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Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4 homolog) (SMAD family member 4) (SMAD 4) (Smad4)

 SMAD4_MOUSE             Reviewed;         551 AA.
P97471; Q6GTP6; Q9CW56;
04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
22-APR-2020, entry version 191.
RecName: Full=Mothers against decapentaplegic homolog 4;
Short=MAD homolog 4;
Short=Mothers against DPP homolog 4;
AltName: Full=Deletion target in pancreatic carcinoma 4 homolog;
AltName: Full=SMAD family member 4;
Short=SMAD 4;
Short=Smad4;
Name=Smad4; Synonyms=Dpc4, Madh4;
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 [MRNA].
STRAIN=A/J; TISSUE=Lung;
PubMed=9166592; DOI=10.1007/s003359900465;
Anna C.H., Devereux T.R.;
"Sequence and chromosomal mapping of the mouse homolog (Madh4) of the human
DPC4/MADH4 gene.";
Mamm. Genome 8:443-444(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Olfactory epithelium;
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 [LARGE SCALE MRNA] OF 67-551.
STRAIN=C57BL/6J; TISSUE=Lung;
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).
[5]
INTERACTION WITH ZNF8.
PubMed=12370310; DOI=10.1128/mcb.22.21.7633-7644.2002;
Jiao K., Zhou Y., Hogan B.L.M.;
"Identification of mZnf8, a mouse Kruppel-like transcriptional repressor,
as a novel nuclear interaction partner of Smad1.";
Mol. Cell. Biol. 22:7633-7644(2002).
[6]
FUNCTION, DNA-BINDING, AND IDENTIFICATION IN A COMPLEX WITH SMAD1 AND YY1.
PubMed=15329343; DOI=10.1242/dev.01344;
Lee K.H., Evans S., Ruan T.Y., Lassar A.B.;
"SMAD-mediated modulation of YY1 activity regulates the BMP response and
cardiac-specific expression of a GATA4/5/6-dependent chick Nkx2.5
enhancer.";
Development 131:4709-4723(2004).
[7]
INTERACTION WITH ZC3H3.
PubMed=16115198; DOI=10.1111/j.1365-2443.2005.00887.x;
Collart C., Remacle J.E., Barabino S., van Grunsven L.A., Nelles L.,
Schellens A., Van de Putte T., Pype S., Huylebroeck D., Verschueren K.;
"Smicl is a novel Smad interacting protein and cleavage and polyadenylation
specificity factor associated protein.";
Genes Cells 10:897-906(2005).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung;
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).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=24076600; DOI=10.1038/ng.2772;
Sartori R., Schirwis E., Blaauw B., Bortolanza S., Zhao J., Enzo E.,
Stantzou A., Mouisel E., Toniolo L., Ferry A., Stricker S., Goldberg A.L.,
Dupont S., Piccolo S., Amthor H., Sandri M.;
"BMP signaling controls muscle mass.";
Nat. Genet. 45:1309-1318(2013).
[10]
X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 9-140 IN COMPLEX WITH DNA,
ZINC_BINDING SITES, AND SUBUNIT.
PubMed=20147459; DOI=10.1093/nar/gkq046;
Baburajendran N., Palasingam P., Narasimhan K., Sun W., Prabhakar S.,
Jauch R., Kolatkar P.R.;
"Structure of Smad1 MH1/DNA complex reveals distinctive rearrangements of
BMP and TGF-beta effectors.";
Nucleic Acids Res. 38:3477-3488(2010).
-!- FUNCTION: Common SMAD (co-SMAD) is the coactivator and mediator of
signal transduction by TGF-beta (transforming growth factor). Component
of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the
nucleus and is required for the TGF-mediated signaling. Promotes
binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an
activation function required for SMAD1 or SMAD2 to stimulate
transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex
which forms at the AP1 promoter site; required for synergistic
transcriptional activity in response to TGF-beta. May act as a tumor
suppressor. Positively regulates PDPK1 kinase activity by stimulating
its dissociation from the 14-3-3 protein YWHAQ which acts as a negative
regulator (By similarity). Acts synergistically with SMAD1 and YY1 in
bone morphogenetic protein (BMP)-mediated cardiac-specific gene
expression (PubMed:15329343). Binds to SMAD binding elements (SBEs)
(5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac
activating regions (PubMed:15329343). In muscle physiology, plays a
central role in the balance between atrophy and hypertrophy. When
recruited by MSTN, promotes atrophy response via phosphorylated
SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment
by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8.
{ECO:0000250, ECO:0000269|PubMed:15329343,
ECO:0000269|PubMed:24076600}.
-!- SUBUNIT: Monomer (By similarity). Heterotrimer; with a C-terminally
phosphorylated R-SMAD molecule and to form the transcriptionally active
SMAD2/3-SMAD4 complex (By similarity). Found in a ternary complex
composed of SMAD4, STK11/LKB1 and STK11IP. Interacts with ATF2, COPS5,
DACH1, MSG1, SKI, STK11/LKB1, STK11IP and TRIM33. Associates with
ZNF423 or ZNF521 in response to BMP2 leading to activate transcription
of BMP target genes. Interacts with USP9X. Interacts with RBPMS.
Interacts with WWTR1 (via coiled-coil domain). Interacts with CITED1
and CITED2 (By similarity). Interacts with PDPK1 (via PH domain) (By
similarity). Interacts with VPS39; this interaction affects heterodimer
formation with SMAD3, but not with SMAD2, and leads to inhibition of
SMAD3-dependent transcription activation (By similarity). Interactions
with VPS39 and SMAD2 may be mutually exclusive (By similarity).
Interacts (via MH2 domain) with ZNF451 (via N-terminal zinc-finger
domains) (By similarity). Identified in a complex that contains at
least ZNF451, SMAD2, SMAD3 and SMAD4 (By similarity). Found in a
complex with SMAD1 and YY1 (PubMed:15329343). Interacts with ZC3H3
(PubMed:16115198). Interacts weakly with ZNF8 (PubMed:12370310).
Interacts with NUP93 and IPO7; translocates SMAD4 to the nucleus
through the NPC upon BMP7 stimulation resulting in activation of SMAD4
signaling (By similarity). Interacts with CREB3L1, the interaction
takes place upon TGFB1 induction and SMAD4 acts as CREB3L1 coactivator
to induce the expression of genes involved in the assembly of collagen
extracellular matrix (By similarity). Interacts with DLX1 (By
similarity). Interacts with ZBTB7A; the interaction is direct and
stimulated by TGFB1 (By similarity). Interacts with CREBBP; the
recruitment of this transcriptional coactivator is negatively regulated
by ZBTB7A (By similarity). Interacts with EP300; the interaction with
this transcriptional coactivator is negatively regulated by ZBTB7A (By
similarity). Interacts with HDAC1 (By similarity). Interacts (via MH2
domain) with ZMIZ1 (via SP-RING-type domain); in the TGF-beta signaling
pathway increases the activity of the SMAD3/SMAD4 transcriptional
complex (By similarity). {ECO:0000250|UniProtKB:O70437,
ECO:0000250|UniProtKB:Q13485, ECO:0000269|PubMed:12370310,
ECO:0000269|PubMed:15329343, ECO:0000269|PubMed:16115198,
ECO:0000269|PubMed:20147459}.
-!- INTERACTION:
P97471; Q8R1H0: Hopx; NbExp=2; IntAct=EBI-5259270, EBI-6913924;
P97471; Q60698: Ski; NbExp=3; IntAct=EBI-5259270, EBI-15969860;
P97471; Q62432: Smad2; NbExp=3; IntAct=EBI-5259270, EBI-2337932;
P97471; Q8BUN5: Smad3; NbExp=6; IntAct=EBI-5259270, EBI-2337983;
P97471; O95411: TIAF1; Xeno; NbExp=2; IntAct=EBI-5259270, EBI-302378;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13485}. Nucleus
{ECO:0000250|UniProtKB:Q13485}. Note=In the cytoplasm in the absence of
ligand. Migration to the nucleus when complexed with R-SMAD. PDPK1
prevents its nuclear translocation. {ECO:0000250|UniProtKB:Q13485}.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: The MH1 domain is required for DNA binding.
-!- DOMAIN: The MH2 domain is required for both homomeric and heteromeric
interactions and for transcriptional regulation. Sufficient for nuclear
import (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated by PDPK1. {ECO:0000250}.
-!- PTM: Monoubiquitinated on Lys-518 by E3 ubiquitin-protein ligase
TRIM33. Monoubiquitination hampers its ability to form a stable complex
with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP
signaling cascade. Deubiquitination by USP9X restores its competence to
mediate TGF-beta signaling (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Conditional knockout in muscle leads to muscle
atrophy and weakness. Mutant mice loose significantly more muscle mass
after denervation as compared to wild-type animals and show excessive
proteolysis in denervated muscle. The loss of maximal absolute force
after fasting is greater in mutant mice than in controls.
{ECO:0000269|PubMed:24076600}.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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EMBL; U79748; AAB57905.1; -; mRNA.
EMBL; CH466528; EDL09560.1; -; Genomic_DNA.
EMBL; BC046584; AAH46584.1; -; mRNA.
EMBL; AK004804; BAB23576.1; -; mRNA.
CCDS; CCDS29337.1; -.
RefSeq; NP_032566.2; NM_008540.2.
PDB; 3QSV; X-ray; 2.71 A; A/B/C/D=9-140.
PDBsum; 3QSV; -.
SMR; P97471; -.
BioGrid; 201277; 28.
ComplexPortal; CPX-10; SMAD2-SMAD3-SMAD4 complex.
ComplexPortal; CPX-146; SMAD1-SMAD4 complex.
ComplexPortal; CPX-3251; SMAD2-SMAD4 complex.
ComplexPortal; CPX-3286; SMAD3-SMAD4 complex.
CORUM; P97471; -.
DIP; DIP-29718N; -.
IntAct; P97471; 8.
MINT; P97471; -.
STRING; 10090.ENSMUSP00000025393; -.
iPTMnet; P97471; -.
PhosphoSitePlus; P97471; -.
EPD; P97471; -.
MaxQB; P97471; -.
PaxDb; P97471; -.
PRIDE; P97471; -.
Antibodypedia; 3711; 1002 antibodies.
Ensembl; ENSMUST00000025393; ENSMUSP00000025393; ENSMUSG00000024515.
Ensembl; ENSMUST00000114939; ENSMUSP00000110589; ENSMUSG00000024515.
GeneID; 17128; -.
KEGG; mmu:17128; -.
UCSC; uc008fou.1; mouse.
CTD; 4089; -.
MGI; MGI:894293; Smad4.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
GeneTree; ENSGT00940000157435; -.
HOGENOM; CLU_026736_1_1_1; -.
InParanoid; P97471; -.
KO; K04501; -.
OMA; PQMGPGT; -.
OrthoDB; 905048at2759; -.
TreeFam; TF314923; -.
Reactome; R-MMU-1181150; Signaling by NODAL.
Reactome; R-MMU-1502540; Signaling by Activin.
Reactome; R-MMU-201451; Signaling by BMP.
Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
Reactome; R-MMU-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-MMU-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-8941326; RUNX2 regulates bone development.
Reactome; R-MMU-8941855; RUNX3 regulates CDKN1A transcription.
Reactome; R-MMU-9617828; FOXO-mediated transcription of cell cycle genes.
ChiTaRS; Smad4; mouse.
EvolutionaryTrace; P97471; -.
PRO; PR:P97471; -.
Proteomes; UP000000589; Chromosome 18.
RNAct; P97471; protein.
Bgee; ENSMUSG00000024515; Expressed in rostral migratory stream and 310 other tissues.
Genevisible; P97471; MM.
GO; GO:0032444; C:activin responsive factor complex; ISO:MGI.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005813; C:centrosome; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:BHF-UCL.
GO; GO:0071141; C:SMAD protein complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; IPI:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0005518; F:collagen binding; IPI:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
GO; GO:0031005; F:filamin binding; ISO:MGI.
GO; GO:0070411; F:I-SMAD binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0098772; F:molecular function regulator; IMP:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0070412; F:R-SMAD binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL.
GO; GO:0046332; F:SMAD binding; ISO:MGI.
GO; GO:0043199; F:sulfate binding; ISO:MGI.
GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0030616; F:transforming growth factor beta receptor, common-partner cytoplasmic mediator activity; ISO:MGI.
GO; GO:0009653; P:anatomical structure morphogenesis; IMP:MGI.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
GO; GO:0036302; P:atrioventricular canal development; IGI:BHF-UCL.
GO; GO:0003190; P:atrioventricular valve formation; IGI:BHF-UCL.
GO; GO:0007411; P:axon guidance; IMP:MGI.
GO; GO:0030509; P:BMP signaling pathway; IMP:BHF-UCL.
GO; GO:0003360; P:brainstem development; IMP:MGI.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IGI:MGI.
GO; GO:0003279; P:cardiac septum development; IGI:BHF-UCL.
GO; GO:0030154; P:cell differentiation; IMP:MGI.
GO; GO:0008283; P:cell population proliferation; IMP:MGI.
GO; GO:0006879; P:cellular iron ion homeostasis; IMP:BHF-UCL.
GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI.
GO; GO:0048589; P:developmental growth; IMP:MGI.
GO; GO:0042733; P:embryonic digit morphogenesis; IMP:CACAO.
GO; GO:0060956; P:endocardial cell differentiation; IMP:BHF-UCL.
GO; GO:0007492; P:endoderm development; IMP:MGI.
GO; GO:0042118; P:endothelial cell activation; IMP:BHF-UCL.
GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; IMP:BHF-UCL.
GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:0008585; P:female gonad development; IGI:MGI.
GO; GO:0061040; P:female gonad morphogenesis; IMP:MGI.
GO; GO:0048859; P:formation of anatomical boundary; IMP:MGI.
GO; GO:0007369; P:gastrulation; IMP:MGI.
GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
GO; GO:0001822; P:kidney development; IMP:MGI.
GO; GO:0003220; P:left ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
GO; GO:0008584; P:male gonad development; IMP:MGI.
GO; GO:0048382; P:mesendoderm development; IMP:MGI.
GO; GO:0007498; P:mesoderm development; IMP:MGI.
GO; GO:0072133; P:metanephric mesenchyme morphogenesis; IMP:UniProtKB.
GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IMP:BHF-UCL.
GO; GO:1905305; P:negative regulation of cardiac myofibril assembly; IMP:BHF-UCL.
GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0072134; P:nephrogenic mesenchyme morphogenesis; IMP:UniProtKB.
GO; GO:0014033; P:neural crest cell differentiation; IMP:MGI.
GO; GO:0048663; P:neuron fate commitment; IMP:MGI.
GO; GO:0001649; P:osteoblast differentiation; ISO:MGI.
GO; GO:0003148; P:outflow tract septum morphogenesis; IGI:BHF-UCL.
GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISO:MGI.
GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; ISO:MGI.
GO; GO:0003251; P:positive regulation of cell proliferation involved in heart valve morphogenesis; IMP:BHF-UCL.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
GO; GO:0046881; P:positive regulation of follicle-stimulating hormone secretion; IMP:MGI.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:BHF-UCL.
GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; IMP:BHF-UCL.
GO; GO:0033686; P:positive regulation of luteinizing hormone secretion; IMP:MGI.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IMP:BHF-UCL.
GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
GO; GO:0061614; P:pri-miRNA transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0051098; P:regulation of binding; IDA:MGI.
GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
GO; GO:0051797; P:regulation of hair follicle development; IMP:MGI.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
GO; GO:0032909; P:regulation of transforming growth factor beta2 production; ISO:MGI.
GO; GO:0001666; P:response to hypoxia; ISO:MGI.
GO; GO:0071559; P:response to transforming growth factor beta; ISO:MGI.
GO; GO:0048733; P:sebaceous gland development; IMP:MGI.
GO; GO:0062009; P:secondary palate development; IMP:BHF-UCL.
GO; GO:0072520; P:seminiferous tubule development; IMP:MGI.
GO; GO:0007338; P:single fertilization; IGI:MGI.
GO; GO:0007183; P:SMAD protein complex assembly; ISO:MGI.
GO; GO:0060395; P:SMAD protein signal transduction; ISO:MGI.
GO; GO:0032525; P:somite rostral/caudal axis specification; IMP:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
GO; GO:0048729; P:tissue morphogenesis; IMP:MGI.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0060065; P:uterus development; IGI:MGI.
GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
GO; GO:0042060; P:wound healing; ISO:MGI.
Gene3D; 2.60.200.10; -; 1.
Gene3D; 3.90.520.10; -; 1.
InterPro; IPR013790; Dwarfin.
InterPro; IPR003619; MAD_homology1_Dwarfin-type.
InterPro; IPR013019; MAD_homology_MH1.
InterPro; IPR017855; SMAD-like_dom_sf.
InterPro; IPR001132; SMAD_dom_Dwarfin-type.
InterPro; IPR008984; SMAD_FHA_dom_sf.
InterPro; IPR036578; SMAD_MH1_sf.
PANTHER; PTHR13703; PTHR13703; 1.
Pfam; PF03165; MH1; 1.
Pfam; PF03166; MH2; 1.
SMART; SM00523; DWA; 1.
SMART; SM00524; DWB; 1.
SUPFAM; SSF49879; SSF49879; 1.
SUPFAM; SSF56366; SSF56366; 1.
PROSITE; PS51075; MH1; 1.
PROSITE; PS51076; MH2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cytoplasm; DNA-binding; Isopeptide bond;
Metal-binding; Nucleus; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc.
CHAIN 1..551
/note="Mothers against decapentaplegic homolog 4"
/id="PRO_0000090862"
DOMAIN 18..142
/note="MH1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
DOMAIN 322..551
/note="MH2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
REGION 1..321
/note="Mediates interaction with ZBTB7A"
/evidence="ECO:0000250|UniProtKB:Q13485"
REGION 274..319
/note="SAD"
COMPBIAS 450..465
/note="Poly-Ala"
METAL 71
/note="Zinc"
/evidence="ECO:0000250"
METAL 115
/note="Zinc"
/evidence="ECO:0000250"
METAL 127
/note="Zinc"
/evidence="ECO:0000250"
METAL 132
/note="Zinc"
/evidence="ECO:0000250"
SITE 514
/note="Necessary for heterotrimerization"
/evidence="ECO:0000250"
MOD_RES 37
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:Q13485"
MOD_RES 427
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:Q13485"
MOD_RES 506
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:Q13485"
CROSSLNK 113
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000250|UniProtKB:Q13485"
CROSSLNK 518
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:Q13485"
CONFLICT 257
/note="A -> S (in Ref. 1; AAB57905)"
/evidence="ECO:0000305"
CONFLICT 292
/note="P -> R (in Ref. 1; AAB57905)"
/evidence="ECO:0000305"
HELIX 16..24
/evidence="ECO:0000244|PDB:3QSV"
HELIX 33..47
/evidence="ECO:0000244|PDB:3QSV"
HELIX 51..62
/evidence="ECO:0000244|PDB:3QSV"
TURN 63..65
/evidence="ECO:0000244|PDB:3QSV"
STRAND 73..75
/evidence="ECO:0000244|PDB:3QSV"
STRAND 82..84
/evidence="ECO:0000244|PDB:3QSV"
STRAND 87..89
/evidence="ECO:0000244|PDB:3QSV"
HELIX 91..99
/evidence="ECO:0000244|PDB:3QSV"
STRAND 109..111
/evidence="ECO:0000244|PDB:3QSV"
HELIX 119..121
/evidence="ECO:0000244|PDB:3QSV"
STRAND 124..127
/evidence="ECO:0000244|PDB:3QSV"
HELIX 130..132
/evidence="ECO:0000244|PDB:3QSV"
STRAND 133..135
/evidence="ECO:0000244|PDB:3QSV"
SEQUENCE 551 AA; 60342 MW; 4FBDF5DED4442F86 CRC64;
MDNMSITNTP TSNDACLSIV HSLMCHRQGG ESETFAKRAI ESLVKKLKEK KDELDSLITA
ITTNGAHPSK CVTIQRTLDG RLQVAGRKGF PHVIYARLWR WPDLHKNELK HVKYCQYAFD
LKCDSVCVNP YHYERVVSPG IDLSGLTLQS NAPSMLVKDE YVHDFEGQPS LPTEGHSIQT
IQHPPSNRAS TETYSAPALL APAESNATST TNFPNIPVAS TSQPASILAG SHSEGLLQIA
SGPQPGQQQN GFTAQPATYH HNSTTTWTGS RTAPYTPNLP HHQNGHLQHH PPMPPHPGHY
WPVHNELAFQ PPISNHPAPE YWCSIAYFEM DVQVGETFKV PSSCPVVTVD GYVDPSGGDR
FCLGQLSNVH RTEAIERARL HIGKGVQLEC KGEGDVWVRC LSDHAVFVQS YYLDREAGRA
PGDAVHKIYP SAYIKVFDLR QCHRQMQQQA ATAQAAAAAQ AAAVAGNIPG PGSVGGIAPA
ISLSAAAGIG VDDLRRLCIL RMSFVKGWGP DYPRQSIKET PCWIEIHLHR ALQLLDEVLH
TMPIADPQPL D


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Pathways :
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP32: Translation Factors
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2256: Integrated Pancreatic Cancer Pathway
WP2377: Integrated Pancreatic Cancer Pathway
WP1596: Iron Homeostasis
WP1045: TGF-beta Receptor Signaling Pathway
WP926: TGF-beta Receptor Signaling Pathway
WP1425: BMP signalling and regulation
WP505: TGF Beta Signaling Pathway
WP1591: Heart Development
WP560: TGF Beta Signaling Pathway
WP1058: Senescence and Autophagy
WP940: Senescence and Autophagy
WP1098: Wnt Signaling Pathway
WP252: Androgen Receptor Signaling Pathway
WP980: Wnt Signaling Pathway NetPath
WP179: Cell cycle
WP710: DNA damage response (only ATM dependent)
WP190: Cell cycle
WP809: TGF-beta Receptor Signaling Pathway
WP1164: TGF Beta Signaling Pathway
WP1180: Delta-Notch Signaling Pathway
WP362: TGF-beta Receptor Signaling Pathway
WP199: Delta-Notch Signaling Pathway

Related Genes :
[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)
[Smad4 Dpc4 Madh4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4 homolog) (SMAD family member 4) (SMAD 4) (Smad4)
[SMAD4 MADH4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[Smad4 Madh4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[SMAD1 BSP1 MADH1 MADR1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (JV4-1) (Mad-related protein 1) (SMAD family member 1) (SMAD 1) (Smad1) (hSMAD1) (Transforming growth factor-beta-signaling protein 1) (BSP-1)
[SMAD2 MADH2 MADR2] Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (JV18-1) (Mad-related protein 2) (hMAD-2) (SMAD family member 2) (SMAD 2) (Smad2) (hSMAD2)
[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)
[Smad1 Madh1 Madr1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (Dwarfin-A) (Dwf-A) (Mothers-against-DPP-related 1) (Mad-related protein 1) (mMad1) (SMAD family member 1) (SMAD 1) (Smad1)
[SMAD6 MADH6] Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (SMAD family member 6) (SMAD 6) (Smad6) (hSMAD6)
[SMAD7 MADH7 MADH8] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (Mothers against decapentaplegic homolog 8) (MAD homolog 8) (Mothers against DPP homolog 8) (SMAD family member 7) (SMAD 7) (Smad7) (hSMAD7)
[Smad7 Madh7 Madh8] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (Mothers against decapentaplegic homolog 8) (MAD homolog 8) (Mothers against DPP homolog 8) (SMAD family member 7) (SMAD 7) (Smad7)
[Smad1 Mad1 Madh1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (SMAD family member 1) (SMAD 1) (Smad1)
[Smad3 Madh3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (SMAD family member 3) (SMAD 3) (Smad3)
[Smad3 Madh3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (mMad3) (SMAD family member 3) (SMAD 3) (Smad3)
[SMAD1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (SMAD family member 1) (SMAD 1) (Smad1)
[Smad7 Madh7] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (SMAD family member 7) (SMAD 7) (Smad7)
[SMAD4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (SMAD family member 3) (SMAD 3) (Smad3)
[Smox Dmel\CG2262 DSMAD2 DSmad2 dSMAD2 dSmad2 dsmad2 l(1)G0348 Sad sad Smad SMAD2 Smad2 smad2 SMOX SmoX smox ted tmp CG2262 Dmel_CG2262] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[ZFYVE9 MADHIP SARA SMADIP] Zinc finger FYVE domain-containing protein 9 (Mothers against decapentaplegic homolog-interacting protein) (Madh-interacting protein) (Novel serine protease) (NSP) (Receptor activation anchor) (hSARA) (Smad anchor for receptor activation)
[Dcp1a Mitc1 Smif] mRNA-decapping enzyme 1A (EC 3.-.-.-) (MAD homolog 4-interacting transcription coactivator 1) (Smad4-interacting transcriptional co-activator) (Transcription factor SMIF)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[DNAJA1 DNAJ2 HDJ2 HSJ2 HSPF4] DnaJ homolog subfamily A member 1 (DnaJ protein homolog 2) (HSDJ) (Heat shock 40 kDa protein 4) (Heat shock protein J2) (HSJ-2) (Human DnaJ protein 2) (hDj-2)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[NSMCE3 HCA4 MAGEG1 NDNL2] Non-structural maintenance of chromosomes element 3 homolog (Non-SMC element 3 homolog) (Hepatocellular carcinoma-associated protein 4) (MAGE-G1 antigen) (Melanoma-associated antigen G1) (Necdin-like protein 2)
[KMT2B HRX2 KIAA0304 MLL2 MLL4 TRX2 WBP7] Histone-lysine N-methyltransferase 2B (Lysine N-methyltransferase 2B) (EC 2.1.1.354) (Myeloid/lymphoid or mixed-lineage leukemia protein 4) (Trithorax homolog 2) (WW domain-binding protein 7) (WBP-7)
[DNAJB11 EDJ ERJ3 HDJ9 PSEC0121 UNQ537/PRO1080] DnaJ homolog subfamily B member 11 (APOBEC1-binding protein 2) (ABBP-2) (DnaJ protein homolog 9) (ER-associated DNAJ) (ER-associated Hsp40 co-chaperone) (Endoplasmic reticulum DNA J domain-containing protein 3) (ER-resident protein ERdj3) (ERdj3) (ERj3p) (HEDJ) (Human DnaJ protein 9) (hDj-9) (PWP1-interacting protein 4)
[PLAAT3 HRASLS3 HREV107 PLA2G16] Phospholipase A and acyltransferase 3 (EC 2.3.1.-) (EC 3.1.1.32) (EC 3.1.1.4) (Adipose-specific phospholipase A2) (AdPLA) (Group XVI phospholipase A1/A2) (H-rev 107 protein homolog) (H-REV107) (HREV107-1) (HRAS-like suppressor 1) (HRAS-like suppressor 3) (HRSL3) (HREV107-3) (Renal carcinoma antigen NY-REN-65)
[repD ercc2 DDB_G0267414] General transcription and DNA repair factor IIH helicase subunit XPD (TFIIH subunit XPD) (EC 3.6.4.12) (DNA excision repair cross-complementing protein-2 homolog) (DNA repair protein D) (TFIIH basal transcription factor complex helicase repD subunit)
[SMARCA5 SNF2H WCRF135] SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5 (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin A5) (EC 3.6.4.-) (Sucrose nonfermenting protein 2 homolog) (hSNF2H)

Bibliography :
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