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Q9P0L2

- MARK1_HUMAN

UniProt

Q9P0L2 - MARK1_HUMAN

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Protein
Serine/threonine-protein kinase MARK1
Gene
MARK1, KIAA1477, MARK
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.1 Publication

Enzyme regulationi

Inhibited by phosphorylation at Ser-219 By similarity. Activated by phosphorylation on Thr-215.2 Publications

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
Complete GO annotation...

GO - Biological processi

  1. Wnt signaling pathway Source: UniProtKB-KW
  2. cytoskeleton organization Source: UniProtKB
  3. intracellular signal transduction Source: UniProtKB
  4. microtubule cytoskeleton organization Source: Ensembl
  5. neuron migration Source: UniProtKB
  6. protein phosphorylation Source: UniProtKB
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:MARK1
Synonyms:KIAA1477, MARK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6896. MARK1.

Subcellular locationi

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

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 MARK1
PRO_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-betaBy similarity
Modified residuei403 – 4031Phosphoserine1 Publication
Modified residuei588 – 5881Phosphoserine1 Publication
Modified residuei613 – 6131Phosphothreonine; by PKC/PRKCZ By similarity
Modified residuei666 – 6661Phosphoserine By 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.2 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

ArrayExpressiQ9P0L2.
BgeeiQ9P0L2.
CleanExiHS_MARK1.
GenevestigatoriQ9P0L2.

Organism-specific databases

HPAiHPA007421.
HPA008061.

Interactioni

Protein-protein interaction databases

BioGridi110309. 13 interactions.
DIPiDIP-39777N.
IntActiQ9P0L2. 8 interactions.
MINTiMINT-3975018.
STRINGi9606.ENSP00000355884.

Structurei

Secondary structure

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

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.

Miscellaneous databases

EvolutionaryTraceiQ9P0L2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini60 – 311252Protein kinase
Add
BLAST
Domaini325 – 37046UBA
Add
BLAST
Domaini746 – 79550KA1
Add
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.1 Publication
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 UBA domain.

Phylogenomic databases

eggNOGiCOG0515.
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_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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (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

MSARTPLPTV NERDTENHTS VDGYTEPHIQ PTKSSSRQNI PRCRNSITSA    50
TDEQPHIGNY RLQKTIGKGN FAKVKLARHV LTGREVAVKI IDKTQLNPTS 100
LQKLFREVRI MKILNHPNIV KLFEVIETEK TLYLVMEYAS GGEVFDYLVA 150
HGRMKEKEAR AKFRQIVSAV QYCHQKYIVH RDLKAENLLL DGDMNIKIAD 200
FGFSNEFTVG NKLDTFCGSP PYAAPELFQG KKYDGPEVDV WSLGVILYTL 250
VSGSLPFDGQ NLKELRERVL RGKYRIPFYM STDCENLLKK LLVLNPIKRG 300
SLEQIMKDRW MNVGHEEEEL KPYTEPDPDF NDTKRIDIMV TMGFARDEIN 350
DALINQKYDE VMATYILLGR KPPEFEGGES LSSGNLCQRS RPSSDLNNST 400
LQSPAHLKVQ RSISANQKQR RFSDHAGPSI PPAVSYTKRP QANSVESEQK 450
EEWDKDVARK LGSTTVGSKS EMTASPLVGP ERKKSSTIPS NNVYSGGSMA 500
RRNTYVCERT TDRYVALQNG KDSSLTEMSV SSISSAGSSV ASAVPSARPR 550
HQKSMSTSGH PIKVTLPTIK DGSEAYRPGT TQRVPAASPS AHSISTATPD 600
RTRFPRGSSS RSTFHGEQLR ERRSVAYNGP PASPSHETGA FAHARRGTST 650
GIISKITSKF VRRDPSEGEA SGRTDTSRST SGEPKERDKE EGKDSKPRSL 700
RFTWSMKTTS SMDPNDMMRE IRKVLDANNC DYEQKERFLL FCVHGDARQD 750
SLVQWEMEVC KLPRLSLNGV RFKRISGTSI AFKNIASKIA NELKL 795
Length:795
Mass (Da):89,003
Last modified:January 23, 2007 - v2
Checksum:i71BF6EB76912631B
GO
Isoform 2 (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.

Show »
Length:645
Mass (Da):72,073
Checksum:i7AE395507519DCF6
GO
Isoform 3 (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.

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.

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.
VSP_051702Add
BLAST
Alternative sequencei120 – 14122Missing in isoform 3.
VSP_051703Add
BLAST
Alternative sequencei663 – 67715Missing in isoform 2 and isoform 3.
VSP_051704Add
BLAST

Sequence conflict

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

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]
ENST00000402574; ENSP00000386017; ENSG00000116141. [Q9P0L2-2]
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...

Protein-protein interaction databases

BioGridi 110309. 13 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 ]
ENST00000402574 ; ENSP00000386017 ; ENSG00000116141 . [Q9P0L2-2 ]
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.
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

ArrayExpressi Q9P0L2.
Bgeei Q9P0L2.
CleanExi HS_MARK1.
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_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. "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: Brain.
  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: July 9, 2014
This is version 127 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 (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

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