NP_116126.3; NM_032737.3.
PDB; 2LLL; NMR; -; A=469-589.
PDB; 5BNW; X-ray; 2.40 A; D=403-415.
PDBsum; 2LLL; -.
PDBsum; 5BNW; -.
BMRB; Q03252; -.
SMR; Q03252; -.
BioGRID; 124281; 132.
DIP; DIP-57724N; -.
IntAct; Q03252; 60.
MINT; Q03252; -.
STRING; 9606.ENSP00000327054; -.
iPTMnet; Q03252; -.
MetOSite; Q03252; -.
PhosphoSitePlus; Q03252; -.
SwissPalm; Q03252; -.
BioMuta; LMNB2; -.
DMDM; 23503078; -.
REPRODUCTION-2DPAGE; IPI00009771; -.
EPD; Q03252; -.
jPOST; Q03252; -.
MassIVE; Q03252; -.
MaxQB; Q03252; -.
PaxDb; Q03252; -.
PeptideAtlas; Q03252; -.
PRIDE; Q03252; -.
ProteomicsDB; 58204; -.
ABCD; Q03252; 3 sequenced antibodies.
Antibodypedia; 10783; 351 antibodies.
DNASU; 84823; -.
Ensembl; ENST00000325327; ENSP00000327054; ENSG00000176619.
GeneID; 84823; -.
KEGG; hsa:84823; -.
CTD; 84823; -.
DisGeNET; 84823; -.
GeneCards; LMNB2; -.
HGNC; HGNC:6638; LMNB2.
HPA; ENSG00000176619; Low tissue specificity.
MalaCards; LMNB2; -.
MIM; 150341; gene.
MIM; 608709; phenotype.
MIM; 616540; phenotype.
neXtProt; NX_Q03252; -.
OpenTargets; ENSG00000176619; -.
Orphanet; 79087; Acquired partial lipodystrophy.
Orphanet; 457265; Progressive myoclonic epilepsy type 9.
PharmGKB; PA30404; -.
VEuPathDB; HostDB:ENSG00000176619.10; -.
eggNOG; KOG0977; Eukaryota.
GeneTree; ENSGT00940000160274; -.
InParanoid; Q03252; -.
OMA; MDGNAVT; -.
OrthoDB; 701388at2759; -.
TreeFam; TF101181; -.
PathwayCommons; Q03252; -.
BioGRID-ORCS; 84823; 10 hits in 997 CRISPR screens.
ChiTaRS; LMNB2; human.
GenomeRNAi; 84823; -.
Pharos; Q03252; Tbio.
PRO; PR:Q03252; -.
Proteomes; UP000005640; Chromosome 19.
RNAct; Q03252; protein.
Bgee; ENSG00000176619; Expressed in testis and 163 other tissues.
GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
Gene3D; 1.20.5.1160; -; 2.
Gene3D; 2.60.40.1260; -; 1.
InterPro; IPR018039; IF_conserved.
InterPro; IPR039008; IF_rod_dom.
InterPro; IPR042180; IF_rod_dom_coil1B.
InterPro; IPR001322; Lamin_tail_dom.
InterPro; IPR036415; Lamin_tail_dom_sf.
Pfam; PF00038; Filament; 1.
Pfam; PF00932; LTD; 1.
SMART; SM01391; Filament; 1.
SUPFAM; SSF74853; SSF74853; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
PROSITE; PS51841; LTD; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Coiled coil; Direct protein sequencing;
Disease variant; Epilepsy; Intermediate filament; Isopeptide bond;
Lipoprotein; Membrane; Methylation; Neurodegeneration; Nucleus;
Phosphoprotein; Prenylation; Reference proteome; Ubl conjugation.
CHAIN 1..617
/note="Lamin-B2"
/id="PRO_0000063820"
PROPEP 618..620
/note="Removed in mature form"
/evidence="ECO:0000250"
/id="PRO_0000403470"
DOMAIN 46..402
/note="IF rod"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
DOMAIN 462..579
/note="LTD"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
REGION 1..48
/note="Head"
REGION 1..38
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 49..83
/note="Coil 1A"
REGION 84..95
/note="Linker 1"
REGION 96..229
/note="Coil 1B"
REGION 230..256
/note="Linker 2"
REGION 257..400
/note="Coil 2"
REGION 399..464
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 401..620
/note="Tail"
REGION 581..620
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOTIF 435..440
/note="Nuclear localization signal"
/evidence="ECO:0000255"
COMPBIAS 406..429
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 23
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 34
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:17081983,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 37
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:23186163"
MOD_RES 81
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 316
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 420
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21406692"
MOD_RES 422
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:21406692"
MOD_RES 424
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:21406692"
MOD_RES 426
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:21406692"
MOD_RES 433
/note="Omega-N-methylarginine"
/evidence="ECO:0000250|UniProtKB:P21619"
MOD_RES 497
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 617
/note="Cysteine methyl ester"
/evidence="ECO:0000250"
LIPID 617
/note="S-farnesyl cysteine"
/evidence="ECO:0000250"
CROSSLNK 77
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:25755297,
ECO:0007744|PubMed:28112733"
CROSSLNK 81
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0007744|PubMed:25755297,
ECO:0007744|PubMed:28112733"
CROSSLNK 195
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:25755297,
ECO:0007744|PubMed:28112733"
CROSSLNK 255
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 489
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
VARIANT 157
/note="H -> Y (in EPM9; disrupts fibrillar formation;
dbSNP:rs797045143)"
/evidence="ECO:0000269|PubMed:25954030"
/id="VAR_074170"
VARIANT 235
/note="R -> Q (may be a risk factor for partial acquired
lipodystrophy; dbSNP:rs121912497)"
/evidence="ECO:0000269|PubMed:16826530,
ECO:0000269|PubMed:27535533"
/id="VAR_031063"
VARIANT 236
/note="R -> W (in a colorectal cancer sample; somatic
mutation; dbSNP:rs774297966)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_036370"
VARIANT 252
/note="Y -> H (in APLD)"
/evidence="ECO:0000269|PubMed:22768673"
/id="VAR_074171"
VARIANT 427
/note="A -> T (in APLD; dbSNP:rs57521499)"
/evidence="ECO:0000269|PubMed:16826530"
/id="VAR_031064"
CONFLICT 401
/note="R -> S (in Ref. 5; AAA80979)"
/evidence="ECO:0000305"
CONFLICT 439..475
/note="LEVEEPLGSGPSVLGTGTGGSGGFHLAQQASASGSVS -> WRWRSPWQRPK
RPGHGHGWQRWLPPGPAGLGLGQRH (in Ref. 5; AAA80979)"
/evidence="ECO:0000305"
STRAND 473..479
/evidence="ECO:0007829|PDB:2LLL"
STRAND 484..490
/evidence="ECO:0007829|PDB:2LLL"
STRAND 492..494
/evidence="ECO:0007829|PDB:2LLL"
STRAND 502..507
/evidence="ECO:0007829|PDB:2LLL"
STRAND 512..516
/evidence="ECO:0007829|PDB:2LLL"
STRAND 528..533
/evidence="ECO:0007829|PDB:2LLL"
HELIX 534..536
/evidence="ECO:0007829|PDB:2LLL"
TURN 542..544
/evidence="ECO:0007829|PDB:2LLL"
STRAND 545..548
/evidence="ECO:0007829|PDB:2LLL"
STRAND 552..555
/evidence="ECO:0007829|PDB:2LLL"
STRAND 558..565
/evidence="ECO:0007829|PDB:2LLL"
STRAND 571..580
/evidence="ECO:0007829|PDB:2LLL"
SEQUENCE 620 AA; 69948 MW; A8799BB12B6242B9 CRC64;
MSPPSPGRRR EQRRPRAAAT MATPLPGRAG GPATPLSPTR LSRLQEKEEL RELNDRLAHY
IDRVRALELE NDRLLLKISE KEEVTTREVS GIKALYESEL ADARRVLDET ARERARLQIE
IGKLRAELDE VNKSAKKREG ELTVAQGRVK DLESLFHRSE VELAAALSDK RGLESDVAEL
RAQLAKAEDG HAVAKKQLEK ETLMRVDLEN RCQSLQEELD FRKSVFEEEV RETRRRHERR
LVEVDSSRQQ EYDFKMAQAL EELRSQHDEQ VRLYKLELEQ TYQAKLDSAK LSSDQNDKAA
SAAREELKEA RMRLESLSYQ LSGLQKQASA AEDRIRELEE AMAGERDKFR KMLDAKEQEM
TEMRDVMQQQ LAEYQELLDV KLALDMEINA YRKLLEGEEE RLKLSPSPSS RVTVSRATSS
SSGSLSATGR LGRSKRKRLE VEEPLGSGPS VLGTGTGGSG GFHLAQQASA SGSVSIEEID
LEGKFVQLKN NSDKDQSLGN WRIKRQVLEG EEIAYKFTPK YILRAGQMVT VWAAGAGVAH
SPPSTLVWKG QSSWGTGESF RTVLVNADGE EVAMRTVKKS SVMRENENGE EEEEEAEFGE
EDLFHQQGDP RTTSRGCYVM


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Pathways :
WP493: MAPK signaling pathway

Related Genes :
[Lmnb2] Lamin-B2
[LMNB2 LMN2] Lamin-B2
[] Capsid protein VP0 (EC 2.7.7.48) (EC 3.4.22.28) (EC 3.4.22.46) (EC 3.6.1.15) (Capsid protein VP1) (Capsid protein VP3) (Capsid protein VP4) (Genome polyprotein) (Genome-linked protein VPg1) (Genome-linked protein VPg2) (Genome-linked protein VPg3) (Leader protease) (P1A) (P1B) (P1C) (P1D) (P52) (P56A) (Picornain 3C) (Protease 3C) (Protease P20B) (Protein 2A) (Protein 2C) (Protein 3A) (Protein 3B-1) (Protein 3B-2) (Protein 3B-3) (RNA-directed RNA polymerase 3D-POL) (VP4-VP2) (Virion protein 1) (Virion protein 2) (Virion protein 3) (Virion protein 4) (protein 2B)
[] Capsid protein VP0 (EC 2.7.7.48) (EC 3.4.22.28) (EC 3.4.22.46) (EC 3.6.1.15) (Capsid protein VP1) (Capsid protein VP3) (Capsid protein VP4) (Genome polyprotein) (Genome-linked protein VPg1) (Genome-linked protein VPg2) (Genome-linked protein VPg3) (Leader protease) (P1A) (P1B) (P1C) (P1D) (P52) (P56A) (Picornain 3C) (Protease 3C) (Protease P20B) (Protein 2A) (Protein 2C) (Protein 3A) (Protein 3B-1) (Protein 3B-2) (Protein 3B-3) (RNA-directed RNA polymerase 3D-POL) (VP4-VP2) (Virion protein 1) (Virion protein 2) (Virion protein 3) (Virion protein 4) (protein 2B)
[] Capsid protein VP0 (EC 2.7.7.48) (EC 3.4.22.28) (EC 3.4.22.46) (EC 3.6.1.15) (Capsid protein VP1) (Capsid protein VP3) (Capsid protein VP4) (Genome polyprotein) (Genome-linked protein VPg1) (Genome-linked protein VPg2) (Genome-linked protein VPg3) (Leader protease) (P1A) (P1B) (P1C) (P1D) (P52) (P56A) (Picornain 3C) (Protease 3C) (Protease P20B) (Protein 2A) (Protein 2C) (Protein 3A) (Protein 3B-1) (Protein 3B-2) (Protein 3B-3) (RNA-directed RNA polymerase 3D-POL) (VP4-VP2) (Virion protein 1) (Virion protein 2) (Virion protein 3) (Virion protein 4) (protein 2B)
[] Capsid protein VP0 (EC 2.7.7.48) (EC 3.4.22.28) (EC 3.4.22.46) (EC 3.6.1.15) (Capsid protein VP1) (Capsid protein VP3) (Capsid protein VP4) (Genome polyprotein) (Genome-linked protein VPg1) (Genome-linked protein VPg2) (Genome-linked protein VPg3) (Leader protease) (P1A) (P1B) (P1C) (P1D) (P52) (P56A) (Picornain 3C) (Protease 3C) (Protease P20B) (Protein 2A) (Protein 2C) (Protein 3A) (Protein 3B-1) (Protein 3B-2) (Protein 3B-3) (RNA-directed RNA polymerase 3D-POL) (VP4-VP2) (Virion protein 1) (Virion protein 2) (Virion protein 3) (Virion protein 4) (protein 2B)
[] Capsid protein VP0 (EC 2.7.7.48) (EC 3.4.22.28) (EC 3.4.22.46) (EC 3.6.1.15) (Capsid protein VP1) (Capsid protein VP3) (Capsid protein VP4) (Genome polyprotein) (Genome-linked protein VPg1) (Genome-linked protein VPg2) (Genome-linked protein VPg3) (Leader protease) (P1A) (P1B) (P1C) (P1D) (P52) (P56A) (Picornain 3C) (Protease 3C) (Protease P20B) (Protein 2A) (Protein 2C) (Protein 3A) (Protein 3B-1) (Protein 3B-2) (Protein 3B-3) (RNA-directed RNA polymerase 3D-POL) (VP4-VP2) (Virion protein 1) (Virion protein 2) (Virion protein 3) (Virion protein 4) (protein 2B)
[STX1B STX1B1 STX1B2] Syntaxin-1B (Syntaxin-1B1) (Syntaxin-1B2)
[NABP1 OBFC2A SSB2] SOSS complex subunit B2 (Nucleic acid-binding protein 1) (Oligonucleotide/oligosaccharide-binding fold-containing protein 2A) (Sensor of single-strand DNA complex subunit B2) (Sensor of ssDNA subunit B2) (SOSS-B2) (Single-stranded DNA-binding protein 2) (hSSB2)
[Nabp1 Obfc2a Ssb2] SOSS complex subunit B2 (Nucleic acid-binding protein 1) (Oligonucleotide/oligosaccharide-binding fold-containing protein 2A) (Sensor of single-strand DNA complex subunit B2) (Sensor of ssDNA subunit B2) (SOSS-B2) (Single-stranded DNA-binding protein 2)
[Cyp11b2 Cyp11b-2] Cytochrome P450 11B2, mitochondrial (Aldosterone synthase) (ALDOS) (Aldosterone-synthesizing enzyme) (CYPXIB2) (Corticosterone 18-monooxygenase, CYP11B2) (EC 1.14.15.5) (Cytochrome P-450Aldo) (Cytochrome P-450C18) (Cytochrome P450-Aldo-1) (Steroid 11-beta-hydroxylase, CYP11B2) (EC 1.14.15.4) (Steroid 18-hydroxylase)
[CYP11B2] Cytochrome P450 11B2, mitochondrial (Aldosterone synthase) (ALDOS) (Aldosterone-synthesizing enzyme) (CYPXIB2) (Corticosterone 18-monooxygenase, CYP11B2) (EC 1.14.15.5) (Cytochrome P-450Aldo) (Cytochrome P-450C18) (Steroid 11-beta-hydroxylase, CYP11B2) (EC 1.14.15.4) (Steroid 18-hydroxylase)
[ATP6V1B2 ATP6B2 VPP3] V-type proton ATPase subunit B, brain isoform (V-ATPase subunit B 2) (Endomembrane proton pump 58 kDa subunit) (HO57) (Vacuolar proton pump subunit B 2)
[Cyp11b2 Cyp11b-2] Cytochrome P450 11B2, mitochondrial (Aldosterone synthase) (ALDOS) (Aldosterone-synthesizing enzyme) (CYPXIB2) (Corticosterone 18-monooxygenase, CYP11B2) (EC 1.14.15.5) (Cytochrome P-450Aldo) (Cytochrome P-450C18) (Cytochrome P450C11) (Steroid 11-beta-hydroxylase, CYP11B2) (EC 1.14.15.4) (Steroid 18-hydroxylase)
[EXO70B2 At1g07000 F10K1.28] Exocyst complex component EXO70B2 (AtExo70b2) (Exocyst subunit Exo70 family protein B2)
[Atp6v1b2 Atp6b2 Vat2] V-type proton ATPase subunit B, brain isoform (V-ATPase subunit B 2) (Endomembrane proton pump 58 kDa subunit) (Vacuolar proton pump subunit B 2)
[BDKRB2 BKR2] B2 bradykinin receptor (B2R) (BK-2 receptor)
[Bdkrb2] B2 bradykinin receptor (B2R) (BK-2 receptor)
[Bdkrb2] B2 bradykinin receptor (B2R) (BK-2 receptor)
[SLC35B2 PAPST1 PSEC0149] Adenosine 3'-phospho 5'-phosphosulfate transporter 1 (PAPS transporter 1) (Putative MAPK-activating protein PM15) (Putative NF-kappa-B-activating protein 48) (Solute carrier family 35 member B2)
[ADARB2 ADAR3 RED2] Double-stranded RNA-specific editase B2 (EC 3.5.-.-) (RNA-dependent adenosine deaminase 3) (RNA-editing deaminase 2) (RNA-editing enzyme 2) (dsRNA adenosine deaminase B2)
[ALDH3B2 ALDH8] Aldehyde dehydrogenase family 3 member B2 (EC 1.2.1.3) (Aldehyde dehydrogenase 8)
[SH3GLB2 KIAA1848 PP578] Endophilin-B2 (SH3 domain-containing GRB2-like protein B2)
[CRYBB2 CRYB2 CRYB2A] Beta-crystallin B2 (Beta-B2 crystallin) (Beta-crystallin Bp)
[Slco1b2 Oatp1b2 Slc21a10] Solute carrier organic anion transporter family member 1B2 (Liver-specific organic anion transporter 1) (rLST-1) (Sodium-independent organic anion-transporting polypeptide 4) (OATP-4) (Solute carrier family 21 member 10)
[Slco1b2 Oatp1b2 Slc21a10] Solute carrier organic anion transporter family member 1B2 (Liver-specific organic anion transporter 1) (LST-1) (SLC21A6) (Solute carrier family 21 member 10)
[Cyp2b2 Cyp2b-2] Cytochrome P450 2B2 (EC 1.14.14.1) (CYPIIB2) (Cytochrome P450 PB4) (Cytochrome P450E)
[ifb-2 F10C1.7] Intermediate filament protein ifb-2 (Cel IF B2) (Intermediate filament protein B2) (IF-B2)
[dinB dinP b0231 JW0221] DNA polymerase IV (Pol IV) (EC 2.7.7.7) (Translesion synthesis polymerase IV) (TSL polymerase IV)
[SAFB2 KIAA0138] Scaffold attachment factor B2 (SAF-B2)

Bibliography :
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