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Lamin-B1

 LMNB1_HUMAN             Reviewed;         586 AA.
P20700; B2R6J6; Q3SYN7; Q96EI6;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
02-JUN-2021, entry version 217.
RecName: Full=Lamin-B1;
Flags: Precursor;
Name=LMNB1; Synonyms=LMN2, LMNB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2325650; DOI=10.1128/mcb.10.5.2164;
Pollard K.M., Chan E.K.L., Grant B.J., Sullivan K.F., Tan E.M., Glass C.A.;
"In vitro posttranslational modification of lamin B cloned from a human T-
cell line.";
Mol. Cell. Biol. 10:2164-2175(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7557986; DOI=10.1006/geno.1995.1036;
Lin F., Worman H.J.;
"Structural organization of the human gene (LMNB1) encoding nuclear lamin
B1.";
Genomics 27:230-236(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, and Placenta;
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).
[6]
PROTEIN SEQUENCE OF 2-10; 15-26; 43-49; 80-90; 103-109; 112-123; 125-191;
198-220; 235-250; 259-271; 277-290; 300-312; 321-330; 351-387; 475-483 AND
517-528, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 52-67; 80-90; 112-123; 146-156; 198-208; 210-220;
300-312; 321-330; 351-378 AND 458-473, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[8]
ISOPRENYLATION AT CYS-583.
PubMed=2684976;
Farnsworth C.C., Wolda S.L., Gelb M.H., Glomset J.A.;
"Human lamin B contains a farnesylated cysteine residue.";
J. Biol. Chem. 264:20422-20429(1989).
[9]
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
"Proteomic characterization of the human centrosome by protein correlation
profiling.";
Nature 426:570-574(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-575, 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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20 AND SER-23, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation
analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[12]
INVOLVEMENT IN ADLD.
PubMed=16951681; DOI=10.1038/ng1872;
Padiath Q.S., Saigoh K., Schiffmann R., Asahara H., Yamada T., Koeppen A.,
Hogan K., Ptacek L.J., Fu Y.-H.;
"Lamin B1 duplications cause autosomal dominant leukodystrophy.";
Nat. Genet. 38:1114-1123(2006).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-23 AND THR-575, 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).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, 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).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-157; LYS-271 AND LYS-483, 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).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT THR-3; THR-5; SER-23; SER-375 AND THR-575, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], 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).
[19]
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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-210 AND THR-575, 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).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.m111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5; THR-20; SER-23; THR-25;
SER-28; SER-200; SER-210; SER-232; SER-278; SER-302; SER-375; SER-534 AND
THR-575, 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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-23 AND THR-575, 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).
[24]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-14, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-102; LYS-241 AND LYS-261, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-241, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-145; LYS-241 AND LYS-261, 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).
[28]
INTERACTION WITH SPAG4 AND SEPT12.
PubMed=25775403; DOI=10.1371/journal.pone.0120722;
Yeh C.H., Kuo P.L., Wang Y.Y., Wu Y.Y., Chen M.F., Lin D.Y., Lai T.H.,
Chiang H.S., Lin Y.H.;
"SEPT12/SPAG4/LAMINB1 complexes are required for maintaining the integrity
of the nuclear envelope in postmeiotic male germ cells.";
PLoS ONE 10:E0120722-E0120722(2015).
[29]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-102; LYS-123; LYS-145; LYS-157;
LYS-181; LYS-241; LYS-261; LYS-271; LYS-312; LYS-330; LYS-532 AND LYS-547,
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).
[30]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 311-388, X-RAY CRYSTALLOGRAPHY
(2.0 ANGSTROMS) OF 428-550, DISULFIDE BOND, AND SUBUNIT.
PubMed=22265972; DOI=10.1016/j.febslet.2012.01.007;
Ruan J., Xu C., Bian C., Lam R., Wang J.P., Kania J., Min J., Zang J.;
"Crystal structures of the coil 2B fragment and the globular tail domain of
human lamin B1.";
FEBS Lett. 586:314-318(2012).
[31]
VARIANT VAL-436.
PubMed=24686783; DOI=10.1038/nn.3688;
Johnson J.O., Pioro E.P., Boehringer A., Chia R., Feit H., Renton A.E.,
Pliner H.A., Abramzon Y., Marangi G., Winborn B.J., Gibbs J.R., Nalls M.A.,
Morgan S., Shoai M., Hardy J., Pittman A., Orrell R.W., Malaspina A.,
Sidle K.C., Fratta P., Harms M.B., Baloh R.H., Pestronk A., Weihl C.C.,
Rogaeva E., Zinman L., Drory V.E., Borghero G., Mora G., Calvo A.,
Rothstein J.D., Drepper C., Sendtner M., Singleton A.B., Taylor J.P.,
Cookson M.R., Restagno G., Sabatelli M., Bowser R., Chio A., Traynor B.J.;
"Mutations in the matrin 3 gene cause familial amyotrophic lateral
sclerosis.";
Nat. Neurosci. 17:664-666(2014).
-!- 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: Homodimer. Interacts with lamin-associated polypeptides IA, IB
and 2. Interacts with SPAG4 and SEPT12. {ECO:0000269|PubMed:22265972,
ECO:0000269|PubMed:25775403}.
-!- INTERACTION:
P20700; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-968218, EBI-347573;
P20700; Q9H3R5: CENPH; NbExp=3; IntAct=EBI-968218, EBI-1003700;
P20700; Q9NPF5: DMAP1; NbExp=3; IntAct=EBI-968218, EBI-399105;
P20700; Q9Y6X4: FAM169A; NbExp=3; IntAct=EBI-968218, EBI-1220497;
P20700; P52294: KPNA1; NbExp=4; IntAct=EBI-968218, EBI-358383;
P20700; O60684: KPNA6; NbExp=3; IntAct=EBI-968218, EBI-359923;
P20700; P02545: LMNA; NbExp=10; IntAct=EBI-968218, EBI-351935;
P20700; P02545-1: LMNA; NbExp=5; IntAct=EBI-968218, EBI-351949;
P20700; P02545-2: LMNA; NbExp=19; IntAct=EBI-968218, EBI-351953;
P20700; Q03252: LMNB2; NbExp=5; IntAct=EBI-968218, EBI-2830427;
P20700; Q8TC57: M1AP; NbExp=3; IntAct=EBI-968218, EBI-748182;
P20700; Q9GZQ8: MAP1LC3B; NbExp=14; IntAct=EBI-968218, EBI-373144;
P20700; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-968218, EBI-10232538;
P20700; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-968218, EBI-1105153;
P20700; O95295: SNAPIN; NbExp=3; IntAct=EBI-968218, EBI-296723;
P20700; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-968218, EBI-11952721;
P20700; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-968218, EBI-10180829;
P20700; Q05322: VP24; Xeno; NbExp=6; IntAct=EBI-968218, EBI-6153153;
-!- 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: Leukodystrophy, demyelinating, autosomal dominant, adult-onset
(ADLD) [MIM:169500]: A slowly progressive and fatal demyelinating
leukodystrophy, presenting in the fourth or fifth decade of life.
Clinically characterized by early autonomic abnormalities, pyramidal
and cerebellar dysfunction, and symmetric demyelination of the CNS. It
differs from multiple sclerosis and other demyelinating disorders in
that neuropathology shows preservation of oligodendroglia in the
presence of subtotal demyelination and lack of astrogliosis.
{ECO:0000269|PubMed:16951681}. Note=The disease is 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}.
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EMBL; M34458; AAA36162.1; -; mRNA.
EMBL; L37747; AAC37575.1; -; Genomic_DNA.
EMBL; L37737; AAC37575.1; JOINED; Genomic_DNA.
EMBL; L37738; AAC37575.1; JOINED; Genomic_DNA.
EMBL; L37739; AAC37575.1; JOINED; Genomic_DNA.
EMBL; L37740; AAC37575.1; JOINED; Genomic_DNA.
EMBL; L37741; AAC37575.1; JOINED; Genomic_DNA.
EMBL; L37742; AAC37575.1; JOINED; Genomic_DNA.
EMBL; L37743; AAC37575.1; JOINED; Genomic_DNA.
EMBL; L37744; AAC37575.1; JOINED; Genomic_DNA.
EMBL; L37745; AAC37575.1; JOINED; Genomic_DNA.
EMBL; L37746; AAC37575.1; JOINED; Genomic_DNA.
EMBL; AK312603; BAG35493.1; -; mRNA.
EMBL; CH471086; EAW48846.1; -; Genomic_DNA.
EMBL; BC012295; AAH12295.1; -; mRNA.
EMBL; BC103723; AAI03724.1; -; mRNA.
CCDS; CCDS4140.1; -.
PIR; A34707; VEHULB.
RefSeq; NP_005564.1; NM_005573.3.
PDB; 2KPW; NMR; -; A=439-549.
PDB; 3JT0; X-ray; 2.39 A; A/B=426-558.
PDB; 3TYY; X-ray; 2.40 A; A/B=311-388.
PDB; 3UMN; X-ray; 2.00 A; A/B/C=428-550.
PDB; 5VVX; X-ray; 2.90 A; B/D=389-401.
PDBsum; 2KPW; -.
PDBsum; 3JT0; -.
PDBsum; 3TYY; -.
PDBsum; 3UMN; -.
PDBsum; 5VVX; -.
SMR; P20700; -.
BioGRID; 110187; 187.
CORUM; P20700; -.
DIP; DIP-34897N; -.
IntAct; P20700; 79.
MINT; P20700; -.
STRING; 9606.ENSP00000261366; -.
GlyGen; P20700; 1 site, 1 O-linked glycan (1 site).
iPTMnet; P20700; -.
MetOSite; P20700; -.
PhosphoSitePlus; P20700; -.
SwissPalm; P20700; -.
BioMuta; LMNB1; -.
DMDM; 125953; -.
SWISS-2DPAGE; P20700; -.
EPD; P20700; -.
jPOST; P20700; -.
MassIVE; P20700; -.
MaxQB; P20700; -.
PaxDb; P20700; -.
PeptideAtlas; P20700; -.
PRIDE; P20700; -.
ProteomicsDB; 53773; -.
ABCD; P20700; 3 sequenced antibodies.
Antibodypedia; 3937; 811 antibodies.
CPTC; P20700; 2 antibodies.
DNASU; 4001; -.
Ensembl; ENST00000261366; ENSP00000261366; ENSG00000113368.
GeneID; 4001; -.
KEGG; hsa:4001; -.
UCSC; uc003kud.3; human.
CTD; 4001; -.
DisGeNET; 4001; -.
GeneCards; LMNB1; -.
GeneReviews; LMNB1; -.
HGNC; HGNC:6637; LMNB1.
HPA; ENSG00000113368; Tissue enhanced (lymphoid).
MalaCards; LMNB1; -.
MIM; 150340; gene.
MIM; 169500; phenotype.
neXtProt; NX_P20700; -.
OpenTargets; ENSG00000113368; -.
Orphanet; 99027; Adult-onset autosomal dominant leukodystrophy.
PharmGKB; PA30403; -.
VEuPathDB; HostDB:ENSG00000113368.11; -.
eggNOG; KOG0977; Eukaryota.
GeneTree; ENSGT00940000157199; -.
HOGENOM; CLU_012560_9_2_1; -.
InParanoid; P20700; -.
OMA; ERAWLQI; -.
OrthoDB; 701388at2759; -.
PhylomeDB; P20700; -.
TreeFam; TF101181; -.
PathwayCommons; P20700; -.
Reactome; R-HSA-1221632; Meiotic synapsis.
Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
Reactome; R-HSA-2980766; Nuclear Envelope Breakdown.
Reactome; R-HSA-2995383; Initiation of Nuclear Envelope (NE) Reformation.
Reactome; R-HSA-352238; Breakdown of the nuclear lamina.
Reactome; R-HSA-4419969; Depolymerisation of the Nuclear Lamina.
Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
SIGNOR; P20700; -.
BioGRID-ORCS; 4001; 63 hits in 1002 CRISPR screens.
ChiTaRS; LMNB1; human.
EvolutionaryTrace; P20700; -.
GeneWiki; LMNB1; -.
GenomeRNAi; 4001; -.
Pharos; P20700; Tbio.
PRO; PR:P20700; -.
Proteomes; UP000005640; Chromosome 5.
RNAct; P20700; protein.
Bgee; ENSG00000113368; Expressed in ventricular zone and 184 other tissues.
ExpressionAtlas; P20700; baseline and differential.
Genevisible; P20700; HS.
GO; GO:0005638; C:lamin filament; TAS:ProtInc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; TAS:Reactome.
GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:CAFA.
GO; GO:0043274; F:phospholipase binding; IEA:Ensembl.
GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:Ensembl.
GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
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; Chromosomal rearrangement; Coiled coil;
Direct protein sequencing; Disulfide bond; Intermediate filament;
Isopeptide bond; Leukodystrophy; Lipoprotein; Membrane; Methylation;
Nucleus; Phosphoprotein; Prenylation; Reference proteome; Ubl conjugation.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895"
CHAIN 2..583
/note="Lamin-B1"
/id="PRO_0000063816"
PROPEP 584..586
/note="Removed in mature form"
/evidence="ECO:0000305"
/id="PRO_0000393945"
DOMAIN 32..388
/note="IF rod"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
DOMAIN 430..546
/note="LTD"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
REGION 1..31
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 2..34
/note="Head"
REGION 35..69
/note="Coil 1A"
REGION 70..81
/note="Linker 1"
REGION 82..215
/note="Coil 1B"
REGION 216..243
/note="Linker 2"
REGION 244..386
/note="Coil 2"
REGION 387..586
/note="Tail"
REGION 388..432
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOTIF 415..420
/note="Nuclear localization signal"
/evidence="ECO:0000255"
COMPBIAS 392..408
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 2
/note="N-acetylalanine"
/evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895"
MOD_RES 3
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:20068231"
MOD_RES 5
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163"
MOD_RES 14
/note="Omega-N-methylarginine"
/evidence="ECO:0007744|PubMed:24129315"
MOD_RES 20
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:16964243,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 23
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:16964243,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 25
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 28
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 111
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P14733"
MOD_RES 126
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P70615"
MOD_RES 157
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 158
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P70615"
MOD_RES 200
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 210
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:23186163"
MOD_RES 232
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 271
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 278
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 302
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 330
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P14733"
MOD_RES 375
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:19690332,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
MOD_RES 413
/note="Omega-N-methylarginine"
/evidence="ECO:0000250|UniProtKB:P21619"
MOD_RES 483
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 534
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 575
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:17081983,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 583
/note="Cysteine methyl ester"
/evidence="ECO:0000305"
LIPID 583
/note="S-farnesyl cysteine"
/evidence="ECO:0000269|PubMed:2684976"
DISULFID 317
/note="Interchain"
/evidence="ECO:0000269|PubMed:22265972"
CROSSLNK 102
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:25218447,
ECO:0007744|PubMed:28112733"
CROSSLNK 123
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 145
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:25755297,
ECO:0007744|PubMed:28112733"
CROSSLNK 157
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 181
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 241
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:25114211,
ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
ECO:0007744|PubMed:28112733"
CROSSLNK 261
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:25218447,
ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
CROSSLNK 271
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 312
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 330
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 532
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 547
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
VARIANT 436
/note="A -> V (found in a family with amyotrophic lateral
sclerosis carrying a probable causative mutation in MATR3;
unknown pathological significance; dbSNP:rs1380634377)"
/evidence="ECO:0000269|PubMed:24686783"
/id="VAR_071077"
VARIANT 501
/note="A -> V (in dbSNP:rs36105360)"
/id="VAR_031646"
CONFLICT 382
/note="E -> Q (in Ref. 5; AAH12295)"
/evidence="ECO:0000305"
HELIX 315..381
/evidence="ECO:0007829|PDB:3TYY"
STRAND 432..447
/evidence="ECO:0007829|PDB:3UMN"
STRAND 451..458
/evidence="ECO:0007829|PDB:3UMN"
STRAND 460..462
/evidence="ECO:0007829|PDB:3UMN"
STRAND 470..475
/evidence="ECO:0007829|PDB:3UMN"
STRAND 478..483
/evidence="ECO:0007829|PDB:3UMN"
STRAND 495..500
/evidence="ECO:0007829|PDB:3UMN"
TURN 509..511
/evidence="ECO:0007829|PDB:3UMN"
STRAND 512..515
/evidence="ECO:0007829|PDB:3UMN"
STRAND 523..525
/evidence="ECO:0007829|PDB:3UMN"
STRAND 527..532
/evidence="ECO:0007829|PDB:3UMN"
STRAND 538..546
/evidence="ECO:0007829|PDB:3UMN"
SEQUENCE 586 AA; 66408 MW; 73292877745722C4 CRC64;
MATATPVPPR MGSRAGGPTT PLSPTRLSRL QEKEELRELN DRLAVYIDKV RSLETENSAL
QLQVTEREEV RGRELTGLKA LYETELADAR RALDDTARER AKLQIELGKC KAEHDQLLLN
YAKKESDLNG AQIKLREYEA ALNSKDAALA TALGDKKSLE GDLEDLKDQI AQLEASLAAA
KKQLADETLL KVDLENRCQS LTEDLEFRKS MYEEEINETR RKHETRLVEV DSGRQIEYEY
KLAQALHEMR EQHDAQVRLY KEELEQTYHA KLENARLSSE MNTSTVNSAR EELMESRMRI
ESLSSQLSNL QKESRACLER IQELEDLLAK EKDNSRRMLT DKEREMAEIR DQMQQQLNDY
EQLLDVKLAL DMEISAYRKL LEGEEERLKL SPSPSSRVTV SRASSSRSVR TTRGKRKRVD
VEESEASSSV SISHSASATG NVCIEEIDVD GKFIRLKNTS EQDQPMGGWE MIRKIGDTSV
SYKYTSRYVL KAGQTVTIWA ANAGVTASPP TDLIWKNQNS WGTGEDVKVI LKNSQGEEVA
QRSTVFKTTI PEEEEEEEEA AGVVVEEELF HQQGTPRASN RSCAIM


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Related Genes :
[LMNB1 LMN2 LMNB] Lamin-B1
[Lmnb1] Lamin-B1
[Lmnb1] Lamin-B1
[] 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)
[Lam 2459 74 76 D5 D[[m0]] Dm Dm(0) Dm0 Dm1 Dm2 Dm[[0]] Dm[[1]] Dm[[2]] Dm[[mit]] DM[[O]] Dm[[o]] Dmel\CG6944 DmLamin DmO Dmo jf27 l(2)04643 l(2)25Ec l(2)gdh-7 l(2)gdh7 l(2)jf27 LAM lam Lam Dm0 Lam Dm[[0]] Lam(Dm0) Lam[[Dm0]] LamDm LamDm0 lamDm0 LamDm[[0]] lamDm[[0]] LamDm[[o]] lamin Lamin B lamin B lamin Dm0 Lamin Dm[[0]] lamin Dm[[0]] lamin DmO lamin-B Lamin-B1 LaminB misg nlam CG6944 Dmel_CG6944] Lamin, isoform B (Lamin, isoform C) (Lamin, isoform D)
[glmU AB936_09350 AFY08_02365 AFY14_02365 AWK88_11740 B1N38_14540 B1N39_14005 B1N40_13815 B1O10_14145 B1O25_13625 B4X79_15670 B4X80_14675 B4X87_15550 B4X92_13835 B4Y29_13745 B4Y36_14915 B4Y40_14205 B4Y57_15015 B9O43_14610 D4271_14125 D4862_13765 D4D69_14350 D4D89_14060 D5L36_14255 DKT87_15240 E0I39_14265 E5F60_13745 FJL28_14400 FJU19_13830 FORC68_0197 G3R95_002922 GEJ92_14105 GGA30_08950 GHD54_13635 GHM36_13995 GJW26_13030 GRG85_13405 GYP27_14835 GYP77_14475 GYQ49_11690 GYS91_13240 GYZ27_14255 GZK40_14355 GZT69_14105 M642_13575] Bifunctional protein GlmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157)]
[ppnP IJ22_37960 PN4B1_22570] Pyrimidine/purine nucleoside phosphorylase (EC 2.4.2.1) (EC 2.4.2.2) (Adenosine phosphorylase) (Cytidine phosphorylase) (Guanosine phosphorylase) (EC 2.4.2.15) (Inosine phosphorylase) (Thymidine phosphorylase) (EC 2.4.2.4) (Uridine phosphorylase) (EC 2.4.2.3) (Xanthosine phosphorylase)
[ifb-1 F10C1.2] Intermediate filament protein ifb-1 (Cel IF B1) (Intermediate filament protein B1) (IF-B1)
[HNRNPA2B1 HNRPA2B1] Heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1)
[Hnrnpa2b1 Hnrnp Hnrpa2b1] Heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1)
[Hnrnpa2b1 Hnrpa2b1] Heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1)
[NABP2 OBFC2B SSB1 LP3587] SOSS complex subunit B1 (Nucleic acid-binding protein 2) (Oligonucleotide/oligosaccharide-binding fold-containing protein 2B) (Sensor of single-strand DNA complex subunit B1) (Sensor of ssDNA subunit B1) (SOSS-B1) (Single-stranded DNA-binding protein 1) (hSSB1)
[Bdkrb1 B1bkr Bkr] B1 bradykinin receptor (B1R) (BK-1 receptor) (Kinin B1 receptor) (KB1)
[prs A7N75_02560 A8L61_08015 A8N58_12950 A9809_11025 AB936_09355 AB938_13345 ACY06_13565 AF066_13020 AF314_14375 AFY08_02370 AFY14_02370 AMC55_02400 APE37_08390 ARJ20_13030 ARS65_10220 ART25_13500 ARX85_15155 ARX92_14075 AWK88_11745 B1821_09740 B1N06_08110 B1N38_14545 B1N39_14010 B1N40_13820 B1N45_09855 B1N52_06710 B1N70_11395 B1O10_14150 B1O25_13630 B2H17_08425 B4960_11910 B4P04_10890 B4P23_05215 B4X79_15675 B4X80_14680 B4X87_15555 B4X92_13840 B4Y29_13750 B4Y36_14920 B4Y40_14210 B4Y47_14260 B4Y49_12070 B4Y57_15020 B5K59_14210 B9O43_14615 BBW72_14005 BLH28_05280 C6R69_11050 C7H49_08880 D4271_14130 D4779_09680 D4862_13770 D4920_13960 D4D69_14355 D4D89_14065 D5L36_14260 D5M49_12595 D9T24_08685 DCT16_06250 DKT87_15245 DU018_14880 E0I39_14270 E3W32_13750 E5F58_14470 E5F60_13750 E5H26_12440 EDX87_02420 EK719_12385 EPI21_12355 EXZ73_10100 F4W64_10200 F6515_08920 FA835_06640 FDP75_02370 FJL28_14405 FJU19_13835 FL871_11745 FLQ84_02670 FLQ91_11405 FLQ96_05130 FLR03_09130 FORC68_0198 FR210_14085 FR217_14215 FVI78_14290 FZX01_10370 G0Q20_002543 G3O21_000477 G3R95_002923 GEH47_14035 GEJ92_14110 GEK33_09485 GER99_14465 GF172_05985 GGA30_08955 GGA51_12520 GHD27_05980 GHD54_13640 GHF37_12670 GHM36_14000 GHQ72_14865 GI241_13990 GIH49_05605 GIQ23_05690 GJA60_01375 GJB11_11675 GJW26_13035 GJW51_05160 GRG85_13410 GT011_12760 GUM51_02530 GYK36_12360 GYP27_14840 GYP77_14480 GYQ49_11695 GYS09_12560 GYS13_03895 GYS23_08390 GYS91_13245 GYT70_14980 GYU24_12935 GYU49_12280 GYZ23_08145 GYZ27_14260 GYZ34_05755 GZI09_03020 GZI83_02365 GZK40_14360 GZP37_08460 GZS65_11375 GZT69_14100 HOY96_01375 HRK24_07470 HXD42_10535 HXF15_12615 HXX26_09940 KW30_02400 LH97_05640 LmNIHS28_00023 M642_13580 QU69_12545 ZY91_08280] Ribose-phosphate pyrophosphokinase (RPPK) (EC 2.7.6.1) (5-phospho-D-ribosyl alpha-1-diphosphate) (Phosphoribosyl diphosphate synthase) (Phosphoribosyl pyrophosphate synthase) (P-Rib-PP synthase) (PRPP synthase) (PRPPase)
[UNC93B1 UNC93 UNC93B] Protein unc-93 homolog B1 (Unc-93B1) (hUNC93B1)
[VHA-B1 AT57 At1g76030 T4O12.24] V-type proton ATPase subunit B1 (V-ATPase subunit B1) (V-ATPase 57 kDa subunit) (Vacuolar H(+)-ATPase subunit B isoform 1) (Vacuolar proton pump subunit B1)
[nnrD nnrE PN4B1_41790] Bifunctional NAD(P)H-hydrate repair enzyme (Nicotinamide nucleotide repair protein) [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6)]
[EFNB1 EFL3 EPLG2 LERK2] Ephrin-B1 (EFL-3) (ELK ligand) (ELK-L) (EPH-related receptor tyrosine kinase ligand 2) (LERK-2) [Cleaved into: Ephrin-B1 C-terminal fragment (Ephrin-B1 CTF); Ephrin-B1 intracellular domain (Ephrin-B1 ICD)]
[Efnb1 Epl2 Eplg2 Lerk2 Stra1] Ephrin-B1 (CEK5 receptor ligand) (CEK5-L) (EFL-3) (ELK ligand) (ELK-L) (EPH-related receptor tyrosine kinase ligand 2) (LERK-2) (Stimulated by retinoic acid gene 1 protein) [Cleaved into: Ephrin-B1 C-terminal fragment (Ephrin-B1 CTF); Ephrin-B1 intracellular domain (Ephrin-B1 ICD)]
[Efnb1 Eplg2 Lerk2] Ephrin-B1 (EFL-3) (ELK ligand) (ELK-L) (EPH-related receptor tyrosine kinase ligand 2) (LERK-2) [Cleaved into: Ephrin-B1 C-terminal fragment (Ephrin-B1 CTF); Ephrin-B1 intracellular domain (Ephrin-B1 ICD)]
[EXO70B1 At5g58430 MQJ2.3] Exocyst complex component EXO70B1 (AtExo70b1) (Exocyst subunit Exo70 family protein B1)
[ATP6V1B1 ATP6B1 VATB VPP3] V-type proton ATPase subunit B, kidney isoform (V-ATPase subunit B 1) (Endomembrane proton pump 58 kDa subunit) (Vacuolar proton pump subunit B 1)
[tgrB1 lagB lagB1 DDB_G0280689] Tiger protein B1 (Loose aggregate B1 protein) (Transmembrane, IPT, Ig, E-set, Repeat protein B1)
[Akr7a3 Afar Akr7a1] Aflatoxin B1 aldehyde reductase member 3 (AFB1-AR) (EC 1.-.-.-) (Aflatoxin B1 aldehyde reductase member 1) (rAFAR1)
[coaBC ARX85_02475 ARX92_04200 B1N38_09750 B1N39_07180 B1N40_01570 B9O43_06545 D5M49_03570 GHD54_09680 GYZ27_09590 GZT69_10710] Coenzyme A biosynthesis bifunctional protein CoaBC (DNA/pantothenate metabolism flavoprotein) (Phosphopantothenoylcysteine synthetase/decarboxylase) (PPCS-PPCDC) [Includes: Phosphopantothenoylcysteine decarboxylase (PPC decarboxylase) (PPC-DC) (EC 4.1.1.36) (CoaC); Phosphopantothenate--cysteine ligase (EC 6.3.2.5) (CoaB) (Phosphopantothenoylcysteine synthetase) (PPC synthetase) (PPC-S)]
[Atp6v1b1 Atp6b1] V-type proton ATPase subunit B, kidney isoform (V-ATPase subunit B 1) (Endomembrane proton pump 58 kDa subunit) (Vacuolar proton pump subunit B 1)
[Unc93b1 Unc93b] Protein unc-93 homolog B1 (Unc-93B1)
[Katnb1] Katanin p80 WD40 repeat-containing subunit B1 (Katanin p80 subunit B1) (p80 katanin)
[KATNB1] Katanin p80 WD40 repeat-containing subunit B1 (Katanin p80 subunit B1) (p80 katanin)
[LMNA LMN1] Prelamin-A/C [Cleaved into: Lamin-A/C (70 kDa lamin) (Renal carcinoma antigen NY-REN-32)]

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[34260661] Progesterone depletion results in Lamin B1 loss and induction of cell death in mouse trophoblast giant cells.
[34229273] TFEB protein expression is reduced in aged brains and its overexpression mitigates senescence-associated biomarkers and memory deficits in mice.
[34208028] Etoposide Triggers Cellular Senescence by Inducing Multiple Centrosomes and Primary Cilia in Adrenocortical Tumor Cells.
[34201242] Induction of Stress-Induced Renal Cellular Senescence In Vitro: Impact of Mouse Strain Genetic Diversity.
[34161290] Increased expression of LAP2β eliminates nuclear membrane ruptures in nuclear lamin-deficient neurons and fibroblasts.
[34142149] Efficacy and limitations of senolysis in atherosclerosis.
[34058264] Decreased Lamin B1 Levels Affect Gene Positioning and Expression in Postmitotic Neurons.
[33964137] Biallelic mutations in RNF220 cause laminopathies featuring leukodystrophy, ataxia and deafness.