Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine/threonine-protein kinase MARK1

Gene

Mark1

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

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:Mark1Imported
Synonyms:Emk3Imported, Kiaa1477
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2664902. Mark1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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.
MINTiMINT-4120175.
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

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

eggNOGiKOG0586. Eukaryota.
ENOG410XNQ0. LUCA.
GeneTreeiENSGT00790000122947.
HOVERGENiHBG052453.
InParanoidiQ8VHJ5.
KOiK08798.
OMAiLPRCRNS.
OrthoDBiEOG091G0D1E.
TreeFamiTF315213.

Family and domain databases

Gene3Di3.30.310.80. 1 hit.
InterProiIPR028375. KA1/Ssp2_C.
IPR001772. KA1_dom.
IPR011009. Kinase-like_dom.
IPR033624. MARK/par1.
IPR033627. MARK1.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR015940. UBA.
[Graphical view]
PANTHERiPTHR24346. PTHR24346. 1 hit.
PTHR24346:SF21. PTHR24346:SF21. 1 hit.
PfamiPF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00627. UBA. 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

        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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ8VHJ5.
SMRiQ8VHJ5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230554. 2 interactors.
IntActiQ8VHJ5. 3 interactors.
MINTiMINT-4120175.
STRINGi10090.ENSMUSP00000027929.

PTM databases

iPTMnetiQ8VHJ5.
PhosphoSitePlusiQ8VHJ5.

Proteomic databases

MaxQBiQ8VHJ5.
PaxDbiQ8VHJ5.
PRIDEiQ8VHJ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4139.
MGIiMGI:2664902. Mark1.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0586. Eukaryota.
ENOG410XNQ0. LUCA.
GeneTreeiENSGT00790000122947.
HOVERGENiHBG052453.
InParanoidiQ8VHJ5.
KOiK08798.
OMAiLPRCRNS.
OrthoDBiEOG091G0D1E.
TreeFamiTF315213.

Miscellaneous databases

PROiQ8VHJ5.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026620.
CleanExiMM_MARK1.
ExpressionAtlasiQ8VHJ5. baseline and differential.
GenevisibleiQ8VHJ5. MM.

Family and domain databases

Gene3Di3.30.310.80. 1 hit.
InterProiIPR028375. KA1/Ssp2_C.
IPR001772. KA1_dom.
IPR011009. Kinase-like_dom.
IPR033624. MARK/par1.
IPR033627. MARK1.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR015940. UBA.
[Graphical view]
PANTHERiPTHR24346. PTHR24346. 1 hit.
PTHR24346:SF21. PTHR24346:SF21. 1 hit.
PfamiPF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00627. UBA. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 129 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.