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Q8VHJ5

- MARK1_MOUSE

UniProt

Q8VHJ5 - MARK1_MOUSE

Protein

Serine/threonine-protein kinase MARK1

Gene

Mark1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase involved in cell polarity and microtubule dynamics regulation. Phosphorylates DCX, MAP2, MAP4 and MAPT/TAU. Involved in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3) By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.By similarity
    ATP + [tau protein] = ADP + [tau protein] phosphate.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Inhibited by phosphorylation at Ser-219. Activated by phosphorylation on Thr-215 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei89 – 891ATPBy similarityPROSITE-ProRule annotation
    Active sitei182 – 1821Proton acceptorBy similarityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi66 – 749ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. phosphatidic acid binding Source: UniProtKB
    4. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
    5. phosphatidylserine binding Source: UniProtKB
    6. protein serine/threonine kinase activity Source: UniProtKB
    7. tau-protein kinase activity Source: UniProtKB

    GO - Biological processi

    1. intracellular signal transduction Source: UniProtKB
    2. microtubule cytoskeleton organization Source: Ensembl
    3. neuron migration Source: UniProtKB
    4. protein phosphorylation Source: UniProtKB
    5. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Wnt signaling pathway

    Keywords - Ligandi

    ATP-binding, Lipid-binding, Magnesium, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase MARK1 (EC:2.7.11.1, EC:2.7.11.26)
    Alternative name(s):
    ELKL motif serine/threonine-protein kinase 3
    MAP/microtubule affinity-regulating kinase 1
    PAR1 homolog c
    Short name:
    Par-1c
    Short name:
    mPar-1c
    Gene namesi
    Name:Mark1Imported
    Synonyms:Emk3Imported, Kiaa1477
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:2664902. Mark1.

    Subcellular locationi

    Cell membrane By similarity; Peripheral membrane protein By similarity. Cytoplasmcytoskeleton By similarity
    Note: Appears to localize to an intracellular network.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. cytoskeleton Source: UniProtKB-SubCell
    3. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 795795Serine/threonine-protein kinase MARK1PRO_0000086299Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51PhosphothreonineBy similarity
    Modified residuei208 – 2081PhosphothreonineBy similarity
    Modified residuei215 – 2151Phosphothreonine; by LKB1 and TAOK1By similarity
    Modified residuei219 – 2191Phosphoserine; by GSK3-betaBy similarity
    Modified residuei403 – 4031Phosphoserine1 Publication
    Modified residuei588 – 5881PhosphoserineBy similarity
    Modified residuei613 – 6131Phosphothreonine; by PKC/PRKCZBy similarity
    Modified residuei666 – 6661Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated at Thr-215 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Phosphorylation at Thr-215 by TAOK1 activates the kinase activity, leading to phosphorylation and detachment of MAPT/TAU from microtubules. Phosphorylation at Ser-219 by GSK3-beta (GSK3B) inhibits the kinase activity. Phosphorylation at Thr-613 by PRKCZ/aPKC in polarized epithelial cells inhibits the kinase activity By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ8VHJ5.
    PRIDEiQ8VHJ5.

    PTM databases

    PhosphoSiteiQ8VHJ5.

    Expressioni

    Gene expression databases

    BgeeiQ8VHJ5.
    CleanExiMM_MARK1.
    GenevestigatoriQ8VHJ5.

    Interactioni

    Protein-protein interaction databases

    BioGridi230554. 2 interactions.
    IntActiQ8VHJ5. 2 interactions.
    MINTiMINT-4120175.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VHJ5.
    SMRiQ8VHJ5. Positions 1-371, 696-795.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini60 – 311252Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini329 – 37042UBAPROSITE-ProRule annotationAdd
    BLAST
    Domaini746 – 79550KA1PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The UBA domain does not seem to bind ubiquitin and ubiquitin-like and might play a role in regulating the enzyme conformation and localization. Activation of the kinase activity following phosphorylation at Thr-208 is accompanied by a conformational change that alters the orientation of the UBA domain with respect to the catalytic domain By similarity.By similarity
    The KA1 domain mediates binding to phospholipids and targeting to membranes. Binds phosphatidic acid (PA), phosphatidylserine (PtdSer) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) By similarity.By similarity

    Sequence similaritiesi

    Contains 1 KA1 (kinase-associated) domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 UBA domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00730000110535.
    HOVERGENiHBG052453.
    InParanoidiQ8VHJ5.
    KOiK08798.
    OMAiEHPHIGN.
    OrthoDBiEOG79CXXX.
    TreeFamiTF315213.

    Family and domain databases

    Gene3Di3.30.310.80. 1 hit.
    InterProiIPR028375. KA1/Ssp2_C.
    IPR001772. KA1_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    [Graphical view]
    PfamiPF02149. KA1. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    SM00165. UBA. 1 hit.
    [Graphical view]
    SUPFAMiSSF103243. SSF103243. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50032. KA1. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50030. UBA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8VHJ5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSARTPLPTV NERDTENHTS VDGYTETHIP PAKSSSRQNL PRCRNSITSA    50
    TDEQPHIGNY RLQKTIGKGN FAKVKLARHV LTGREVAVKI IDKTQLNPTS 100
    LQKLFREVRI MKILNHPNIV KLFEVIETEK TLYLVMEYAS GGEVFDYLVA 150
    HGRMKEKEAR AKFRQIVSAV QYCHQKCIVH RDLKAENLLL DADMNIKIAD 200
    FGFSNEFTVG NKLDTFCGSP PYAAPELFQG KKYDGPEVDV WSLGVILYTL 250
    VSGSLPFDGQ NLKELRERVL RGKYRIPFYM STDCENLLKK LLVLNPIKRG 300
    SLEQIMKDRW MNVGHEEEEL KPYSEPELDL SDAKRIDIMV TMGFARDEIN 350
    DALVSQKYDE VMATYILLGR KPPEFEGGES LSSGSLCQRS RPSSDLNNST 400
    LQSPAHLKVQ RSISANQKQR RFSDHAGPSI PPAVSYTKRP QANSVESEQK 450
    EEWGKDTARR LGSTTVGSKS EVTASPLVGP DRKKSTASPS NNVYSGGSMA 500
    RRNTYVCERS TDRYAALQNG RDSSLTEMSA SSMSSAGSTV ASAGPSARPR 550
    HQKSMSTSGH PIKVTLPTIK DGSEAYRPGA AQRVPAASPS AHSISASTPD 600
    RTRFPRGSSS RSTFHGEQLR ERRSAAYNGP PASPSHETGA FAHARRGTST 650
    GIISKITSKF VRRDPSEGEA SGRADTARGS SGDPKERDKD EGKEAKPRSL 700
    RFTWSMKTTS SMDPNDMLRE IRKVLDANTC DYEQKERFLL FCVHGDARQD 750
    SLVQWEMEVC KLPRLSLNGV RFKRISGTSI AFKNIASKIA NELKL 795
    Length:795
    Mass (Da):88,335
    Last modified:July 27, 2011 - v2
    Checksum:iF43F2B541C346697
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321A → T in AAL50826. 1 PublicationCurated
    Sequence conflicti40 – 401L → I in AAL50826. 1 PublicationCurated
    Sequence conflicti110 – 1101I → T in BAD32459. (PubMed:15368895)Curated
    Sequence conflicti276 – 2761I → V in AAL50826. 1 PublicationCurated
    Sequence conflicti318 – 3181E → D in BAD32459. (PubMed:15368895)Curated
    Sequence conflicti331 – 3311S → N in AAL50826. 1 PublicationCurated
    Sequence conflicti385 – 3851S → N in AAL50826. 1 PublicationCurated
    Sequence conflicti454 – 4541G → D in AAL50826. 1 PublicationCurated
    Sequence conflicti579 – 5791G → GS in BAD32459. (PubMed:15368895)Curated
    Sequence conflicti630 – 6301P → R in AAL50826. 1 PublicationCurated
    Sequence conflicti641 – 6411F → L in AAL50826. 1 PublicationCurated
    Sequence conflicti674 – 6741A → T in AAL50826. 1 PublicationCurated
    Sequence conflicti683 – 6831D → E in AAL50826. 1 PublicationCurated
    Sequence conflicti690 – 6901D → E in AAL50826. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF453686 mRNA. Translation: AAL50826.1.
    AC117826 Genomic DNA. No translation available.
    AC131992 Genomic DNA. No translation available.
    AK173181 mRNA. Translation: BAD32459.1.
    CCDSiCCDS35817.1.
    RefSeqiNP_663490.2. NM_145515.2.
    UniGeneiMm.7445.

    Genome annotation databases

    EnsembliENSMUST00000027929; ENSMUSP00000027929; ENSMUSG00000026620.
    GeneIDi226778.
    KEGGimmu:226778.
    UCSCiuc007dyt.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF453686 mRNA. Translation: AAL50826.1 .
    AC117826 Genomic DNA. No translation available.
    AC131992 Genomic DNA. No translation available.
    AK173181 mRNA. Translation: BAD32459.1 .
    CCDSi CCDS35817.1.
    RefSeqi NP_663490.2. NM_145515.2.
    UniGenei Mm.7445.

    3D structure databases

    ProteinModelPortali Q8VHJ5.
    SMRi Q8VHJ5. Positions 1-371, 696-795.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 230554. 2 interactions.
    IntActi Q8VHJ5. 2 interactions.
    MINTi MINT-4120175.

    PTM databases

    PhosphoSitei Q8VHJ5.

    Proteomic databases

    PaxDbi Q8VHJ5.
    PRIDEi Q8VHJ5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027929 ; ENSMUSP00000027929 ; ENSMUSG00000026620 .
    GeneIDi 226778.
    KEGGi mmu:226778.
    UCSCi uc007dyt.2. mouse.

    Organism-specific databases

    CTDi 4139.
    MGIi MGI:2664902. Mark1.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00730000110535.
    HOVERGENi HBG052453.
    InParanoidi Q8VHJ5.
    KOi K08798.
    OMAi EHPHIGN.
    OrthoDBi EOG79CXXX.
    TreeFami TF315213.

    Miscellaneous databases

    NextBioi 378347.
    PROi Q8VHJ5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8VHJ5.
    CleanExi MM_MARK1.
    Genevestigatori Q8VHJ5.

    Family and domain databases

    Gene3Di 3.30.310.80. 1 hit.
    InterProi IPR028375. KA1/Ssp2_C.
    IPR001772. KA1_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    [Graphical view ]
    Pfami PF02149. KA1. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    SM00165. UBA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF103243. SSF103243. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50032. KA1. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50030. UBA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mus musculus Emk3/Mark1 mRNA."
      Darmon Y.M., Le Morvan V.
      Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
      DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-795.
      Tissue: Fetal brain.
    4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.

    Entry informationi

    Entry nameiMARK1_MOUSE
    AccessioniPrimary (citable) accession number: Q8VHJ5
    Secondary accession number(s): E9QL17, Q69ZI7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 111 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3