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Q969V6 (MKL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
MKL/myocardin-like protein 1
Alternative name(s):
Megakaryoblastic leukemia 1 protein
Megakaryocytic acute leukemia protein
Myocardin-related transcription factor A
Short name=MRTF-A
Gene names
Name:MKL1
Synonyms:KIAA1438, MAL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length931 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional coactivator of serum response factor (SRF) with the potential to modulate SRF target genes. Suppresses TNF-induced cell death by inhibiting activation of caspases; its transcriptional activity is indispensable for the antiapoptotic function. It may up-regulate antiapoptotic molecules, which in turn inhibit caspase activation By similarity.

Subunit structure

Forms with SCAI and SRF a nuclear ternary complex which binds the CArG consensus motif (CArG box) on DNA via SRF. Interacts with ACTB; interaction with ACTB prevents interaction with SCAI. Interacts with MKL2 By similarity. Ref.11

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Binding to globular actin is required to maintain cytoplasmic localization By similarity. Ref.11

Tissue specificity

Ubiquitously expressed, has been detected in lung, placenta, small intestine, liver, kidney, spleen, thymus, colon, muscle, heart and brain.

Domain

The N-terminal region is required for nuclear localization and the C-terminal region mediates transcriptional activity By similarity.

The RPEL repeats mediate binding to globular actin By similarity.

Involvement in disease

A chromosomal aberration involving MKL1 may be a cause of acute megakaryoblastic leukemia. Translocation t(1;22)(p13;q13) with RBM15. Although both reciprocal fusion transcripts are detected in acute megakaryoblastic leukemia (AMKL, FAB-M7), the RBM15-MKL1 chimeric protein has all the putative functional domains encoded by each gene and is the candidate oncogene.

Sequence similarities

Contains 2 RPEL repeats.

Contains 1 SAP domain.

Sequence caution

The sequence AAK56920.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA92676.2 differs from that shown. Reason: Erroneous initiation.

The sequence CAC38828.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAC38829.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityChromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   DomainCoiled coil
Repeat
   LigandActin-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 14970199. Source: BHF-UCL

smooth muscle cell differentiation

Inferred from mutant phenotype PubMed 14970199. Source: BHF-UCL

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 14970199. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 14970199. Source: BHF-UCL

   Molecular_functionactin monomer binding

Inferred from sequence or structural similarity. Source: UniProtKB

leucine zipper domain binding

Inferred from physical interaction PubMed 14970199. Source: BHF-UCL

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription regulatory region sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SRFP118312EBI-493122,EBI-493034

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 931931MKL/myocardin-like protein 1
PRO_0000126625

Regions

Repeat24 – 4926RPEL 1
Repeat68 – 9326RPEL 2
Domain347 – 38135SAP
Region1 – 256256Mediates interaction with SCAI and ACTB By similarity
Coiled coil515 – 56349 Potential
Compositional bias264 – 28623Gln-rich
Compositional bias564 – 811248Pro-rich

Sites

Site3 – 42Breakpoint for translocation to form RBM15-MKL1

Amino acid modifications

Modified residue61Phosphoserine Ref.8 Ref.14
Modified residue3051Phosphothreonine Ref.9
Modified residue4501Phosphothreonine Ref.9 Ref.13 Ref.14
Modified residue4541Phosphoserine Ref.13 Ref.14

Natural variations

Natural variant6481S → G. Ref.5 Ref.7
Corresponds to variant rs878756 [ dbSNP | Ensembl ].
VAR_021409

Secondary structure

........... 931
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q969V6 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 6EDE5E2C56D89609

FASTA93198,919
        10         20         30         40         50         60 
MPPLKSPAAF HEQRRSLERA RTEDYLKRKI RSRPERSELV RMHILEETSA EPSLQAKQLK 

        70         80         90        100        110        120 
LKRARLADDL NEKIAQRPGP MELVEKNILP VESSLKEAII VGQVNYPKVA DSSSFDEDSS 

       130        140        150        160        170        180 
DALSPEQPAS HESQGSVPSP LEARVSEPLL SATSASPTQV VSQLPMGRDS REMLFLAEQP 

       190        200        210        220        230        240 
PLPPPPLLPP SLTNGTTIPT AKSTPTLIKQ SQPKSASEKS QRSKKAKELK PKVKKLKYHQ 

       250        260        270        280        290        300 
YIPPDQKQDR GAPPMDSSYA KILQQQQLFL QLQILNQQQQ QHHNYQAILP APPKSAGEAL 

       310        320        330        340        350        360 
GSSGTPPVRS LSTTNSSSSS GAPGPCGLAR QNSTSLTGKP GALPANLDDM KVAELKQELK 

       370        380        390        400        410        420 
LRSLPVSGTK TELIERLRAY QDQISPVPGA PKAPAATSIL HKAGEVVVAF PAARLSTGPA 

       430        440        450        460        470        480 
LVAAGLAPAE VVVATVASSG VVKFGSTGST PPVSPTPSER SLLSTGDENS TPGDTFGEMV 

       490        500        510        520        530        540 
TSPLTQLTLQ ASPLQILVKE EGPRAGSCCL SPGGRAELEG RDKDQMLQEK DKQIEALTRM 

       550        560        570        580        590        600 
LRQKQQLVER LKLQLEQEKR AQQPAPAPAP LGTPVKQENS FSSCQLSQQP LGPAHPFNPS 

       610        620        630        640        650        660 
LAAPATNHID PCAVAPGPPS VVVKQEALQP EPEPVPAPQL LLGPQGPSLI KGVAPPTLIT 

       670        680        690        700        710        720 
DSTGTHLVLT VTNKNADSPG LSSGSPQQPS SQPGSPAPAP SAQMDLEHPL QPLFGTPTSL 

       730        740        750        760        770        780 
LKKEPPGYEE AMSQQPKQQE NGSSSQQMDD LFDILIQSGE ISADFKEPPS LPGKEKPSPK 

       790        800        810        820        830        840 
TVCGSPLAAQ PSPSAELPQA APPPPGSPSL PGRLEDFLES STGLPLLTSG HDGPEPLSLI 

       850        860        870        880        890        900 
DDLHSQMLSS TAILDHPPSP MDTSELHFVP EPSSTMGLDL ADGHLDSMDW LELSSGGPVL 

       910        920        930 
SLAPLSTTAP SLFSTDFLDG HDLQLHWDSC L 

« Hide

References

« Hide 'large scale' references
[1]"Fusion of two novel genes, RBM15 and MKL1, in the t(1;22)(p13;q13) of acute megakaryoblastic leukemia."
Ma Z., Morris S.W., Valentine V., Li M., Herbrick J.-A., Cui X., Bouman D., Li Y., Mehta P.K., Nizetic D., Kaneko Y., Chan G.C.F., Chan L.C., Squire J., Scherer S.W., Hitzler J.K.
Nat. Genet. 28:220-221(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION WITH RBM15.
[2]"Involvement of a human gene related to the Drosophila spen gene in the recurrent t(1;22) translocation of acute megakaryocytic leukemia."
Mercher T., Coniat M.B.-L., Monni R., Mauchauffe M., Khac F.N., Gressin L., Mugneret F., Leblanc T., Dastugue N., Berger R., Bernard O.A.
Proc. Natl. Acad. Sci. U.S.A. 98:5776-5779(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION WITH RBM15.
Tissue: Blood.
[3]"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[5]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-648.
[6]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 195-931, VARIANT GLY-648.
Tissue: Testis.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-305 AND THR-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"SCAI acts as a suppressor of cancer cell invasion through the transcriptional control of beta1-integrin."
Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J., Nollau P., Grosse R.
Nat. Cell Biol. 11:557-568(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCAI AND SRF, SUBCELLULAR LOCATION.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450 AND SER-454, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; THR-450 AND SER-454, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Northeast structural genomics consortium target HR4547E."
Northeast structural genomics consortium (NESG)
Submitted (JUN-2010) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 336-396.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ297257 mRNA. Translation: CAC38826.1.
AF364035 mRNA. Translation: AAK56920.1. Different initiation.
CR456522 mRNA. Translation: CAG30408.1.
AJ297258 mRNA. Translation: CAC38827.1.
AF368061 mRNA. Translation: AAK54721.1.
AJ303089 mRNA. Translation: CAC38828.1. Different initiation.
AJ303090 mRNA. Translation: CAC38829.1. Different initiation.
AB037859 mRNA. Translation: BAA92676.2. Different initiation.
AL022238 Genomic DNA. Translation: CAI18985.1.
AL713710 mRNA. Translation: CAD28507.2.
RefSeqNP_001269589.1. NM_001282660.1.
NP_001269590.1. NM_001282661.1.
NP_065882.1. NM_020831.4.
XP_005261751.1. XM_005261694.1.
UniGeneHs.654688.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KVUNMR-A333-396[»]
2KW9NMR-A336-396[»]
ProteinModelPortalQ969V6.
SMRQ969V6. Positions 1-91, 333-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121642. 13 interactions.
IntActQ969V6. 4 interactions.
MINTMINT-4713067.
STRING9606.ENSP00000347847.

PTM databases

PhosphoSiteQ969V6.

Polymorphism databases

DMDM32363202.

Proteomic databases

PaxDbQ969V6.
PRIDEQ969V6.

Protocols and materials databases

DNASU57591.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355630; ENSP00000347847; ENSG00000196588.
ENST00000407029; ENSP00000385835; ENSG00000196588.
GeneID57591.
KEGGhsa:57591.
UCSCuc003ayv.1. human.

Organism-specific databases

CTD57591.
GeneCardsGC22M040807.
HGNCHGNC:14334. MKL1.
HPAHPA030782.
MIM606078. gene.
neXtProtNX_Q969V6.
PharmGKBPA30827.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG82832.
HOGENOMHOG000038001.
HOVERGENHBG036493.
InParanoidQ969V6.
OMAAQMDLEH.
OrthoDBEOG7FR7G1.
PhylomeDBQ969V6.
TreeFamTF326024.

Gene expression databases

ArrayExpressQ969V6.
BgeeQ969V6.
CleanExHS_MAL.
HS_MKL1.
GenevestigatorQ969V6.

Family and domain databases

Gene3D1.10.720.30. 1 hit.
InterProIPR004018. RPEL_repeat.
IPR003034. SAP_dom.
[Graphical view]
PfamPF02755. RPEL. 2 hits.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTSM00707. RPEL. 2 hits.
SM00513. SAP. 1 hit.
[Graphical view]
PROSITEPS51073. RPEL. 2 hits.
PS50800. SAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMKL1. human.
EvolutionaryTraceQ969V6.
GeneWikiMKL1.
GenomeRNAi57591.
NextBio64178.
PROQ969V6.
SOURCESearch...

Entry information

Entry nameMKL1_HUMAN
AccessionPrimary (citable) accession number: Q969V6
Secondary accession number(s): Q8TCL1 expand/collapse secondary AC list , Q96SC5, Q96SC6, Q9P2B0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM