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

 MINT_MOUSE              Reviewed;        3644 AA.
Q62504; Q80TN9; Q99PS4; Q9QZW2;
10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
10-OCT-2003, sequence version 2.
16-JAN-2019, entry version 166.
RecName: Full=Msx2-interacting protein;
AltName: Full=SMART/HDAC1-associated repressor protein;
AltName: Full=SPEN homolog;
Name=Spen; Synonyms=Kiaa0929, Mint, Sharp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-112.
STRAIN=C57BL/6J; TISSUE=Egg;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 49-3644 (ISOFORM 1), FUNCTION,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DNA-BINDING, AND INTERACTION
WITH MSX2.
TISSUE=Testis;
PubMed=10451362; DOI=10.1021/bi990967j;
Newberry E.P., Latifi T., Towler D.A.;
"The RRM domain of MINT, a novel msx2 binding protein, recognizes and
regulates the rat osteocalcin promoter.";
Biochemistry 38:10678-10690(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 69-3644 (ISOFORM 2), AND VARIANTS
THR-348; PHE-762; PHE-773 AND LEU-933.
STRAIN=ICR; TISSUE=Brain;
Sakamoto T., Gotou T., Isagawa Y., Mimura H., Kimura K., Kawaichi M.;
"MINT/spen negatively regulates Notch signaling by inhibiting RBP-
J/Su(H) activity.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 318-578, AND VARIANT THR-348.
TISSUE=Cochlea;
PubMed=9119401; DOI=10.1006/geno.1996.4526;
Crozet F., El-Amraoui A., Blanchard S., Lenoir M., Ripoll C., Vago P.,
Hamel C., Fizames C., Levi-Acobas F., Depetris D., Mattei M.-G.,
Weil D., Pujol R., Petit C.;
"Cloning of the genes encoding two murine and human cochlear
unconventional type I myosins.";
Genomics 40:332-341(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2600-3644 (ISOFORM 3).
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[6]
SEQUENCE REVISION.
Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[7]
TISSUE SPECIFICITY.
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]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=12594956; DOI=10.1016/S1074-7613(03)00029-3;
Kuroda K., Han H., Tani S., Tanigaki K., Tun T., Furukawa T.,
Taniguchi Y., Kurooka H., Hamada Y., Toyokuni S., Honjo T.;
"Regulation of marginal zone B cell development by MINT, a suppressor
of Notch/RBP-J signaling pathway.";
Immunity 18:301-312(2003).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15131132; DOI=10.1074/jbc.M314098200;
Sierra O.L., Cheng S.L., Loewy A.P., Charlton-Kachigian N.,
Towler D.A.;
"MINT, the Msx2 interacting nuclear matrix target, enhances Runx2-
dependent activation of the osteocalcin fibroblast growth factor
response element.";
J. Biol. Chem. 279:32913-32923(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1395, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852; SER-855; SER-869
AND SER-1395, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Kidney, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
FUNCTION, AND INTERACTION WITH HIPK3.
PubMed=20484411; DOI=10.1210/me.2010-0029;
Sierra O.L., Towler D.A.;
"Runx2 trans-activation mediated by the MSX2-interacting nuclear
target requires homeodomain interacting protein kinase-3.";
Mol. Endocrinol. 24:1478-1497(2010).
-!- 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). 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:0000269|PubMed:10451362, ECO:0000269|PubMed:12594956,
ECO:0000269|PubMed:15131132, ECO:0000269|PubMed:20484411}.
-!- SUBUNIT: Interacts with NCOR2, HDAC1, HDAC2, RBBP4, MBD3 and
MTA1L1. Interacts with the nuclear receptors RAR and PPARD.
Interacts with RAR in absence of ligand. Binds to the steroid
receptor RNA coactivator SRA (By similarity). Interacts with MSX2.
Interacts with RBPSUH; this interaction may prevent the
interaction between RBPSUH and NOTCH1. Binds to HIPK3.
{ECO:0000250, ECO:0000269|PubMed:10451362,
ECO:0000269|PubMed:20484411}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10451362,
ECO:0000269|PubMed:15131132}. Note=Associates with chromatin.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q62504-1; Sequence=Displayed;
Name=2;
IsoId=Q62504-2; Sequence=VSP_008564;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q62504-3; Sequence=VSP_013802, VSP_013803, VSP_013804;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in testis. Expressed at lower
level in brain, lung, spleen, liver and kidney. Weakly expressed
in cardiac and skeletal muscles and ovary. In spleen, it is
expressed in follicular B-cells, while it is weakly expressed in
marginal zone B-cells. {ECO:0000269|PubMed:10451362,
ECO:0000269|PubMed:12374742, ECO:0000269|PubMed:12594956}.
-!- DOMAIN: The RID domain mediates the interaction with nuclear
receptors.
-!- DOMAIN: The SPOC domain, which mediates the interaction with
NCOR2, is essential for the repressive activity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the RRM Spen family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD55931.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAB01562.1; Type=Erroneous termination; Positions=394; Note=Translated as Leu.; Evidence={ECO:0000305};
Sequence=CAB01562.1; Type=Frameshift; Positions=446, 561; Evidence={ECO:0000305};
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EMBL; BY726481; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AF156529; AAD55931.1; ALT_INIT; mRNA.
EMBL; AB055980; BAB32786.1; -; mRNA.
EMBL; Z78160; CAB01562.1; ALT_SEQ; mRNA.
EMBL; AK122402; BAC65684.3; -; Transcribed_RNA.
RefSeq; NP_062737.2; NM_019763.2.
UniGene; Mm.299906; -.
ProteinModelPortal; Q62504; -.
SMR; Q62504; -.
BioGrid; 207942; 1.
CORUM; Q62504; -.
IntAct; Q62504; 4.
MINT; Q62504; -.
STRING; 10090.ENSMUSP00000101412; -.
iPTMnet; Q62504; -.
PhosphoSitePlus; Q62504; -.
jPOST; Q62504; -.
PaxDb; Q62504; -.
PeptideAtlas; Q62504; -.
PRIDE; Q62504; -.
GeneID; 56381; -.
KEGG; mmu:56381; -.
CTD; 23013; -.
MGI; MGI:1891706; Spen.
eggNOG; KOG0112; Eukaryota.
eggNOG; ENOG410ZT33; LUCA.
HOGENOM; HOG000231295; -.
HOVERGEN; HBG045583; -.
InParanoid; Q62504; -.
OrthoDB; 367857at2759; -.
PhylomeDB; Q62504; -.
ChiTaRS; Spen; mouse.
PRO; PR:Q62504; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0017053; C:transcriptional repressor complex; ISO:MGI.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISO:MGI.
GO; GO:0003697; F:single-stranded DNA binding; IDA:MGI.
GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0050769; P:positive regulation of neurogenesis; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
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.
Gene3D; 3.30.70.330; -; 4.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
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; 3.
Pfam; PF07744; SPOC; 1.
SMART; SM00360; RRM; 4.
SUPFAM; SSF100939; SSF100939; 1.
SUPFAM; SSF54928; SSF54928; 2.
PROSITE; PS50102; RRM; 4.
PROSITE; PS50917; SPOC; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Coiled coil; Complete proteome;
DNA-binding; Methylation; Notch signaling pathway; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor;
RNA-binding; Transcription; Transcription regulation.
CHAIN 1 3644 Msx2-interacting protein.
/FTId=PRO_0000081628.
DOMAIN 6 81 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 336 416 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 439 514 RRM 3. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 518 590 RRM 4. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 2216 2704 RID.
DOMAIN 3478 3644 SPOC. {ECO:0000255|PROSITE-
ProRule:PRU00249}.
DNA_BIND 1 574
REGION 2138 2462 Interaction with MSX2.
{ECO:0000269|PubMed:10451362}.
REGION 2706 2845 Interaction with RBPSUH.
COILED 559 575 {ECO:0000255}.
COILED 822 850 {ECO:0000255}.
COILED 1185 1206 {ECO:0000255}.
COILED 1509 1544 {ECO:0000255}.
COILED 1607 1627 {ECO:0000255}.
COMPBIAS 125 277 Arg-rich.
COMPBIAS 236 326 Ser-rich.
COMPBIAS 648 721 Tyr-rich.
COMPBIAS 702 832 Arg-rich.
COMPBIAS 2101 2233 Ala-rich.
COMPBIAS 2377 2518 Pro-rich.
COMPBIAS 2950 3475 Pro-rich.
MOD_RES 99 99 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 108 108 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 647 647 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 747 747 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 749 749 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 758 758 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 762 762 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 792 792 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 852 852 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 855 855 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 869 869 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1077 1077 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 1183 1183 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 1209 1209 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 1237 1237 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 1267 1267 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 1276 1276 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 1283 1283 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 1293 1293 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 1298 1298 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 1302 1302 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 1348 1348 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 1395 1395 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1397 1397 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 1454 1454 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 1456 1456 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 1634 1634 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 1844 1844 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 1915 1915 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 1936 1936 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 1965 1965 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 2128 2128 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 2134 2134 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 2171 2171 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 2366 2366 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 2419 2419 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 2450 2450 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 2454 2454 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 2458 2458 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 2491 2491 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 2913 2913 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 2925 2925 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 3088 3088 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 3096 3096 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q96T58}.
MOD_RES 3413 3413 Phosphoserine.
{ECO:0000250|UniProtKB:Q96T58}.
VAR_SEQ 618 640 Missing (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_008564.
VAR_SEQ 3318 3322 PPEGE -> RKPAFF (in isoform 3).
{ECO:0000303|PubMed:12693553}.
/FTId=VSP_013802.
VAR_SEQ 3550 3552 ETD -> RLE (in isoform 3).
{ECO:0000303|PubMed:12693553}.
/FTId=VSP_013803.
VAR_SEQ 3553 3644 Missing (in isoform 3).
{ECO:0000303|PubMed:12693553}.
/FTId=VSP_013804.
VARIANT 348 348 I -> T. {ECO:0000269|PubMed:9119401,
ECO:0000269|Ref.3}.
VARIANT 762 762 S -> F. {ECO:0000269|Ref.3}.
VARIANT 773 773 S -> F. {ECO:0000269|Ref.3}.
VARIANT 933 933 S -> L. {ECO:0000269|Ref.3}.
CONFLICT 366 366 V -> E (in Ref. 4; CAB01562).
{ECO:0000305}.
CONFLICT 394 394 L -> B (in Ref. 4; CAB01562).
{ECO:0000305}.
CONFLICT 409 409 V -> E (in Ref. 4; CAB01562).
{ECO:0000305}.
CONFLICT 413 413 V -> E (in Ref. 4; CAB01562).
{ECO:0000305}.
CONFLICT 430 430 I -> K (in Ref. 4; CAB01562).
{ECO:0000305}.
CONFLICT 454 462 DLRNIFQRF -> EPSETSFSAL (in Ref. 4;
CAB01562). {ECO:0000305}.
CONFLICT 511 511 F -> L (in Ref. 4; CAB01562).
{ECO:0000305}.
CONFLICT 527 527 S -> P (in Ref. 4; CAB01562).
{ECO:0000305}.
CONFLICT 537 537 H -> N (in Ref. 4; CAB01562).
{ECO:0000305}.
CONFLICT 566 566 A -> V (in Ref. 4; CAB01562).
{ECO:0000305}.
CONFLICT 569 569 A -> V (in Ref. 4; CAB01562).
{ECO:0000305}.
CONFLICT 573 577 TKGRK -> DQGQE (in Ref. 4; CAB01562).
{ECO:0000305}.
CONFLICT 754 754 R -> G (in Ref. 3; BAB32786).
{ECO:0000305}.
CONFLICT 1524 1524 D -> A (in Ref. 3; BAB32786).
{ECO:0000305}.
CONFLICT 1560 1560 H -> Y (in Ref. 3; BAB32786).
{ECO:0000305}.
CONFLICT 1570 1570 F -> L (in Ref. 3; BAB32786).
{ECO:0000305}.
CONFLICT 1574 1574 R -> G (in Ref. 3; BAB32786).
{ECO:0000305}.
CONFLICT 1609 1609 Q -> R (in Ref. 3; BAB32786).
{ECO:0000305}.
CONFLICT 1659 1659 I -> V (in Ref. 3; BAB32786).
{ECO:0000305}.
CONFLICT 1669 1669 S -> F (in Ref. 3; BAB32786).
{ECO:0000305}.
CONFLICT 1705 1705 V -> A (in Ref. 3; BAB32786).
{ECO:0000305}.
CONFLICT 1815 1815 A -> V (in Ref. 3; BAB32786).
{ECO:0000305}.
CONFLICT 2097 2097 G -> A (in Ref. 3; BAB32786).
{ECO:0000305}.
CONFLICT 2201 2202 Missing (in Ref. 3; BAB32786).
{ECO:0000305}.
CONFLICT 2322 2322 A -> V (in Ref. 3; BAB32786).
{ECO:0000305}.
CONFLICT 2385 2385 P -> Q (in Ref. 3; BAB32786).
{ECO:0000305}.
CONFLICT 2502 2502 R -> K (in Ref. 3; BAB32786).
{ECO:0000305}.
CONFLICT 2505 2505 E -> K (in Ref. 3; BAB32786).
{ECO:0000305}.
CONFLICT 2519 2519 D -> N (in Ref. 3; BAB32786).
{ECO:0000305}.
CONFLICT 2554 2554 T -> S (in Ref. 3; BAB32786).
{ECO:0000305}.
CONFLICT 2679 2688 LVSTPAGPVN -> VGEHPWWARD (in Ref. 3;
BAB32786). {ECO:0000305}.
CONFLICT 3010 3010 L -> P (in Ref. 3; BAB32786 and 5;
BAC65684). {ECO:0000305}.
SEQUENCE 3644 AA; 398754 MW; 9C7EC49A81A7DA4A CRC64;
MVRETRHLWV GNLPENVREE KIIEHFKRYG RVESVKILPK RGSEGGVAAF VDFVDIKSAQ
KAHNSVNKMG DRDLRTDYNE PGTIPSAARG LDETVSIASR SREVSGFRGS AGGPAYGPPP
SLHAREGRYE RRLDGASDNR ERAYEHSAYG HHERGTGAFD RTRHYDQDYY RDPRERTLQH
GLYYTSRSRS PNRFDAHDPR YEPRAREQFT LPSVVHRDIY RDDITREVRG RRPERSYQHS
RSRSPHSSQS RNQSPQRLAS QASRPTRSPS GSGSRSRSSS SDSISSSSSS SNTDSSDSSS
TASDDSPARS VQSAAVPAPT SQLLSSLEKD EPRKSFGIKV QNLPVRSIDT SLKDGLFHEF
KKFGKVTSVQ IHGASEERYG LVFFRQQEDQ EKALTASKGK LFFGMQIEVT AWVGPETESE
NEFRPLDERI DEFHPKATRT LFIGNLEKTT TYHDLRNIFQ RFGEIVDIDI KKVNGVPQYA
FLQYCDIASV CKAIKKMDGE YLGNNRLKLG FGKSMPTNCV WLDGLSSNVS DQYLTRHFCR
YGPVVKVVFD RLKGMALVLY SEIEDAQAAV KETKGRKIGG NKIKVDFANR ESQLAFYHCM
EKSGQDMRDF YEMLTERRAG QMAQSKHEDW SADAQSPHKC REERRGSYEY SQERTYYENV
RTPGTYPEDS RRDYPARGRE FYSEWETYQG EYYDSRYYDE PREYREYRSD PYEQDIREYS
YRQRERERER ERFESDRDHE RRPIERSQSP VHLRRPQSPG VSPAHSERLP SDSERRLYRR
SSERSGSCSS VSPPRYDKLE KARLERYTKN EKADKERTFD PERVERERRI VRKEKGEKDK
AERQKRKGKA HSPSSQPSET EQENDREQSP EKPRGSTKLS RDRADKEGPA KNRLELVPCV
VLTRVKEKEG KVIEHPPPEK LKARLGRDTT KASALDQKPQ AAQGEPAKSD PARGKALREK
VLPSHAEVGE KEGRTKLRKH LKAEQTPELS ALDLEKLEAR KRRFADSGLK IEKQKPEIKK
TSPETEDTRI LLKKQPDTSR DGVLLREGES ERKPVRKEIL KRESKKTKLE RLNSALSPKD
CQDPAAVSAG SGSRPSSDVH AGLGELTHGS VETQETQPKK AIPSKPQPKQ LQLLENQGPE
KEEVRKNYCR PREEPAEHRA GQEKPHGGNA EEKLGIDIDH TQSYRKQMEQ SRRKQRMEME
IAKAEKFGSP KKDVDDYERR SLVHEVGKPP QDVTDDSPPS KKRRTDHVDF DICTKRERNY
RSSRQISEDS ERTSCSPSVR HGSFHDDDDP RGSPRLVSVK GSPKGDEKGL PYPNAAVRDD
PLKCNPYDSG KREQTADTAK IKLSVLNSEG EPSRWDPPMK QDPSRFDVSF PNSVIKRDSL
RKRSVRDLEP GEVPSDSDED AEHRSQSPRA SSFYDSPRLS FLLRDRDQKL RERDERLASS
LERNKFYSFA LDKTITPDTK ALLERAKSLS SSREENWSFL DWDSRFANFR NNKDKEKVDS
APRPIPSWYM KKKKIRTDSE GKLDDKKDER REEEQERQEL FASRFLHSSI FEQDSKRLQH
LERKSEESDF PPGRLYGRQA SEGANSTSDS VQEPVVLFHS RFMELTRMQQ KEKEKDQKPK
EAEKQEEPET HPKTPEPAAE TKEPEPKAPV SAGLPAVTIT VVTPEPASSA PEKAEEAAEA
PSPAGEKPAE PAPVSEETKL VSEPVSVPVE QPRQSDVPPG EDSRDSQDSA ALAPSAPQES
AATDAVPCVN AEPLTPGTTV SQVESSVDPK PSSPQPLSKL TQRSEEAEEG KVEKPDTTPS
TEPDATQNAG VASEAQPPAS EDVEANPPVA AKDRKTNKSK RSKTSVQAAA ASVVEKPVTR
KSERIDREKL KRSSSPRGEA QKLLELKMEA EKITRTASKS SGGDTEHPEP SLPLSRSRRR
NVRSVYATMT DHESRSPAKE PVEQPRVTRK RLERELQEAV VPPTTPRRGR PPKTRRRAEE
DGEHERKEPA ETPRPAEGWR SPRSQKSAAA AGPQGKRGRN EQKVEAAAEA GAQASTREGN
PKSRGEREAA SEPKRDRRDP STDKSGPDTF PVEVLERKPP EKTYKSKRGR ARSTRSGMDR
AAHQRSLEMA ARAAGQAADK EAGPAAASPQ ESESPQKGSG SSPQLANNPA DPDREAEEES
ASASTAPPEG TQLARQIELE QAVQNIAKLP EPSAAAASKG TATATATAAS EEPAPEHGHK
PAHQASETEL AAAIGSIISD ASGEPENFSA PPSVPPGSQT HPREGMEPGL HEAESGILET
GTATESSAPQ VSALDPPEGS ADTKETRGNS GDSVQEAKGS KAEVTPPRKD KGRQKTTRRR
KRNANKKVVA ITETRASEAE QTQSESPAAE EATAATPEAP QEEKPSEKPP SPPAECTFDP
SKTPPAESLS QENSAAEKTP CKAPVLPALP PLSQPALMDD GPQARFKVHS IIESDPVTPP
SDSGIPPPTI PLVTIAKLPP PVIPGGVPHQ SPPPKVTEWI TRQEEPRAQS TPSPALPPDT
KASDMDTSSS TLRKILMDPK YVSATGVTST SVTTAIAEPV SAPCLQEAPA PPCDPKHPPL
EGVSAAAVPN ADTQASEVPV AADKEKVAPV IAPKITSVIS RMPVSIDLEN SQKITLAKPA
PQTLTGLVSA LTGLVNVSLV PVNALKGPVK GSVATLKGLV STPAGPVNLL KGPVNVLTGP
VNVLTTPVSA TVGTVNAAPG PVTAACGVTA TTGTAAVTGA VTAPAAKGKQ RASSNENSRF
HPGSMSVIDD RPADTGSGAG LRVNTSEGVV LLSYSGQKTE GPQRISAKIS QIPPASAMDI
EFQQSVSKSQ VKADSITPTQ SAPKGPQTPS AFANVAAHST LVLTAQTYNA SPVISSVKTD
RPSLEKPEPI HLSVSTPVTQ GGTVKVLTQG INTPPVLVHN QLVLTPSIVT TNKKLADPVT
LKIETKVLQP ANLGPTLTPH HPPALPSKLP AEVNHVPSGP STPADRTIAH LATPKPDTHS
PRPTGPTPGL FPRPCHPSST TSTALSTNAT VMLAAGIPVP QFISSIHPEQ SVIMPPHSIT
QTVSLGHLSQ GEVRMSTPTL PSITYSIRPE TLHSPRAPLQ PQQIEARAPQ RVGTPQPATT
GVPALATQHP PEEEVHYHLP VARAAAPVQS EVLVMQSEYR LHPYTVPRDV RIMVHPHVTA
VSEQPRATEG VVKVPPANKA PQQLVKEAVK TSDAKAVPAP APVPVPVPVP TPAPPPHGEA
RILTVTPSSQ LQGLPLTPPV VVTHGVQIVH SSGELFQEYR YGDVRTYHAP AQQLTHTQFP
VASSISLASR TKTSAQVPPE GEPLQSTQSA QPAPSTQATQ PIPPAPPCQP SQLSQPAQPP
SGKIPQVSQE AKGTQTGGVE QTRLPAIPTN RPSEPHAQLQ RAPVETAQPA HPSPVSVSMK
PDLPSPLSSQ AAPKQPLFVP ANSGPSTPPG LALPHAEVQP APKQESSPHG TPQRPVDMVQ
LLKKYPIVWQ GLLALKNDTA AVQLHFVSGN NVLAHRSLPL SEGGPPLRIA QRMRLEASQL
EGVARRMTVE TDYCLLLALP CGRDQEDVVS QTESLKAAFI TYLQAKQAAG IINVPNPGSN
QPAYVLQIFP PCEFSESHLS RLAPDLLASI SNISPHLMIV IASV


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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1049: G Protein Signaling Pathways
WP1064: Delta-Notch Signaling Pathway
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining

Related Genes :
[MSX2 HOX8] Homeobox protein MSX-2 (Homeobox protein Hox-8)
[HDAC1 RPD3L1] Histone deacetylase 1 (HD1) (EC 3.5.1.98)
[Hdac1] Histone deacetylase 1 (HD1) (EC 3.5.1.98)
[Hdac1] Histone deacetylase 1 (HD1) (EC 3.5.1.98)
[HDAC1] Histone deacetylase 1 (HD1) (EC 3.5.1.98)
[HDAC1] Histone deacetylase 1 (HD1) (EC 3.5.1.98)
[Pias2 Miz1 Piasx] E3 SUMO-protein ligase PIAS2 (EC 2.3.2.27) (Androgen receptor-interacting protein 3) (ARIP3) (DAB2-interacting protein) (DIP) (Msx-interacting zinc finger protein) (Protein inhibitor of activated STAT x) (Protein inhibitor of activated STAT2) (RING-type E3 ubiquitin transferase PIAS2)
[Hdac9 Hdac7b Hdrp Mitr] Histone deacetylase 9 (HD9) (EC 3.5.1.98) (Histone deacetylase 7B) (HD7b) (Histone deacetylase-related protein) (MEF2-interacting transcription repressor MITR)
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (hMAD-3) (JV15-2) (SMAD family member 3) (SMAD 3) (Smad3) (hSMAD3)
[TRIM28 KAP1 RNF96 TIF1B] Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-associated protein 1) (KAP-1) (KRAB-interacting protein 1) (KRIP-1) (Nuclear corepressor KAP-1) (RING finger protein 96) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28)
[Maged1 Nrage] Melanoma-associated antigen D1 (Dlxin-1) (MAGE-D1 antigen) (Neurotrophin receptor-interacting MAGE homolog)
[HDAC9 HDAC7 HDAC7B HDRP KIAA0744 MITR] Histone deacetylase 9 (HD9) (EC 3.5.1.98) (Histone deacetylase 7B) (HD7) (HD7b) (Histone deacetylase-related protein) (MEF2-interacting transcription repressor MITR)
[MAGED1 NRAGE PP2250 PRO2292] Melanoma-associated antigen D1 (MAGE tumor antigen CCF) (MAGE-D1 antigen) (Neurotrophin receptor-interacting MAGE homolog)
[TSHZ3 KIAA1474 TSH3 ZNF537] Teashirt homolog 3 (Zinc finger protein 537)
[Tshz3 Kiaa1474 Tsh3 Zfp537 Znf537] Teashirt homolog 3 (Zinc finger protein 537)
[PIAS2 PIASX] E3 SUMO-protein ligase PIAS2 (EC 2.3.2.-) (Androgen receptor-interacting protein 3) (ARIP3) (DAB2-interacting protein) (DIP) (E3 SUMO-protein transferase PIAS2) (Msx-interacting zinc finger protein) (Miz1) (PIAS-NY protein) (Protein inhibitor of activated STAT x) (Protein inhibitor of activated STAT2)
[NRIP1] Nuclear receptor-interacting protein 1 (Nuclear factor RIP140) (Receptor-interacting protein 140)
[EP300 P300] Histone acetyltransferase p300 (p300 HAT) (EC 2.3.1.48) (E1A-associated protein p300) (Histone butyryltransferase p300) (EC 2.3.1.-) (Histone crotonyltransferase p300) (EC 2.3.1.-) (Protein propionyltransferase p300) (EC 2.3.1.-)
[SMAD4 DPC4 MADH4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4) (SMAD family member 4) (SMAD 4) (Smad4) (hSMAD4)
[Pias2 Miz1 Piasx] E3 SUMO-protein ligase PIAS2 (EC 2.3.2.-) (Androgen receptor-interacting protein 3) (ARIP3) (DAB2-interacting protein) (DIP) (E3 SUMO-protein transferase PIAS2) (Msx-interacting-zinc finger protein) (Protein inhibitor of activated STAT x) (Protein inhibitor of activated STAT2)
[SUV39H1 KMT1A SUV39H] Histone-lysine N-methyltransferase SUV39H1 (EC 2.1.1.43) (Histone H3-K9 methyltransferase 1) (H3-K9-HMTase 1) (Lysine N-methyltransferase 1A) (Position-effect variegation 3-9 homolog) (Suppressor of variegation 3-9 homolog 1) (Su(var)3-9 homolog 1)
[HDAC2] Histone deacetylase 2 (HD2) (EC 3.5.1.98)
[DNTTIP1 C20orf167 TDIF1] Deoxynucleotidyltransferase terminal-interacting protein 1 (Terminal deoxynucleotidyltransferase-interacting factor 1) (TdIF1) (TdT-interacting factor 1)
[RAD1 REC1] Cell cycle checkpoint protein RAD1 (hRAD1) (EC 3.1.11.2) (DNA repair exonuclease rad1 homolog) (Rad1-like DNA damage checkpoint protein)
[RB1] Retinoblastoma-associated protein (p105-Rb) (pRb) (Rb) (pp110)
[DACT1 DPR1 HNG3] Dapper homolog 1 (hDPR1) (Dapper antagonist of catenin 1) (Hepatocellular carcinoma novel gene 3 protein)
[APPL1 APPL DIP13A KIAA1428] DCC-interacting protein 13-alpha (Dip13-alpha) (Adapter protein containing PH domain, PTB domain and leucine zipper motif 1)
[SMARCA4 BAF190A BRG1 SNF2B SNF2L4] Transcription activator BRG1 (EC 3.6.4.-) (ATP-dependent helicase SMARCA4) (BRG1-associated factor 190A) (BAF190A) (Mitotic growth and transcription activator) (Protein BRG-1) (Protein brahma homolog 1) (SNF2-beta) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4)
[BAZ2A KIAA0314 TIP5] Bromodomain adjacent to zinc finger domain protein 2A (Transcription termination factor I-interacting protein 5) (TTF-I-interacting protein 5) (Tip5) (hWALp3)
[RCHY1 ARNIP CHIMP PIRH2 RNF199 ZNF363] RING finger and CHY zinc finger domain-containing protein 1 (EC 2.3.2.27) (Androgen receptor N-terminal-interacting protein) (CH-rich-interacting match with PLAG1) (E3 ubiquitin-protein ligase Pirh2) (RING finger protein 199) (RING-type E3 ubiquitin transferase RCHY1) (Zinc finger protein 363) (p53-induced RING-H2 protein) (hPirh2)

Bibliography :