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Protein

Serine/threonine-protein kinase MARK1

Gene

Mark1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarity

Enzyme regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei89ATPPROSITE-ProRule annotationBy similarity1
Active sitei182Proton acceptorPROSITE-ProRule annotationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi66 – 74ATPPROSITE-ProRule annotationBy similarity9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processWnt signaling pathway
LigandATP-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:Mark1Imported
Synonyms:Emk3Imported, Kiaa1477
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2664902 Mark1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000862991 – 795Serine/threonine-protein kinase MARK1Add BLAST795

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5PhosphothreonineBy similarity1
Modified residuei208PhosphothreonineBy similarity1
Modified residuei215Phosphothreonine; by LKB1 and TAOK1By similarity1
Modified residuei219Phosphoserine; by GSK3-betaBy similarity1
Modified residuei382PhosphoserineCombined sources1
Modified residuei390PhosphoserineCombined sources1
Modified residuei393PhosphoserineCombined sources1
Modified residuei403PhosphoserineCombined sources1
Modified residuei423PhosphoserineCombined sources1
Modified residuei444PhosphoserineBy similarity1
Modified residuei475PhosphoserineCombined sources1
Modified residuei588PhosphoserineBy similarity1
Modified residuei613Phosphothreonine; by PKC/PRKCZBy similarity1
Modified residuei666PhosphoserineCombined sources1

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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8VHJ5
PaxDbiQ8VHJ5
PRIDEiQ8VHJ5

PTM databases

iPTMnetiQ8VHJ5
PhosphoSitePlusiQ8VHJ5

Expressioni

Gene expression databases

BgeeiENSMUSG00000026620
CleanExiMM_MARK1
ExpressionAtlasiQ8VHJ5 baseline and differential
GenevisibleiQ8VHJ5 MM

Interactioni

Protein-protein interaction databases

BioGridi230554, 2 interactors
IntActiQ8VHJ5, 3 interactors
MINTiQ8VHJ5
STRINGi10090.ENSMUSP00000027929

Structurei

3D structure databases

ProteinModelPortaliQ8VHJ5
SMRiQ8VHJ5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini60 – 311Protein kinasePROSITE-ProRule annotationAdd BLAST252
Domaini329 – 370UBAPROSITE-ProRule annotationAdd BLAST42
Domaini746 – 795KA1PROSITE-ProRule annotationAdd BLAST50

Domaini

The UBA domain does not seem to bind ubiquitin and ubiquitin-like and might play a role in regulating the enzyme conformation and localization. Activation of the kinase activity following phosphorylation at Thr-208 is accompanied by a conformational change that alters the orientation of the UBA domain with respect to the catalytic domain (By similarity).By similarity
The KA1 domain mediates binding to phospholipids and targeting to membranes. Binds phosphatidic acid (PA), phosphatidylserine (PtdSer) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) (By similarity).By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0586 Eukaryota
ENOG410XNQ0 LUCA
GeneTreeiENSGT00900000140806
HOVERGENiHBG052453
InParanoidiQ8VHJ5
KOiK08798
OMAiLPRCRNS
OrthoDBiEOG091G0D1E
TreeFamiTF315213

Family and domain databases

InterProiView protein in InterPro
IPR028375 KA1/Ssp2_C
IPR001772 KA1_dom
IPR011009 Kinase-like_dom_sf
IPR033627 MARK1
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
IPR015940 UBA
PANTHERiPTHR24346:SF21 PTHR24346:SF21, 1 hit
PfamiView protein in Pfam
PF02149 KA1, 1 hit
PF00069 Pkinase, 1 hit
PF00627 UBA, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SM00165 UBA, 1 hit
SUPFAMiSSF103243 SSF103243, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
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

Sequencei

Sequence statusi: Complete.

Q8VHJ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSARTPLPTV NERDTENHTS VDGYTETHIP PAKSSSRQNL PRCRNSITSA
60 70 80 90 100
TDEQPHIGNY RLQKTIGKGN FAKVKLARHV LTGREVAVKI IDKTQLNPTS
110 120 130 140 150
LQKLFREVRI MKILNHPNIV KLFEVIETEK TLYLVMEYAS GGEVFDYLVA
160 170 180 190 200
HGRMKEKEAR AKFRQIVSAV QYCHQKCIVH RDLKAENLLL DADMNIKIAD
210 220 230 240 250
FGFSNEFTVG NKLDTFCGSP PYAAPELFQG KKYDGPEVDV WSLGVILYTL
260 270 280 290 300
VSGSLPFDGQ NLKELRERVL RGKYRIPFYM STDCENLLKK LLVLNPIKRG
310 320 330 340 350
SLEQIMKDRW MNVGHEEEEL KPYSEPELDL SDAKRIDIMV TMGFARDEIN
360 370 380 390 400
DALVSQKYDE VMATYILLGR KPPEFEGGES LSSGSLCQRS RPSSDLNNST
410 420 430 440 450
LQSPAHLKVQ RSISANQKQR RFSDHAGPSI PPAVSYTKRP QANSVESEQK
460 470 480 490 500
EEWGKDTARR LGSTTVGSKS EVTASPLVGP DRKKSTASPS NNVYSGGSMA
510 520 530 540 550
RRNTYVCERS TDRYAALQNG RDSSLTEMSA SSMSSAGSTV ASAGPSARPR
560 570 580 590 600
HQKSMSTSGH PIKVTLPTIK DGSEAYRPGA AQRVPAASPS AHSISASTPD
610 620 630 640 650
RTRFPRGSSS RSTFHGEQLR ERRSAAYNGP PASPSHETGA FAHARRGTST
660 670 680 690 700
GIISKITSKF VRRDPSEGEA SGRADTARGS SGDPKERDKD EGKEAKPRSL
710 720 730 740 750
RFTWSMKTTS SMDPNDMLRE IRKVLDANTC DYEQKERFLL FCVHGDARQD
760 770 780 790
SLVQWEMEVC KLPRLSLNGV RFKRISGTSI AFKNIASKIA NELKL
Length:795
Mass (Da):88,335
Last modified:July 27, 2011 - v2
Checksum:iF43F2B541C346697
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti32A → T in AAL50826 (Ref. 1) Curated1
Sequence conflicti40L → I in AAL50826 (Ref. 1) Curated1
Sequence conflicti110I → T in BAD32459 (PubMed:15368895).Curated1
Sequence conflicti276I → V in AAL50826 (Ref. 1) Curated1
Sequence conflicti318E → D in BAD32459 (PubMed:15368895).Curated1
Sequence conflicti331S → N in AAL50826 (Ref. 1) Curated1
Sequence conflicti385S → N in AAL50826 (Ref. 1) Curated1
Sequence conflicti454G → D in AAL50826 (Ref. 1) Curated1
Sequence conflicti579G → GS in BAD32459 (PubMed:15368895).Curated1
Sequence conflicti630P → R in AAL50826 (Ref. 1) Curated1
Sequence conflicti641F → L in AAL50826 (Ref. 1) Curated1
Sequence conflicti674A → T in AAL50826 (Ref. 1) Curated1
Sequence conflicti683D → E in AAL50826 (Ref. 1) Curated1
Sequence conflicti690D → E in AAL50826 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiMARK1_MOUSE
AccessioniPrimary (citable) accession number: Q8VHJ5
Secondary accession number(s): E9QL17, Q69ZI7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: July 27, 2011
Last modified: May 23, 2018
This is version 137 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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