Skip Header

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

Serine/threonine-protein kinase MARK2

Gene

MARK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase involved in cell polarity and microtubule dynamics regulation. Phosphorylates 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.10 Publications

Catalytic activityi

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

Cofactori

Mg2+By similarity

Enzyme regulationi

Inhibited by PAK5; inhibition is independent of the kinase activity of PAK5 (By similarity). Activated by phosphorylation on Thr-208. Inhibited by phosphorylation at Ser-212 and Thr-596. Inhibited by hymenialdisine. Specifically inhibited by the H.pylori CagA peptide FPLKRHDKVDDLSK that mimics host substrates and binds to the kinase substrate-binding site.By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei82ATPPROSITE-ProRule annotationBy similarity1
Active sitei175Proton acceptorPROSITE-ProRule annotationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi59 – 67ATPPROSITE-ProRule annotationBy similarity9

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • lipid binding Source: UniProtKB-KW
  • magnesium ion binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein kinase activator activity Source: ParkinsonsUK-UCL
  • protein serine/threonine kinase activity Source: UniProtKB
  • tau-protein kinase activity Source: UniProtKB

GO - Biological processi

  • activation of protein kinase activity Source: ParkinsonsUK-UCL
  • establishment of cell polarity Source: UniProtKB
  • establishment or maintenance of epithelial cell apical/basal polarity Source: UniProtKB
  • intracellular signal transduction Source: UniProtKB
  • microtubule cytoskeleton organization Source: InterPro
  • mitochondrion localization Source: ParkinsonsUK-UCL
  • mitophagy Source: ParkinsonsUK-UCL
  • neuron migration Source: UniProtKB
  • peptidyl-threonine phosphorylation Source: ParkinsonsUK-UCL
  • positive regulation of neuron projection development Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of axonogenesis Source: UniProtKB
  • regulation of cytoskeleton organization Source: UniProtKB
  • 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

Enzyme and pathway databases

BioCyciZFISH:HS01072-MONOMER.
SignaLinkiQ7KZI7.
SIGNORiQ7KZI7.

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
PAR1 homolog
PAR1 homolog b
Short name:
Par-1b
Short name:
Par1b
Gene namesi
Name:MARK2Imported
Synonyms:EMK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:3332. MARK2.

Subcellular locationi

GO - Cellular componenti

  • actin filament Source: UniProtKB
  • cell-cell adherens junction Source: BHF-UCL
  • lateral plasma membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • microtubule bundle Source: UniProtKB
  • mitochondrion Source: ParkinsonsUK-UCL
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi208T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. 1 Publication1
Mutagenesisi596T → A: Loss of membrane dissociation and binding to YWHAZ. 2 Publications1

Organism-specific databases

DisGeNETi2011.
OpenTargetsiENSG00000072518.
PharmGKBiPA35047.

Chemistry databases

ChEMBLiCHEMBL3831.
GuidetoPHARMACOLOGYi2098.

Polymorphism and mutation databases

BioMutaiMARK2.
DMDMi62510922.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000863011 – 788Serine/threonine-protein kinase MARK2Add BLAST788

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40PhosphoserineCombined sources1
Modified residuei58Phosphothreonine; by autocatalysisBy similarity1
Modified residuei91Phosphoserine; by CaMK1By similarity1
Modified residuei92Phosphoserine; by CaMK1By similarity1
Modified residuei93Phosphoserine; by CaMK1By similarity1
Modified residuei208Phosphothreonine; by LKB1 and TAOK1Combined sources1 Publication1
Modified residuei212Phosphoserine; by GSK3-betaBy similarity1
Modified residuei274Phosphoserine; by autocatalysisBy similarity1
Modified residuei275Phosphothreonine; by autocatalysisBy similarity1
Modified residuei294Phosphothreonine; by CaMK1By similarity1
Modified residuei409PhosphoserineCombined sources1
Modified residuei456PhosphoserineCombined sources1
Modified residuei467PhosphothreonineCombined sources1
Modified residuei486PhosphoserineCombined sources1
Modified residuei493PhosphoserineCombined sources1
Modified residuei569PhosphoserineCombined sources1
Modified residuei571PhosphoserineCombined sources1
Modified residuei592PhosphoserineCombined sources1
Modified residuei596Phosphothreonine; by PKC/PRKCZCombined sources2 Publications1
Modified residuei619PhosphoserineCombined sources1
Modified residuei722PhosphoserineCombined sources1
Isoform 13 (identifier: Q7KZI7-13)
Modified residuei376PhosphoserineCombined sources1
Isoform 14 (identifier: Q7KZI7-14)
Modified residuei376PhosphoserineCombined sources1
Isoform 15 (identifier: Q7KZI7-15)
Modified residuei409PhosphoserineCombined sources1
Isoform 16 (identifier: Q7KZI7-16)
Modified residuei409PhosphoserineCombined sources1

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-596 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.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ7KZI7.
MaxQBiQ7KZI7.
PaxDbiQ7KZI7.
PeptideAtlasiQ7KZI7.
PRIDEiQ7KZI7.

PTM databases

iPTMnetiQ7KZI7.
PhosphoSitePlusiQ7KZI7.

Expressioni

Tissue specificityi

High levels of expression in heart, brain, skeletal muscle and pancreas, lower levels observed in lung, liver and kidney.1 Publication

Gene expression databases

BgeeiENSG00000072518.
CleanExiHS_MARK2.
ExpressionAtlasiQ7KZI7. baseline and differential.
GenevisibleiQ7KZI7. HS.

Organism-specific databases

HPAiHPA038790.

Interactioni

Subunit structurei

Homodimer. Interacts with PAK5; leading to inhibit the protein kinase activity (By similarity). Interacts with MTCL1 isoform 1; the interaction is direct and increases MARK2 microtubule-binding ability. Interacts (when phosphorylated at Thr-596) with YWHAZ. In case of infection, interacts with H.pylori CagA, leading to inhibit kinase activity and junctional and polarity defects.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPTP106362EBI-516560,EBI-366182
MAPTP10636-82EBI-516560,EBI-366233
PARD6GQ9BYG42EBI-516560,EBI-295417
YWHABP319463EBI-516560,EBI-359815
YWHAGP619812EBI-516560,EBI-359832
YWHAHQ049178EBI-516560,EBI-306940
YWHAZP631046EBI-516560,EBI-347088

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi108326. 98 interactors.
DIPiDIP-31321N.
IntActiQ7KZI7. 57 interactors.
MINTiMINT-1149196.
STRINGi9606.ENSP00000385751.

Chemistry databases

BindingDBiQ7KZI7.

Structurei

Secondary structure

1788
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi53 – 60Combined sources8
Beta strandi66 – 72Combined sources7
Turni73 – 75Combined sources3
Beta strandi78 – 86Combined sources9
Helixi91 – 106Combined sources16
Beta strandi115 – 120Combined sources6
Beta strandi122 – 129Combined sources8
Helixi137 – 144Combined sources8
Helixi149 – 168Combined sources20
Helixi178 – 180Combined sources3
Beta strandi181 – 183Combined sources3
Beta strandi189 – 191Combined sources3
Helixi213 – 215Combined sources3
Helixi218 – 221Combined sources4
Helixi228 – 245Combined sources18
Helixi255 – 264Combined sources10
Helixi275 – 284Combined sources10
Helixi289 – 291Combined sources3
Helixi295 – 299Combined sources5
Helixi302 – 305Combined sources4
Helixi326 – 334Combined sources9
Helixi339 – 347Combined sources9
Helixi353 – 361Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IECX-ray2.20A/B/C/D49-363[»]
5EAKX-ray2.80A/B39-364[»]
ProteinModelPortaliQ7KZI7.
SMRiQ7KZI7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7KZI7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini53 – 304Protein kinasePROSITE-ProRule annotationAdd BLAST252
Domaini323 – 362UBAPROSITE-ProRule annotationAdd BLAST40
Domaini739 – 788KA1PROSITE-ProRule annotationAdd BLAST50

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.1 Publication
The KA1 domain mediates binding to phospholipids and targeting to membranes.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

eggNOGiKOG0586. Eukaryota.
ENOG410XNQ0. LUCA.
GeneTreeiENSGT00790000122947.
HOVERGENiHBG052453.
InParanoidiQ7KZI7.
KOiK08798.
OMAiANNCQCE.
OrthoDBiEOG091G0D1E.
PhylomeDBiQ7KZI7.
TreeFamiTF315213.

Family and domain databases

Gene3Di3.30.310.80. 1 hit.
InterProiIPR028375. KA1/Ssp2_C.
IPR001772. KA1_dom.
IPR011009. Kinase-like_dom.
IPR033624. MARK/par1.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR015940. UBA.
[Graphical view]
PANTHERiPTHR24346. PTHR24346. 1 hit.
PfamiPF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00627. UBA. 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 (16)i

Sequence statusi: Complete.

This entry describes 16 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Isoform 1Curated (identifier: Q7KZI7-1) [UniParc]FASTAAdd to basket
Also known as: Alpha

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
MSSARTPLPT LNERDTEQPT LGHLDSKPSS KSNMIRGRNS 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
ANPKQRRFSD QAAGPAIPTS NSYSKKTQSN NAENKRPEED RESGRKASST
460 470 480 490 500
AKVPASPLPG LERKKTTPTP STNSVLSTST NRSRNSPLLE RASLGQASIQ
510 520 530 540 550
NGKDSLTMPG SRASTASASA AVSAARPRQH QKSMSASVHP NKASGLPPTE
560 570 580 590 600
SNCEVPRPST APQRVPVASP SAHNISSSGG APDRTNFPRG VSSRSTFHAG
610 620 630 640 650
QLRQVRDQQN LPYGVTPASP SGHSQGRRGA SGSIFSKFTS KFVRRNLSFR
660 670 680 690 700
FARRNLNEPE SKDRVETLRP HVVGSGGNDK EKEEFREAKP RSLRFTWSMK
710 720 730 740 750
TTSSMEPNEM MREIRKVLDA NSCQSELHEK YMLLCMHGTP GHEDFVQWEM
760 770 780
EVCKLPRLSL NGVRFKRISG TSMAFKNIAS KIANELKL
Note: Produced by alternative promoter usage. No experimental confirmation available.
Length:788
Mass (Da):87,911
Last modified:April 12, 2005 - v2
Checksum:iF307BF4DDB543A70
GO
Isoform 21 Publication (identifier: Q7KZI7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     505-558: Missing.

Note: Produced by alternative splicing of isoform 6.1 Publication
Show »
Length:701
Mass (Da):78,851
Checksum:i3D68318CFDCA31EE
GO
Isoform 31 Publication (identifier: Q7KZI7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     644-652: Missing.

Note: Produced by alternative splicing of isoform 6.1 Publication
Show »
Length:746
Mass (Da):83,184
Checksum:i58F2BBE10943C90F
GO
Isoform 41 Publication (identifier: Q7KZI7-4) [UniParc]FASTAAdd to basket
Also known as: Par-1Balpha1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     505-558: Missing.
     644-652: Missing.

Note: Produced by alternative splicing of isoform 1.1 Publication
Show »
Length:725
Mass (Da):81,280
Checksum:iD676331938A84716
GO
Isoform 5 (identifier: Q7KZI7-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     505-558: Missing.
     654-668: Missing.

Note: Produced by alternative splicing of isoform 1.
Show »
Length:719
Mass (Da):80,647
Checksum:iEC39154CF73E9858
GO
Isoform 6Curated (identifier: Q7KZI7-6) [UniParc]FASTAAdd to basket
Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.

Note: Produced by alternative promoter usage. No experimental confirmation available.
Show »
Length:755
Mass (Da):84,333
Checksum:i493CD8C6DC3A4C06
GO
Isoform 7Curated (identifier: Q7KZI7-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     505-558: Missing.
     644-652: Missing.

Note: Produced by alternative splicing of isoform 6. No experimental confirmation available.Curated
Show »
Length:692
Mass (Da):77,702
Checksum:i4BD9AA1F872638A6
GO
Isoform 8Curated (identifier: Q7KZI7-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     644-652: Missing.

Note: Produced by alternative splicing of isoform 1. No experimental confirmation available.Curated
Show »
Length:779
Mass (Da):86,762
Checksum:i5AF7014EB5639857
GO
Isoform 9Curated (identifier: Q7KZI7-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     505-558: Missing.

Note: Produced by alternative splicing of isoform 1. No experimental confirmation available.Curated
Show »
Length:734
Mass (Da):82,429
Checksum:i60D126D3C8967186
GO
Isoform 10Curated (identifier: Q7KZI7-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     505-558: Missing.
     654-668: Missing.

Note: Produced by alternative splicing of isoform 6. No experimental confirmation available.Curated
Show »
Length:686
Mass (Da):77,069
Checksum:i9389E28076FDDAF8
GO
Isoform 11Curated (identifier: Q7KZI7-11) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     654-668: Missing.

Note: Produced by alternative splicing of isoform 1. No experimental confirmation available.
Show »
Length:773
Mass (Da):86,129
Checksum:i0378FF0433C4D901
GO
Isoform 12Curated (identifier: Q7KZI7-12) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     654-668: Missing.

Note: Produced by alternative splicing of isoform 6. No experimental confirmation available.Curated
Show »
Length:740
Mass (Da):82,551
Checksum:i6220FC8C1A308548
GO
Isoform 13 (identifier: Q7KZI7-13) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     412-412: Missing.
     505-558: Missing.
     644-652: Missing.

Note: Produced by alternative splicing of isoform 6.Combined sources
Show »
Length:691
Mass (Da):77,631
Checksum:i2216B4AE7BCF31BE
GO
Isoform 14 (identifier: Q7KZI7-14) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     412-412: Missing.
     644-652: Missing.

Note: Produced by alternative splicing of isoform 6.Combined sources
Show »
Length:745
Mass (Da):83,113
Checksum:i54CA1DAF4B6E02CF
GO
Isoform 15 (identifier: Q7KZI7-15) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     412-412: Missing.
     505-558: Missing.
     645-668: Missing.

Note: Produced by alternative splicing of isoform 1.Combined sources
Show »
Length:709
Mass (Da):79,427
Checksum:iF30B3AB6B60B3621
GO
Isoform 16 (identifier: Q7KZI7-16) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     412-412: Missing.
     505-558: Missing.
     644-652: Missing.

Note: Produced by alternative splicing of isoform 1.Combined sources
Show »
Length:724
Mass (Da):81,209
Checksum:i9D8FB211F5B08149
GO

Sequence cautioni

The sequence AAK82368 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti192A → G in CAA80914 (PubMed:8274451).Curated1
Sequence conflicti236L → C in CAA80914 (PubMed:8274451).Curated1
Sequence conflicti389 – 390PS → QF in CAA66229 (PubMed:9730619).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0517051 – 33Missing in isoform 2, isoform 3, isoform 6, isoform 7, isoform 10, isoform 12, isoform 13 and isoform 14. 2 PublicationsAdd BLAST33
Alternative sequenceiVSP_039872412Missing in isoform 13, isoform 14, isoform 15 and isoform 16. Curated1
Alternative sequenceiVSP_051706505 – 558Missing in isoform 2, isoform 4, isoform 5, isoform 7, isoform 9, isoform 10, isoform 13, isoform 15 and isoform 16. 4 PublicationsAdd BLAST54
Alternative sequenceiVSP_051707644 – 652Missing in isoform 3, isoform 4, isoform 7, isoform 8, isoform 13, isoform 14 and isoform 16. 3 Publications9
Alternative sequenceiVSP_041853645 – 668Missing in isoform 15. CuratedAdd BLAST24
Alternative sequenceiVSP_051708654 – 668Missing in isoform 5, isoform 11, isoform 10 and isoform 12. 3 PublicationsAdd BLAST15

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97630 mRNA. Translation: CAA66229.1.
AB188493 mRNA. Translation: BAD37141.1.
BT007342 mRNA. Translation: AAP36006.1.
AP003780 Genomic DNA. No translation available.
BC008771 mRNA. Translation: AAH08771.2.
BC084540 mRNA. Translation: AAH84540.1.
AF387638 mRNA. Translation: AAK82368.1. Different initiation.
Z25427 mRNA. Translation: CAA80914.1.
CCDSiCCDS41665.1. [Q7KZI7-14]
CCDS53649.1. [Q7KZI7-1]
CCDS53650.1. [Q7KZI7-5]
CCDS53651.1. [Q7KZI7-15]
CCDS8051.2. [Q7KZI7-16]
PIRiG01025.
I38217.
RefSeqiNP_001034558.2. NM_001039469.2. [Q7KZI7-1]
NP_001156768.1. NM_001163296.1. [Q7KZI7-5]
NP_001156769.1. NM_001163297.1. [Q7KZI7-15]
NP_004945.4. NM_004954.4. [Q7KZI7-16]
NP_059672.2. NM_017490.3. [Q7KZI7-14]
UniGeneiHs.567261.

Genome annotation databases

EnsembliENST00000350490; ENSP00000294247; ENSG00000072518. [Q7KZI7-15]
ENST00000361128; ENSP00000355091; ENSG00000072518. [Q7KZI7-5]
ENST00000402010; ENSP00000385751; ENSG00000072518. [Q7KZI7-1]
ENST00000408948; ENSP00000386128; ENSG00000072518. [Q7KZI7-13]
ENST00000508192; ENSP00000425765; ENSG00000072518. [Q7KZI7-16]
ENST00000509502; ENSP00000423974; ENSG00000072518. [Q7KZI7-14]
ENST00000513765; ENSP00000421075; ENSG00000072518. [Q7KZI7-6]
GeneIDi2011.
KEGGihsa:2011.
UCSCiuc001nxv.5. human. [Q7KZI7-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97630 mRNA. Translation: CAA66229.1.
AB188493 mRNA. Translation: BAD37141.1.
BT007342 mRNA. Translation: AAP36006.1.
AP003780 Genomic DNA. No translation available.
BC008771 mRNA. Translation: AAH08771.2.
BC084540 mRNA. Translation: AAH84540.1.
AF387638 mRNA. Translation: AAK82368.1. Different initiation.
Z25427 mRNA. Translation: CAA80914.1.
CCDSiCCDS41665.1. [Q7KZI7-14]
CCDS53649.1. [Q7KZI7-1]
CCDS53650.1. [Q7KZI7-5]
CCDS53651.1. [Q7KZI7-15]
CCDS8051.2. [Q7KZI7-16]
PIRiG01025.
I38217.
RefSeqiNP_001034558.2. NM_001039469.2. [Q7KZI7-1]
NP_001156768.1. NM_001163296.1. [Q7KZI7-5]
NP_001156769.1. NM_001163297.1. [Q7KZI7-15]
NP_004945.4. NM_004954.4. [Q7KZI7-16]
NP_059672.2. NM_017490.3. [Q7KZI7-14]
UniGeneiHs.567261.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IECX-ray2.20A/B/C/D49-363[»]
5EAKX-ray2.80A/B39-364[»]
ProteinModelPortaliQ7KZI7.
SMRiQ7KZI7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108326. 98 interactors.
DIPiDIP-31321N.
IntActiQ7KZI7. 57 interactors.
MINTiMINT-1149196.
STRINGi9606.ENSP00000385751.

Chemistry databases

BindingDBiQ7KZI7.
ChEMBLiCHEMBL3831.
GuidetoPHARMACOLOGYi2098.

PTM databases

iPTMnetiQ7KZI7.
PhosphoSitePlusiQ7KZI7.

Polymorphism and mutation databases

BioMutaiMARK2.
DMDMi62510922.

Proteomic databases

EPDiQ7KZI7.
MaxQBiQ7KZI7.
PaxDbiQ7KZI7.
PeptideAtlasiQ7KZI7.
PRIDEiQ7KZI7.

Protocols and materials databases

DNASUi2011.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000350490; ENSP00000294247; ENSG00000072518. [Q7KZI7-15]
ENST00000361128; ENSP00000355091; ENSG00000072518. [Q7KZI7-5]
ENST00000402010; ENSP00000385751; ENSG00000072518. [Q7KZI7-1]
ENST00000408948; ENSP00000386128; ENSG00000072518. [Q7KZI7-13]
ENST00000508192; ENSP00000425765; ENSG00000072518. [Q7KZI7-16]
ENST00000509502; ENSP00000423974; ENSG00000072518. [Q7KZI7-14]
ENST00000513765; ENSP00000421075; ENSG00000072518. [Q7KZI7-6]
GeneIDi2011.
KEGGihsa:2011.
UCSCiuc001nxv.5. human. [Q7KZI7-1]

Organism-specific databases

CTDi2011.
DisGeNETi2011.
GeneCardsiMARK2.
HGNCiHGNC:3332. MARK2.
HPAiHPA038790.
MIMi600526. gene.
neXtProtiNX_Q7KZI7.
OpenTargetsiENSG00000072518.
PharmGKBiPA35047.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0586. Eukaryota.
ENOG410XNQ0. LUCA.
GeneTreeiENSGT00790000122947.
HOVERGENiHBG052453.
InParanoidiQ7KZI7.
KOiK08798.
OMAiANNCQCE.
OrthoDBiEOG091G0D1E.
PhylomeDBiQ7KZI7.
TreeFamiTF315213.

Enzyme and pathway databases

BioCyciZFISH:HS01072-MONOMER.
SignaLinkiQ7KZI7.
SIGNORiQ7KZI7.

Miscellaneous databases

ChiTaRSiMARK2. human.
EvolutionaryTraceiQ7KZI7.
GeneWikiiMARK2.
GenomeRNAii2011.
PROiQ7KZI7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000072518.
CleanExiHS_MARK2.
ExpressionAtlasiQ7KZI7. baseline and differential.
GenevisibleiQ7KZI7. HS.

Family and domain databases

Gene3Di3.30.310.80. 1 hit.
InterProiIPR028375. KA1/Ssp2_C.
IPR001772. KA1_dom.
IPR011009. Kinase-like_dom.
IPR033624. MARK/par1.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR015940. UBA.
[Graphical view]
PANTHERiPTHR24346. PTHR24346. 1 hit.
PfamiPF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]
SUPFAMiSSF103243. SSF103243. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50032. KA1. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMARK2_HUMAN
AccessioniPrimary (citable) accession number: Q7KZI7
Secondary accession number(s): Q15449
, Q15524, Q5XGA3, Q68A18, Q96HB3, Q96RG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: April 12, 2005
Last modified: November 30, 2016
This is version 141 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.