MARK1
entrez
4139
canonical
uniprot
Q9P0L2
canonical
ensembl
ENSG00000116141
resolver
ensp
ENSP00000355884
resolver
ensp
ENSP00000355885
resolver
ensp
ENSP00000386017
resolver
ensp
ENSP00000483424
resolver
ensp
ENSP00000503257
resolver
ensp
ENSP00000524052
resolver
ensp
ENSP00000792833
resolver
ensp
ENSP00000792834
resolver
enst
ENST00000402574
resolver
enst
ENST00000611084
resolver
genesymbol
MARK1
resolver
genesymbol_syn
KIAA1477
resolver
genesymbol_syn
MARK
resolver
hgnc
HGNC:6896
resolver
uniprot
A0A087X0I6
resolver
uniprot
A0A0A0MSF1
resolver
uniprot
B4DIB3
resolver
uniprot
D3DTB0
resolver
uniprot
D3DTB1
resolver
uniprot
Q2HIY1
resolver
uniprot
Q5VTF9
resolver
uniprot
Q5VTG0
resolver
uniprot
Q96SW9
resolver
uniprot
Q9P251
resolver
uniprot
X5D2M4
resolver
uniprot_entry
A0A087X0I6_HUMAN
resolver
uniprot_entry
A0A0A0MSF1_HUMAN
resolver
uniprot_entry
B4DIB3_HUMAN
resolver
uniprot_entry
MARK1_HUMAN
resolver
uniprot_entry
X5D2M4_HUMAN
resolver
uniprot_sec
D3DTB0
resolver
uniprot_sec
D3DTB1
resolver
uniprot_sec
Q2HIY1
resolver
uniprot_sec
Q5VTF9
resolver
uniprot_sec
Q5VTG0
resolver
uniprot_sec
Q96SW9
resolver
uniprot_sec
Q9P251
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by phosphorylation at Ser-219 (By similarity). Activated by phosphorylation on Thr-215. {ECO:0000250, ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:17573348}.
uniprot
proteins
amino_acid_sequence
MSARTPLPTVNERDTENHTSVDGYTEPHIQPTKSSSRQNIPRCRNSITSATDEQPHIGNYRLQKTIGKGNFAKVKLARHVLTGREVAVKIIDKTQLNPTSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKYIVHRDLKAENLLLDGDMNIKIADFGFSNEFTVGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKLLVLNPIKRGSLEQIMKDRWMNVGHEEEELKPYTEPDPDFNDTKRIDIMVTMGFARDEINDALINQKYDEVMATYILLGRKPPEFEGGESLSSGNLCQRSRPSSDLNNSTLQSPAHLKVQRSISANQKQRRFSDHAGPSIPPAVSYTKRPQANSVESEQKEEWDKDVARKLGSTTVGSKSEMTASPLVGPERKKSSTIPSNNVYSGGSMARRNTYVCERTTDRYVALQNGKDSSLTEMSVSSISSAGSSVASAVPSARPRHQKSMSTSGHPIKVTLPTIKDGSEAYRPGTTQRVPAASPSAHSISTATPDRTRFPRGSSSRSTFHGEQLRERRSVAYNGPPASPSHETGAFAHARRGTSTGIISKITSKFVRRDPSEGEASGRTDTSRSTSGEPKERDKEEGKDSKPRSLRFTWSMKTTSSMDPNDMMREIRKVLDANNCDYEQKERFLLFCVHGDARQDSLVQWEMEVCKLPRLSLNGVRFKRISGTSIAFKNIASKIANELKL
uniprot
proteins
disease_involvement
DISEASE: Note=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.
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 DCX, MAP2 and MAP4. Phosphorylates the microtubule-associated protein MAPT/TAU (PubMed:23666762). 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). {ECO:0000269|PubMed:11433294, ECO:0000269|PubMed:17573348, ECO:0000269|PubMed:23666762}.
uniprot
proteins
mass_dalton
89003
uniprot
proteins
mutagenesis
MUTAGEN 215; /note="T->A: Prevents phosphorylation and activation by STK11/LKB1 complex."; /evidence="ECO:0000269|PubMed:14976552"; MUTAGEN 215; /note="T->E: Constitutively active."; /evidence="ECO:0000269|PubMed:14976552"; MUTAGEN 698; /note="R->S: Impairs phospholipid-binding, targeting to membrane and vesicle-binding; when associated with S-701."; /evidence="ECO:0000269|PubMed:21145462"; MUTAGEN 701; /note="R->S: Impairs phospholipid-binding, targeting to membrane and vesicle-binding; when associated with S-698."; /evidence="ECO:0000269|PubMed:21145462"; MUTAGEN 771..773; /note="RFK->AFA: Impairs phospholipid-binding."; /evidence="ECO:0000269|PubMed:21145462
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000250, ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:17573348}.
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
10819331
uniprot
proteins
pubmed
11089574
uniprot
proteins
pubmed
11433294
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14976552
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16803889
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17573348
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18492799
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19559622
uniprot
proteins
pubmed
20071654
uniprot
proteins
pubmed
21145462
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23666762
uniprot
proteins
pubmed
9108484
uniprot
proteins
sequence_length
795
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21145462}; Peripheral membrane protein {ECO:0000269|PubMed:21145462}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:23666762}. Cell projection, dendrite {ECO:0000269|PubMed:23666762}. Note=Appears to localize to an intracellular network. {ECO:0000250}.
uniprot
proteins