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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891ATPPROSITE-ProRule annotationBy similarity
Active sitei182 – 1821Proton acceptorPROSITE-ProRule annotationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi66 – 749ATPPROSITE-ProRule annotationBy similarity

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
ProteomesiUP000000589 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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 795795Serine/threonine-protein kinase MARK1PRO_0000086299Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51PhosphothreonineBy similarity
Modified residuei208 – 2081PhosphothreonineBy similarity
Modified residuei215 – 2151Phosphothreonine; by LKB1 and TAOK1By similarity
Modified residuei219 – 2191Phosphoserine; by GSK3-betaBy similarity
Modified residuei403 – 4031Phosphoserine1 Publication
Modified residuei588 – 5881PhosphoserineBy similarity
Modified residuei613 – 6131Phosphothreonine; by PKC/PRKCZBy 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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8VHJ5.
PaxDbiQ8VHJ5.
PRIDEiQ8VHJ5.

PTM databases

PhosphoSiteiQ8VHJ5.

Expressioni

Gene expression databases

BgeeiQ8VHJ5.
CleanExiMM_MARK1.
GenevisibleiQ8VHJ5. MM.

Interactioni

Protein-protein interaction databases

BioGridi230554. 2 interactions.
IntActiQ8VHJ5. 2 interactions.
MINTiMINT-4120175.
STRINGi10090.ENSMUSP00000027929.

Structurei

3D structure databases

ProteinModelPortaliQ8VHJ5.
SMRiQ8VHJ5. Positions 11-371, 696-795.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini60 – 311252Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini329 – 37042UBAPROSITE-ProRule annotationAdd
BLAST
Domaini746 – 79550KA1PROSITE-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. 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

eggNOGiCOG0515.
GeneTreeiENSGT00790000122947.
HOVERGENiHBG052453.
InParanoidiQ8VHJ5.
KOiK08798.
OMAiSDHVGPS.
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.
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

        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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321A → T in AAL50826 (Ref. 1) Curated
Sequence conflicti40 – 401L → I in AAL50826 (Ref. 1) Curated
Sequence conflicti110 – 1101I → T in BAD32459 (PubMed:15368895).Curated
Sequence conflicti276 – 2761I → V in AAL50826 (Ref. 1) Curated
Sequence conflicti318 – 3181E → D in BAD32459 (PubMed:15368895).Curated
Sequence conflicti331 – 3311S → N in AAL50826 (Ref. 1) Curated
Sequence conflicti385 – 3851S → N in AAL50826 (Ref. 1) Curated
Sequence conflicti454 – 4541G → D in AAL50826 (Ref. 1) Curated
Sequence conflicti579 – 5791G → GS in BAD32459 (PubMed:15368895).Curated
Sequence conflicti630 – 6301P → R in AAL50826 (Ref. 1) Curated
Sequence conflicti641 – 6411F → L in AAL50826 (Ref. 1) Curated
Sequence conflicti674 – 6741A → T in AAL50826 (Ref. 1) Curated
Sequence conflicti683 – 6831D → E in AAL50826 (Ref. 1) Curated
Sequence conflicti690 – 6901D → E in AAL50826 (Ref. 1) Curated

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. Positions 11-371, 696-795.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230554. 2 interactions.
IntActiQ8VHJ5. 2 interactions.
MINTiMINT-4120175.
STRINGi10090.ENSMUSP00000027929.

PTM databases

PhosphoSiteiQ8VHJ5.

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

eggNOGiCOG0515.
GeneTreeiENSGT00790000122947.
HOVERGENiHBG052453.
InParanoidiQ8VHJ5.
KOiK08798.
OMAiSDHVGPS.
OrthoDBiEOG79CXXX.
TreeFamiTF315213.

Miscellaneous databases

NextBioi378347.
PROiQ8VHJ5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VHJ5.
CleanExiMM_MARK1.
GenevisibleiQ8VHJ5. MM.

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.
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]
ProtoNetiSearch...

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: June 24, 2015
This is version 117 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

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 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.