Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q05512

- MARK2_MOUSE

UniProt

Q05512 - MARK2_MOUSE

Protein

Serine/threonine-protein kinase MARK2

Gene

Mark2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.
    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. Activated by phosphorylation on Thr-208. Inhibited by phosphorylation at Ser-212 and Thr-593. Inhibited by hymenialdisine By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei82 – 821ATPPROSITE-ProRule annotation
    Active sitei175 – 1751Proton acceptorPROSITE-ProRule annotation

    Regions

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. lipid binding Source: UniProtKB-KW
    3. magnesium ion binding Source: UniProtKB
    4. protein serine/threonine kinase activity Source: UniProtKB
    5. 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

    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:
    mPar-1b
    Gene namesi
    Name:Mark2
    Synonyms:Emk
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:99638. Mark2.

    Subcellular locationi

    Cell membrane By similarity; Peripheral membrane protein By similarity. Lateral cell membrane By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasm By similarity
    Note: Phosphorylation at Thr-593 by PRKCZ/aPKC and subsequent interaction with 14-3-3 protein YWHAZ promotes relocation from the cell membrane to the cytoplasm.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice have no embryonic defect and are viable. They do not display obvious neuronal phenotype, possibly due to genetic redundancy with Mark1, Mark3 and Mark4. They however show an overall proportionate dwarfism and a peculiar hypofertility: homozygotes are not fertile when intercrossed, but are fertile in other types of crosses. They also show immune-cell dysfunction. As mice age, they develop splenomegaly, lymphadenopathy, membranoproliferative glomerulonephritis, and lymphocytic infiltrates in the lungs, parotid glands and kidneys. Moreover, mice are lean, insulin hypersensitive, resistant to high-fat-diet-induced weight gain, and hypermetabolic.3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 776776Serine/threonine-protein kinase MARK2PRO_0000086302Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei40 – 401PhosphoserineBy similarity
    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 TAOK1
    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 – 4091PhosphoserineBy similarity
    Modified residuei453 – 4531Phosphoserine1 Publication
    Modified residuei483 – 4831PhosphoserineBy similarity
    Modified residuei490 – 4901PhosphoserineBy similarity
    Modified residuei566 – 5661PhosphoserineBy similarity
    Modified residuei593 – 5931Phosphothreonine; by PKC/PRKCZBy similarity
    Modified residuei616 – 6161PhosphoserineBy similarity
    Modified residuei710 – 7101PhosphoserineBy similarity

    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-593 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 By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ05512.
    PaxDbiQ05512.
    PRIDEiQ05512.

    PTM databases

    PhosphoSiteiQ05512.

    Expressioni

    Tissue specificityi

    Highly expressed in adult kidney and testis, lower levels in heart, brain, spleen, lung and liver. Expressed in the head and neural fold in 8 dpc embryos, the limb buds, telencephalic vesicles, eyes, branchial archs and heart at 11.5 dpc, the ectoderm at 13 dpc and epiderm, hair and whisker follicles at 15 dpc.1 Publication

    Gene expression databases

    ArrayExpressiQ05512.
    BgeeiQ05512.
    CleanExiMM_MARK2.
    GenevestigatoriQ05512.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with PAK7/PAK5; leading to inhibit the protein kinase activity By similarity. Interacts (when phosphorylated at Thr-593) with YWHAZ. Interacts with PAK7/PAK5 By similarity. Interacts with MTCL1; the interaction is direct and increases MARK2 microtubule-binding ability By similarity.By similarity

    Protein-protein interaction databases

    BioGridi199437. 7 interactions.
    IntActiQ05512. 3 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05512.
    SMRiQ05512. Positions 13-363, 677-776.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini53 – 304252Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini323 – 36240UBAPROSITE-ProRule annotationAdd
    BLAST
    Domaini727 – 77650KA1PROSITE-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.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.
    HOGENOMiHOG000233025.
    HOVERGENiHBG052453.
    InParanoidiQ05512.
    KOiK08798.
    OrthoDBiEOG79CXXX.
    PhylomeDBiQ05512.

    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q05512-1) [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

    MSSARTPLPT LNERDTEQPT LGHLDSKPSS KSNMLRGRNS ATSADEQPHI    50
    GNYRLLKTIG KGNFAKVKLA RHILTGKEVA VKIIDKTQLN SSSLQKLFRE 100
    VRIMKVLNHP NIVKLFEVIE TEKTLYLVME YASGGEVFDY LVAHGRMKEK 150
    EARAKFRQIV SAVQYCHQKF IVHRDLKAEN LLLDADMNIK IADFGFSNEF 200
    TFGNKLDTFC GSPPYAAPEL FQGKKIDGPE VDVWSLGVIL YTLVSGSLPF 250
    DGQNLKELRE RVLRGKYRIP FYMSTDCENL LKKFLILNPS KRGTLEQIMK 300
    DRWMNVGHED DELKPYVEPL PDYKDPRRTE LMVSMGYTRE EIQDSLVGQR 350
    YNEVMATYLL LGYKSSELEG DTITLKPRPS ADLTNSSAPS PSHKVQRSVS 400
    ANPKQRRSSD QAVPAIPTSN SYSKKTQSNN AENKRPEEET GRKASSTAKV 450
    PASPLPGLDR KKTTPAPSTN SVLSTSTNRS RNSPLLDRAS LGQASIQNGK 500
    DSLTMPGSRA STASASAAVS AARPRQHQKS MSASVHPNKA SGLPPTESNC 550
    EVPRPSTAPQ RVPVASPSAH NISSSSGAPD RTNFPRGVSS RSTFHAGQLR 600
    QVRDQQNLPY GVTPASPSGH SQGRRGASGS IFSKFTSKFV RRNLNEPESK 650
    DRVETLRPHV VGSGGTDKDK EEFREAKPRS LRFTWSMKTT SSMEPNEMMR 700
    EIRKVLDANS CQSELHERYM LLCVHGTPGH ENFVQWEMEV CKLPRLSLNG 750
    VRFKRISGTS MAFKNIASKI ANELKL 776
    Length:776
    Mass (Da):86,306
    Last modified:January 23, 2007 - v3
    Checksum:i533C8DE0B5EC507E
    GO
    Isoform 2 (identifier: Q05512-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         321-339: PDYKDPRRTELMVSMGYTR → LTTGPRDRVDGVNGLHT

    Note: No experimental confirmation available.

    Show »
    Length:774
    Mass (Da):85,798
    Checksum:iA16080EE5F864414
    GO
    Isoform 3 (identifier: Q05512-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         502-555: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:722
    Mass (Da):80,824
    Checksum:iA5FF894FBA51F656
    GO
    Isoform 4 (identifier: Q05512-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         502-555: Missing.
         640-640: V → VRRNLSFRFA

    Note: No experimental confirmation available.

    Show »
    Length:731
    Mass (Da):81,972
    Checksum:iAC87AD0A923FB943
    GO

    Sequence cautioni

    The sequence BAC32312.1 differs from that shown. Reason: Frameshift at position 772.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti161 – 1622SA → LH in CAA50040. (PubMed:8358177)Curated
    Sequence conflicti368 – 3681L → P in CAA50040. (PubMed:8358177)Curated
    Sequence conflicti760 – 7601S → Y in BAC32312. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei321 – 33919PDYKD…MGYTR → LTTGPRDRVDGVNGLHT in isoform 2. 1 PublicationVSP_013341Add
    BLAST
    Alternative sequencei502 – 55554Missing in isoform 3 and isoform 4. 2 PublicationsVSP_013342Add
    BLAST
    Alternative sequencei640 – 6401V → VRRNLSFRFA in isoform 4. 1 PublicationVSP_022597

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70764 mRNA. Translation: CAA50040.1.
    AK045329 mRNA. Translation: BAC32312.1. Frameshift.
    AK172444 mRNA. Translation: BAE43007.1.
    BC058556 mRNA. Translation: AAH58556.1.
    CCDSiCCDS37903.1. [Q05512-4]
    CCDS37904.1. [Q05512-1]
    CCDS50378.1. [Q05512-3]
    PIRiI48609.
    RefSeqiNP_001073857.1. NM_001080388.2.
    NP_001073858.1. NM_001080389.2.
    NP_001073859.1. NM_001080390.2.
    NP_031954.2. NM_007928.3.
    UniGeneiMm.258986.

    Genome annotation databases

    EnsembliENSMUST00000032557; ENSMUSP00000032557; ENSMUSG00000024969.
    ENSMUST00000164205; ENSMUSP00000127827; ENSMUSG00000024969.
    GeneIDi13728.
    KEGGimmu:13728.
    UCSCiuc008gks.1. mouse. [Q05512-4]
    uc008gkt.1. mouse. [Q05512-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70764 mRNA. Translation: CAA50040.1 .
    AK045329 mRNA. Translation: BAC32312.1 . Frameshift.
    AK172444 mRNA. Translation: BAE43007.1 .
    BC058556 mRNA. Translation: AAH58556.1 .
    CCDSi CCDS37903.1. [Q05512-4 ]
    CCDS37904.1. [Q05512-1 ]
    CCDS50378.1. [Q05512-3 ]
    PIRi I48609.
    RefSeqi NP_001073857.1. NM_001080388.2.
    NP_001073858.1. NM_001080389.2.
    NP_001073859.1. NM_001080390.2.
    NP_031954.2. NM_007928.3.
    UniGenei Mm.258986.

    3D structure databases

    ProteinModelPortali Q05512.
    SMRi Q05512. Positions 13-363, 677-776.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199437. 7 interactions.
    IntActi Q05512. 3 interactions.

    PTM databases

    PhosphoSitei Q05512.

    Proteomic databases

    MaxQBi Q05512.
    PaxDbi Q05512.
    PRIDEi Q05512.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000032557 ; ENSMUSP00000032557 ; ENSMUSG00000024969 .
    ENSMUST00000164205 ; ENSMUSP00000127827 ; ENSMUSG00000024969 .
    GeneIDi 13728.
    KEGGi mmu:13728.
    UCSCi uc008gks.1. mouse. [Q05512-4 ]
    uc008gkt.1. mouse. [Q05512-3 ]

    Organism-specific databases

    CTDi 2011.
    MGIi MGI:99638. Mark2.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00730000110535.
    HOGENOMi HOG000233025.
    HOVERGENi HBG052453.
    InParanoidi Q05512.
    KOi K08798.
    OrthoDBi EOG79CXXX.
    PhylomeDBi Q05512.

    Miscellaneous databases

    NextBioi 284516.
    PROi Q05512.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q05512.
    Bgeei Q05512.
    CleanExi MM_MARK2.
    Genevestigatori Q05512.

    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. "Emk, a protein kinase with homologs in yeast maps to mouse chromosome 19."
      Inglis J.D., Lee M., Hill R.E.
      Mamm. Genome 4:401-403(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Embryo.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
      Strain: NOD.
      Tissue: Spleen.
    3. "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 3).
      Strain: 129.
      Tissue: Mammary gland.
    4. "EMK protein kinase-null mice: dwarfism and hypofertility associated with alterations in the somatotrope and prolactin pathways."
      Bessone S., Vidal F., Le Bouc Y., Epelbaum J., Bluet-Pajot M.T., Darmon M.
      Dev. Biol. 214:87-101(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    5. "Immune system dysfunction and autoimmune disease in mice lacking Emk (Par-1) protein kinase."
      Hurov J.B., Stappenbeck T.S., Zmasek C.M., White L.S., Ranganath S.H., Russell J.H., Chan A.C., Murphy K.M., Piwnica-Worms H.
      Mol. Cell. Biol. 21:3206-3219(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    7. "Loss of the Par-1b/MARK2 polarity kinase leads to increased metabolic rate, decreased adiposity, and insulin hypersensitivity in vivo."
      Hurov J.B., Huang M., White L.S., Lennerz J., Choi C.S., Cho Y.R., Kim H.J., Prior J.L., Piwnica-Worms D., Cantley L.C., Kim J.K., Shulman G.I., Piwnica-Worms H.
      Proc. Natl. Acad. Sci. U.S.A. 104:5680-5685(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    8. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMARK2_MOUSE
    AccessioniPrimary (citable) accession number: Q05512
    Secondary accession number(s): Q3T9L3, Q6PDR4, Q8BR95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 148 of the entry and version 3 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