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Q8VHJ5

- MARK1_MOUSE

UniProt

Q8VHJ5 - MARK1_MOUSE

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Protein

Serine/threonine-protein kinase MARK1

Gene
Mark1, Emk3, Kiaa1477
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Magnesium By similarity.By similarity

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891ATP By similarityBy similarity
Active sitei182 – 1821Proton acceptor By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi66 – 749ATP By similarityBy similarity

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase MARK1 (EC:2.7.11.1, EC:2.7.11.26)
Alternative name(s):
ELKL motif serine/threonine-protein kinase 3
MAP/microtubule affinity-regulating kinase 1
PAR1 homolog c
Short name:
Par-1c
Short name:
mPar-1c
Gene namesi
Name:Mark1
Synonyms:Emk3, Kiaa1477
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:2664902. Mark1.

Subcellular locationi

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51Phosphothreonine By similarity
Modified residuei208 – 2081Phosphothreonine By similarity
Modified residuei215 – 2151Phosphothreonine; by LKB1 and TAOK1 By similarityBy similarity
Modified residuei219 – 2191Phosphoserine; by GSK3-beta By similarityBy similarity
Modified residuei403 – 4031Phosphoserine1 Publication
Modified residuei588 – 5881Phosphoserine By similarity
Modified residuei613 – 6131Phosphothreonine; by PKC/PRKCZ By similarity
Modified residuei666 – 6661Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8VHJ5.
PRIDEiQ8VHJ5.

PTM databases

PhosphoSiteiQ8VHJ5.

Expressioni

Gene expression databases

BgeeiQ8VHJ5.
CleanExiMM_MARK1.
GenevestigatoriQ8VHJ5.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini60 – 311252Protein kinaseAdd
BLAST
Domaini329 – 37042UBAAdd
BLAST
Domaini746 – 79550KA1Add
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.
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.

Sequence similaritiesi

Contains 1 UBA domain.

Phylogenomic databases

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

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q8VHJ5-1 [UniParc]FASTAAdd to Basket

« Hide

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

Sequence conflict

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

Sequence databases

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

Genome annotation databases

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

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSitei Q8VHJ5.

Proteomic databases

PaxDbi Q8VHJ5.
PRIDEi Q8VHJ5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

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

Miscellaneous databases

NextBioi 378347.
PROi Q8VHJ5.
SOURCEi Search...

Gene expression databases

Bgeei Q8VHJ5.
CleanExi MM_MARK1.
Genevestigatori Q8VHJ5.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Mus musculus Emk3/Mark1 mRNA."
    Darmon Y.M., Le Morvan V.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-795.
    Tissue: Fetal brain.
  4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiMARK1_MOUSE
AccessioniPrimary (citable) accession number: Q8VHJ5
Secondary accession number(s): E9QL17, Q69ZI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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