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Q969V6

- MKL1_HUMAN

UniProt

Q969V6 - MKL1_HUMAN

Protein

MKL/myocardin-like protein 1

Gene

MKL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei3 – 42Breakpoint for translocation to form RBM15-MKL1

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. actin monomer binding Source: UniProtKB
    3. leucine zipper domain binding Source: BHF-UCL
    4. protein binding Source: UniProtKB
    5. sequence-specific DNA binding transcription factor activity Source: Ensembl
    6. transcription coactivator activity Source: UniProtKB
    7. transcription regulatory region sequence-specific DNA binding Source: Ensembl

    GO - Biological processi

    1. negative regulation of apoptotic signaling pathway Source: Ensembl
    2. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    3. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    4. positive regulation of transcription via serum response element binding Source: UniProtKB
    5. smooth muscle cell differentiation Source: BHF-UCL
    6. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:MKL1
    Synonyms:KIAA1438, MAL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:14334. MKL1.

    Subcellular locationi

    Nucleus 2 Publications. Cytoplasm By similarity
    Note: Binding to globular actin is required to maintain cytoplasmic localization. Nuclear localization is regulated by MICAL2, which mediates depolymerization of nuclear globular actin, promoting retention of MKL1 in the nucleus and subsequent formation of an active complex with SRF (PubMed:24440334).1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA30827.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 931931MKL/myocardin-like protein 1PRO_0000126625Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei6 – 61Phosphoserine2 Publications
    Modified residuei305 – 3051Phosphothreonine1 Publication
    Modified residuei450 – 4501Phosphothreonine3 Publications
    Modified residuei454 – 4541Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ969V6.
    PaxDbiQ969V6.
    PRIDEiQ969V6.

    PTM databases

    PhosphoSiteiQ969V6.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiQ969V6.
    BgeeiQ969V6.
    CleanExiHS_MAL.
    HS_MKL1.
    GenevestigatoriQ969V6.

    Organism-specific databases

    HPAiHPA030782.

    Interactioni

    Subunit structurei

    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.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SRFP118312EBI-493122,EBI-493034

    Protein-protein interaction databases

    BioGridi121642. 13 interactions.
    IntActiQ969V6. 4 interactions.
    MINTiMINT-4713067.
    STRINGi9606.ENSP00000347847.

    Structurei

    Secondary structure

    1
    931
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni345 – 3495
    Helixi352 – 36110
    Helixi370 – 38213
    Beta strandi388 – 3903
    Beta strandi392 – 3943

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KVUNMR-A336-396[»]
    2KW9NMR-A336-396[»]
    ProteinModelPortaliQ969V6.
    SMRiQ969V6. Positions 1-91, 333-396.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ969V6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati24 – 4926RPEL 1Add
    BLAST
    Repeati68 – 9326RPEL 2Add
    BLAST
    Domaini347 – 38135SAPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 256256Mediates interaction with SCAI and ACTBBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili515 – 56349Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi264 – 28623Gln-richAdd
    BLAST
    Compositional biasi564 – 811248Pro-richAdd
    BLAST

    Domaini

    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

    Sequence similaritiesi

    Contains 2 RPEL repeats.PROSITE-ProRule annotation
    Contains 1 SAP domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG82832.
    HOGENOMiHOG000038001.
    HOVERGENiHBG036493.
    InParanoidiQ969V6.
    OMAiAQMDLEH.
    OrthoDBiEOG7FR7G1.
    PhylomeDBiQ969V6.
    TreeFamiTF326024.

    Family and domain databases

    Gene3Di1.10.720.30. 1 hit.
    InterProiIPR004018. RPEL_repeat.
    IPR003034. SAP_dom.
    [Graphical view]
    PfamiPF02755. RPEL. 2 hits.
    PF02037. SAP. 1 hit.
    [Graphical view]
    SMARTiSM00707. RPEL. 2 hits.
    SM00513. SAP. 1 hit.
    [Graphical view]
    PROSITEiPS51073. RPEL. 2 hits.
    PS50800. SAP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q969V6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPLKSPAAF HEQRRSLERA RTEDYLKRKI RSRPERSELV RMHILEETSA    50
    EPSLQAKQLK LKRARLADDL NEKIAQRPGP MELVEKNILP VESSLKEAII 100
    VGQVNYPKVA DSSSFDEDSS DALSPEQPAS HESQGSVPSP LEARVSEPLL 150
    SATSASPTQV VSQLPMGRDS REMLFLAEQP PLPPPPLLPP SLTNGTTIPT 200
    AKSTPTLIKQ SQPKSASEKS QRSKKAKELK PKVKKLKYHQ YIPPDQKQDR 250
    GAPPMDSSYA KILQQQQLFL QLQILNQQQQ QHHNYQAILP APPKSAGEAL 300
    GSSGTPPVRS LSTTNSSSSS GAPGPCGLAR QNSTSLTGKP GALPANLDDM 350
    KVAELKQELK LRSLPVSGTK TELIERLRAY QDQISPVPGA PKAPAATSIL 400
    HKAGEVVVAF PAARLSTGPA LVAAGLAPAE VVVATVASSG VVKFGSTGST 450
    PPVSPTPSER SLLSTGDENS TPGDTFGEMV TSPLTQLTLQ ASPLQILVKE 500
    EGPRAGSCCL SPGGRAELEG RDKDQMLQEK DKQIEALTRM LRQKQQLVER 550
    LKLQLEQEKR AQQPAPAPAP LGTPVKQENS FSSCQLSQQP LGPAHPFNPS 600
    LAAPATNHID PCAVAPGPPS VVVKQEALQP EPEPVPAPQL LLGPQGPSLI 650
    KGVAPPTLIT DSTGTHLVLT VTNKNADSPG LSSGSPQQPS SQPGSPAPAP 700
    SAQMDLEHPL QPLFGTPTSL LKKEPPGYEE AMSQQPKQQE NGSSSQQMDD 750
    LFDILIQSGE ISADFKEPPS LPGKEKPSPK TVCGSPLAAQ PSPSAELPQA 800
    APPPPGSPSL PGRLEDFLES STGLPLLTSG HDGPEPLSLI DDLHSQMLSS 850
    TAILDHPPSP MDTSELHFVP EPSSTMGLDL ADGHLDSMDW LELSSGGPVL 900
    SLAPLSTTAP SLFSTDFLDG HDLQLHWDSC L 931
    Length:931
    Mass (Da):98,919
    Last modified:December 1, 2001 - v1
    Checksum:i6EDE5E2C56D89609
    GO

    Sequence cautioni

    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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti648 – 6481S → G.2 Publications
    Corresponds to variant rs878756 [ dbSNP | Ensembl ].
    VAR_021409

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS14003.1.
    RefSeqiNP_001269589.1. NM_001282660.1.
    NP_001269590.1. NM_001282661.1.
    NP_065882.1. NM_020831.4.
    XP_005261751.1. XM_005261694.1.
    UniGeneiHs.654688.

    Genome annotation databases

    EnsembliENST00000355630; ENSP00000347847; ENSG00000196588.
    ENST00000407029; ENSP00000385835; ENSG00000196588.
    GeneIDi57591.
    KEGGihsa:57591.
    UCSCiuc003ayv.1. human.

    Polymorphism databases

    DMDMi32363202.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS14003.1.
    RefSeqi NP_001269589.1. NM_001282660.1.
    NP_001269590.1. NM_001282661.1.
    NP_065882.1. NM_020831.4.
    XP_005261751.1. XM_005261694.1.
    UniGenei Hs.654688.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KVU NMR - A 336-396 [» ]
    2KW9 NMR - A 336-396 [» ]
    ProteinModelPortali Q969V6.
    SMRi Q969V6. Positions 1-91, 333-396.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121642. 13 interactions.
    IntActi Q969V6. 4 interactions.
    MINTi MINT-4713067.
    STRINGi 9606.ENSP00000347847.

    PTM databases

    PhosphoSitei Q969V6.

    Polymorphism databases

    DMDMi 32363202.

    Proteomic databases

    MaxQBi Q969V6.
    PaxDbi Q969V6.
    PRIDEi Q969V6.

    Protocols and materials databases

    DNASUi 57591.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355630 ; ENSP00000347847 ; ENSG00000196588 .
    ENST00000407029 ; ENSP00000385835 ; ENSG00000196588 .
    GeneIDi 57591.
    KEGGi hsa:57591.
    UCSCi uc003ayv.1. human.

    Organism-specific databases

    CTDi 57591.
    GeneCardsi GC22M040807.
    HGNCi HGNC:14334. MKL1.
    HPAi HPA030782.
    MIMi 606078. gene.
    neXtProti NX_Q969V6.
    PharmGKBi PA30827.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG82832.
    HOGENOMi HOG000038001.
    HOVERGENi HBG036493.
    InParanoidi Q969V6.
    OMAi AQMDLEH.
    OrthoDBi EOG7FR7G1.
    PhylomeDBi Q969V6.
    TreeFami TF326024.

    Miscellaneous databases

    ChiTaRSi MKL1. human.
    EvolutionaryTracei Q969V6.
    GeneWikii MKL1.
    GenomeRNAii 57591.
    NextBioi 64178.
    PROi Q969V6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q969V6.
    Bgeei Q969V6.
    CleanExi HS_MAL.
    HS_MKL1.
    Genevestigatori Q969V6.

    Family and domain databases

    Gene3Di 1.10.720.30. 1 hit.
    InterProi IPR004018. RPEL_repeat.
    IPR003034. SAP_dom.
    [Graphical view ]
    Pfami PF02755. RPEL. 2 hits.
    PF02037. SAP. 1 hit.
    [Graphical view ]
    SMARTi SM00707. RPEL. 2 hits.
    SM00513. SAP. 1 hit.
    [Graphical view ]
    PROSITEi PS51073. RPEL. 2 hits.
    PS50800. SAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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. 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. 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. "Redox modification of nuclear actin by MICAL-2 regulates SRF signaling."
      Lundquist M.R., Storaska A.J., Liu T.C., Larsen S.D., Evans T., Neubig R.R., Jaffrey S.R.
      Cell 156:563-576(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    16. "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.

    Entry informationi

    Entry nameiMKL1_HUMAN
    AccessioniPrimary (citable) accession number: Q969V6
    Secondary accession number(s): Q8TCL1
    , Q96SC5, Q96SC6, Q9P2B0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2003
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 129 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3