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Q9P0L2 (MARK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MARK1
Synonyms:KIAA1477, MARK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length795 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.10 Ref.11

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.1

ATP + [tau protein] = ADP + [tau protein] phosphate.

Cofactor

Magnesium By similarity. Ref.1

Enzyme regulation

Inhibited by phosphorylation at Ser-219 By similarity. Activated by phosphorylation on Thr-215. Ref.1 Ref.11

Subcellular location

Cell membrane; Peripheral membrane protein. Cytoplasmcytoskeleton By similarity. Note: Appears to localize to an intracellular network By similarity. Ref.22

Tissue specificity

Highly expressed in heart, skeletal muscle, brain, fetal brain and fetal kidney. Ref.8

Domain

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. Ref.22

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). Ref.22

Post-translational modification

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. Ref.1 Ref.11

Involvement in disease

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.

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 (Ref.9).

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.

Contains 1 KA1 (kinase-associated) domain.

Contains 1 protein kinase domain.

Contains 1 UBA domain.

Sequence caution

The sequence BAA96001.1 differs from that shown. Reason: Erroneous initiation.

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

Ontologies

Keywords
   Biological processWnt signaling pathway
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Lipid-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular signal transduction

Inferred from direct assay Ref.1. Source: UniProtKB

microtubule cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

neuron migration

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeleton

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule cytoskeleton

Traceable author statement Ref.8. Source: ProtInc

plasma membrane

Inferred from direct assay Ref.22. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.1. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.1. Source: UniProtKB

phosphatidic acid binding

Inferred from direct assay Ref.22. Source: UniProtKB

phosphatidylinositol-4,5-bisphosphate binding

Inferred from direct assay Ref.22. Source: UniProtKB

phosphatidylserine binding

Inferred from direct assay Ref.22. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

tau-protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.22 (identifier: Q9P0L2-1)

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.
Isoform 2 (identifier: Q9P0L2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-135: Missing.
     663-677: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9P0L2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     120-141: Missing.
     663-677: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 795795Serine/threonine-protein kinase MARK1
PRO_0000086298

Regions

Domain60 – 311252Protein kinase
Domain325 – 37046UBA
Domain746 – 79550KA1
Nucleotide binding66 – 749ATP By similarity UniProtKB Q9H0K1

Sites

Active site1821Proton acceptor By similarity UniProtKB Q9H0K1
Binding site891ATP By similarity UniProtKB O08678

Amino acid modifications

Modified residue51Phosphothreonine Ref.14
Modified residue2081Phosphothreonine Ref.11
Modified residue2151Phosphothreonine; by LKB1 and TAOK1 Ref.1
Modified residue2191Phosphoserine; by GSK3-beta UniProtKB O08678
Modified residue4031Phosphoserine Ref.14
Modified residue5881Phosphoserine Ref.15
Modified residue6131Phosphothreonine; by PKC/PRKCZ By similarity
Modified residue6661Phosphoserine By similarity

Natural variations

Alternative sequence1 – 135135Missing in isoform 2.
VSP_051702
Alternative sequence120 – 14122Missing in isoform 3.
VSP_051703
Alternative sequence663 – 67715Missing in isoform 2 and isoform 3.
VSP_051704
Natural variant2331Y → C in a gastric adenocarcinoma sample; somatic mutation. Ref.23
VAR_040760
Natural variant3551N → T in an ovarian serous carcinoma sample; somatic mutation. Ref.23
VAR_040761
Natural variant5301V → M. Ref.23
Corresponds to variant rs56212551 [ dbSNP | Ensembl ].
VAR_040762
Natural variant5781P → L. Ref.23
Corresponds to variant rs55691439 [ dbSNP | Ensembl ].
VAR_040763
Natural variant6451R → G.
Corresponds to variant rs12123778 [ dbSNP | Ensembl ].
VAR_030018
Natural variant6911E → G. Ref.23
Corresponds to variant rs55688276 [ dbSNP | Ensembl ].
VAR_040764

Experimental info

Mutagenesis2151T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. Ref.1
Mutagenesis2151T → E: Constitutively active. Ref.1
Mutagenesis6981R → S: Impairs phospholipid-binding, targeting to membrane and vesicle-binding; when associated with S-701. Ref.22
Mutagenesis7011R → S: Impairs phospholipid-binding, targeting to membrane and vesicle-binding; when associated with S-698. Ref.22
Mutagenesis771 – 7733RFK → AFA: Impairs phospholipid-binding. Ref.22
Sequence conflict161E → V in AAF72103. Ref.2
Sequence conflict201S → T in AAF72103. Ref.2
Sequence conflict5221D → N in BAB55152. Ref.4
Sequence conflict5441V → A in BAB55152. Ref.4
Sequence conflict7631P → A in BAB55152. Ref.4
Sequence conflict7941K → M in BAA96001. Ref.3

Secondary structure

.............................................................. 795
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 71BF6EB76912631B

FASTA79589,003
        10         20         30         40         50         60 
MSARTPLPTV NERDTENHTS VDGYTEPHIQ PTKSSSRQNI PRCRNSITSA TDEQPHIGNY 

        70         80         90        100        110        120 
RLQKTIGKGN FAKVKLARHV LTGREVAVKI IDKTQLNPTS LQKLFREVRI MKILNHPNIV 

       130        140        150        160        170        180 
KLFEVIETEK TLYLVMEYAS GGEVFDYLVA HGRMKEKEAR AKFRQIVSAV QYCHQKYIVH 

       190        200        210        220        230        240 
RDLKAENLLL DGDMNIKIAD FGFSNEFTVG NKLDTFCGSP PYAAPELFQG KKYDGPEVDV 

       250        260        270        280        290        300 
WSLGVILYTL VSGSLPFDGQ NLKELRERVL RGKYRIPFYM STDCENLLKK LLVLNPIKRG 

       310        320        330        340        350        360 
SLEQIMKDRW MNVGHEEEEL KPYTEPDPDF NDTKRIDIMV TMGFARDEIN DALINQKYDE 

       370        380        390        400        410        420 
VMATYILLGR KPPEFEGGES LSSGNLCQRS RPSSDLNNST LQSPAHLKVQ RSISANQKQR 

       430        440        450        460        470        480 
RFSDHAGPSI PPAVSYTKRP QANSVESEQK EEWDKDVARK LGSTTVGSKS EMTASPLVGP 

       490        500        510        520        530        540 
ERKKSSTIPS NNVYSGGSMA RRNTYVCERT TDRYVALQNG KDSSLTEMSV SSISSAGSSV 

       550        560        570        580        590        600 
ASAVPSARPR HQKSMSTSGH PIKVTLPTIK DGSEAYRPGT TQRVPAASPS AHSISTATPD 

       610        620        630        640        650        660 
RTRFPRGSSS RSTFHGEQLR ERRSVAYNGP PASPSHETGA FAHARRGTST GIISKITSKF 

       670        680        690        700        710        720 
VRRDPSEGEA SGRTDTSRST SGEPKERDKE EGKDSKPRSL RFTWSMKTTS SMDPNDMMRE 

       730        740        750        760        770        780 
IRKVLDANNC DYEQKERFLL FCVHGDARQD SLVQWEMEVC KLPRLSLNGV RFKRISGTSI 

       790 
AFKNIASKIA NELKL 

« Hide

Isoform 2 [UniParc].

Checksum: 7AE395507519DCF6
Show »

FASTA64572,073
Isoform 3 [UniParc].

Checksum: D6F1BCD8E884661D
Show »

FASTA75884,911

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001273057.1. NM_001286128.1.
NP_061120.3. NM_018650.4.
UniGeneHs.497806.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HAKX-ray2.60A/B/C/D/E/F/G/H45-371[»]
3OSEX-ray1.70A683-795[»]
ProteinModelPortalQ9P0L2.
SMRQ9P0L2. Positions 29-371, 696-795.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110309. 13 interactions.
IntActQ9P0L2. 8 interactions.
MINTMINT-3975018.
STRING9606.ENSP00000355884.

Chemistry

BindingDBQ9P0L2.
ChEMBLCHEMBL5940.
GuidetoPHARMACOLOGY2097.

PTM databases

PhosphoSiteQ9P0L2.

Polymorphism databases

DMDM124056494.

Proteomic databases

PaxDbQ9P0L2.
PRIDEQ9P0L2.

Protocols and materials databases

DNASU4139.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366917; ENSP00000355884; ENSG00000116141. [Q9P0L2-1]
ENST00000366918; ENSP00000355885; ENSG00000116141. [Q9P0L2-3]
ENST00000402574; ENSP00000386017; ENSG00000116141. [Q9P0L2-2]
GeneID4139.
KEGGhsa:4139.
UCSCuc001hmm.4. human. [Q9P0L2-3]
uc001hmn.4. human. [Q9P0L2-1]

Organism-specific databases

CTD4139.
GeneCardsGC01P220701.
HGNCHGNC:6896. MARK1.
HPAHPA007421.
HPA008061.
MIM606511. gene.
neXtProtNX_Q9P0L2.
PharmGKBPA30639.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG052453.
InParanoidQ9P0L2.
KOK08798.
OMAEHPHIGN.
OrthoDBEOG79CXXX.
PhylomeDBQ9P0L2.
TreeFamTF315213.

Enzyme and pathway databases

SignaLinkQ9P0L2.

Gene expression databases

ArrayExpressQ9P0L2.
BgeeQ9P0L2.
CleanExHS_MARK1.
GenevestigatorQ9P0L2.

Family and domain databases

Gene3D3.30.310.80. 1 hit.
InterProIPR028375. 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]
PfamPF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]
SUPFAMSSF103243. SSF103243. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50032. 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]
ProtoNetSearch...

Other

ChiTaRSMARK1. human.
EvolutionaryTraceQ9P0L2.
GeneWikiMARK1.
GenomeRNAi4139.
NextBio16256.
PROQ9P0L2.
SOURCESearch...

Entry information

Entry nameMARK1_HUMAN
AccessionPrimary (citable) accession number: Q9P0L2
Secondary accession number(s): D3DTB0 expand/collapse secondary AC list , D3DTB1, Q2HIY1, Q5VTF9, Q5VTG0, Q96SW9, Q9P251
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM