UniProtKB - Q8K4J6 (MRTFA_MOUSE)
Myocardin-related transcription factor A
Mrtfa
Functioni
Transcription coactivator that associates with the serum response factor (SRF) transcription factor to control expression of genes regulating the cytoskeleton during development, morphogenesis and cell migration (PubMed:12019265, PubMed:12732141, PubMed:17588931, PubMed:19350017, PubMed:24732378).
The SRF-MRTFA complex activity responds to Rho GTPase-induced changes in cellular globular actin (G-actin) concentration, thereby coupling cytoskeletal gene expression to cytoskeletal dynamics (PubMed:24732378).
MRTFA binds G-actin via its RPEL repeats, regulating activity of the MRTFA-SRF complex (PubMed:12732141, PubMed:17588931).
Activity is also regulated by filamentous actin (F-actin) in the nucleus (PubMed:23558171, PubMed:25759381).
7 PublicationsCaution
GO - Molecular functioni
- actin binding Source: MGI
- actin monomer binding Source: UniProtKB
- DNA-binding transcription factor activity Source: MGI
- leucine zipper domain binding Source: MGI
- transcription cis-regulatory region binding Source: MGI
- transcription coactivator activity Source: UniProtKB
GO - Biological processi
- actin cytoskeleton organization Source: UniProtKB
- forebrain development Source: MGI
- negative regulation of apoptotic signaling pathway Source: MGI
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
- neuron migration Source: MGI
- neuron projection development Source: MGI
- positive regulation of pri-miRNA transcription by RNA polymerase II Source: MGI
- positive regulation of transcription, DNA-templated Source: MGI
- positive regulation of transcription by RNA polymerase II Source: UniProtKB
- positive regulation of transcription via serum response element binding Source: UniProtKB
- regulation of transcription by RNA polymerase II Source: MGI
- smooth muscle cell differentiation Source: MGI
- wound healing, spreading of cells Source: MGI
Keywordsi
Molecular function | Actin-binding |
Biological process | Transcription, Transcription regulation |
Enzyme and pathway databases
Reactomei | R-MMU-3899300, SUMOylation of transcription cofactors R-MMU-5663220, RHO GTPases Activate Formins |
Names & Taxonomyi
Protein namesi | Recommended name: Myocardin-related transcription factor ACuratedShort name: MRTF-A1 Publication Alternative name(s): Basic SAP coiled-coil transcription activator1 Publication MKL/myocardin-like protein 1 Megakaryoblastic leukemia 1 protein homolog Megakaryocytic acute leukemia protein homolog2 Publications |
Gene namesi | Name:Mrtfa Synonyms:Bsac1 Publication, Mal2 Publications, Mkl1Imported |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:2384495, Mrtfa |
VEuPathDBi | HostDB:ENSMUSG00000042292 |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 6 Publications
Nucleus
- Nucleus 7 Publications
Note: Subcellular location is tightly regulated by actin both in cytoplasm and nucleus: high levels of G-actin in the nucleus observed during serum deprivation lead to low levels of nuclear MRTFA, while reduced levels of nuclear G-actin result in accumulation of MRTFA in the nucleus (PubMed:17588931, PubMed:21673315). G-actin-binding in the cytoplasm inhibits nuclear import by masking the nuclear localization signal (NLS) (PubMed:17588931, PubMed:21673315). In contrast, binding to nuclear globular actin (G-actin) promotes nuclear export to the cytoplasm (PubMed:17588931). Nuclear localization is regulated by MICAL2, which mediates depolymerization of nuclear actin, which decreases nuclear G-actin pool, thereby promoting retention of MRTFA in the nucleus and subsequent formation of an active complex with SRF (By similarity).By similarity2 Publications
Cytosol
- cytosol Source: MGI
Nucleus
- nucleoplasm Source: MGI
- nucleus Source: UniProtKB
Other locations
- cytoplasm Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 24 | R → A in 123-1A: Reduced interaction with G-actin, leading to a constitutively active SRF-MRTFA complex; when associated with A-68 and A-112. 1 Publication | 1 | |
Mutagenesisi | 45 | F → A or D: Induces a nuclear accumulation in unstimulated cells. 1 Publication | 1 | |
Mutagenesisi | 48 | Q → A or D: Induces a nuclear accumulation in unstimulated cells. 1 Publication | 1 | |
Mutagenesisi | 52 | L → A or D: Induces a nuclear accumulation in unstimulated cells. 1 Publication | 1 | |
Mutagenesisi | 54 | R → A: Impaired interaction with G-actin, leading to nuclear accumulation in unstimulated cells. 1 Publication | 1 | |
Mutagenesisi | 56 | R → A: Impaired interaction with G-actin, leading to nuclear accumulation in unstimulated cells. 1 Publication | 1 | |
Mutagenesisi | 68 | R → A in 123-1A: Reduced interaction with G-actin, leading to a constitutively active SRF-MRTFA complex; when associated with A-24 and A-112. 1 Publication | 1 | |
Mutagenesisi | 89 | L → A or D: Does not induce a nuclear accumulation in unstimulated cells. 1 Publication | 1 | |
Mutagenesisi | 92 | K → A or D: Does not induce a nuclear accumulation in unstimulated cells. 1 Publication | 1 | |
Mutagenesisi | 96 | L → A: Induces a nuclear accumulation in unstimulated cells. 1 Publication | 1 | |
Mutagenesisi | 96 | L → D: Induces a nuclear decrease in unstimulated cells. 1 Publication | 1 | |
Mutagenesisi | 98 | R → A: Impaired interaction with G-actin, leading to cytoplasmic accumulation. 1 Publication | 1 | |
Mutagenesisi | 100 | R → A: Impaired interaction with G-actin, leading to cytoplasmic accumulation. 1 Publication | 1 | |
Mutagenesisi | 112 | R → A in 123-1A: Reduced interaction with G-actin, leading to a constitutively active SRF-MRTFA complex; when associated with A-24 and A-68. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000126626 | 1 – 964 | Myocardin-related transcription factor AAdd BLAST | 964 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 41 | Phosphoserine1 Publication | 1 | |
Modified residuei | 159 | Phosphoserine1 Publication | 1 | |
Modified residuei | 174 | Phosphoserine1 Publication | 1 | |
Modified residuei | 191 | Phosphoserine1 Publication | 1 | |
Modified residuei | 349 | Phosphoserine1 Publication | 1 | |
Modified residuei | 351 | Phosphoserine1 Publication | 1 | |
Modified residuei | 352 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 355 | Phosphoserine1 Publication | 1 | |
Modified residuei | 358 | Phosphoserine1 Publication | 1 | |
Modified residuei | 360 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 371 | PhosphoserineBy similarity | 1 | |
Modified residuei | 423 | Phosphoserine1 Publication | 1 | |
Modified residuei | 484 | Phosphoserine1 Publication | 1 | |
Modified residuei | 485 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 487 | Phosphoserine1 Publication | 1 | |
Modified residuei | 488 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 492 | Phosphoserine1 Publication | 1 | |
Modified residuei | 494 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 496 | Phosphoserine1 Publication | 1 | |
Modified residuei | 520 | Phosphoserine1 Publication | 1 | |
Modified residuei | 530 | Phosphoserine1 Publication | 1 | |
Modified residuei | 544 | Phosphoserine1 Publication | 1 | |
Modified residuei | 548 | Phosphoserine1 Publication | 1 | |
Modified residuei | 605 | Phosphoserine1 Publication | 1 | |
Modified residuei | 606 | Phosphoserine1 Publication | 1 | |
Modified residuei | 651 | Phosphoserine1 Publication | 1 | |
Modified residuei | 687 | Phosphoserine1 Publication | 1 | |
Modified residuei | 718 | Phosphoserine1 Publication | 1 | |
Modified residuei | 724 | Phosphoserine1 Publication | 1 | |
Modified residuei | 728 | Phosphoserine1 Publication | 1 | |
Modified residuei | 810 | Phosphoserine1 Publication | 1 | |
Modified residuei | 822 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 826 | Phosphoserine1 Publication | 1 | |
Modified residuei | 840 | Phosphoserine1 Publication | 1 | |
Modified residuei | 842 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 892 | Phosphoserine1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
PhosphoproteinProteomic databases
EPDi | Q8K4J6 |
MaxQBi | Q8K4J6 |
PaxDbi | Q8K4J6 |
PRIDEi | Q8K4J6 |
ProteomicsDBi | 295952 [Q8K4J6-1] 295953 [Q8K4J6-2] |
PTM databases
iPTMneti | Q8K4J6 |
PhosphoSitePlusi | Q8K4J6 |
Expressioni
Tissue specificityi
Developmental stagei
Gene expression databases
Bgeei | ENSMUSG00000042292, Expressed in granulocyte and 299 other tissues |
ExpressionAtlasi | Q8K4J6, baseline and differential |
Genevisiblei | Q8K4J6, MM |
Interactioni
Subunit structurei
Interacts with SRF, forming the SRF-MRTFA nuclear complex which binds the 5'-CArG-3' consensus motif (CArG box) on DNA via SRF (PubMed:12732141, PubMed:19350017).
Interacts (via RPEL repeats) with globular actin (G-actin), thereby regulating its subcellular location and activity of the complex formed with SRF (PubMed:12732141, PubMed:17588931, PubMed:19350017, PubMed:19008859, PubMed:27304076, PubMed:21673315). Either forms a trivalent (by binding three G-actin monomers) or pentavalent (by binding five G-actin monomers) complex with G-actin (PubMed:21673315).
Forms a nuclear ternary complex with SCAI and SRF, leading to suppress MRTFA-induced SRF transcriptional activity (PubMed:19350017).
Interacts with beta-actin (ACTB); interaction with ACTB prevents interaction with SCAI (PubMed:19350017).
Interacts with MRTFB (By similarity).
By similarity6 PublicationsBinary interactionsi
Q8K4J6
GO - Molecular functioni
- actin binding Source: MGI
- actin monomer binding Source: UniProtKB
- leucine zipper domain binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 230180, 2 interactors |
DIPi | DIP-60884N |
ELMi | Q8K4J6 |
IntActi | Q8K4J6, 7 interactors |
MINTi | Q8K4J6 |
STRINGi | 10090.ENSMUSP00000105207 |
Miscellaneous databases
RNActi | Q8K4J6, protein |
Structurei
Secondary structure
3D structure databases
SMRi | Q8K4J6 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q8K4J6 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 15 – 40 | RPEL 1Add BLAST | 26 | |
Repeati | 59 – 84 | RPEL 2Add BLAST | 26 | |
Repeati | 103 – 128 | RPEL 3Add BLAST | 26 | |
Domaini | 385 – 419 | SAPPROSITE-ProRule annotationAdd BLAST | 35 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 291 | Mediates interaction with SCAI and ACTB1 PublicationAdd BLAST | 291 | |
Regioni | 41 – 58 | Intervening spacer sequence 11 PublicationAdd BLAST | 18 | |
Regioni | 85 – 102 | Intervening spacer sequence 21 PublicationAdd BLAST | 18 | |
Regioni | 145 – 292 | DisorderedSequence analysisAdd BLAST | 148 | |
Regioni | 328 – 371 | DisorderedSequence analysisAdd BLAST | 44 | |
Regioni | 484 – 508 | DisorderedSequence analysisAdd BLAST | 25 | |
Regioni | 638 – 673 | DisorderedSequence analysisAdd BLAST | 36 | |
Regioni | 706 – 779 | DisorderedSequence analysisAdd BLAST | 74 | |
Regioni | 796 – 849 | DisorderedSequence analysisAdd BLAST | 54 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 552 – 600 | Sequence analysisAdd BLAST | 49 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 145 – 198 | Polar residuesSequence analysisAdd BLAST | 54 | |
Compositional biasi | 340 – 371 | Polar residuesSequence analysisAdd BLAST | 32 | |
Compositional biasi | 722 – 749 | Pro residuesSequence analysisAdd BLAST | 28 | |
Compositional biasi | 764 – 779 | Polar residuesSequence analysisAdd BLAST | 16 | |
Compositional biasi | 816 – 843 | Pro residuesSequence analysisAdd BLAST | 28 |
Domaini
Keywords - Domaini
Coiled coil, RepeatPhylogenomic databases
eggNOGi | ENOG502R5FB, Eukaryota |
GeneTreei | ENSGT00950000182979 |
InParanoidi | Q8K4J6 |
OrthoDBi | 190145at2759 |
PhylomeDBi | Q8K4J6 |
TreeFami | TF326024 |
Family and domain databases
DisProti | DP01999 |
Gene3Di | 1.10.720.30, 1 hit |
IDEALi | IID50055 |
InterProi | View protein in InterPro IPR029992, MRTF-A IPR043451, Myocardin-like IPR004018, RPEL_repeat IPR003034, SAP_dom IPR036361, SAP_dom_sf |
PANTHERi | PTHR22793, PTHR22793, 1 hit PTHR22793:SF6, PTHR22793:SF6, 1 hit |
Pfami | View protein in Pfam PF02755, RPEL, 3 hits PF02037, SAP, 1 hit |
SMARTi | View protein in SMART SM00707, RPEL, 3 hits SM00513, SAP, 1 hit |
SUPFAMi | SSF68906, SSF68906, 1 hit |
PROSITEi | View protein in PROSITE PS51073, RPEL, 3 hits PS50800, SAP, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MTLLEPEMLM MAVQSVLQLK LQQRRTREEL VSQGIMPPLK SPAAFHEQRR
60 70 80 90 100
SLERARTEDY LKRKIRSRPE RAELVRMHIL EETSAEPSLQ AKQLKLKRAR
110 120 130 140 150
LADDLNEKIA QRPGPMELVE KNILPVESSL KEAIIVGQVN YPKVADSSSF
160 170 180 190 200
DEDSSDALSP EQPASHESQG SVPSPLESRV SDPLPSATSI SPTQVLSQLP
210 220 230 240 250
MAPDPGETLF LAEQPPLPPA PLLPPSLANG SIVPTAKPAP TLIKQSQPKS
260 270 280 290 300
ASEKSQRSKK AKELKPKVKK LKYHQYIPPD QKQDKGAPAM DSSYAKILQQ
310 320 330 340 350
QQLFLQLQIL NQQQQQQQQQ HYNYQAILPA PPKPSAETPG SSAPTPSRSL
360 370 380 390 400
STSSSPSSGT PGPSGLARQS STALAAKPGA LPANLDDMKV AELKQELKLR
410 420 430 440 450
SLPVSGTKTE LIERLRAYQD QVSPAPGAPK APATTSVLSK AGEVVVAFPA
460 470 480 490 500
ALLSTGSALV TAGLAPAEMV VATVTSNGMV KFGSTGSTPP VSPTPSERSL
510 520 530 540 550
LSTGDENSTP GDAFGEMVTS PLTQLTLQAS PLQIVKEEGA RAASCCLSPG
560 570 580 590 600
ARAELEGLDK DQMLQEKDKQ IEELTRMLQQ KQQLVELLRL QLEQQKRAQQ
610 620 630 640 650
PAPASSPVKR ESGFSSCQLS CQPQGSAHAF GSGLVVPTTN HGDTQAPAPE
660 670 680 690 700
SPPVVVKQEA GPPEPDLAPS SQLLLGSQGT SFLKRVSPPT LVTDSTGTHL
710 720 730 740 750
ILTVTNKSAD GPGLPAGSPQ QPLSQPGSPA PGPPAQMDLE HPPQPPFATP
760 770 780 790 800
TSLLKKEPPG YEETVTQQPK QQENGSSSQH MDDLFDILIQ SGEISADFKE
810 820 830 840 850
PPSLPGKEKS PPAAAAYGPP LTPQPSPLSE LPQAAPPPGS PTLPGRLEDF
860 870 880 890 900
LESSTGLPLL TSGHEGPEPL SLIDDLHSQM LSSSAILDHP PSPMDTSELH
910 920 930 940 950
FAPEPSSGMG LDLAVGHLDS MDWLELSSGG PVLSLAPLST AAPSLFSMDF
960
LDGHDLQLHW DSCL
Computationally mapped potential isoform sequencesi
There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A668KL76 | A0A668KL76_MOUSE | Phosphatase and actin regulator | Mrtfa | 108 | Annotation score: | ||
D3YUG5 | D3YUG5_MOUSE | Myocardin-related transcription fac... | Mrtfa Mkl1 | 705 | Annotation score: | ||
D3YUI2 | D3YUI2_MOUSE | Myocardin-related transcription fac... | Mrtfa Mkl1 | 979 | Annotation score: | ||
A0A5F8MQ33 | A0A5F8MQ33_MOUSE | Myocardin-related transcription fac... | Mrtfa | 1,029 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 53 | E → Q in BAC31809 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 724 | S → D in BAC40873 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 728 | S → F in AAM94258 (PubMed:12019265).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_007652 | 1 – 35 | Missing in isoform 2. 3 PublicationsAdd BLAST | 35 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF385582 mRNA Translation: AAM94258.1 AF532597 mRNA Translation: AAN33041.1 AK044188 mRNA Translation: BAC31809.1 AK089416 mRNA Translation: BAC40873.1 BC050941 mRNA Translation: AAH50941.1 |
CCDSi | CCDS37147.1 [Q8K4J6-1] |
RefSeqi | NP_001076005.1, NM_001082536.1 NP_694629.2, NM_153049.3 [Q8K4J6-1] |
Genome annotation databases
Ensembli | ENSMUST00000109579; ENSMUSP00000105207; ENSMUSG00000042292 [Q8K4J6-1] ENSMUST00000149582; ENSMUSP00000117745; ENSMUSG00000042292 [Q8K4J6-2] |
GeneIDi | 223701 |
KEGGi | mmu:223701 |
UCSCi | uc007wwc.2, mouse [Q8K4J6-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF385582 mRNA Translation: AAM94258.1 AF532597 mRNA Translation: AAN33041.1 AK044188 mRNA Translation: BAC31809.1 AK089416 mRNA Translation: BAC40873.1 BC050941 mRNA Translation: AAH50941.1 |
CCDSi | CCDS37147.1 [Q8K4J6-1] |
RefSeqi | NP_001076005.1, NM_001082536.1 NP_694629.2, NM_153049.3 [Q8K4J6-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2V51 | X-ray | 2.35 | E/F | 16-41 | [»] | |
2V52 | X-ray | 1.45 | M | 54-85 | [»] | |
2YJE | X-ray | 3.10 | M | 16-142 | [»] | |
2YJF | X-ray | 3.50 | M | 16-142 | [»] | |
SMRi | Q8K4J6 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 230180, 2 interactors |
DIPi | DIP-60884N |
ELMi | Q8K4J6 |
IntActi | Q8K4J6, 7 interactors |
MINTi | Q8K4J6 |
STRINGi | 10090.ENSMUSP00000105207 |
PTM databases
iPTMneti | Q8K4J6 |
PhosphoSitePlusi | Q8K4J6 |
Proteomic databases
EPDi | Q8K4J6 |
MaxQBi | Q8K4J6 |
PaxDbi | Q8K4J6 |
PRIDEi | Q8K4J6 |
ProteomicsDBi | 295952 [Q8K4J6-1] 295953 [Q8K4J6-2] |
Protocols and materials databases
Antibodypediai | 26780, 335 antibodies from 33 providers |
DNASUi | 223701 |
Genome annotation databases
Ensembli | ENSMUST00000109579; ENSMUSP00000105207; ENSMUSG00000042292 [Q8K4J6-1] ENSMUST00000149582; ENSMUSP00000117745; ENSMUSG00000042292 [Q8K4J6-2] |
GeneIDi | 223701 |
KEGGi | mmu:223701 |
UCSCi | uc007wwc.2, mouse [Q8K4J6-1] |
Organism-specific databases
CTDi | 57591 |
MGIi | MGI:2384495, Mrtfa |
VEuPathDBi | HostDB:ENSMUSG00000042292 |
Phylogenomic databases
eggNOGi | ENOG502R5FB, Eukaryota |
GeneTreei | ENSGT00950000182979 |
InParanoidi | Q8K4J6 |
OrthoDBi | 190145at2759 |
PhylomeDBi | Q8K4J6 |
TreeFami | TF326024 |
Enzyme and pathway databases
Reactomei | R-MMU-3899300, SUMOylation of transcription cofactors R-MMU-5663220, RHO GTPases Activate Formins |
Miscellaneous databases
BioGRID-ORCSi | 223701, 5 hits in 65 CRISPR screens |
ChiTaRSi | Smarca4, mouse |
EvolutionaryTracei | Q8K4J6 |
PROi | PR:Q8K4J6 |
RNActi | Q8K4J6, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000042292, Expressed in granulocyte and 299 other tissues |
ExpressionAtlasi | Q8K4J6, baseline and differential |
Genevisiblei | Q8K4J6, MM |
Family and domain databases
DisProti | DP01999 |
Gene3Di | 1.10.720.30, 1 hit |
IDEALi | IID50055 |
InterProi | View protein in InterPro IPR029992, MRTF-A IPR043451, Myocardin-like IPR004018, RPEL_repeat IPR003034, SAP_dom IPR036361, SAP_dom_sf |
PANTHERi | PTHR22793, PTHR22793, 1 hit PTHR22793:SF6, PTHR22793:SF6, 1 hit |
Pfami | View protein in Pfam PF02755, RPEL, 3 hits PF02037, SAP, 1 hit |
SMARTi | View protein in SMART SM00707, RPEL, 3 hits SM00513, SAP, 1 hit |
SUPFAMi | SSF68906, SSF68906, 1 hit |
PROSITEi | View protein in PROSITE PS51073, RPEL, 3 hits PS50800, SAP, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | MRTFA_MOUSE | |
Accessioni | Q8K4J6Primary (citable) accession number: Q8K4J6 Secondary accession number(s): Q642U1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 27, 2003 |
Last sequence update: | June 27, 2003 | |
Last modified: | February 23, 2022 | |
This is version 167 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references