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Q9P0L2

- MARK1_HUMAN

UniProt

Q9P0L2 - MARK1_HUMAN

Protein

Serine/threonine-protein kinase MARK1

Gene

MARK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      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).2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication
    ATP + [tau protein] = ADP + [tau protein] phosphate.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Inhibited by phosphorylation at Ser-219 By similarity. Activated by phosphorylation on Thr-215.By similarity2 Publications

    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. cytoskeleton organization Source: UniProtKB
    2. intracellular signal transduction Source: UniProtKB
    3. microtubule cytoskeleton organization Source: Ensembl
    4. neuron migration Source: UniProtKB
    5. protein phosphorylation Source: UniProtKB
    6. 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

    Enzyme and pathway databases

    SignaLinkiQ9P0L2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase MARK1 (EC:2.7.11.1, EC:2.7.11.26)
    Alternative name(s):
    MAP/microtubule affinity-regulating kinase 1
    PAR1 homolog c
    Short name:
    Par-1c
    Short name:
    Par1c
    Gene namesi
    Name:MARK1Imported
    Synonyms:KIAA1477Imported, MARKImported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6896. MARK1.

    Subcellular locationi

    Cell membrane 1 Publication; Peripheral membrane protein 1 Publication. Cytoplasmcytoskeleton By similarity
    Note: Appears to localize to an intracellular network.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoskeleton Source: UniProtKB
    3. microtubule cytoskeleton Source: ProtInc
    4. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Genetic variations in MARK1 may be associated with susceptibility to autism. MARK1 is overexpressed in the prefrontal cortex of patients with autism and causes changes in the function of cortical dendrites.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi215 – 2151T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. 1 Publication
    Mutagenesisi215 – 2151T → E: Constitutively active. 1 Publication
    Mutagenesisi698 – 6981R → S: Impairs phospholipid-binding, targeting to membrane and vesicle-binding; when associated with S-701. 1 Publication
    Mutagenesisi701 – 7011R → S: Impairs phospholipid-binding, targeting to membrane and vesicle-binding; when associated with S-698. 1 Publication
    Mutagenesisi771 – 7733RFK → AFA: Impairs phospholipid-binding.

    Organism-specific databases

    PharmGKBiPA30639.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 795795Serine/threonine-protein kinase MARK1PRO_0000086298Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51Phosphothreonine1 Publication
    Modified residuei208 – 2081Phosphothreonine1 Publication
    Modified residuei215 – 2151Phosphothreonine; by LKB1 and TAOK11 Publication
    Modified residuei219 – 2191Phosphoserine; by GSK3-beta
    Modified residuei403 – 4031Phosphoserine1 Publication
    Modified residuei588 – 5881Phosphoserine1 Publication
    Modified residuei613 – 6131Phosphothreonine; by PKC/PRKCZBy similarity
    Modified residuei666 – 6661PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylation at Thr-613 by PRKCZ/aPKC in polarized epithelial cells inhibits the kinase activity By similarity. 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.By similarity4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9P0L2.
    PaxDbiQ9P0L2.
    PRIDEiQ9P0L2.

    PTM databases

    PhosphoSiteiQ9P0L2.

    Expressioni

    Tissue specificityi

    Highly expressed in heart, skeletal muscle, brain, fetal brain and fetal kidney.1 Publication

    Gene expression databases

    ArrayExpressiQ9P0L2.
    BgeeiQ9P0L2.
    CleanExiHS_MARK1.
    GenevestigatoriQ9P0L2.

    Organism-specific databases

    HPAiHPA007421.
    HPA008061.

    Interactioni

    Protein-protein interaction databases

    BioGridi110309. 13 interactions.
    DIPiDIP-39777N.
    IntActiQ9P0L2. 8 interactions.
    MINTiMINT-3975018.
    STRINGi9606.ENSP00000355884.

    Structurei

    Secondary structure

    1
    795
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi60 – 689
    Beta strandi70 – 7910
    Turni80 – 823
    Beta strandi85 – 928
    Helixi98 – 11316
    Beta strandi122 – 1276
    Beta strandi129 – 1368
    Helixi144 – 1518
    Helixi156 – 17621
    Helixi185 – 1873
    Beta strandi188 – 1903
    Beta strandi196 – 1983
    Beta strandi221 – 2233
    Helixi225 – 2295
    Helixi236 – 25217
    Helixi262 – 27110
    Helixi282 – 29110
    Helixi296 – 2983
    Helixi302 – 3065
    Helixi309 – 3124
    Beta strandi316 – 3183
    Helixi333 – 34210
    Helixi346 – 3549
    Helixi360 – 3678
    Helixi714 – 72714
    Beta strandi731 – 7366
    Beta strandi739 – 7457
    Turni747 – 7504
    Beta strandi753 – 76210
    Helixi763 – 7653
    Beta strandi767 – 77711
    Helixi779 – 79214

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HAKX-ray2.60A/B/C/D/E/F/G/H45-371[»]
    3OSEX-ray1.70A683-795[»]
    ProteinModelPortaliQ9P0L2.
    SMRiQ9P0L2. Positions 29-371, 696-795.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9P0L2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini60 – 311252Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini325 – 37046UBAPROSITE-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).1 Publication

    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.
    HOVERGENiHBG052453.
    InParanoidiQ9P0L2.
    KOiK08798.
    OMAiEHPHIGN.
    OrthoDBiEOG79CXXX.
    PhylomeDBiQ9P0L2.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9P0L2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSARTPLPTV NERDTENHTS VDGYTEPHIQ PTKSSSRQNI PRCRNSITSA    50
    TDEQPHIGNY RLQKTIGKGN FAKVKLARHV LTGREVAVKI IDKTQLNPTS 100
    LQKLFREVRI MKILNHPNIV KLFEVIETEK TLYLVMEYAS GGEVFDYLVA 150
    HGRMKEKEAR AKFRQIVSAV QYCHQKYIVH RDLKAENLLL DGDMNIKIAD 200
    FGFSNEFTVG NKLDTFCGSP PYAAPELFQG KKYDGPEVDV WSLGVILYTL 250
    VSGSLPFDGQ NLKELRERVL RGKYRIPFYM STDCENLLKK LLVLNPIKRG 300
    SLEQIMKDRW MNVGHEEEEL KPYTEPDPDF NDTKRIDIMV TMGFARDEIN 350
    DALINQKYDE VMATYILLGR KPPEFEGGES LSSGNLCQRS RPSSDLNNST 400
    LQSPAHLKVQ RSISANQKQR RFSDHAGPSI PPAVSYTKRP QANSVESEQK 450
    EEWDKDVARK LGSTTVGSKS EMTASPLVGP ERKKSSTIPS NNVYSGGSMA 500
    RRNTYVCERT TDRYVALQNG KDSSLTEMSV SSISSAGSSV ASAVPSARPR 550
    HQKSMSTSGH PIKVTLPTIK DGSEAYRPGT TQRVPAASPS AHSISTATPD 600
    RTRFPRGSSS RSTFHGEQLR ERRSVAYNGP PASPSHETGA FAHARRGTST 650
    GIISKITSKF VRRDPSEGEA SGRTDTSRST SGEPKERDKE EGKDSKPRSL 700
    RFTWSMKTTS SMDPNDMMRE IRKVLDANNC DYEQKERFLL FCVHGDARQD 750
    SLVQWEMEVC KLPRLSLNGV RFKRISGTSI AFKNIASKIA NELKL 795
    Length:795
    Mass (Da):89,003
    Last modified:January 23, 2007 - v2
    Checksum:i71BF6EB76912631B
    GO
    Isoform 2Curated (identifier: Q9P0L2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-135: Missing.
         663-677: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:645
    Mass (Da):72,073
    Checksum:i7AE395507519DCF6
    GO
    Isoform 3Curated (identifier: Q9P0L2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         120-141: Missing.
         663-677: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:758
    Mass (Da):84,911
    Checksum:iD6F1BCD8E884661D
    GO

    Sequence cautioni

    The sequence BAB55152.1 differs from that shown. Reason: Frameshift at position 763.
    The sequence BAA96001.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161E → V in AAF72103. 1 PublicationCurated
    Sequence conflicti20 – 201S → T in AAF72103. 1 PublicationCurated
    Sequence conflicti522 – 5221D → N in BAB55152. (PubMed:14702039)Curated
    Sequence conflicti544 – 5441V → A in BAB55152. (PubMed:14702039)Curated
    Sequence conflicti763 – 7631P → A in BAB55152. (PubMed:14702039)Curated
    Sequence conflicti794 – 7941K → M in BAA96001. (PubMed:10819331)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti233 – 2331Y → C in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040760
    Natural varianti355 – 3551N → T in an ovarian serous carcinoma sample; somatic mutation. 1 Publication
    VAR_040761
    Natural varianti530 – 5301V → M.1 Publication
    Corresponds to variant rs56212551 [ dbSNP | Ensembl ].
    VAR_040762
    Natural varianti578 – 5781P → L.1 Publication
    Corresponds to variant rs55691439 [ dbSNP | Ensembl ].
    VAR_040763
    Natural varianti645 – 6451R → G.
    Corresponds to variant rs12123778 [ dbSNP | Ensembl ].
    VAR_030018
    Natural varianti691 – 6911E → G.1 Publication
    Corresponds to variant rs55688276 [ dbSNP | Ensembl ].
    VAR_040764

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 135135Missing in isoform 2. 1 PublicationVSP_051702Add
    BLAST
    Alternative sequencei120 – 14122Missing in isoform 3. 1 PublicationVSP_051703Add
    BLAST
    Alternative sequencei663 – 67715Missing in isoform 2 and isoform 3. 2 PublicationsVSP_051704Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF154845 mRNA. Translation: AAF72103.1.
    AB040910 mRNA. Translation: BAA96001.1. Different initiation.
    AK027493 mRNA. Translation: BAB55152.1. Frameshift.
    AL592406, AC096640 Genomic DNA. Translation: CAH72462.1.
    AL592406, AC096640 Genomic DNA. Translation: CAH72463.1.
    CH471100 Genomic DNA. Translation: EAW93299.1.
    CH471100 Genomic DNA. Translation: EAW93300.1.
    CH471100 Genomic DNA. Translation: EAW93302.1.
    BC113869 mRNA. Translation: AAI13870.1.
    BC114478 mRNA. Translation: AAI14479.1.
    CCDSiCCDS31029.2. [Q9P0L2-1]
    CCDS65789.1. [Q9P0L2-3]
    RefSeqiNP_001273057.1. NM_001286128.1. [Q9P0L2-3]
    NP_061120.3. NM_018650.4. [Q9P0L2-1]
    UniGeneiHs.497806.

    Genome annotation databases

    EnsembliENST00000366917; ENSP00000355884; ENSG00000116141. [Q9P0L2-1]
    ENST00000366918; ENSP00000355885; ENSG00000116141. [Q9P0L2-3]
    ENST00000402574; ENSP00000386017; ENSG00000116141. [Q9P0L2-2]
    GeneIDi4139.
    KEGGihsa:4139.
    UCSCiuc001hmm.4. human. [Q9P0L2-3]
    uc001hmn.4. human. [Q9P0L2-1]

    Polymorphism databases

    DMDMi124056494.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF154845 mRNA. Translation: AAF72103.1 .
    AB040910 mRNA. Translation: BAA96001.1 . Different initiation.
    AK027493 mRNA. Translation: BAB55152.1 . Frameshift.
    AL592406 , AC096640 Genomic DNA. Translation: CAH72462.1 .
    AL592406 , AC096640 Genomic DNA. Translation: CAH72463.1 .
    CH471100 Genomic DNA. Translation: EAW93299.1 .
    CH471100 Genomic DNA. Translation: EAW93300.1 .
    CH471100 Genomic DNA. Translation: EAW93302.1 .
    BC113869 mRNA. Translation: AAI13870.1 .
    BC114478 mRNA. Translation: AAI14479.1 .
    CCDSi CCDS31029.2. [Q9P0L2-1 ]
    CCDS65789.1. [Q9P0L2-3 ]
    RefSeqi NP_001273057.1. NM_001286128.1. [Q9P0L2-3 ]
    NP_061120.3. NM_018650.4. [Q9P0L2-1 ]
    UniGenei Hs.497806.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HAK X-ray 2.60 A/B/C/D/E/F/G/H 45-371 [» ]
    3OSE X-ray 1.70 A 683-795 [» ]
    ProteinModelPortali Q9P0L2.
    SMRi Q9P0L2. Positions 29-371, 696-795.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110309. 13 interactions.
    DIPi DIP-39777N.
    IntActi Q9P0L2. 8 interactions.
    MINTi MINT-3975018.
    STRINGi 9606.ENSP00000355884.

    Chemistry

    BindingDBi Q9P0L2.
    ChEMBLi CHEMBL5940.
    GuidetoPHARMACOLOGYi 2097.

    PTM databases

    PhosphoSitei Q9P0L2.

    Polymorphism databases

    DMDMi 124056494.

    Proteomic databases

    MaxQBi Q9P0L2.
    PaxDbi Q9P0L2.
    PRIDEi Q9P0L2.

    Protocols and materials databases

    DNASUi 4139.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366917 ; ENSP00000355884 ; ENSG00000116141 . [Q9P0L2-1 ]
    ENST00000366918 ; ENSP00000355885 ; ENSG00000116141 . [Q9P0L2-3 ]
    ENST00000402574 ; ENSP00000386017 ; ENSG00000116141 . [Q9P0L2-2 ]
    GeneIDi 4139.
    KEGGi hsa:4139.
    UCSCi uc001hmm.4. human. [Q9P0L2-3 ]
    uc001hmn.4. human. [Q9P0L2-1 ]

    Organism-specific databases

    CTDi 4139.
    GeneCardsi GC01P220701.
    HGNCi HGNC:6896. MARK1.
    HPAi HPA007421.
    HPA008061.
    MIMi 606511. gene.
    neXtProti NX_Q9P0L2.
    PharmGKBi PA30639.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG052453.
    InParanoidi Q9P0L2.
    KOi K08798.
    OMAi EHPHIGN.
    OrthoDBi EOG79CXXX.
    PhylomeDBi Q9P0L2.
    TreeFami TF315213.

    Enzyme and pathway databases

    SignaLinki Q9P0L2.

    Miscellaneous databases

    ChiTaRSi MARK1. human.
    EvolutionaryTracei Q9P0L2.
    GeneWikii MARK1.
    GenomeRNAii 4139.
    NextBioi 16256.
    PROi Q9P0L2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9P0L2.
    Bgeei Q9P0L2.
    CleanExi HS_MARK1.
    Genevestigatori Q9P0L2.

    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. "LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1."
      Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A., Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G., Alessi D.R.
      EMBO J. 23:833-843(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME REGULATION, PHOSPHORYLATION AT THR-215, MUTAGENESIS OF THR-215.
    2. "Cloning and isolating human MARK."
      Zhou H.J., Huang X.W., Zhou Y., Hu S.L., Yuan J.G., Qiang B.Q.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain1 Publication.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. "MARK - a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption."
      Drewes G., Ebneth A., Preuss U., Mandelkow E.-M., Mandelkow E.
      Cell 89:297-308(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. "Microtubule-affinity regulating kinase (MARK) is tightly associated with neurofibrillary tangles in Alzheimer brain: a fluorescence resonance energy transfer study."
      Chin J.Y., Knowles R.B., Schneider A., Drewes G., Mandelkow E.M., Hyman B.T.
      J. Neuropathol. Exp. Neurol. 59:966-971(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NEUROFIBRILLARY TANGLES IN ALZHEIMER BRAIN.
    10. "PAR-1 is a Dishevelled-associated kinase and a positive regulator of Wnt signalling."
      Sun T.-Q., Lu B., Feng J.-J., Reinhard C., Jan Y.N., Fantl W.J., Williams L.T.
      Nat. Cell Biol. 3:628-636(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Suppression of tubulin polymerization by the LKB1-microtubule-associated protein/microtubule affinity-regulating kinase signaling."
      Kojima Y., Miyoshi H., Clevers H.C., Oshima M., Aoki M., Taketo M.M.
      J. Biol. Chem. 282:23532-23540(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-208, ENZYME REGULATION, FUNCTION.
    12. "Convergent evidence identifying MAP/microtubule affinity-regulating kinase 1 (MARK1) as a susceptibility gene for autism."
      Maussion G., Carayol J., Lepagnol-Bestel A.M., Tores F., Loe-Mie Y., Milbreta U., Rousseau F., Fontaine K., Renaud J., Moalic J.M., Philippi A., Chedotal A., Gorwood P., Ramoz N., Hager J., Simonneau M.
      Hum. Mol. Genet. 17:2541-2551(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSSIBLE INVOLVEMENT IN AUTISM.
    13. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5 AND SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "The tau of MARK: a polarized view of the cytoskeleton."
      Matenia D., Mandelkow E.M.
      Trends Biochem. Sci. 34:332-342(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    18. "Structure and function of polarity-inducing kinase family MARK/Par-1 within the branch of AMPK/Snf1-related kinases."
      Marx A., Nugoor C., Panneerselvam S., Mandelkow E.
      FASEB J. 24:1637-1648(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Structural variations in the catalytic and ubiquitin-associated domains of microtubule-associated protein/microtubule affinity regulating kinase (MARK) 1 and MARK2."
      Marx A., Nugoor C., Muller J., Panneerselvam S., Timm T., Bilang M., Mylonas E., Svergun D.I., Mandelkow E.M., Mandelkow E.
      J. Biol. Chem. 281:27586-27599(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 45-371.
    22. "Kinase associated-1 domains drive MARK/PAR1 kinases to membrane targets by binding acidic phospholipids."
      Moravcevic K., Mendrola J.M., Schmitz K.R., Wang Y.H., Slochower D., Janmey P.A., Lemmon M.A.
      Cell 143:966-977(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 683-795, DOMAIN KA1, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-698; ARG-701; 771-ARG--LYS-773 AND 773-LYS-ARG-774.
    23. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-233; THR-355; MET-530; LEU-578 AND GLY-691.

    Entry informationi

    Entry nameiMARK1_HUMAN
    AccessioniPrimary (citable) accession number: Q9P0L2
    Secondary accession number(s): D3DTB0
    , D3DTB1, Q2HIY1, Q5VTF9, Q5VTG0, Q96SW9, Q9P251
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 128 of the entry and version 2 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

    Miscellaneous

    Phosphorylation of MAPT/tau by MARK1 could play a role in early steps of Alzheimer disease. Pathological aggregation of MAPT/tau to neurofibrillary tangles, filamentous structures consisting of paired helical filaments (PHFs), is one of the hallmarks of Alzheimer disease. Hyperphosphorylation by MARK1 could be the initial step for this abnormal aggregation of tau in Alzheimer disease and animal models of tauopathy (PubMed:11089574).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3