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Msx2-interacting protein (SMART/HDAC1-associated repressor protein) (SPEN homolog)

 MINT_HUMAN              Reviewed;        3664 AA.
Q96T58; Q9H9A8; Q9NWH5; Q9UQ01; Q9Y556;
10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
22-NOV-2017, entry version 173.
RecName: Full=Msx2-interacting protein;
AltName: Full=SMART/HDAC1-associated repressor protein;
AltName: Full=SPEN homolog;
Name=SPEN; Synonyms=KIAA0929, MINT, SHARP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION,
RNA-BINDING, AND INTERACTION WITH NCOR2; HDAC1; HDAC2; RBBP4; MBD3;
RAR AND MTA1L1.
TISSUE=Liver, and Pituitary;
PubMed=11331609; DOI=10.1101/gad.871201;
Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C.,
Hon M., Evans R.M.;
"Sharp, an inducible cofactor that integrates nuclear receptor
repression and activation.";
Genes Dev. 15:1140-1151(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 294-3664.
Rhodes S., Huckle E.;
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 793-1595, AND VARIANT
PRO-1091.
TISSUE=Embryo, and Teratocarcinoma;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2002-3664.
TISSUE=Brain;
PubMed=10231032; DOI=10.1093/dnares/6.1.63;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:63-70(1999).
[6]
INTERACTION WITH PPARD.
PubMed=11867749; DOI=10.1073/pnas.052707099;
Shi Y., Hon M., Evans R.M.;
"The peroxisome proliferator-activated receptor delta, an integrator
of transcriptional repression and nuclear receptor signaling.";
Proc. Natl. Acad. Sci. U.S.A. 99:2613-2618(2002).
[7]
FUNCTION, AND INTERACTION WITH RBPSUH.
PubMed=12374742; DOI=10.1093/emboj/cdf549;
Oswald F., Kostezka U., Astrahantseff K., Bourteele S., Dillinger K.,
Zechner U., Ludwig L., Wilda M., Hameister H., Knoechel W., Liptay S.,
Schmid R.M.;
"SHARP is a novel component of the Notch/RBP-Jkappa signalling
pathway.";
EMBO J. 21:5417-5426(2002).
[8]
INTERACTION WITH EBV BSFL2/BMLF1.
PubMed=16129689; DOI=10.1074/jbc.M501725200;
Hiriart E., Gruffat H., Buisson M., Mikaelian I., Keppler S.,
Meresse P., Mercher T., Bernard O.A., Sergeant A., Manet E.;
"Interaction of the Epstein-Barr virus mRNA export factor EB2 with
human Spen proteins SHARP, OTT1, and a novel member of the family,
OTT3, links Spen proteins with splicing regulation and mRNA export.";
J. Biol. Chem. 280:36935-36945(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1268; SER-1278;
SER-1283; SER-1380 AND SER-1382, 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).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736; SER-740; SER-1194;
SER-1287; SER-1380; SER-1382; THR-1439; THR-1441; SER-1897; SER-2120;
SER-2126; SER-2366; THR-2421; THR-2938; THR-2950 AND SER-3433, 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).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1222; SER-1268;
SER-1278; THR-1947; SER-2452 AND THR-2460, 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309; SER-623; SER-727;
SER-1252; SER-1268; SER-1278; SER-1287; SER-1333; THR-1633; SER-1897;
SER-2101; SER-2120 AND SER-2159, 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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727; SER-1062; SER-1222;
SER-1261; SER-1268; SER-1278; SER-1380; SER-1382; SER-2101 AND
SER-2120, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-188; SER-190;
SER-725; SER-727; SER-736; SER-740; SER-770; SER-847; SER-1062;
THR-1140; SER-1168; SER-1194; SER-1222; SER-1268; SER-1278; SER-1283;
SER-1287; SER-1333; SER-1380; SER-1382; THR-1619; THR-1633; THR-1826;
SER-1918; SER-2101; SER-2126; SER-2159; THR-2163; THR-2393; THR-2421;
SER-2481 AND SER-2493, 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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1062; SER-1268;
SER-1278; THR-2393; SER-2456; SER-2481 AND SER-2486, 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).
[18]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-108; ARG-3113 AND ARG-3121,
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).
[19]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF SPOC DOMAIN.
PubMed=12897056; DOI=10.1101/gad.266203;
Ariyoshi M., Schwabe J.W.R.;
"A conserved structural motif reveals the essential transcriptional
repression function of Spen proteins and their role in developmental
signaling.";
Genes Dev. 17:1909-1920(2003).
[20]
VARIANTS [LARGE SCALE ANALYSIS] HIS-990 AND ILE-1488.
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).
-!- FUNCTION: May serve as a nuclear matrix platform that organizes
and integrates transcriptional responses. In osteoblasts, supports
transcription activation: synergizes with RUNX2 to enhance FGFR2-
mediated activation of the osteocalcin FGF-responsive element
(OCFRE) (By similarity). Has also been shown to be an essential
corepressor protein, which probably regulates different key
pathways such as the Notch pathway. Negative regulator of the
Notch pathway via its interaction with RBPSUH, which prevents the
association between NOTCH1 and RBPSUH, and therefore suppresses
the transactivation activity of Notch signaling. Blocks the
differentiation of precursor B-cells into marginal zone B-cells.
Probably represses transcription via the recruitment of large
complexes containing histone deacetylase proteins. May bind both
to DNA and RNA. {ECO:0000250, ECO:0000269|PubMed:11331609,
ECO:0000269|PubMed:12374742}.
-!- SUBUNIT: Interacts with MSX2 and HIPK3 (By similarity). Interacts
with NCOR2, HDAC1, HDAC2, RBBP4, MBD3 and MTA1L1. Interacts with
RBPSUH; this interaction may prevent the interaction between
RBPSUH and NOTCH1. Interacts with the nuclear receptors RAR and
PPARD. Interacts with RAR in absence of ligand. Binds to the
steroid receptor RNA coactivator SRA. Interacts with Epstein-Barr
virus BSFL2/BMLF1. {ECO:0000250, ECO:0000269|PubMed:11331609,
ECO:0000269|PubMed:11867749, ECO:0000269|PubMed:12374742,
ECO:0000269|PubMed:16129689}.
-!- INTERACTION:
P16333:NCK1; NbExp=3; IntAct=EBI-765739, EBI-389883;
Q9Y618:NCOR2; NbExp=5; IntAct=EBI-765739, EBI-80830;
Q06330:RBPJ; NbExp=2; IntAct=EBI-765739, EBI-632552;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11331609}.
Note=Associates with chromatin.
-!- TISSUE SPECIFICITY: Expressed at high level in brain, testis,
spleen and thymus. Expressed at intermediate level in kidney,
liver, mammary gland and skin.
-!- INDUCTION: By 17-beta-estradiol. {ECO:0000269|PubMed:11331609}.
-!- DOMAIN: The RID domain mediates the interaction with nuclear
receptors. {ECO:0000250}.
-!- DOMAIN: The SPOC domain, which mediates the interaction with
NCOR2, is essential for the repressive activity.
-!- SIMILARITY: Belongs to the RRM Spen family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA91405.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB14324.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAB51072.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF356524; AAK52750.1; -; mRNA.
EMBL; AL034555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL450998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL096858; CAB51072.1; ALT_INIT; mRNA.
EMBL; AK000882; BAA91405.1; ALT_INIT; mRNA.
EMBL; AK022949; BAB14324.1; ALT_INIT; mRNA.
EMBL; AB023146; BAA76773.1; -; mRNA.
CCDS; CCDS164.1; -.
RefSeq; NP_055816.2; NM_015001.2.
UniGene; Hs.744843; -.
PDB; 1OW1; X-ray; 1.80 A; A=3470-3664.
PDB; 2RT5; NMR; -; A=3496-3664.
PDB; 4P6Q; X-ray; 2.00 A; A=335-620.
PDBsum; 1OW1; -.
PDBsum; 2RT5; -.
PDBsum; 4P6Q; -.
ProteinModelPortal; Q96T58; -.
SMR; Q96T58; -.
BioGrid; 116655; 49.
CORUM; Q96T58; -.
DIP; DIP-34569N; -.
IntAct; Q96T58; 26.
STRING; 9606.ENSP00000364912; -.
iPTMnet; Q96T58; -.
PhosphoSitePlus; Q96T58; -.
SwissPalm; Q96T58; -.
BioMuta; SPEN; -.
DMDM; 41688816; -.
EPD; Q96T58; -.
MaxQB; Q96T58; -.
PaxDb; Q96T58; -.
PeptideAtlas; Q96T58; -.
PRIDE; Q96T58; -.
Ensembl; ENST00000375759; ENSP00000364912; ENSG00000065526.
GeneID; 23013; -.
KEGG; hsa:23013; -.
UCSC; uc001axk.2; human.
CTD; 23013; -.
DisGeNET; 23013; -.
EuPathDB; HostDB:ENSG00000065526.10; -.
GeneCards; SPEN; -.
H-InvDB; HIX0159662; -.
HGNC; HGNC:17575; SPEN.
HPA; HPA015825; -.
HPA; HPA050257; -.
MIM; 613484; gene.
neXtProt; NX_Q96T58; -.
OpenTargets; ENSG00000065526; -.
PharmGKB; PA134895302; -.
eggNOG; KOG0112; Eukaryota.
eggNOG; ENOG410XSAC; LUCA.
GeneTree; ENSGT00530000063730; -.
HOGENOM; HOG000231295; -.
HOVERGEN; HBG045583; -.
InParanoid; Q96T58; -.
OMA; WRSPRSQ; -.
OrthoDB; EOG091G00NR; -.
PhylomeDB; Q96T58; -.
TreeFam; TF315637; -.
SIGNOR; Q96T58; -.
ChiTaRS; SPEN; human.
EvolutionaryTrace; Q96T58; -.
GeneWiki; SPEN; -.
GenomeRNAi; 23013; -.
PRO; PR:Q96T58; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000065526; -.
CleanEx; HS_SPEN; -.
ExpressionAtlas; Q96T58; baseline and differential.
Genevisible; Q96T58; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0017053; C:transcriptional repressor complex; IDA:BHF-UCL.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003676; F:nucleic acid binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL.
GO; GO:0001191; F:transcriptional repressor activity, RNA polymerase II transcription factor binding; IDA:BHF-UCL.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0050769; P:positive regulation of neurogenesis; IMP:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd12348; RRM1_SHARP; 1.
CDD; cd12349; RRM2_SHARP; 1.
CDD; cd12350; RRM3_SHARP; 1.
CDD; cd12351; RRM4_SHARP; 1.
Gene3D; 2.40.290.10; -; 1.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR034172; SHARP_RRM1.
InterPro; IPR034173; SHARP_RRM2.
InterPro; IPR034174; SHARP_RRM3.
InterPro; IPR034175; SHARP_RRM4.
InterPro; IPR016194; SPOC-like_C_dom_sf.
InterPro; IPR012921; SPOC_C.
InterPro; IPR010912; SPOC_met.
Pfam; PF00076; RRM_1; 4.
Pfam; PF07744; SPOC; 1.
SMART; SM00360; RRM; 4.
SUPFAM; SSF100939; SSF100939; 1.
SUPFAM; SSF54928; SSF54928; 3.
PROSITE; PS50102; RRM; 4.
PROSITE; PS50917; SPOC; 1.
1: Evidence at protein level;
3D-structure; Activator; Coiled coil; Complete proteome; DNA-binding;
Host-virus interaction; Methylation; Notch signaling pathway; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor;
RNA-binding; Transcription; Transcription regulation.
CHAIN 1 3664 Msx2-interacting protein.
/FTId=PRO_0000081627.
DOMAIN 6 81 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 335 415 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 438 513 RRM 3. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 517 589 RRM 4. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 2201 2707 RID.
DOMAIN 3498 3664 SPOC. {ECO:0000255|PROSITE-
ProRule:PRU00249}.
DNA_BIND 1 573 {ECO:0000250}.
REGION 2130 2464 Interaction with MSX2. {ECO:0000250}.
REGION 2709 2870 Interaction with RBPSUH. {ECO:0000250}.
COILED 688 715 {ECO:0000255}.
COILED 977 1004 {ECO:0000255}.
COILED 1170 1191 {ECO:0000255}.
COILED 1408 1428 {ECO:0000255}.
COILED 1496 1529 {ECO:0000255}.
COILED 1592 1612 {ECO:0000255}.
COILED 1928 1944 {ECO:0000255}.
COMPBIAS 125 277 Arg-rich.
COMPBIAS 240 325 Ser-rich.
COMPBIAS 616 810 Arg-rich.
COMPBIAS 624 697 Tyr-rich.
COMPBIAS 2428 2520 Pro-rich.
COMPBIAS 3220 3482 Pro-rich.
MOD_RES 99 99 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 108 108 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 623 623 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 725 725 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 727 727 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 736 736 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 740 740 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 770 770 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 830 830 Phosphoserine.
{ECO:0000250|UniProtKB:Q62504}.
MOD_RES 833 833 Phosphoserine.
{ECO:0000250|UniProtKB:Q62504}.
MOD_RES 847 847 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1062 1062 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1140 1140 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1168 1168 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1194 1194 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1222 1222 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1252 1252 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1261 1261 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1268 1268 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1278 1278 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1283 1283 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163}.
MOD_RES 1287 1287 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1333 1333 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1380 1380 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1382 1382 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1439 1439 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1441 1441 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1619 1619 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1633 1633 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1826 1826 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1897 1897 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 1918 1918 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1947 1947 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 2101 2101 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 2120 2120 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 2126 2126 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 2159 2159 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2163 2163 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2366 2366 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2393 2393 Phosphothreonine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 2421 2421 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 2452 2452 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 2456 2456 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2460 2460 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 2481 2481 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 2486 2486 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2493 2493 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2938 2938 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2950 2950 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 3113 3113 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 3121 3121 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 3433 3433 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VARIANT 970 970 A -> V (in dbSNP:rs848208).
/FTId=VAR_017119.
VARIANT 990 990 D -> H (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035483.
VARIANT 1091 1091 L -> P (in dbSNP:rs848209).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_017120.
VARIANT 1363 1363 D -> E (in dbSNP:rs12095818).
/FTId=VAR_052208.
VARIANT 1488 1488 R -> I (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035484.
VARIANT 2360 2360 N -> D (in dbSNP:rs848210).
/FTId=VAR_017121.
CONFLICT 956 956 G -> D (in Ref. 4). {ECO:0000305}.
STRAND 336 340 {ECO:0000244|PDB:4P6Q}.
HELIX 348 359 {ECO:0000244|PDB:4P6Q}.
HELIX 360 362 {ECO:0000244|PDB:4P6Q}.
STRAND 365 371 {ECO:0000244|PDB:4P6Q}.
TURN 374 376 {ECO:0000244|PDB:4P6Q}.
STRAND 378 385 {ECO:0000244|PDB:4P6Q}.
HELIX 386 395 {ECO:0000244|PDB:4P6Q}.
TURN 396 398 {ECO:0000244|PDB:4P6Q}.
STRAND 407 410 {ECO:0000244|PDB:4P6Q}.
HELIX 414 422 {ECO:0000244|PDB:4P6Q}.
STRAND 438 444 {ECO:0000244|PDB:4P6Q}.
HELIX 451 458 {ECO:0000244|PDB:4P6Q}.
STRAND 464 472 {ECO:0000244|PDB:4P6Q}.
STRAND 475 485 {ECO:0000244|PDB:4P6Q}.
HELIX 486 496 {ECO:0000244|PDB:4P6Q}.
STRAND 507 510 {ECO:0000244|PDB:4P6Q}.
STRAND 517 522 {ECO:0000244|PDB:4P6Q}.
HELIX 530 537 {ECO:0000244|PDB:4P6Q}.
HELIX 538 540 {ECO:0000244|PDB:4P6Q}.
STRAND 543 549 {ECO:0000244|PDB:4P6Q}.
TURN 550 553 {ECO:0000244|PDB:4P6Q}.
STRAND 554 560 {ECO:0000244|PDB:4P6Q}.
HELIX 562 572 {ECO:0000244|PDB:4P6Q}.
STRAND 575 577 {ECO:0000244|PDB:4P6Q}.
STRAND 583 586 {ECO:0000244|PDB:4P6Q}.
HELIX 589 601 {ECO:0000244|PDB:4P6Q}.
HELIX 609 618 {ECO:0000244|PDB:4P6Q}.
HELIX 3501 3504 {ECO:0000244|PDB:1OW1}.
STRAND 3507 3515 {ECO:0000244|PDB:1OW1}.
STRAND 3518 3529 {ECO:0000244|PDB:1OW1}.
HELIX 3531 3537 {ECO:0000244|PDB:1OW1}.
STRAND 3541 3543 {ECO:0000244|PDB:2RT5}.
STRAND 3547 3549 {ECO:0000244|PDB:1OW1}.
STRAND 3551 3554 {ECO:0000244|PDB:1OW1}.
HELIX 3557 3566 {ECO:0000244|PDB:1OW1}.
TURN 3570 3572 {ECO:0000244|PDB:1OW1}.
STRAND 3573 3580 {ECO:0000244|PDB:1OW1}.
HELIX 3585 3598 {ECO:0000244|PDB:1OW1}.
HELIX 3600 3606 {ECO:0000244|PDB:1OW1}.
STRAND 3608 3614 {ECO:0000244|PDB:1OW1}.
TURN 3617 3619 {ECO:0000244|PDB:2RT5}.
STRAND 3624 3629 {ECO:0000244|PDB:1OW1}.
HELIX 3633 3642 {ECO:0000244|PDB:1OW1}.
HELIX 3644 3650 {ECO:0000244|PDB:1OW1}.
TURN 3651 3653 {ECO:0000244|PDB:1OW1}.
STRAND 3657 3663 {ECO:0000244|PDB:1OW1}.
SEQUENCE 3664 AA; 402248 MW; 5228C58533E5B27B CRC64;
MVRETRHLWV GNLPENVREE KIIEHFKRYG RVESVKILPK RGSEGGVAAF VDFVDIKSAQ
KAHNSVNKMG DRDLRTDYNE PGTIPSAARG LDDTVSIASR SREVSGFRGG GGGPAYGPPP
SLHAREGRYE RRLDGASDNR ERAYEHSAYG HHERGTGGFD RTRHYDQDYY RDPRERTLQH
GLYYASRSRS PNRFDAHDPR YEPRAREQFT LPSVVHRDIY RDDITREVRG RRPERNYQHS
RSRSPHSSQS RNQSPQRLAS QASRPTRSPS GSGSRSRSSS SDSISSSSST SSDSSDSSSS
SSDDSPARSV QSAAVPAPTS QLLSSLEKDE PRKSFGIKVQ NLPVRSTDTS LKDGLFHEFK
KFGKVTSVQI HGTSEERYGL VFFRQQEDQE KALTASKGKL FFGMQIEVTA WIGPETESEN
EFRPLDERID EFHPKATRTL FIGNLEKTTT YHDLRNIFQR FGEIVDIDIK KVNGVPQYAF
LQYCDIASVC KAIKKMDGEY LGNNRLKLGF GKSMPTNCVW LDGLSSNVSD QYLTRHFCRY
GPVVKVVFDR LKGMALVLYN EIEYAQAAVK ETKGRKIGGN KIKVDFANRE SQLAFYHCME
KSGQDIRDFY EMLAERREER RASYDYNQDR TYYESVRTPG TYPEDSRRDY PARGREFYSE
WETYQGDYYE SRYYDDPREY RDYRNDPYEQ DIREYSYRQR ERERERERFE SDRDRDHERR
PIERSQSPVH LRRPQSPGAS PSQAERLPSD SERRLYSRSS DRSGSCSSLS PPRYEKLDKS
RLERYTKNEK TDKERTFDPE RVERERRLIR KEKVEKDKTD KQKRKGKVHS PSSQSSETDQ
ENEREQSPEK PRSCNKLSRE KADKEGIAKN RLELMPCVVL TRVKEKEGKV IDHTPVEKLK
AKLDNDTVKS SALDQKLQVS QTEPAKSDLS KLESVRMKVP KEKGLSSHVE VVEKEGRLKA
RKHLKPEQPA DGVSAVDLEK LEARKRRFAD SNLKAEKQKP EVKKSSPEME DARVLSKKQP
DVSSREVILL REGEAERKPV RKEILKRESK KIKLDRLNTV ASPKDCQELA SISVGSGSRP
SSDLQARLGE LAGESVENQE VQSKKPIPSK PQLKQLQVLD DQGPEREDVR KNYCSLRDET
PERKSGQEKS HSVNTEEKIG IDIDHTQSYR KQMEQSRRKQ QMEMEIAKSE KFGSPKKDVD
EYERRSLVHE VGKPPQDVTD DSPPSKKKRM DHVDFDICTK RERNYRSSRQ ISEDSERTGG
SPSVRHGSFH EDEDPIGSPR LLSVKGSPKV DEKVLPYSNI TVREESLKFN PYDSSRREQM
ADMAKIKLSV LNSEDELNRW DSQMKQDAGR FDVSFPNSII KRDSLRKRSV RDLEPGEVPS
DSDEDGEHKS HSPRASALYE SSRLSFLLRD REDKLRERDE RLSSSLERNK FYSFALDKTI
TPDTKALLER AKSLSSSREE NWSFLDWDSR FANFRNNKDK EKVDSAPRPI PSWYMKKKKI
RTDSEGKMDD KKEDHKEEEQ ERQELFASRF LHSSIFEQDS KRLQHLERKE EDSDFISGRI
YGKQTSEGAN STTDSIQEPV VLFHSRFMEL TRMQQKEKEK DQKPKEVEKQ EDTENHPKTP
ESAPENKDSE LKTPPSVGPP SVTVVTLESA PSALEKTTGD KTVEAPLVTE EKTVEPATVS
EEAKPASEPA PAPVEQLEQV DLPPGADPDK EAAMMPAGVE EGSSGDQPPY LDAKPPTPGA
SFSQAESNVD PEPDSTQPLS KPAQKSEEAN EPKAEKPDAT ADAEPDANQK AEAAPESQPP
ASEDLEVDPP VAAKDKKPNK SKRSKTPVQA AAVSIVEKPV TRKSERIDRE KLKRSNSPRG
EAQKLLELKM EAEKITRTAS KNSAADLEHP EPSLPLSRTR RRNVRSVYAT MGDHENRSPV
KEPVEQPRVT RKRLERELQE AAAVPTTPRR GRPPKTRRRA DEEEENEAKE PAETLKPPEG
WRSPRSQKTA AGGGPQGKKG KNEPKVDATR PEATTEVGPQ IGVKESSMEP KAAEEEAGSE
QKRDRKDAGT DKNPPETAPV EVVEKKPAPE KNSKSKRGRS RNSRLAVDKS ASLKNVDAAV
SPRGAAAQAG ERESGVVAVS PEKSESPQKE DGLSSQLKSD PVDPDKEPEK EDVSASGPSP
EATQLAKQME LEQAVEHIAK LAEASASAAY KADAPEGLAP EDRDKPAHQA SETELAAAIG
SIINDISGEP ENFPAPPPYP GESQTDLQPP AGAQALQPSE EGMETDEAVS GILETEAATE
SSRPPVNAPD PSAGPTDTKE ARGNSSETSH SVPEAKGSKE VEVTLVRKDK GRQKTTRSRR
KRNTNKKVVA PVESHVPESN QAQGESPAAN EGTTVQHPEA PQEEKQSEKP HSTPPQSCTS
DLSKIPSTEN SSQEISVEER TPTKASVPPD LPPPPQPAPV DEEPQARFRV HSIIESDPVT
PPSDPSIPIP TLPSVTAAKL SPPVASGGIP HQSPPTKVTE WITRQEEPRA QSTPSPALPP
DTKASDVDTS SSTLRKILMD PKYVSATSVT STSVTTAIAE PVSAAPCLHE APPPPVDSKK
PLEEKTAPPV TNNSEIQASE VLVAADKEKV APVIAPKITS VISRMPVSID LENSQKITLA
KPAPQTLTGL VSALTGLVNV SLVPVNALKG PVKGSVTTLK SLVSTPAGPV NVLKGPVNVL
TGPVNVLTTP VNATVGTVNA APGTVNAAAS AVNATASAVT VTAGAVTAAS GGVTATTGTV
TMAGAVIAPS TKCKQRASAN ENSRFHPGSM PVIDDRPADA GSGAGLRVNT SEGVVLLSYS
GQKTEGPQRI SAKISQIPPA SAMDIEFQQS VSKSQVKPDS VTASQPPSKG PQAPAGYANV
ATHSTLVLTA QTYNASPVIS SVKADRPSLE KPEPIHLSVS TPVTQGGTVK VLTQGINTPP
VLVHNQLVLT PSIVTTNKKL ADPVTLKIET KVLQPANLGS TLTPHHPPAL PSKLPTEVNH
VPSGPSIPAD RTVSHLAAAK LDAHSPRPSG PGPSSFPRAS HPSSTASTAL STNATVMLAA
GIPVPQFISS IHPEQSVIMP PHSITQTVSL SHLSQGEVRM NTPTLPSITY SIRPEALHSP
RAPLQPQQIE VRAPQRASTP QPAPAGVPAL ASQHPPEEEV HYHLPVARAT APVQSEVLVM
QSEYRLHPYT VPRDVRIMVH PHVTAVSEQP RAADGVVKVP PASKAPQQPG KEAAKTPDAK
AAPTPTPAPV PVPVPLPAPA PAPHGEARIL TVTPSNQLQG LPLTPPVVVT HGVQIVHSSG
ELFQEYRYGD IRTYHPPAQL THTQFPAASS VGLPSRTKTA AQGPPPEGEP LQPPQPVQST
QPAQPAPPCP PSQLGQPGQP PSSKMPQVSQ EAKGTQTGVE QPRLPAGPAN RPPEPHTQVQ
RAQAETGPTS FPSPVSVSMK PDLPVSLPTQ TAPKQPLFVP TTSGPSTPPG LVLPHTEFQP
APKQDSSPHL TSQRPVDMVQ LLKKYPIVWQ GLLALKNDTA AVQLHFVSGN NVLAHRSLPL
SEGGPPLRIA QRMRLEATQL EGVARRMTVE TDYCLLLALP CGRDQEDVVS QTESLKAAFI
TYLQAKQAAG IINVPNPGSN QPAYVLQIFP PCEFSESHLS RLAPDLLASI SNISPHLMIV
IASV


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