Skip Header

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

Q9P0L2

- MARK1_HUMAN

UniProt

Q9P0L2 - MARK1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Serine/threonine-protein kinase MARK1

Gene

MARK1

Organism
Homo sapiens (Human)
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).2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication
ATP + [tau protein] = ADP + [tau protein] phosphate.

Cofactori

Magnesium.By similarity

Enzyme regulationi

Inhibited by phosphorylation at Ser-219 (By similarity). Activated by phosphorylation on Thr-215.By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891ATPBy similarityPROSITE-ProRule annotation
Active sitei182 – 1821Proton acceptorBy similarityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi66 – 749ATPBy similarityPROSITE-ProRule annotation

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. cytoskeleton organization Source: UniProtKB
  2. intracellular signal transduction Source: UniProtKB
  3. microtubule cytoskeleton organization Source: Ensembl
  4. neuron migration Source: UniProtKB
  5. protein phosphorylation Source: UniProtKB
  6. 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

Enzyme and pathway databases

SignaLinkiQ9P0L2.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase MARK1 (EC:2.7.11.1, EC:2.7.11.26)
Alternative name(s):
MAP/microtubule affinity-regulating kinase 1
PAR1 homolog c
Short name:
Par-1c
Short name:
Par1c
Gene namesi
Name:MARK1Imported
Synonyms:KIAA1477Imported, MARKImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6896. MARK1.

Subcellular locationi

Cell membrane 1 Publication; Peripheral membrane protein 1 Publication. Cytoplasmcytoskeleton By similarity
Note: Appears to localize to an intracellular network.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB
  3. microtubule cytoskeleton Source: ProtInc
  4. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Genetic variations in MARK1 may be associated with susceptibility to autism. MARK1 is overexpressed in the prefrontal cortex of patients with autism and causes changes in the function of cortical dendrites.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi215 – 2151T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. 1 Publication
Mutagenesisi215 – 2151T → E: Constitutively active. 1 Publication
Mutagenesisi698 – 6981R → S: Impairs phospholipid-binding, targeting to membrane and vesicle-binding; when associated with S-701. 1 Publication
Mutagenesisi701 – 7011R → S: Impairs phospholipid-binding, targeting to membrane and vesicle-binding; when associated with S-698. 1 Publication
Mutagenesisi771 – 7733RFK → AFA: Impairs phospholipid-binding. 1 Publication

Organism-specific databases

PharmGKBiPA30639.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 795795Serine/threonine-protein kinase MARK1PRO_0000086298Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51Phosphothreonine1 Publication
Modified residuei208 – 2081Phosphothreonine1 Publication
Modified residuei215 – 2151Phosphothreonine; by LKB1 and TAOK11 Publication
Modified residuei219 – 2191Phosphoserine; by GSK3-beta
Modified residuei403 – 4031Phosphoserine1 Publication
Modified residuei588 – 5881Phosphoserine1 Publication
Modified residuei613 – 6131Phosphothreonine; by PKC/PRKCZBy similarity
Modified residuei666 – 6661PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation at Thr-613 by PRKCZ/aPKC in polarized epithelial cells inhibits the kinase activity (By similarity). 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.By similarity4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9P0L2.
PaxDbiQ9P0L2.
PRIDEiQ9P0L2.

PTM databases

PhosphoSiteiQ9P0L2.

Expressioni

Tissue specificityi

Highly expressed in heart, skeletal muscle, brain, fetal brain and fetal kidney.1 Publication

Gene expression databases

BgeeiQ9P0L2.
CleanExiHS_MARK1.
ExpressionAtlasiQ9P0L2. baseline and differential.
GenevestigatoriQ9P0L2.

Organism-specific databases

HPAiHPA007421.
HPA008061.

Interactioni

Protein-protein interaction databases

BioGridi110309. 14 interactions.
DIPiDIP-39777N.
IntActiQ9P0L2. 8 interactions.
MINTiMINT-3975018.
STRINGi9606.ENSP00000355884.

Structurei

Secondary structure

1
795
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi60 – 689Combined sources
Beta strandi70 – 7910Combined sources
Turni80 – 823Combined sources
Beta strandi85 – 928Combined sources
Helixi98 – 11316Combined sources
Beta strandi122 – 1276Combined sources
Beta strandi129 – 1368Combined sources
Helixi144 – 1518Combined sources
Helixi156 – 17621Combined sources
Helixi185 – 1873Combined sources
Beta strandi188 – 1903Combined sources
Beta strandi196 – 1983Combined sources
Beta strandi221 – 2233Combined sources
Helixi225 – 2295Combined sources
Helixi236 – 25217Combined sources
Helixi262 – 27110Combined sources
Helixi282 – 29110Combined sources
Helixi296 – 2983Combined sources
Helixi302 – 3065Combined sources
Helixi309 – 3124Combined sources
Beta strandi316 – 3183Combined sources
Helixi333 – 34210Combined sources
Helixi346 – 3549Combined sources
Helixi360 – 3678Combined sources
Helixi714 – 72714Combined sources
Beta strandi731 – 7366Combined sources
Beta strandi739 – 7457Combined sources
Turni747 – 7504Combined sources
Beta strandi753 – 76210Combined sources
Helixi763 – 7653Combined sources
Beta strandi767 – 77711Combined sources
Helixi779 – 79214Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HAKX-ray2.60A/B/C/D/E/F/G/H45-371[»]
3OSEX-ray1.70A683-795[»]
ProteinModelPortaliQ9P0L2.
SMRiQ9P0L2. Positions 29-371, 696-795.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P0L2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini60 – 311252Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini325 – 37046UBAPROSITE-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).1 Publication

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.
GeneTreeiENSGT00760000118892.
HOVERGENiHBG052453.
InParanoidiQ9P0L2.
KOiK08798.
OMAiEHPHIGN.
OrthoDBiEOG79CXXX.
PhylomeDBiQ9P0L2.
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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9P0L2-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSARTPLPTV NERDTENHTS VDGYTEPHIQ PTKSSSRQNI 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 QYCHQKYIVH RDLKAENLLL DGDMNIKIAD
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 KPYTEPDPDF NDTKRIDIMV TMGFARDEIN
360 370 380 390 400
DALINQKYDE VMATYILLGR KPPEFEGGES LSSGNLCQRS RPSSDLNNST
410 420 430 440 450
LQSPAHLKVQ RSISANQKQR RFSDHAGPSI PPAVSYTKRP QANSVESEQK
460 470 480 490 500
EEWDKDVARK LGSTTVGSKS EMTASPLVGP ERKKSSTIPS NNVYSGGSMA
510 520 530 540 550
RRNTYVCERT TDRYVALQNG KDSSLTEMSV SSISSAGSSV ASAVPSARPR
560 570 580 590 600
HQKSMSTSGH PIKVTLPTIK DGSEAYRPGT TQRVPAASPS AHSISTATPD
610 620 630 640 650
RTRFPRGSSS RSTFHGEQLR ERRSVAYNGP PASPSHETGA FAHARRGTST
660 670 680 690 700
GIISKITSKF VRRDPSEGEA SGRTDTSRST SGEPKERDKE EGKDSKPRSL
710 720 730 740 750
RFTWSMKTTS SMDPNDMMRE IRKVLDANNC DYEQKERFLL FCVHGDARQD
760 770 780 790
SLVQWEMEVC KLPRLSLNGV RFKRISGTSI AFKNIASKIA NELKL
Length:795
Mass (Da):89,003
Last modified:January 23, 2007 - v2
Checksum:i71BF6EB76912631B
GO
Isoform 2Curated (identifier: Q9P0L2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-135: Missing.
     663-677: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:645
Mass (Da):72,073
Checksum:i7AE395507519DCF6
GO
Isoform 3Curated (identifier: Q9P0L2-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     120-141: Missing.
     663-677: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:758
Mass (Da):84,911
Checksum:iD6F1BCD8E884661D
GO

Sequence cautioni

The sequence BAB55152.1 differs from that shown. Reason: Frameshift at position 763.
The sequence BAA96001.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161E → V in AAF72103. 1 PublicationCurated
Sequence conflicti20 – 201S → T in AAF72103. 1 PublicationCurated
Sequence conflicti522 – 5221D → N in BAB55152. (PubMed:14702039)Curated
Sequence conflicti544 – 5441V → A in BAB55152. (PubMed:14702039)Curated
Sequence conflicti763 – 7631P → A in BAB55152. (PubMed:14702039)Curated
Sequence conflicti794 – 7941K → M in BAA96001. (PubMed:10819331)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti233 – 2331Y → C in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040760
Natural varianti355 – 3551N → T in an ovarian serous carcinoma sample; somatic mutation. 1 Publication
VAR_040761
Natural varianti530 – 5301V → M.1 Publication
Corresponds to variant rs56212551 [ dbSNP | Ensembl ].
VAR_040762
Natural varianti578 – 5781P → L.1 Publication
Corresponds to variant rs55691439 [ dbSNP | Ensembl ].
VAR_040763
Natural varianti645 – 6451R → G.
Corresponds to variant rs12123778 [ dbSNP | Ensembl ].
VAR_030018
Natural varianti691 – 6911E → G.1 Publication
Corresponds to variant rs55688276 [ dbSNP | Ensembl ].
VAR_040764

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 135135Missing in isoform 2. 1 PublicationVSP_051702Add
BLAST
Alternative sequencei120 – 14122Missing in isoform 3. 1 PublicationVSP_051703Add
BLAST
Alternative sequencei663 – 67715Missing in isoform 2 and isoform 3. 2 PublicationsVSP_051704Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF154845 mRNA. Translation: AAF72103.1.
AB040910 mRNA. Translation: BAA96001.1. Different initiation.
AK027493 mRNA. Translation: BAB55152.1. Frameshift.
AL592406, AC096640 Genomic DNA. Translation: CAH72462.1.
AL592406, AC096640 Genomic DNA. Translation: CAH72463.1.
CH471100 Genomic DNA. Translation: EAW93299.1.
CH471100 Genomic DNA. Translation: EAW93300.1.
CH471100 Genomic DNA. Translation: EAW93302.1.
BC113869 mRNA. Translation: AAI13870.1.
BC114478 mRNA. Translation: AAI14479.1.
CCDSiCCDS31029.2. [Q9P0L2-1]
CCDS65789.1. [Q9P0L2-3]
RefSeqiNP_001273057.1. NM_001286128.1. [Q9P0L2-3]
NP_061120.3. NM_018650.4. [Q9P0L2-1]
UniGeneiHs.497806.

Genome annotation databases

EnsembliENST00000366917; ENSP00000355884; ENSG00000116141. [Q9P0L2-1]
ENST00000366918; ENSP00000355885; ENSG00000116141. [Q9P0L2-3]
GeneIDi4139.
KEGGihsa:4139.
UCSCiuc001hmm.4. human. [Q9P0L2-3]
uc001hmn.4. human. [Q9P0L2-1]

Polymorphism databases

DMDMi124056494.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF154845 mRNA. Translation: AAF72103.1 .
AB040910 mRNA. Translation: BAA96001.1 . Different initiation.
AK027493 mRNA. Translation: BAB55152.1 . Frameshift.
AL592406 , AC096640 Genomic DNA. Translation: CAH72462.1 .
AL592406 , AC096640 Genomic DNA. Translation: CAH72463.1 .
CH471100 Genomic DNA. Translation: EAW93299.1 .
CH471100 Genomic DNA. Translation: EAW93300.1 .
CH471100 Genomic DNA. Translation: EAW93302.1 .
BC113869 mRNA. Translation: AAI13870.1 .
BC114478 mRNA. Translation: AAI14479.1 .
CCDSi CCDS31029.2. [Q9P0L2-1 ]
CCDS65789.1. [Q9P0L2-3 ]
RefSeqi NP_001273057.1. NM_001286128.1. [Q9P0L2-3 ]
NP_061120.3. NM_018650.4. [Q9P0L2-1 ]
UniGenei Hs.497806.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HAK X-ray 2.60 A/B/C/D/E/F/G/H 45-371 [» ]
3OSE X-ray 1.70 A 683-795 [» ]
ProteinModelPortali Q9P0L2.
SMRi Q9P0L2. Positions 29-371, 696-795.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110309. 14 interactions.
DIPi DIP-39777N.
IntActi Q9P0L2. 8 interactions.
MINTi MINT-3975018.
STRINGi 9606.ENSP00000355884.

Chemistry

BindingDBi Q9P0L2.
ChEMBLi CHEMBL5940.
GuidetoPHARMACOLOGYi 2097.

PTM databases

PhosphoSitei Q9P0L2.

Polymorphism databases

DMDMi 124056494.

Proteomic databases

MaxQBi Q9P0L2.
PaxDbi Q9P0L2.
PRIDEi Q9P0L2.

Protocols and materials databases

DNASUi 4139.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366917 ; ENSP00000355884 ; ENSG00000116141 . [Q9P0L2-1 ]
ENST00000366918 ; ENSP00000355885 ; ENSG00000116141 . [Q9P0L2-3 ]
GeneIDi 4139.
KEGGi hsa:4139.
UCSCi uc001hmm.4. human. [Q9P0L2-3 ]
uc001hmn.4. human. [Q9P0L2-1 ]

Organism-specific databases

CTDi 4139.
GeneCardsi GC01P220701.
HGNCi HGNC:6896. MARK1.
HPAi HPA007421.
HPA008061.
MIMi 606511. gene.
neXtProti NX_Q9P0L2.
PharmGKBi PA30639.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118892.
HOVERGENi HBG052453.
InParanoidi Q9P0L2.
KOi K08798.
OMAi EHPHIGN.
OrthoDBi EOG79CXXX.
PhylomeDBi Q9P0L2.
TreeFami TF315213.

Enzyme and pathway databases

SignaLinki Q9P0L2.

Miscellaneous databases

ChiTaRSi MARK1. human.
EvolutionaryTracei Q9P0L2.
GeneWikii MARK1.
GenomeRNAii 4139.
NextBioi 16256.
PROi Q9P0L2.
SOURCEi Search...

Gene expression databases

Bgeei Q9P0L2.
CleanExi HS_MARK1.
ExpressionAtlasi Q9P0L2. baseline and differential.
Genevestigatori Q9P0L2.

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.
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. "LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1."
    Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A., Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G., Alessi D.R.
    EMBO J. 23:833-843(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME REGULATION, PHOSPHORYLATION AT THR-215, MUTAGENESIS OF THR-215.
  2. "Cloning and isolating human MARK."
    Zhou H.J., Huang X.W., Zhou Y., Hu S.L., Yuan J.G., Qiang B.Q.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain1 Publication.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  8. "MARK - a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption."
    Drewes G., Ebneth A., Preuss U., Mandelkow E.-M., Mandelkow E.
    Cell 89:297-308(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. "Microtubule-affinity regulating kinase (MARK) is tightly associated with neurofibrillary tangles in Alzheimer brain: a fluorescence resonance energy transfer study."
    Chin J.Y., Knowles R.B., Schneider A., Drewes G., Mandelkow E.M., Hyman B.T.
    J. Neuropathol. Exp. Neurol. 59:966-971(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NEUROFIBRILLARY TANGLES IN ALZHEIMER BRAIN.
  10. "PAR-1 is a Dishevelled-associated kinase and a positive regulator of Wnt signalling."
    Sun T.-Q., Lu B., Feng J.-J., Reinhard C., Jan Y.N., Fantl W.J., Williams L.T.
    Nat. Cell Biol. 3:628-636(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Suppression of tubulin polymerization by the LKB1-microtubule-associated protein/microtubule affinity-regulating kinase signaling."
    Kojima Y., Miyoshi H., Clevers H.C., Oshima M., Aoki M., Taketo M.M.
    J. Biol. Chem. 282:23532-23540(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-208, ENZYME REGULATION, FUNCTION.
  12. "Convergent evidence identifying MAP/microtubule affinity-regulating kinase 1 (MARK1) as a susceptibility gene for autism."
    Maussion G., Carayol J., Lepagnol-Bestel A.M., Tores F., Loe-Mie Y., Milbreta U., Rousseau F., Fontaine K., Renaud J., Moalic J.M., Philippi A., Chedotal A., Gorwood P., Ramoz N., Hager J., Simonneau M.
    Hum. Mol. Genet. 17:2541-2551(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN AUTISM.
  13. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5 AND SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "The tau of MARK: a polarized view of the cytoskeleton."
    Matenia D., Mandelkow E.M.
    Trends Biochem. Sci. 34:332-342(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  18. "Structure and function of polarity-inducing kinase family MARK/Par-1 within the branch of AMPK/Snf1-related kinases."
    Marx A., Nugoor C., Panneerselvam S., Mandelkow E.
    FASEB J. 24:1637-1648(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Structural variations in the catalytic and ubiquitin-associated domains of microtubule-associated protein/microtubule affinity regulating kinase (MARK) 1 and MARK2."
    Marx A., Nugoor C., Muller J., Panneerselvam S., Timm T., Bilang M., Mylonas E., Svergun D.I., Mandelkow E.M., Mandelkow E.
    J. Biol. Chem. 281:27586-27599(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 45-371.
  22. "Kinase associated-1 domains drive MARK/PAR1 kinases to membrane targets by binding acidic phospholipids."
    Moravcevic K., Mendrola J.M., Schmitz K.R., Wang Y.H., Slochower D., Janmey P.A., Lemmon M.A.
    Cell 143:966-977(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 683-795, DOMAIN KA1, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-698; ARG-701; 771-ARG--LYS-773 AND 773-LYS-ARG-774.
  23. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-233; THR-355; MET-530; LEU-578 AND GLY-691.

Entry informationi

Entry nameiMARK1_HUMAN
AccessioniPrimary (citable) accession number: Q9P0L2
Secondary accession number(s): D3DTB0
, D3DTB1, Q2HIY1, Q5VTF9, Q5VTG0, Q96SW9, Q9P251
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: January 23, 2007
Last modified: October 29, 2014
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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Phosphorylation of MAPT/tau by MARK1 could play a role in early steps of Alzheimer disease. Pathological aggregation of MAPT/tau to neurofibrillary tangles, filamentous structures consisting of paired helical filaments (PHFs), is one of the hallmarks of Alzheimer disease. Hyperphosphorylation by MARK1 could be the initial step for this abnormal aggregation of tau in Alzheimer disease and animal models of tauopathy (PubMed:11089574).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3