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O08679

- MARK2_RAT

UniProt

O08679 - MARK2_RAT

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Protein

Serine/threonine-protein kinase MARK2

Gene

Mark2

Organism
Rattus norvegicus (Rat)
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 CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4, MAPT/TAU and RAB11FIP2. Plays a key role in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Regulates epithelial cell polarity by phosphorylating RAB11FIP2. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Regulates axogenesis by phosphorylating KIF13B, promoting interaction between KIF13B and 14-3-3 and inhibiting microtubule-dependent accumulation of KIF13B. Also required for neurite outgrowth and establishment of neuronal polarity. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). Modulates the developmental decision to build a columnar versus a hepatic epithelial cell apparently by promoting a switch from a direct to a transcytotic mode of apical protein delivery. Essential for the asymmetric development of membrane domains of polarized epithelial cells.5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.By similarity
ATP + [tau protein] = ADP + [tau protein] phosphate.

Cofactori

Magnesium.By similarity

Enzyme regulationi

Inhibited by hymenialdisine By similarity. Activated by phosphorylation on Thr-208 by STK11/LKB1 and TAOK1. Inhibited by phosphorylation at Ser-212 or Thr-539. Inhibited by PAK7/PAK5; inhibition is independent of the kinase activity of PAK7/PAK5.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei82 – 821ATPBy similarityPROSITE-ProRule annotation
Active sitei175 – 1751Proton acceptorBy similarityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi59 – 679ATPBy similarityPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. lipid binding Source: UniProtKB-KW
  3. magnesium ion binding Source: UniProtKB
  4. poly(A) RNA binding Source: Ensembl
  5. protein serine/threonine kinase activity Source: UniProtKB
  6. tau-protein kinase activity Source: UniProtKB

GO - Biological processi

  1. establishment of cell polarity Source: UniProtKB
  2. establishment or maintenance of epithelial cell apical/basal polarity Source: UniProtKB
  3. intracellular signal transduction Source: UniProtKB
  4. neuron migration Source: UniProtKB
  5. positive regulation of neuron projection development Source: UniProtKB
  6. protein autophosphorylation Source: UniProtKB
  7. protein phosphorylation Source: UniProtKB
  8. regulation of axonogenesis Source: UniProtKB
  9. regulation of cytoskeleton organization Source: UniProtKB
  10. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Differentiation, Wnt signaling pathway

Keywords - Ligandi

ATP-binding, Lipid-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase MARK2 (EC:2.7.11.1, EC:2.7.11.26)
Alternative name(s):
ELKL motif kinase 1
Short name:
EMK-1
MAP/microtubule affinity-regulating kinase 2
Gene namesi
Name:Mark2Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi708483. Mark2.

Subcellular locationi

Cell membrane 1 Publication; Peripheral membrane protein 1 Publication. Cytoplasm By similarity. Lateral cell membrane By similarity. Cytoplasmcytoskeleton By similarity
Note: Phosphorylation at Thr-539 by PRKCZ/aPKC and subsequent interaction with 14-3-3 protein YWHAZ promotes relocation from the cell membrane to the cytoplasm.By similarity

GO - Cellular componenti

  1. actin filament Source: UniProtKB
  2. basal cortex Source: Ensembl
  3. lateral plasma membrane Source: UniProtKB
  4. membrane Source: UniProtKB
  5. microtubule bundle Source: UniProtKB
  6. nucleus Source: Ensembl
  7. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi82 – 821K → A: Loss of kinase activity. 1 Publication
Mutagenesisi91 – 933SSS → AAA: Loss of phosphorylation by CaMK1, decrease in kinase activity and ability to promote neurite outgrowth; when associated with A-294. 1 Publication
Mutagenesisi208 – 2081T → A: Abolishes activation of serine/threonine-protein kinase activity and only basal activity remains. 3 Publications
Mutagenesisi208 – 2081T → E: Phosphomimetic mutant that leads to activation but not in presence of GSK3-beta. 3 Publications
Mutagenesisi212 – 2121S → A: Loss of activity; neither activated by TAOK1 nor by STK11/LKB1. 3 Publications
Mutagenesisi294 – 2941T → A: Loss of phosphorylation by CaMK1, decrease in kinase activity and ability to promote neurite outgrowth; when associated with 91-A--A-93. 1 Publication
Mutagenesisi539 – 5391T → A: Abolishes phosphorylation by PKC/PRKCZ. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 722722Serine/threonine-protein kinase MARK2PRO_0000086303Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401PhosphoserineBy similarity
Modified residuei58 – 581Phosphothreonine; by autocatalysis1 Publication
Modified residuei91 – 911Phosphoserine; by CaMK11 Publication
Modified residuei92 – 921Phosphoserine; by CaMK11 Publication
Modified residuei93 – 931Phosphoserine; by CaMK11 Publication
Modified residuei208 – 2081Phosphothreonine; by LKB1 and TAOK11 Publication
Modified residuei212 – 2121Phosphoserine; by GSK3-beta3 Publications
Modified residuei274 – 2741Phosphoserine; by autocatalysis1 Publication
Modified residuei275 – 2751Phosphothreonine; by autocatalysis1 Publication
Modified residuei294 – 2941Phosphothreonine; by CaMK11 Publication
Modified residuei409 – 4091PhosphoserineBy similarity
Modified residuei453 – 4531PhosphoserineBy similarity
Modified residuei483 – 4831PhosphoserineBy similarity
Modified residuei490 – 4901PhosphoserineBy similarity
Modified residuei512 – 5121PhosphoserineBy similarity
Modified residuei539 – 5391Phosphothreonine; by PKC/PRKCZ1 Publication
Modified residuei562 – 5621PhosphoserineBy similarity
Modified residuei656 – 6561PhosphoserineBy similarity

Post-translational modificationi

Autophosphorylated. Phosphorylated at Thr-208 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Phosphorylation at Thr-208 by TAOK1 activates the kinase activity, leading to phosphorylation and detachment of MAPT/TAU from microtubules. Phosphorylation at Ser-212 by GSK3-beta (GSK3B) inhibits the kinase activity. Phosphorylation by CaMK1 promotes activity and is required to promote neurite outgrowth. Phosphorylation at Thr-539 by PRKCZ/aPKC in polarized epithelial cells inhibits the kinase activity and promotes binding to 14-3-3 protein YWHAZ, leading to relocation from cell membrane to cytoplasm.5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO08679.
PRIDEiO08679.

PTM databases

PhosphoSiteiO08679.

Expressioni

Gene expression databases

GenevestigatoriO08679.

Interactioni

Subunit structurei

Homodimer. Interacts (when phosphorylated at Thr-539) with YWHAZ. Interacts with MTCL1; the interaction is direct and increases MARK2 microtubule-binding ability By similarity. Interacts with PAK7/PAK5; leading to inhibit the protein kinase activity.By similarity2 Publications

Protein-protein interaction databases

DIPiDIP-29029N.
STRINGi10116.ENSRNOP00000028765.

Structurei

Secondary structure

1
722
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi53 – 619Combined sources
Beta strandi63 – 7210Combined sources
Turni73 – 753Combined sources
Beta strandi78 – 858Combined sources
Helixi86 – 883Combined sources
Helixi91 – 10616Combined sources
Beta strandi115 – 1206Combined sources
Beta strandi122 – 1309Combined sources
Helixi137 – 1448Combined sources
Helixi149 – 16820Combined sources
Helixi178 – 1803Combined sources
Beta strandi181 – 1833Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi202 – 2054Combined sources
Turni208 – 2114Combined sources
Helixi213 – 2153Combined sources
Helixi219 – 2224Combined sources
Helixi229 – 24517Combined sources
Helixi255 – 26410Combined sources
Helixi275 – 28410Combined sources
Helixi289 – 2913Combined sources
Helixi295 – 2984Combined sources
Helixi302 – 3054Combined sources
Helixi326 – 3349Combined sources
Helixi339 – 3479Combined sources
Helixi353 – 3619Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y8GX-ray2.50A/B39-364[»]
1ZMUX-ray2.90A/B39-364[»]
1ZMVX-ray3.10A/B39-364[»]
1ZMWX-ray2.80A/B39-364[»]
2R0IX-ray2.20A/B39-364[»]
2WZJX-ray2.79A/B/C/D/E/F39-364[»]
ProteinModelPortaliO08679.
SMRiO08679. Positions 49-363, 626-722.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO08679.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 304252Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini323 – 36240UBAPROSITE-ProRule annotationAdd
BLAST
Domaini673 – 72250KA1PROSITE-ProRule annotationAdd
BLAST

Domaini

The KA1 domain mediates binding to phospholipids and targeting to membranes.By similarity
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

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.
HOGENOMiHOG000233025.
HOVERGENiHBG052453.
InParanoidiO08679.
KOiK08798.
OMAiHERYMLL.
OrthoDBiEOG79CXXX.

Family and domain databases

Gene3Di3.30.310.80. 1 hit.
InterProiIPR028375. KA1/Ssp2_C.
IPR001772. KA1_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view]
PfamiPF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]
SUPFAMiSSF103243. SSF103243. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50032. KA1. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O08679-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSARTPLPT LNERDTEQPT LGHLDSKPSS KSNMLRGRNS ATSADEQPHI
60 70 80 90 100
GNYRLLKTIG KGNFAKVKLA RHILTGKEVA VKIIDKTQLN SSSLQKLFRE
110 120 130 140 150
VRIMKVLNHP NIVKLFEVIE TEKTLYLVME YASGGEVFDY LVAHGRMKEK
160 170 180 190 200
EARAKFRQIV SAVQYCHQKF IVHRDLKAEN LLLDADMNIK IADFGFSNEF
210 220 230 240 250
TFGNKLDTFC GSPPYAAPEL FQGKKYDGPE VDVWSLGVIL YTLVSGSLPF
260 270 280 290 300
DGQNLKELRE RVLRGKYRIP FYMSTDCENL LKKFLILNPS KRGTLEQIMK
310 320 330 340 350
DRWMNVGHED DELKPYVEPL PDYKDPRRTE LMVSMGYTRE EIQDSLVGQR
360 370 380 390 400
YNEVMATYLL LGYKSSELEG DTITLKPRPS ADLTNSSAPS PSHKVQRSVS
410 420 430 440 450
ANPKQRRSSD QAVPAIPTSN SYSKKTQSNN AENKRPEEET GRKASSTAKV
460 470 480 490 500
PASPLPGLDR KKTTPTPSTN SVLSTSTNRS RNSPLLDRAS LGQASIQNGK
510 520 530 540 550
DSTAPQRVPV ASPSAHNISS SSGAPDRTNF PRGVSSRSTF HAGQLRQVRD
560 570 580 590 600
QQNLPFGVTP ASPSGHSQGR RGASGSIFSK FTSKFVRRNL NEPESKDRVE
610 620 630 640 650
TLRPHVVGGG GTDKEKEEFR EAKPRSLRFT WSMKTTSSME PNEMMREIRK
660 670 680 690 700
VLDANSCQSE LHERYMLLCV HGTPGHENFV QWEMEVCKLP RLSLNGVRFK
710 720
RISGTSMAFK NIASKIANEL KL
Length:722
Mass (Da):80,872
Last modified:July 1, 1997 - v1
Checksum:i2CBAFD1C38007ECC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z83869 mRNA. Translation: CAB06295.1.
RefSeqiNP_067731.1. NM_021699.1.
UniGeneiRn.42926.

Genome annotation databases

EnsembliENSRNOT00000028763; ENSRNOP00000028763; ENSRNOG00000021184.
GeneIDi60328.
KEGGirno:60328.
UCSCiRGD:708483. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z83869 mRNA. Translation: CAB06295.1 .
RefSeqi NP_067731.1. NM_021699.1.
UniGenei Rn.42926.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Y8G X-ray 2.50 A/B 39-364 [» ]
1ZMU X-ray 2.90 A/B 39-364 [» ]
1ZMV X-ray 3.10 A/B 39-364 [» ]
1ZMW X-ray 2.80 A/B 39-364 [» ]
2R0I X-ray 2.20 A/B 39-364 [» ]
2WZJ X-ray 2.79 A/B/C/D/E/F 39-364 [» ]
ProteinModelPortali O08679.
SMRi O08679. Positions 49-363, 626-722.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29029N.
STRINGi 10116.ENSRNOP00000028765.

PTM databases

PhosphoSitei O08679.

Proteomic databases

PaxDbi O08679.
PRIDEi O08679.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000028763 ; ENSRNOP00000028763 ; ENSRNOG00000021184 .
GeneIDi 60328.
KEGGi rno:60328.
UCSCi RGD:708483. rat.

Organism-specific databases

CTDi 2011.
RGDi 708483. Mark2.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118892.
HOGENOMi HOG000233025.
HOVERGENi HBG052453.
InParanoidi O08679.
KOi K08798.
OMAi HERYMLL.
OrthoDBi EOG79CXXX.

Miscellaneous databases

EvolutionaryTracei O08679.
NextBioi 611957.

Gene expression databases

Genevestigatori O08679.

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

  1. "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: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-DawleyImported.
    Tissue: BrainImported.
  2. "MARKK, a Ste20-like kinase, activates the polarity-inducing kinase MARK/PAR-1."
    Timm T., Li X.Y., Biernat J., Jiao J., Mandelkow E., Vandekerckhove J., Mandelkow E.M.
    EMBO J. 22:5090-5101(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT THR-58; THR-208; SER-212; SER-274 AND THR-275, MUTAGENESIS OF THR-208 AND SER-212.
  3. "MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons."
    Mandelkow E.M., Thies E., Trinczek B., Biernat J., Mandelkow E.
    J. Cell Biol. 167:99-110(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Doublecortin microtubule affinity is regulated by a balance of kinase and phosphatase activity at the leading edge of migrating neurons."
    Schaar B.T., Kinoshita K., McConnell S.K.
    Neuron 41:203-213(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF DCX, SUBCELLULAR LOCATION.
  5. "GSK-3beta directly phosphorylates and activates MARK2/PAR-1."
    Kosuga S., Tashiro E., Kajioka T., Ueki M., Shimizu Y., Imoto M.
    J. Biol. Chem. 280:42715-42722(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-212, MUTAGENESIS OF THR-208 AND SER-212.
  6. "PAK5 kinase is an inhibitor of MARK/Par-1, which leads to stable microtubules and dynamic actin."
    Matenia D., Griesshaber B., Li X.Y., Thiessen A., Johne C., Jiao J., Mandelkow E., Mandelkow E.M.
    Mol. Biol. Cell 16:4410-4422(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAK7.
  7. "Microtubule affinity-regulating kinase 2 functions downstream of the PAR-3/PAR-6/atypical PKC complex in regulating hippocampal neuronal polarity."
    Chen Y.M., Wang Q.J., Hu H.S., Yu P.C., Zhu J., Drewes G., Piwnica-Worms H., Luo Z.G.
    Proc. Natl. Acad. Sci. U.S.A. 103:8534-8539(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-539, MUTAGENESIS OF THR-539, FUNCTION.
  8. "A calcium- and calmodulin-dependent kinase Ialpha/microtubule affinity regulating kinase 2 signaling cascade mediates calcium-dependent neurite outgrowth."
    Uboha N.V., Flajolet M., Nairn A.C., Picciotto M.R.
    J. Neurosci. 27:4413-4423(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-91; SER-92; SER-93 AND THR-294, MUTAGENESIS OF LYS-82; 91-SER--SER-93 AND THR-294.
  9. "Glycogen synthase kinase (GSK) 3beta directly phosphorylates Serine 212 in the regulatory loop and inhibits microtubule affinity-regulating kinase (MARK) 2."
    Timm T., Balusamy K., Li X., Biernat J., Mandelkow E., Mandelkow E.M.
    J. Biol. Chem. 283:18873-18882(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-212, MUTAGENESIS OF THR-208 AND SER-212.
  10. "Accurate balance of the polarity kinase MARK2/Par-1 is required for proper cortical neuronal migration."
    Sapir T., Sapoznik S., Levy T., Finkelshtein D., Shmueli A., Timm T., Mandelkow E.M., Reiner O.
    J. Neurosci. 28:5710-5720(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Structure of the catalytic and ubiquitin-associated domains of the protein kinase MARK/Par-1."
    Panneerselvam S., Marx A., Mandelkow E.M., Mandelkow E.
    Structure 14:173-183(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 39-364 OF WILD-TYPE AND MUTANT THR-208 AND SER-212, SUBUNIT.
  12. "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: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 39-364.

Entry informationi

Entry nameiMARK2_RAT
AccessioniPrimary (citable) accession number: O08679
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: July 1, 1997
Last modified: October 29, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3