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Q7KZI7

- MARK2_HUMAN

UniProt

Q7KZI7 - MARK2_HUMAN

Protein

Serine/threonine-protein kinase MARK2

Gene

MARK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (12 Apr 2005)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4, MAPT/TAU, and RAB11FIP2. Plays a key role in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Regulates epithelial cell polarity by phosphorylating RAB11FIP2. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Regulates axogenesis by phosphorylating KIF13B, promoting interaction between KIF13B and 14-3-3 and inhibiting microtubule-dependent accumulation of KIF13B. Also required for neurite outgrowth and establishment of neuronal polarity. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). Modulates the developmental decision to build a columnar versus a hepatic epithelial cell apparently by promoting a switch from a direct to a transcytotic mode of apical protein delivery. Essential for the asymmetric development of membrane domains of polarized epithelial cells.10 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 PAK7/PAK5; inhibition is independent of the kinase activity of PAK7/PAK5 By similarity. Activated by phosphorylation on Thr-208. Inhibited by phosphorylation at Ser-212 and Thr-596. Inhibited by hymenialdisine. Specifically inhibited by the H.pylori CagA peptide FPLKRHDKVDDLSK that mimics host substrates and binds to the kinase substrate-binding site.By similarity2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei82 – 821ATPBy similarityPROSITE-ProRule annotation
    Active sitei175 – 1751Proton acceptorBy similarityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi59 – 679ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. lipid binding Source: UniProtKB-KW
    3. magnesium ion binding Source: UniProtKB
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein serine/threonine kinase activity Source: UniProtKB
    7. tau-protein kinase activity Source: UniProtKB

    GO - Biological processi

    1. establishment of cell polarity Source: UniProtKB
    2. establishment or maintenance of epithelial cell apical/basal polarity Source: UniProtKB
    3. intracellular signal transduction Source: UniProtKB
    4. neuron migration Source: UniProtKB
    5. positive regulation of neuron projection development Source: UniProtKB
    6. protein autophosphorylation Source: UniProtKB
    7. protein phosphorylation Source: UniProtKB
    8. regulation of axonogenesis Source: UniProtKB
    9. regulation of cytoskeleton organization Source: UniProtKB
    10. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Differentiation, Wnt signaling pathway

    Keywords - Ligandi

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

    Enzyme and pathway databases

    SignaLinkiQ7KZI7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase MARK2 (EC:2.7.11.1, EC:2.7.11.26)
    Alternative name(s):
    ELKL motif kinase 1
    Short name:
    EMK-1
    MAP/microtubule affinity-regulating kinase 2
    PAR1 homolog
    PAR1 homolog b
    Short name:
    Par-1b
    Short name:
    Par1b
    Gene namesi
    Name:MARK2Imported
    Synonyms:EMK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:3332. MARK2.

    Subcellular locationi

    Cell membrane; Peripheral membrane protein. Cytoplasm. Lateral cell membrane. Cytoplasmcytoskeleton
    Note: Phosphorylation at Thr-596 by PRKCZ/aPKC and subsequent interaction with 14-3-3 protein YWHAZ promotes relocation from the cell membrane to the cytoplasm.

    GO - Cellular componenti

    1. actin filament Source: UniProtKB
    2. basal cortex Source: Ensembl
    3. lateral plasma membrane Source: UniProtKB
    4. membrane Source: UniProtKB
    5. microtubule bundle Source: UniProtKB
    6. nucleus Source: Ensembl
    7. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi208 – 2081T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. 1 Publication
    Mutagenesisi596 – 5961T → A: Loss of membrane dissociation and binding to YWHAZ. 2 Publications

    Organism-specific databases

    PharmGKBiPA35047.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 788788Serine/threonine-protein kinase MARK2PRO_0000086301Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei40 – 401Phosphoserine1 Publication
    Modified residuei58 – 581Phosphothreonine; by autocatalysisBy similarity
    Modified residuei91 – 911Phosphoserine; by CaMK1By similarity
    Modified residuei92 – 921Phosphoserine; by CaMK1By similarity
    Modified residuei93 – 931Phosphoserine; by CaMK1By similarity
    Modified residuei208 – 2081Phosphothreonine; by LKB1 and TAOK12 Publications
    Modified residuei212 – 2121Phosphoserine; by GSK3-betaBy similarity
    Modified residuei274 – 2741Phosphoserine; by autocatalysisBy similarity
    Modified residuei275 – 2751Phosphothreonine; by autocatalysisBy similarity
    Modified residuei294 – 2941Phosphothreonine; by CaMK1By similarity
    Modified residuei409 – 4091Phosphoserine2 Publications
    Modified residuei456 – 4561Phosphoserine5 Publications
    Modified residuei486 – 4861Phosphoserine5 Publications
    Modified residuei493 – 4931Phosphoserine1 Publication
    Modified residuei569 – 5691Phosphoserine1 Publication
    Modified residuei596 – 5961Phosphothreonine; by PKC/PRKCZ2 Publications
    Modified residuei619 – 6191Phosphoserine1 Publication
    Modified residuei722 – 7221Phosphoserine1 Publication

    Post-translational modificationi

    Autophosphorylated. Phosphorylated at Thr-208 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Phosphorylation at Thr-208 by TAOK1 activates the kinase activity, leading to phosphorylation and detachment of MAPT/TAU from microtubules. Phosphorylation at Ser-212 by GSK3-beta (GSK3B) inhibits the kinase activity. Phosphorylation by CaMK1 promotes activity and is required to promote neurite outgrowth. Phosphorylation at Thr-596 by PRKCZ/aPKC in polarized epithelial cells inhibits the kinase activity and promotes binding to 14-3-3 protein YWHAZ, leading to relocation from cell membrane to cytoplasm.11 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ7KZI7.
    PaxDbiQ7KZI7.
    PRIDEiQ7KZI7.

    PTM databases

    PhosphoSiteiQ7KZI7.

    Expressioni

    Tissue specificityi

    High levels of expression in heart, brain, skeletal muscle and pancreas, lower levels observed in lung, liver and kidney.1 Publication

    Gene expression databases

    ArrayExpressiQ7KZI7.
    BgeeiQ7KZI7.
    CleanExiHS_MARK2.
    GenevestigatoriQ7KZI7.

    Organism-specific databases

    HPAiHPA038790.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with PAK7/PAK5; leading to inhibit the protein kinase activity By similarity. Interacts with MTCL1 isoform 1; the interaction is direct and increases MARK2 microtubule-binding ability. Interacts (when phosphorylated at Thr-596) with YWHAZ. In case of infection, interacts with H.pylori CagA, leading to inhibit kinase activity and junctional and polarity defects.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PARD6GQ9BYG42EBI-516560,EBI-295417
    YWHABP319463EBI-516560,EBI-359815
    YWHAGP619812EBI-516560,EBI-359832
    YWHAHQ049178EBI-516560,EBI-306940
    YWHAZP631046EBI-516560,EBI-347088

    Protein-protein interaction databases

    BioGridi108326. 52 interactions.
    DIPiDIP-31321N.
    IntActiQ7KZI7. 34 interactions.
    MINTiMINT-1149196.
    STRINGi9606.ENSP00000389184.

    Structurei

    Secondary structure

    1
    788
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi53 – 608
    Beta strandi66 – 727
    Turni73 – 753
    Beta strandi78 – 869
    Helixi91 – 10616
    Beta strandi115 – 1206
    Beta strandi122 – 1298
    Helixi137 – 1448
    Helixi149 – 16820
    Helixi178 – 1803
    Beta strandi181 – 1833
    Beta strandi189 – 1913
    Helixi213 – 2153
    Helixi218 – 2214
    Helixi228 – 24518
    Helixi255 – 26410
    Helixi275 – 28410
    Helixi289 – 2913
    Helixi295 – 2995
    Helixi302 – 3054
    Helixi326 – 3349
    Helixi339 – 3479
    Helixi353 – 3619

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3IECX-ray2.20A/B/C/D49-363[»]
    ProteinModelPortaliQ7KZI7.
    SMRiQ7KZI7. Positions 19-363, 689-788.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7KZI7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini53 – 304252Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini323 – 36240UBAPROSITE-ProRule annotationAdd
    BLAST
    Domaini739 – 78850KA1PROSITE-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.1 Publication
    The KA1 domain mediates binding to phospholipids and targeting to membranes.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.
    HOVERGENiHBG052453.
    InParanoidiQ7KZI7.
    KOiK08798.
    OMAiHERYMLL.
    OrthoDBiEOG79CXXX.
    PhylomeDBiQ7KZI7.
    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 (16)i

    Sequence statusi: Complete.

    This entry describes 16 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform 1Curated (identifier: Q7KZI7-1) [UniParc]FASTAAdd to Basket

    Also known as: Alpha

    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

    MSSARTPLPT LNERDTEQPT LGHLDSKPSS KSNMIRGRNS ATSADEQPHI    50
    GNYRLLKTIG KGNFAKVKLA RHILTGKEVA VKIIDKTQLN SSSLQKLFRE 100
    VRIMKVLNHP NIVKLFEVIE TEKTLYLVME YASGGEVFDY LVAHGRMKEK 150
    EARAKFRQIV SAVQYCHQKF IVHRDLKAEN LLLDADMNIK IADFGFSNEF 200
    TFGNKLDTFC GSPPYAAPEL FQGKKYDGPE VDVWSLGVIL YTLVSGSLPF 250
    DGQNLKELRE RVLRGKYRIP FYMSTDCENL LKKFLILNPS KRGTLEQIMK 300
    DRWMNVGHED DELKPYVEPL PDYKDPRRTE LMVSMGYTRE EIQDSLVGQR 350
    YNEVMATYLL LGYKSSELEG DTITLKPRPS ADLTNSSAPS PSHKVQRSVS 400
    ANPKQRRFSD QAAGPAIPTS NSYSKKTQSN NAENKRPEED RESGRKASST 450
    AKVPASPLPG LERKKTTPTP STNSVLSTST NRSRNSPLLE RASLGQASIQ 500
    NGKDSLTMPG SRASTASASA AVSAARPRQH QKSMSASVHP NKASGLPPTE 550
    SNCEVPRPST APQRVPVASP SAHNISSSGG APDRTNFPRG VSSRSTFHAG 600
    QLRQVRDQQN LPYGVTPASP SGHSQGRRGA SGSIFSKFTS KFVRRNLSFR 650
    FARRNLNEPE SKDRVETLRP HVVGSGGNDK EKEEFREAKP RSLRFTWSMK 700
    TTSSMEPNEM MREIRKVLDA NSCQSELHEK YMLLCMHGTP GHEDFVQWEM 750
    EVCKLPRLSL NGVRFKRISG TSMAFKNIAS KIANELKL 788

    Note: Produced by alternative promoter usage. No experimental confirmation available.

    Length:788
    Mass (Da):87,911
    Last modified:April 12, 2005 - v2
    Checksum:iF307BF4DDB543A70
    GO
    Isoform 21 Publication (identifier: Q7KZI7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: Missing.
         505-558: Missing.

    Note: Produced by alternative splicing of isoform 6.1 Publication

    Show »
    Length:701
    Mass (Da):78,851
    Checksum:i3D68318CFDCA31EE
    GO
    Isoform 31 Publication (identifier: Q7KZI7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: Missing.
         644-652: Missing.

    Note: Produced by alternative splicing of isoform 6.1 Publication

    Show »
    Length:746
    Mass (Da):83,184
    Checksum:i58F2BBE10943C90F
    GO
    Isoform 41 Publication (identifier: Q7KZI7-4) [UniParc]FASTAAdd to Basket

    Also known as: Par-1Balpha1 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         505-558: Missing.
         644-652: Missing.

    Note: Produced by alternative splicing of isoform 1.1 Publication

    Show »
    Length:725
    Mass (Da):81,280
    Checksum:iD676331938A84716
    GO
    Isoform 5 (identifier: Q7KZI7-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         505-558: Missing.
         654-668: Missing.

    Note: Produced by alternative splicing of isoform 1.

    Show »
    Length:719
    Mass (Da):80,647
    Checksum:iEC39154CF73E9858
    GO
    Isoform 6Curated (identifier: Q7KZI7-6) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: Missing.

    Note: Produced by alternative promoter usage. No experimental confirmation available.

    Show »
    Length:755
    Mass (Da):84,333
    Checksum:i493CD8C6DC3A4C06
    GO
    Isoform 7Curated (identifier: Q7KZI7-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: Missing.
         505-558: Missing.
         644-652: Missing.

    Note: Produced by alternative splicing of isoform 6. No experimental confirmation available.Curated

    Show »
    Length:692
    Mass (Da):77,702
    Checksum:i4BD9AA1F872638A6
    GO
    Isoform 8Curated (identifier: Q7KZI7-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         644-652: Missing.

    Note: Produced by alternative splicing of isoform 1. No experimental confirmation available.Curated

    Show »
    Length:779
    Mass (Da):86,762
    Checksum:i5AF7014EB5639857
    GO
    Isoform 9Curated (identifier: Q7KZI7-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         505-558: Missing.

    Note: Produced by alternative splicing of isoform 1. No experimental confirmation available.Curated

    Show »
    Length:734
    Mass (Da):82,429
    Checksum:i60D126D3C8967186
    GO
    Isoform 10Curated (identifier: Q7KZI7-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: Missing.
         505-558: Missing.
         654-668: Missing.

    Note: Produced by alternative splicing of isoform 6. No experimental confirmation available.Curated

    Show »
    Length:686
    Mass (Da):77,069
    Checksum:i9389E28076FDDAF8
    GO
    Isoform 11Curated (identifier: Q7KZI7-11) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         654-668: Missing.

    Note: Produced by alternative splicing of isoform 1. No experimental confirmation available.

    Show »
    Length:773
    Mass (Da):86,129
    Checksum:i0378FF0433C4D901
    GO
    Isoform 12Curated (identifier: Q7KZI7-12) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: Missing.
         654-668: Missing.

    Note: Produced by alternative splicing of isoform 6. No experimental confirmation available.Curated

    Show »
    Length:740
    Mass (Da):82,551
    Checksum:i6220FC8C1A308548
    GO
    Isoform 13 (identifier: Q7KZI7-13) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: Missing.
         412-412: Missing.
         505-558: Missing.
         644-652: Missing.

    Note: Produced by alternative splicing of isoform 6. Contains a phosphoserine at position 376.

    Show »
    Length:691
    Mass (Da):77,631
    Checksum:i2216B4AE7BCF31BE
    GO
    Isoform 14 (identifier: Q7KZI7-14) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: Missing.
         412-412: Missing.
         644-652: Missing.

    Note: Produced by alternative splicing of isoform 6. Contains a phosphoserine at position 376.

    Show »
    Length:745
    Mass (Da):83,113
    Checksum:i54CA1DAF4B6E02CF
    GO
    Isoform 15 (identifier: Q7KZI7-15) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         412-412: Missing.
         505-558: Missing.
         645-668: Missing.

    Note: Produced by alternative splicing of isoform 1. Contains a phosphoserine at position 409.

    Show »
    Length:709
    Mass (Da):79,427
    Checksum:iF30B3AB6B60B3621
    GO
    Isoform 16 (identifier: Q7KZI7-16) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         412-412: Missing.
         505-558: Missing.
         644-652: Missing.

    Note: Produced by alternative splicing of isoform 1. Contains a phosphoserine at position 409.

    Show »
    Length:724
    Mass (Da):81,209
    Checksum:i9D8FB211F5B08149
    GO

    Sequence cautioni

    The sequence AAK82368.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti192 – 1921A → G in CAA80914. (PubMed:8274451)Curated
    Sequence conflicti236 – 2361L → C in CAA80914. (PubMed:8274451)Curated
    Sequence conflicti389 – 3902PS → QF in CAA66229. (PubMed:9730619)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3333Missing in isoform 2, isoform 3, isoform 6, isoform 7, isoform 10, isoform 12, isoform 13 and isoform 14. 2 PublicationsVSP_051705Add
    BLAST
    Alternative sequencei412 – 4121Missing in isoform 13, isoform 14, isoform 15 and isoform 16. CuratedVSP_039872
    Alternative sequencei505 – 55854Missing in isoform 2, isoform 4, isoform 5, isoform 7, isoform 9, isoform 10, isoform 13, isoform 15 and isoform 16. 4 PublicationsVSP_051706Add
    BLAST
    Alternative sequencei644 – 6529Missing in isoform 3, isoform 4, isoform 7, isoform 8, isoform 13, isoform 14 and isoform 16. 3 PublicationsVSP_051707
    Alternative sequencei645 – 66824Missing in isoform 15. CuratedVSP_041853Add
    BLAST
    Alternative sequencei654 – 66815Missing in isoform 5, isoform 11, isoform 10 and isoform 12. 3 PublicationsVSP_051708Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X97630 mRNA. Translation: CAA66229.1.
    AB188493 mRNA. Translation: BAD37141.1.
    BT007342 mRNA. Translation: AAP36006.1.
    AP003780 Genomic DNA. No translation available.
    BC008771 mRNA. Translation: AAH08771.2.
    BC084540 mRNA. Translation: AAH84540.1.
    AF387638 mRNA. Translation: AAK82368.1. Different initiation.
    Z25427 mRNA. Translation: CAA80914.1.
    CCDSiCCDS41665.1. [Q7KZI7-14]
    CCDS53649.1. [Q7KZI7-1]
    CCDS53650.1. [Q7KZI7-5]
    CCDS53651.1. [Q7KZI7-15]
    CCDS8051.2. [Q7KZI7-16]
    PIRiG01025.
    I38217.
    RefSeqiNP_001034558.2. NM_001039469.2. [Q7KZI7-1]
    NP_001156768.1. NM_001163296.1. [Q7KZI7-5]
    NP_001156769.1. NM_001163297.1. [Q7KZI7-15]
    NP_004945.4. NM_004954.4. [Q7KZI7-16]
    NP_059672.2. NM_017490.3. [Q7KZI7-14]
    XP_006718504.1. XM_006718441.1. [Q7KZI7-8]
    XP_006718506.1. XM_006718443.1. [Q7KZI7-11]
    XP_006718509.1. XM_006718446.1. [Q7KZI7-4]
    UniGeneiHs.567261.

    Genome annotation databases

    EnsembliENST00000350490; ENSP00000294247; ENSG00000072518. [Q7KZI7-15]
    ENST00000361128; ENSP00000355091; ENSG00000072518. [Q7KZI7-5]
    ENST00000377810; ENSP00000367041; ENSG00000072518. [Q7KZI7-13]
    ENST00000402010; ENSP00000385751; ENSG00000072518. [Q7KZI7-1]
    ENST00000408948; ENSP00000386128; ENSG00000072518. [Q7KZI7-13]
    ENST00000508192; ENSP00000425765; ENSG00000072518. [Q7KZI7-16]
    ENST00000509502; ENSP00000423974; ENSG00000072518. [Q7KZI7-14]
    ENST00000513765; ENSP00000421075; ENSG00000072518. [Q7KZI7-6]
    GeneIDi2011.
    KEGGihsa:2011.
    UCSCiuc001nxv.4. human. [Q7KZI7-16]
    uc001nxw.3. human. [Q7KZI7-1]
    uc001nxx.3. human. [Q7KZI7-5]
    uc001nxy.3. human. [Q7KZI7-15]
    uc001nxz.4. human. [Q7KZI7-14]

    Polymorphism databases

    DMDMi62510922.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X97630 mRNA. Translation: CAA66229.1 .
    AB188493 mRNA. Translation: BAD37141.1 .
    BT007342 mRNA. Translation: AAP36006.1 .
    AP003780 Genomic DNA. No translation available.
    BC008771 mRNA. Translation: AAH08771.2 .
    BC084540 mRNA. Translation: AAH84540.1 .
    AF387638 mRNA. Translation: AAK82368.1 . Different initiation.
    Z25427 mRNA. Translation: CAA80914.1 .
    CCDSi CCDS41665.1. [Q7KZI7-14 ]
    CCDS53649.1. [Q7KZI7-1 ]
    CCDS53650.1. [Q7KZI7-5 ]
    CCDS53651.1. [Q7KZI7-15 ]
    CCDS8051.2. [Q7KZI7-16 ]
    PIRi G01025.
    I38217.
    RefSeqi NP_001034558.2. NM_001039469.2. [Q7KZI7-1 ]
    NP_001156768.1. NM_001163296.1. [Q7KZI7-5 ]
    NP_001156769.1. NM_001163297.1. [Q7KZI7-15 ]
    NP_004945.4. NM_004954.4. [Q7KZI7-16 ]
    NP_059672.2. NM_017490.3. [Q7KZI7-14 ]
    XP_006718504.1. XM_006718441.1. [Q7KZI7-8 ]
    XP_006718506.1. XM_006718443.1. [Q7KZI7-11 ]
    XP_006718509.1. XM_006718446.1. [Q7KZI7-4 ]
    UniGenei Hs.567261.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3IEC X-ray 2.20 A/B/C/D 49-363 [» ]
    ProteinModelPortali Q7KZI7.
    SMRi Q7KZI7. Positions 19-363, 689-788.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108326. 52 interactions.
    DIPi DIP-31321N.
    IntActi Q7KZI7. 34 interactions.
    MINTi MINT-1149196.
    STRINGi 9606.ENSP00000389184.

    Chemistry

    BindingDBi Q7KZI7.
    ChEMBLi CHEMBL3831.
    GuidetoPHARMACOLOGYi 2098.

    PTM databases

    PhosphoSitei Q7KZI7.

    Polymorphism databases

    DMDMi 62510922.

    Proteomic databases

    MaxQBi Q7KZI7.
    PaxDbi Q7KZI7.
    PRIDEi Q7KZI7.

    Protocols and materials databases

    DNASUi 2011.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000350490 ; ENSP00000294247 ; ENSG00000072518 . [Q7KZI7-15 ]
    ENST00000361128 ; ENSP00000355091 ; ENSG00000072518 . [Q7KZI7-5 ]
    ENST00000377810 ; ENSP00000367041 ; ENSG00000072518 . [Q7KZI7-13 ]
    ENST00000402010 ; ENSP00000385751 ; ENSG00000072518 . [Q7KZI7-1 ]
    ENST00000408948 ; ENSP00000386128 ; ENSG00000072518 . [Q7KZI7-13 ]
    ENST00000508192 ; ENSP00000425765 ; ENSG00000072518 . [Q7KZI7-16 ]
    ENST00000509502 ; ENSP00000423974 ; ENSG00000072518 . [Q7KZI7-14 ]
    ENST00000513765 ; ENSP00000421075 ; ENSG00000072518 . [Q7KZI7-6 ]
    GeneIDi 2011.
    KEGGi hsa:2011.
    UCSCi uc001nxv.4. human. [Q7KZI7-16 ]
    uc001nxw.3. human. [Q7KZI7-1 ]
    uc001nxx.3. human. [Q7KZI7-5 ]
    uc001nxy.3. human. [Q7KZI7-15 ]
    uc001nxz.4. human. [Q7KZI7-14 ]

    Organism-specific databases

    CTDi 2011.
    GeneCardsi GC11P063606.
    HGNCi HGNC:3332. MARK2.
    HPAi HPA038790.
    MIMi 600526. gene.
    neXtProti NX_Q7KZI7.
    PharmGKBi PA35047.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG052453.
    InParanoidi Q7KZI7.
    KOi K08798.
    OMAi HERYMLL.
    OrthoDBi EOG79CXXX.
    PhylomeDBi Q7KZI7.
    TreeFami TF315213.

    Enzyme and pathway databases

    SignaLinki Q7KZI7.

    Miscellaneous databases

    ChiTaRSi MARK2. human.
    EvolutionaryTracei Q7KZI7.
    GeneWikii MARK2.
    GenomeRNAii 2011.
    NextBioi 8141.
    PROi Q7KZI7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7KZI7.
    Bgeei Q7KZI7.
    CleanExi HS_MARK2.
    Genevestigatori Q7KZI7.

    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. "Human serine/threonine protein kinase EMK1: genome structure and cDNA cloning of isoforms produced by alternative splicing."
      Espinosa L., Navarro E.
      Cytogenet. Cell Genet. 81:278-282(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY.
      Tissue: ColonImported.
    2. Sugiyama A., Inoue H., Oka M.
      Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
      Tissue: KidneyImported.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-755 (ISOFORM 1).
      Tissue: KidneyImported and PlacentaImported.
    6. "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: NUCLEOTIDE SEQUENCE [MRNA] OF 28-788 (ISOFORM 4), FUNCTION.
    7. "Identification of 21 novel human protein kinases, including 3 members of a family related to the cell cycle regulator nimA of Aspergillus nidulans."
      Schultz S.J., Nigg E.A.
      Cell Growth Differ. 4:821-830(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 190-237.
    8. "Protein kinase MARK/PAR-1 is required for neurite outgrowth and establishment of neuronal polarity."
      Biernat J., Wu Y.Z., Timm T., Zheng-Fischhofer Q., Mandelkow E., Meijer L., Mandelkow E.M.
      Mol. Biol. Cell 13:4013-4028(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    9. "Splicing alterations in human renal allografts: detection of a new splice variant of protein kinase Par1/Emk1 whose expression is associated with an increase of inflammation in protocol biopsies of transplanted patients."
      Hueso M., Beltran V., Moreso F., Ciriero E., Fulladosa X., Grinyo J.M., Seron D., Navarro E.
      Biochim. Biophys. Acta 1689:58-65(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ALTERNATIVE PROMOTER USAGE.
    10. "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: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-208, MUTAGENESIS OF THR-208.
    11. "Par-1 promotes a hepatic mode of apical protein trafficking in MDCK cells."
      Cohen D., Rodriguez-Boulan E., Musch A.
      Proc. Natl. Acad. Sci. U.S.A. 101:13792-13797(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Atypical PKC phosphorylates PAR-1 kinases to regulate localization and activity."
      Hurov J.B., Watkins J.L., Piwnica-Worms H.
      Curr. Biol. 14:736-741(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-596, MUTAGENESIS OF THR-596, SUBCELLULAR LOCATION.
    13. "aPKC acts upstream of PAR-1b in both the establishment and maintenance of mammalian epithelial polarity."
      Suzuki A., Hirata M., Kamimura K., Maniwa R., Yamanaka T., Mizuno K., Kishikawa M., Hirose H., Amano Y., Izumi N., Miwa Y., Ohno S.
      Curr. Biol. 14:1425-1435(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-596, MUTAGENESIS OF THR-596, INTERACTION WITH YWHAZ.
    14. "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-486, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "MARK2/EMK1/Par-1Balpha phosphorylation of Rab11-family interacting protein 2 is necessary for the timely establishment of polarity in Madin-Darby canine kidney cells."
      Ducharme N.A., Hales C.M., Lapierre L.A., Ham A.J., Oztan A., Apodaca G., Goldenring J.R.
      Mol. Biol. Cell 17:3625-3637(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF RAB11FIP2.
    16. "New role for hPar-1 kinases EMK and C-TAK1 in regulating localization and activity of class IIa histone deacetylases."
      Dequiedt F., Martin M., Von Blume J., Vertommen D., Lecomte E., Mari N., Heinen M.F., Bachmann M., Twizere J.C., Huang M.C., Rider M.H., Piwnica-Worms H., Seufferlein T., Kettmann R.
      Mol. Cell. Biol. 26:7086-7102(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC7.
    17. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Helicobacter pylori CagA targets PAR1/MARK kinase to disrupt epithelial cell polarity."
      Saadat I., Higashi H., Obuse C., Umeda M., Murata-Kamiya N., Saito Y., Lu H., Ohnishi N., Azuma T., Suzuki A., Ohno S., Hatakeyama M.
      Nature 447:330-333(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH H.PYLORI CAGA.
    19. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456 AND SER-486, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    21. "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 SER-409; SER-456; SER-486 AND SER-493, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "Glucose controls CREB activity in islet cells via regulated phosphorylation of TORC2."
      Jansson D., Ng A.C., Fu A., Depatie C., Al Azzabi M., Screaton R.A.
      Proc. Natl. Acad. Sci. U.S.A. 105:10161-10166(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CRTC2.
    23. "The ubiquitin-associated domain of AMPK-related kinases regulates conformation and LKB1-mediated phosphorylation and activation."
      Jaleel M., Villa F., Deak M., Toth R., Prescott A.R., Van Aalten D.M., Alessi D.R.
      Biochem. J. 394:545-555(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN UBA.
    24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376 (ISOFORMS 13 AND 14), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409 (ISOFORMS 15 AND 16), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. "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].
    26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-208; SER-409; SER-456; SER-486 AND SER-722, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376 (ISOFORMS 13 AND 14), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Par1b/MARK2 phosphorylates kinesin-like motor protein GAKIN/KIF13B to regulate axon formation."
      Yoshimura Y., Terabayashi T., Miki H.
      Mol. Cell. Biol. 30:2206-2219(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF KIF13B.
    28. "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.
    29. "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.
    30. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "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-40; SER-486 AND SER-619, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. "The novel PAR-1-binding protein MTCL1 has crucial roles in organizing microtubules in polarizing epithelial cells."
      Sato Y., Akitsu M., Amano Y., Yamashita K., Ide M., Shimada K., Yamashita A., Hirano H., Arakawa N., Maki T., Hayashi I., Ohno S., Suzuki A.
      J. Cell Sci. 126:4671-4683(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MTCL1, SUBCELLULAR LOCATION.
    34. "Helicobacter pylori CagA inhibits PAR1-MARK family kinases by mimicking host substrates."
      Nesic D., Miller M.C., Quinkert Z.T., Stein M., Chait B.T., Stebbins C.E.
      Nat. Struct. Mol. Biol. 17:130-132(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 49-363 IN COMPLEX WITH H.PYLORI CAGA PEPTIDE INHIBITOR.

    Entry informationi

    Entry nameiMARK2_HUMAN
    AccessioniPrimary (citable) accession number: Q7KZI7
    Secondary accession number(s): Q15449
    , Q15524, Q5XGA3, Q68A18, Q96HB3, Q96RG0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: April 12, 2005
    Last modified: October 1, 2014
    This is version 119 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3