MARK2
entrez
2011
canonical
uniprot
Q7KZI7
canonical
ensembl
ENSG00000072518
resolver
ensp
ENSP00000294247
resolver
ensp
ENSP00000355091
resolver
ensp
ENSP00000385751
resolver
ensp
ENSP00000423974
resolver
ensp
ENSP00000425765
resolver
genesymbol
MARK2
resolver
genesymbol_syn
EMK1
resolver
hgnc
HGNC:3332
resolver
uniprot
A0A140VJP1
resolver
uniprot
A8K2S4
resolver
uniprot
Q15449
resolver
uniprot
Q15524
resolver
uniprot
Q5XGA3
resolver
uniprot
Q68A18
resolver
uniprot
Q96HB3
resolver
uniprot
Q96RG0
resolver
uniprot_entry
A0A140VJP1_HUMAN
resolver
uniprot_entry
A8K2S4_HUMAN
resolver
uniprot_entry
MARK2_HUMAN
resolver
uniprot_sec
Q15449
resolver
uniprot_sec
Q15524
resolver
uniprot_sec
Q5XGA3
resolver
uniprot_sec
Q68A18
resolver
uniprot_sec
Q96HB3
resolver
uniprot_sec
Q96RG0
resolver
activity_regulation
ACTIVITY REGULATION: 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. {ECO:0000250, ECO:0000269|PubMed:12429843, ECO:0000269|PubMed:14976552}.
uniprot
proteins
amino_acid_sequence
MSSARTPLPTLNERDTEQPTLGHLDSKPSSKSNMIRGRNSATSADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDELKPYVEPLPDYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGYKSSELEGDTITLKPRPSADLTNSSAPSPSHKVQRSVSANPKQRRFSDQAAGPAIPTSNSYSKKTQSNNAENKRPEEDRESGRKASSTAKVPASPLPGLERKKTTPTPSTNSVLSTSTNRSRNSPLLERASLGQASIQNGKDSLTMPGSRASTASASAAVSAARPRQHQKSMSASVHPNKASGLPPTESNCEVPRPSTAPQRVPVASPSAHNISSSGGAPDRTNFPRGVSSRSTFHAGQLRQVRDQQNLPYGVTPASPSGHSQGRRGASGSIFSKFTSKFVRRNLSFRFARRNLNEPESKDRVETLRPHVVGSGGNDKEKEEFREAKPRSLRFTWSMKTTSSMEPNEMMREIRKVLDANSCQSELHEKYMLLCMHGTPGHEDFVQWEMEVCKLPRLSLNGVRFKRISGTSMAFKNIASKIANELKL
uniprot
proteins
disease_involvement
DISEASE: Intellectual developmental disorder, autosomal dominant 76 (MRD76) [MIM:621285]: An autosomal dominant disorder characterized by developmental delay, impaired intellectual development, speech and language deficits, and autism. More variable features include seizures, motor delay, behavior problems, eye abnormalities, and distinctive facial features. {ECO:0000269|PubMed:39419027, ECO:0000269|PubMed:40542891}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
ec_number
2.7.11.26
uniprot
proteins
function
FUNCTION: Serine/threonine-protein kinase (PubMed:23666762). Involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4 and RAB11FIP2. Phosphorylates the microtubule-associated protein MAPT/TAU (PubMed:23666762). 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 disheveled 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. Phosphorylates UBAC2 at 'Ser-223' during ER stress or starvation-induced autophagy, promoting UBAC2 dimerization and interaction with GABARAP to mediate ER-phagy (PubMed:39284914). {ECO:0000269|PubMed:11433294, ECO:0000269|PubMed:12429843, ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:15158914, ECO:0000269|PubMed:15324659, ECO:0000269|PubMed:15365179, ECO:0000269|PubMed:16775013, ECO:0000269|PubMed:16980613, ECO:0000269|PubMed:18626018, ECO:0000269|PubMed:20194617, ECO:0000269|PubMed:23666762, ECO:0000269|PubMed:39284914}.
uniprot
proteins
mass_dalton
87911
uniprot
proteins
mutagenesis
MUTAGEN 208; /note="T->A: Prevents phosphorylation and activation by STK11/LKB1 complex."; /evidence="ECO:0000269|PubMed:14976552"; MUTAGEN 596; /note="T->A: Loss of membrane dissociation and binding to YWHAZ."; /evidence="ECO:0000269|PubMed:15084291, ECO:0000269|PubMed:15324659
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:15084291, ECO:0000269|PubMed:15324659}.
uniprot
proteins
protein_family
CAMK Ser/Thr protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
SNF1 subfamily
uniprot
proteins
pubmed
11433294
uniprot
proteins
pubmed
12429843
uniprot
proteins
pubmed
14976552
uniprot
proteins
pubmed
15084291
uniprot
proteins
pubmed
15158914
uniprot
proteins
pubmed
15324659
uniprot
proteins
pubmed
15365179
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16396636
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
16775013
uniprot
proteins
pubmed
16959763
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
16980613
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17507984
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18626018
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19559622
uniprot
proteins
pubmed
19966800
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20071654
uniprot
proteins
pubmed
20194617
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23666762
uniprot
proteins
pubmed
23902687
uniprot
proteins
pubmed
39284914
uniprot
proteins
pubmed
39419027
uniprot
proteins
pubmed
40542891
uniprot
proteins
pubmed
8274451
uniprot
proteins
pubmed
9730619
uniprot
proteins
sequence_length
788
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cytoplasm. Lateral cell membrane. Cytoplasm, cytoskeleton. Cell projection, dendrite {ECO:0000269|PubMed:23666762}. Cytoplasm {ECO:0000269|PubMed:23666762}. Note=Phosphorylation at Thr-596 by PRKCZ/aPKC and subsequent interaction with 14-3-3 protein YWHAZ promotes relocation from the cell membrane to the cytoplasm.
uniprot
proteins