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Q8VHJ5 (MARK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase MARK1

EC=2.7.11.1
EC=2.7.11.26
Alternative name(s):
ELKL motif serine/threonine-protein kinase 3
MAP/microtubule affinity-regulating kinase 1
PAR1 homolog c
Short name=Par-1c
Short name=mPar-1c
Gene names
Name:Mark1
Synonyms:Emk3, Kiaa1477
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length795 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. UniProtKB Q9POL2

ATP + [tau protein] = ADP + [tau protein] phosphate.

Cofactor

Magnesium By similarity. UniProtKB Q9POL2

Enzyme regulation

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

Subcellular location

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

Domain

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.

The KA1 domain mediates binding to phospholipids and targeting to membranes. Binds phosphatidic acid (PA), phosphatidylserine (PtdSer) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) By similarity.

Post-translational modification

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

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.

Contains 1 KA1 (kinase-associated) domain.

Contains 1 protein kinase domain.

Contains 1 UBA domain.

Ontologies

Keywords
   Biological processWnt signaling pathway
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
   LigandATP-binding
Lipid-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

neuron migration

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

magnesium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidic acid binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-4,5-bisphosphate binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylserine binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

tau-protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 795795Serine/threonine-protein kinase MARK1
PRO_0000086299

Regions

Domain60 – 311252Protein kinase
Domain329 – 37042UBA
Domain746 – 79550KA1
Nucleotide binding66 – 749ATP By similarity UniProtKB Q9H0K1

Sites

Active site1821Proton acceptor By similarity UniProtKB Q9H0K1
Binding site891ATP By similarity UniProtKB O08678

Amino acid modifications

Modified residue51Phosphothreonine By similarity
Modified residue2081Phosphothreonine By similarity
Modified residue2151Phosphothreonine; by LKB1 and TAOK1 By similarity UniProtKB O08678
Modified residue2191Phosphoserine; by GSK3-beta By similarity UniProtKB O08678
Modified residue4031Phosphoserine Ref.4
Modified residue5881Phosphoserine By similarity
Modified residue6131Phosphothreonine; by PKC/PRKCZ By similarity
Modified residue6661Phosphoserine Ref.4

Experimental info

Sequence conflict321A → T in AAL50826. Ref.1
Sequence conflict401L → I in AAL50826. Ref.1
Sequence conflict1101I → T in BAD32459. Ref.3
Sequence conflict2761I → V in AAL50826. Ref.1
Sequence conflict3181E → D in BAD32459. Ref.3
Sequence conflict3311S → N in AAL50826. Ref.1
Sequence conflict3851S → N in AAL50826. Ref.1
Sequence conflict4541G → D in AAL50826. Ref.1
Sequence conflict5791G → GS in BAD32459. Ref.3
Sequence conflict6301P → R in AAL50826. Ref.1
Sequence conflict6411F → L in AAL50826. Ref.1
Sequence conflict6741A → T in AAL50826. Ref.1
Sequence conflict6831D → E in AAL50826. Ref.1
Sequence conflict6901D → E in AAL50826. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8VHJ5 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: F43F2B541C346697

FASTA79588,335
        10         20         30         40         50         60 
MSARTPLPTV NERDTENHTS VDGYTETHIP PAKSSSRQNL PRCRNSITSA TDEQPHIGNY 

        70         80         90        100        110        120 
RLQKTIGKGN FAKVKLARHV LTGREVAVKI IDKTQLNPTS LQKLFREVRI MKILNHPNIV 

       130        140        150        160        170        180 
KLFEVIETEK TLYLVMEYAS GGEVFDYLVA HGRMKEKEAR AKFRQIVSAV QYCHQKCIVH 

       190        200        210        220        230        240 
RDLKAENLLL DADMNIKIAD FGFSNEFTVG NKLDTFCGSP PYAAPELFQG KKYDGPEVDV 

       250        260        270        280        290        300 
WSLGVILYTL VSGSLPFDGQ NLKELRERVL RGKYRIPFYM STDCENLLKK LLVLNPIKRG 

       310        320        330        340        350        360 
SLEQIMKDRW MNVGHEEEEL KPYSEPELDL SDAKRIDIMV TMGFARDEIN DALVSQKYDE 

       370        380        390        400        410        420 
VMATYILLGR KPPEFEGGES LSSGSLCQRS RPSSDLNNST LQSPAHLKVQ RSISANQKQR 

       430        440        450        460        470        480 
RFSDHAGPSI PPAVSYTKRP QANSVESEQK EEWGKDTARR LGSTTVGSKS EVTASPLVGP 

       490        500        510        520        530        540 
DRKKSTASPS NNVYSGGSMA RRNTYVCERS TDRYAALQNG RDSSLTEMSA SSMSSAGSTV 

       550        560        570        580        590        600 
ASAGPSARPR HQKSMSTSGH PIKVTLPTIK DGSEAYRPGA AQRVPAASPS AHSISASTPD 

       610        620        630        640        650        660 
RTRFPRGSSS RSTFHGEQLR ERRSAAYNGP PASPSHETGA FAHARRGTST GIISKITSKF 

       670        680        690        700        710        720 
VRRDPSEGEA SGRADTARGS SGDPKERDKD EGKEAKPRSL RFTWSMKTTS SMDPNDMLRE 

       730        740        750        760        770        780 
IRKVLDANTC DYEQKERFLL FCVHGDARQD SLVQWEMEVC KLPRLSLNGV RFKRISGTSI 

       790 
AFKNIASKIA NELKL 

« Hide

References

« Hide 'large scale' references
[1]"Mus musculus Emk3/Mark1 mRNA."
Darmon Y.M., Le Morvan V.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-795.
Tissue: Fetal brain.
[4]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF453686 mRNA. Translation: AAL50826.1.
AC117826 Genomic DNA. No translation available.
AC131992 Genomic DNA. No translation available.
AK173181 mRNA. Translation: BAD32459.1.
CCDSCCDS35817.1.
RefSeqNP_663490.2. NM_145515.2.
UniGeneMm.7445.

3D structure databases

ProteinModelPortalQ8VHJ5.
SMRQ8VHJ5. Positions 1-371, 696-795.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid230554. 2 interactions.
IntActQ8VHJ5. 2 interactions.
MINTMINT-4120175.

PTM databases

PhosphoSiteQ8VHJ5.

Proteomic databases

PaxDbQ8VHJ5.
PRIDEQ8VHJ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027929; ENSMUSP00000027929; ENSMUSG00000026620.
GeneID226778.
KEGGmmu:226778.
UCSCuc007dyt.2. mouse.

Organism-specific databases

CTD4139.
MGIMGI:2664902. Mark1.
RougeSearch...

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000110535.
HOVERGENHBG052453.
InParanoidQ8VHJ5.
KOK08798.
OMAEHPHIGN.
OrthoDBEOG79CXXX.
TreeFamTF315213.

Gene expression databases

BgeeQ8VHJ5.
CleanExMM_MARK1.
GenevestigatorQ8VHJ5.

Family and domain databases

Gene3D3.30.310.80. 1 hit.
InterProIPR028375. 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]
PfamPF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]
SUPFAMSSF103243. SSF103243. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50032. 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]
ProtoNetSearch...

Other

NextBio378347.
PROQ8VHJ5.
SOURCESearch...

Entry information

Entry nameMARK1_MOUSE
AccessionPrimary (citable) accession number: Q8VHJ5
Secondary accession number(s): E9QL17, Q69ZI7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot