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Tonsoku-like protein (Inhibitor of kappa B-related protein) (I-kappa-B-related protein) (IkappaBR) (NF-kappa-B inhibitor-like protein 2) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor-like 2)

 TONSL_HUMAN             Reviewed;        1378 AA.
Q96HA7; B5MDP0; C9JKB1; C9JNV8; Q13006; Q9UGJ2;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
08-APR-2008, sequence version 2.
12-SEP-2018, entry version 153.
RecName: Full=Tonsoku-like protein;
AltName: Full=Inhibitor of kappa B-related protein;
Short=I-kappa-B-related protein;
Short=IkappaBR;
AltName: Full=NF-kappa-B inhibitor-like protein 2;
AltName: Full=Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor-like 2;
Name=TONSL; Synonyms=IKBR, NFKBIL2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
AND VARIANT SER-493.
TISSUE=Cervix carcinoma;
PubMed=7738005; DOI=10.1074/jbc.270.18.10680;
Ray P., Zhang D.H., Elias J.A., Ray A.;
"Cloning of a differentially expressed I kappa B-related protein.";
J. Biol. Chem. 270:10680-10685(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-1378 (ISOFORM 1), AND
VARIANT VAL-714.
TISSUE=Brain;
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-671, AND VARIANT SER-493.
PubMed=11246458; DOI=10.1046/j.1469-1809.2000.6410015.x;
Norman D.A., Barton P.J.;
"Isolation, sequence, and chromosomal localisation of the human
IkappaBR gene (NFKBIL2).";
Ann. Hum. Genet. 64:15-23(2000).
[5]
SUBCELLULAR LOCATION.
PubMed=9242696; DOI=10.1074/jbc.272.32.20191;
Ray P., Yang L., Zhang D.H., Ghosh S.K., Ray A.;
"Selective up-regulation of cytokine-induced RANTES gene expression in
lung epithelial cells by overexpression of IkappaBR.";
J. Biol. Chem. 272:20191-20197(1997).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719, AND 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).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE MMS22L-TONSL
COMPLEX.
PubMed=21055983; DOI=10.1016/j.molcel.2010.10.024;
O'Donnell L., Panier S., Wildenhain J., Tkach J.M., Al-Hakim A.,
Landry M.C., Escribano-Diaz C., Szilard R.K., Young J.T., Munro M.,
Canny M.D., Kolas N.K., Zhang W., Harding S.M., Ylanko J., Mendez M.,
Mullin M., Sun T., Habermann B., Datti A., Bristow R.G., Gingras A.C.,
Tyers M.D., Brown G.W., Durocher D.;
"The MMS22L-TONSL complex mediates recovery from replication stress
and homologous recombination.";
Mol. Cell 40:619-631(2010).
[8]
FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE MMS22L-TONSL
COMPLEX, AND DOMAIN.
PubMed=21055984; DOI=10.1016/j.molcel.2010.10.023;
Duro E., Lundin C., Ask K., Sanchez-Pulido L., MacArtney T.J.,
Toth R., Ponting C.P., Groth A., Helleday T., Rouse J.;
"Identification of the MMS22L-TONSL complex that promotes homologous
recombination.";
Mol. Cell 40:632-644(2010).
[9]
FUNCTION, AND IDENTIFICATION IN THE MMS22L-TONSL COMPLEX.
PubMed=21055985; DOI=10.1016/j.molcel.2010.10.022;
O'Connell B.C., Adamson B., Lydeard J.R., Sowa M.E., Ciccia A.,
Bredemeyer A.L., Schlabach M., Gygi S.P., Elledge S.J., Harper J.W.;
"A genome-wide camptothecin sensitivity screen identifies a mammalian
MMS22L-NFKBIL2 complex required for genomic stability.";
Mol. Cell 40:645-657(2010).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719, 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).
[11]
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719, 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).
-!- FUNCTION: Component of the MMS22L-TONSL complex, a complex that
stimulates the recombination-dependent repair of stalled or
collapsed replication forks. The MMS22L-TONSL complex is required
to maintain genome integrity during DNA replication by promoting
homologous recombination-mediated repair of replication fork-
associated double-strand breaks. It may act by mediating the
assembly of RAD51 filaments on ssDNA. Within the complex, may act
as a scaffold. {ECO:0000269|PubMed:21055983,
ECO:0000269|PubMed:21055984, ECO:0000269|PubMed:21055985,
ECO:0000269|PubMed:7738005}.
-!- SUBUNIT: Component of the MMS22L-TONSL complex, a complex at least
composed of MMS22L and TONSL/NFKBIL2. Interacts with the MCM
complex, the FACT complex and the RPA complex. Binds histones.
{ECO:0000269|PubMed:21055983, ECO:0000269|PubMed:21055984,
ECO:0000269|PubMed:21055985}.
-!- INTERACTION:
Q6ZRQ5:MMS22L; NbExp=5; IntAct=EBI-1052467, EBI-718662;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mainly nuclear.
Localizes to DNA damage sites, accumulates at stressed replication
forks.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96HA7-1; Sequence=Displayed;
Name=2;
IsoId=Q96HA7-2; Sequence=VSP_032686;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in heart, skeletal muscle and
tracheal epithelial cells. {ECO:0000269|PubMed:7738005}.
-!- DOMAIN: The ANK repeats mediate the interaction with the MCM
complex and histones, while the LRR repeats mediate the
interaction with MMS22L. {ECO:0000269|PubMed:21055984}.
-!- SIMILARITY: Belongs to the Tonsoku family. {ECO:0000305}.
-!- CAUTION: Was reported to share sequence similarities with IKBKB
and therefore named 'NF-kappa-B inhibitor-like protein 2'
(PubMed:7738005). However, the sequence similarity is remote and
effects as regulator of NF-kappa-B are probably indirect and
require additional evidence (PubMed:9242696).
{ECO:0000305|PubMed:7738005, ECO:0000305|PubMed:9242696}.
-!- SEQUENCE CAUTION:
Sequence=AAA85819.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=AAH08782.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAB63467.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; U16258; AAA85819.1; ALT_FRAME; mRNA.
EMBL; AC084125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF205589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC008782; AAH08782.1; ALT_INIT; mRNA.
EMBL; AJ249601; CAB63467.1; ALT_SEQ; Genomic_DNA.
CCDS; CCDS34968.2; -. [Q96HA7-1]
PIR; A56429; A56429.
RefSeq; NP_038460.4; NM_013432.4. [Q96HA7-1]
UniGene; Hs.675285; -.
PDB; 5JA4; X-ray; 2.42 A; D=512-692.
PDBsum; 5JA4; -.
ProteinModelPortal; Q96HA7; -.
SMR; Q96HA7; -.
BioGrid; 110863; 37.
IntAct; Q96HA7; 22.
MINT; Q96HA7; -.
STRING; 9606.ENSP00000386239; -.
iPTMnet; Q96HA7; -.
PhosphoSitePlus; Q96HA7; -.
BioMuta; TONSL; -.
DMDM; 182662416; -.
EPD; Q96HA7; -.
MaxQB; Q96HA7; -.
PaxDb; Q96HA7; -.
PeptideAtlas; Q96HA7; -.
PRIDE; Q96HA7; -.
ProteomicsDB; 76723; -.
ProteomicsDB; 76724; -. [Q96HA7-2]
DNASU; 4796; -.
Ensembl; ENST00000409379; ENSP00000386239; ENSG00000160949. [Q96HA7-1]
Ensembl; ENST00000647028; ENSP00000494329; ENSG00000285453. [Q96HA7-1]
GeneID; 4796; -.
KEGG; hsa:4796; -.
UCSC; uc011llg.3; human. [Q96HA7-1]
CTD; 4796; -.
DisGeNET; 4796; -.
EuPathDB; HostDB:ENSG00000160949.16; -.
GeneCards; TONSL; -.
H-InvDB; HIX0007858; -.
HGNC; HGNC:7801; TONSL.
HPA; HPA024679; -.
HPA; HPA046494; -.
MIM; 604546; gene.
neXtProt; NX_Q96HA7; -.
OpenTargets; ENSG00000160949; -.
PharmGKB; PA31605; -.
eggNOG; KOG0504; Eukaryota.
eggNOG; KOG4308; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00760000119090; -.
HOGENOM; HOG000113022; -.
HOVERGEN; HBG107999; -.
InParanoid; Q96HA7; -.
KO; K09257; -.
OMA; PCFQKAL; -.
OrthoDB; EOG091G015L; -.
PhylomeDB; Q96HA7; -.
TreeFam; TF326440; -.
ChiTaRS; TONSL; human.
GenomeRNAi; 4796; -.
PRO; PR:Q96HA7; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000160949; Expressed in 93 organ(s), highest expression level in mucosa of transverse colon.
CleanEx; HS_NFKBIL2; -.
ExpressionAtlas; Q96HA7; baseline and differential.
Genevisible; Q96HA7; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0043596; C:nuclear replication fork; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; TAS:ProtInc.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
GO; GO:0031297; P:replication fork processing; IMP:UniProtKB.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.10; -; 2.
Gene3D; 1.25.40.20; -; 1.
Gene3D; 3.80.10.10; -; 2.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
Pfam; PF12796; Ank_2; 1.
Pfam; PF13516; LRR_6; 2.
Pfam; PF13181; TPR_8; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 3.
SMART; SM00028; TPR; 7.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF48452; SSF48452; 3.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 3.
PROSITE; PS50293; TPR_REGION; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; ANK repeat; Complete proteome;
Cytoplasm; DNA damage; DNA repair; Leucine-rich repeat; Methylation;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
TPR repeat.
CHAIN 1 1378 Tonsoku-like protein.
/FTId=PRO_0000326634.
REPEAT 27 60 TPR 1.
REPEAT 67 100 TPR 2.
REPEAT 107 147 TPR 3.
REPEAT 162 195 TPR 4.
REPEAT 202 235 TPR 5.
REPEAT 242 275 TPR 6.
REPEAT 311 344 TPR 7.
REPEAT 352 385 TPR 8.
REPEAT 528 557 ANK 1.
REPEAT 561 590 ANK 2.
REPEAT 597 626 ANK 3.
REPEAT 1069 1093 LRR 1.
REPEAT 1097 1122 LRR 2.
REPEAT 1128 1151 LRR 3.
REPEAT 1188 1212 LRR 4.
REPEAT 1247 1270 LRR 5.
REPEAT 1275 1300 LRR 6.
REPEAT 1331 1354 LRR 7.
COMPBIAS 448 509 Glu-rich.
MOD_RES 719 719 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 797 797 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q6NZL6}.
VAR_SEQ 631 641 GLSPLETLQQW -> ASARWRRCSSG (in isoform
2). {ECO:0000303|PubMed:7738005}.
/FTId=VSP_032686.
VARIANT 488 488 V -> M (in dbSNP:rs2229314).
/FTId=VAR_042411.
VARIANT 493 493 G -> S (in dbSNP:rs2229315).
{ECO:0000269|PubMed:11246458,
ECO:0000269|PubMed:7738005}.
/FTId=VAR_042412.
VARIANT 714 714 A -> V (in dbSNP:rs7830832).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_042413.
VARIANT 1276 1276 P -> L (in dbSNP:rs4925856).
/FTId=VAR_042414.
CONFLICT 193 194 EQ -> DE (in Ref. 1; AAA85819).
{ECO:0000305}.
CONFLICT 268 268 A -> R (in Ref. 1; AAA85819).
{ECO:0000305}.
CONFLICT 427 427 P -> A (in Ref. 4; CAB63467).
{ECO:0000305}.
CONFLICT 482 482 A -> R (in Ref. 1; AAA85819).
{ECO:0000305}.
CONFLICT 516 516 R -> P (in Ref. 1; AAA85819).
{ECO:0000305}.
HELIX 532 539 {ECO:0000244|PDB:5JA4}.
HELIX 542 551 {ECO:0000244|PDB:5JA4}.
HELIX 565 572 {ECO:0000244|PDB:5JA4}.
HELIX 575 583 {ECO:0000244|PDB:5JA4}.
TURN 594 597 {ECO:0000244|PDB:5JA4}.
HELIX 601 607 {ECO:0000244|PDB:5JA4}.
HELIX 611 616 {ECO:0000244|PDB:5JA4}.
HELIX 634 644 {ECO:0000244|PDB:5JA4}.
HELIX 651 668 {ECO:0000244|PDB:5JA4}.
SEQUENCE 1378 AA; 150929 MW; 8E3013861864DCDE CRC64;
MSLERELRQL SKAKAKAQRA GQRREEAALC HQLGELLAGH GRYAEALEQH WQELQLRERA
DDPLGCAVAH RKIGERLAEM EDYPAALQHQ HQYLELAHSL RNHTELQRAW ATIGRTHLDI
YDHCQSRDAL LQAQAAFEKS LAIVDEELEG TLAQGELNEM RTRLYLNLGL TFESLQQTAL
CNDYFRKSIF LAEQNHLYED LFRARYNLGT IHWRAGQHSQ AMRCLEGARE CAHTMRKRFM
ESECCVVIAQ VLQDLGDFLA AKRALKKAYR LGSQKPVQRA AICQNLQHVL AVVRLQQQLE
EAEGRDPQGA MVICEQLGDL FSKAGDFPRA AEAYQKQLRF AELLDRPGAE RAIIHVSLAT
TLGDMKDHHG AVRHYEEELR LRSGNVLEEA KTWLNIALSR EEAGDAYELL APCFQKALSC
AQQAQRPQLQ RQVLQHLHTV QLRLQPQEAP ETETRLRELS VAEDEDEEEE AEEAAATAES
EALEAGEVEL SEGEDDTDGL TPQLEEDEEL QGHLGRRKGS KWNRRNDMGE TLLHRACIEG
QLRRVQDLVR QGHPLNPRDY CGWTPLHEAC NYGHLEIVRF LLDHGAAVDD PGGQGCEGIT
PLHDALNCGH FEVAELLLER GASVTLRTRK GLSPLETLQQ WVKLYRRDLD LETRQKARAM
EMLLQAAASG QDPHSSQAFH TPSSLLFDPE TSPPLSPCPE PPSNSTRLPE ASQAHVRVSP
GQAAPAMARP RRSRHGPASS SSSSEGEDSA GPARPSQKRP RCSATAQRVA AWTPGPASNR
EAATASTSRA AYQAAIRGVG SAQSRLGPGP PRGHSKALAP QAALIPEEEC LAGDWLELDM
PLTRSRRPRP RGTGDNRRPS STSGSDSEES RPRARAKQVR LTCMQSCSAP VNAGPSSLAS
EPPGSPSTPR VSEPSGDSSA AGQPLGPAPP PPIRVRVQVQ DHLFLIPVPH SSDTHSVAWL
AEQAAQRYYQ TCGLLPRLTL RKEGALLAPQ DLIPDVLQSN DEVLAEVTSW DLPPLTDRYR
RACQSLGQGE HQQVLQAVEL QGLGLSFSAC SLALDQAQLT PLLRALKLHT ALRELRLAGN
RLGDKCVAEL VAALGTMPSL ALLDLSSNHL GPEGLRQLAM GLPGQATLQS LEELDLSMNP
LGDGCGQSLA SLLHACPLLS TLRLQACGFG PSFFLSHQTA LGSAFQDAEH LKTLSLSYNA
LGAPALARTL QSLPAGTLLH LELSSVAAGK GDSDLMEPVF RYLAKEGCAL AHLTLSANHL
GDKAVRDLCR CLSLCPSLIS LDLSANPEIS CASLEELLST LQKRPQGLSF LGLSGCAVQG
PLGLGLWDKI AAQLRELQLC SRRLCAEDRD ALRQLQPSRP GPGECTLDHG SKLFFRRL


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Tel 01 43 25 01 50

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GENTAUR GmbH
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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