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 MARK1

Gene

MARK1

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 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).2 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 phosphorylation at Ser-219 (By similarity). Activated by phosphorylation on Thr-215.By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei89ATPPROSITE-ProRule annotationBy similarity1
Active sitei182Proton acceptorPROSITE-ProRule annotationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi66 – 74ATPPROSITE-ProRule annotationBy similarity9

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • phosphatidic acid binding Source: UniProtKB
  • phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  • phosphatidylserine binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • tau-protein kinase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciZFISH:HS03987-MONOMER.
SignaLinkiQ9P0L2.
SIGNORiQ9P0L2.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:MARK1Imported
Synonyms:KIAA1477Imported, MARKImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6896. MARK1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB
  • microtubule cytoskeleton Source: ProtInc
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi215T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. 1 Publication1
Mutagenesisi215T → E: Constitutively active. 1 Publication1
Mutagenesisi698R → S: Impairs phospholipid-binding, targeting to membrane and vesicle-binding; when associated with S-701. 1 Publication1
Mutagenesisi701R → S: Impairs phospholipid-binding, targeting to membrane and vesicle-binding; when associated with S-698. 1 Publication1
Mutagenesisi771 – 773RFK → AFA: Impairs phospholipid-binding. 1 Publication3

Keywords - Diseasei

Autism, Autism spectrum disorder

Organism-specific databases

DisGeNETi4139.
OpenTargetsiENSG00000116141.
PharmGKBiPA30639.

Chemistry databases

ChEMBLiCHEMBL5940.
GuidetoPHARMACOLOGYi2097.

Polymorphism and mutation databases

BioMutaiMARK1.
DMDMi124056494.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000862981 – 795Serine/threonine-protein kinase MARK1Add BLAST795

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5PhosphothreonineCombined sources1
Modified residuei208Phosphothreonine1 Publication1
Modified residuei215Phosphothreonine; by LKB1 and TAOK11 Publication1
Modified residuei219Phosphoserine; by GSK3-betaBy similarity1
Modified residuei382PhosphoserineBy similarity1
Modified residuei390PhosphoserineBy similarity1
Modified residuei393PhosphoserineBy similarity1
Modified residuei403PhosphoserineCombined sources1
Modified residuei423PhosphoserineBy similarity1
Modified residuei444PhosphoserineBy similarity1
Modified residuei475PhosphoserineBy similarity1
Modified residuei588PhosphoserineCombined sources1
Modified residuei613Phosphothreonine; by PKC/PRKCZBy similarity1
Modified residuei666PhosphoserineBy similarity1

Post-translational modificationi

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.By similarity2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9P0L2.
MaxQBiQ9P0L2.
PaxDbiQ9P0L2.
PeptideAtlasiQ9P0L2.
PRIDEiQ9P0L2.

PTM databases

iPTMnetiQ9P0L2.
PhosphoSitePlusiQ9P0L2.

Expressioni

Tissue specificityi

Highly expressed in heart, skeletal muscle, brain, fetal brain and fetal kidney.1 Publication

Gene expression databases

BgeeiENSG00000116141.
CleanExiHS_MARK1.
ExpressionAtlasiQ9P0L2. baseline and differential.
GenevisibleiQ9P0L2. HS.

Organism-specific databases

HPAiHPA007421.
HPA008061.

Interactioni

Protein-protein interaction databases

BioGridi110309. 16 interactors.
DIPiDIP-39777N.
IntActiQ9P0L2. 10 interactors.
MINTiMINT-3975018.
STRINGi9606.ENSP00000355884.

Chemistry databases

BindingDBiQ9P0L2.

Structurei

Secondary structure

1795
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi60 – 68Combined sources9
Beta strandi70 – 79Combined sources10
Turni80 – 82Combined sources3
Beta strandi85 – 92Combined sources8
Helixi98 – 113Combined sources16
Beta strandi122 – 127Combined sources6
Beta strandi129 – 136Combined sources8
Helixi144 – 151Combined sources8
Helixi156 – 176Combined sources21
Helixi185 – 187Combined sources3
Beta strandi188 – 190Combined sources3
Beta strandi196 – 198Combined sources3
Beta strandi221 – 223Combined sources3
Helixi225 – 229Combined sources5
Helixi236 – 252Combined sources17
Helixi262 – 271Combined sources10
Helixi282 – 291Combined sources10
Helixi296 – 298Combined sources3
Helixi302 – 306Combined sources5
Helixi309 – 312Combined sources4
Beta strandi316 – 318Combined sources3
Helixi333 – 342Combined sources10
Helixi346 – 354Combined sources9
Helixi360 – 367Combined sources8
Helixi714 – 727Combined sources14
Beta strandi731 – 736Combined sources6
Beta strandi739 – 745Combined sources7
Turni747 – 750Combined sources4
Beta strandi753 – 762Combined sources10
Helixi763 – 765Combined sources3
Beta strandi767 – 777Combined sources11
Helixi779 – 792Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HAKX-ray2.60A/B/C/D/E/F/G/H45-371[»]
3OSEX-ray1.70A683-795[»]
ProteinModelPortaliQ9P0L2.
SMRiQ9P0L2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P0L2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini60 – 311Protein kinasePROSITE-ProRule annotationAdd BLAST252
Domaini325 – 370UBAPROSITE-ProRule annotationAdd BLAST46
Domaini746 – 795KA1PROSITE-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 (By similarity).By similarity
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).1 Publication

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.
InParanoidiQ9P0L2.
KOiK08798.
PhylomeDBiQ9P0L2.
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.
IPR033627. MARK1.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR015940. UBA.
[Graphical view]
PANTHERiPTHR24346. PTHR24346. 1 hit.
PTHR24346:SF21. PTHR24346:SF21. 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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9P0L2-1) [UniParc]FASTAAdd to basket

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
MSARTPLPTV NERDTENHTS VDGYTEPHIQ PTKSSSRQNI PRCRNSITSA
60 70 80 90 100
TDEQPHIGNY RLQKTIGKGN FAKVKLARHV LTGREVAVKI IDKTQLNPTS
110 120 130 140 150
LQKLFREVRI MKILNHPNIV KLFEVIETEK TLYLVMEYAS GGEVFDYLVA
160 170 180 190 200
HGRMKEKEAR AKFRQIVSAV QYCHQKYIVH RDLKAENLLL DGDMNIKIAD
210 220 230 240 250
FGFSNEFTVG NKLDTFCGSP PYAAPELFQG KKYDGPEVDV WSLGVILYTL
260 270 280 290 300
VSGSLPFDGQ NLKELRERVL RGKYRIPFYM STDCENLLKK LLVLNPIKRG
310 320 330 340 350
SLEQIMKDRW MNVGHEEEEL KPYTEPDPDF NDTKRIDIMV TMGFARDEIN
360 370 380 390 400
DALINQKYDE VMATYILLGR KPPEFEGGES LSSGNLCQRS RPSSDLNNST
410 420 430 440 450
LQSPAHLKVQ RSISANQKQR RFSDHAGPSI PPAVSYTKRP QANSVESEQK
460 470 480 490 500
EEWDKDVARK LGSTTVGSKS EMTASPLVGP ERKKSSTIPS NNVYSGGSMA
510 520 530 540 550
RRNTYVCERT TDRYVALQNG KDSSLTEMSV SSISSAGSSV ASAVPSARPR
560 570 580 590 600
HQKSMSTSGH PIKVTLPTIK DGSEAYRPGT TQRVPAASPS AHSISTATPD
610 620 630 640 650
RTRFPRGSSS RSTFHGEQLR ERRSVAYNGP PASPSHETGA FAHARRGTST
660 670 680 690 700
GIISKITSKF VRRDPSEGEA SGRTDTSRST SGEPKERDKE EGKDSKPRSL
710 720 730 740 750
RFTWSMKTTS SMDPNDMMRE IRKVLDANNC DYEQKERFLL FCVHGDARQD
760 770 780 790
SLVQWEMEVC KLPRLSLNGV RFKRISGTSI AFKNIASKIA NELKL
Length:795
Mass (Da):89,003
Last modified:January 23, 2007 - v2
Checksum:i71BF6EB76912631B
GO
Isoform 2Curated (identifier: Q9P0L2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-135: Missing.
     663-677: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:645
Mass (Da):72,073
Checksum:i7AE395507519DCF6
GO
Isoform 3Curated (identifier: Q9P0L2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     120-141: Missing.
     663-677: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:758
Mass (Da):84,911
Checksum:iD6F1BCD8E884661D
GO

Sequence cautioni

The sequence BAA96001 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAB55152 differs from that shown. Reason: Frameshift at position 763.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti16E → V in AAF72103 (Ref. 2) Curated1
Sequence conflicti20S → T in AAF72103 (Ref. 2) Curated1
Sequence conflicti522D → N in BAB55152 (PubMed:14702039).Curated1
Sequence conflicti544V → A in BAB55152 (PubMed:14702039).Curated1
Sequence conflicti763P → A in BAB55152 (PubMed:14702039).Curated1
Sequence conflicti794K → M in BAA96001 (PubMed:10819331).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_040760233Y → C in a gastric adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_040761355N → T in an ovarian serous carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_040762530V → M.1 PublicationCorresponds to variant rs56212551dbSNPEnsembl.1
Natural variantiVAR_040763578P → L.1 PublicationCorresponds to variant rs55691439dbSNPEnsembl.1
Natural variantiVAR_030018645R → G.Corresponds to variant rs12123778dbSNPEnsembl.1
Natural variantiVAR_040764691E → G.1 PublicationCorresponds to variant rs55688276dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0517021 – 135Missing in isoform 2. 1 PublicationAdd BLAST135
Alternative sequenceiVSP_051703120 – 141Missing in isoform 3. 1 PublicationAdd BLAST22
Alternative sequenceiVSP_051704663 – 677Missing in isoform 2 and isoform 3. 2 PublicationsAdd BLAST15

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31029.2. [Q9P0L2-1]
CCDS65789.1. [Q9P0L2-3]
RefSeqiNP_001273057.1. NM_001286128.1. [Q9P0L2-3]
NP_061120.3. NM_018650.4. [Q9P0L2-1]
UniGeneiHs.497806.

Genome annotation databases

EnsembliENST00000366917; ENSP00000355884; ENSG00000116141. [Q9P0L2-1]
ENST00000366918; ENSP00000355885; ENSG00000116141. [Q9P0L2-3]
GeneIDi4139.
KEGGihsa:4139.
UCSCiuc001hmm.6. human. [Q9P0L2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31029.2. [Q9P0L2-1]
CCDS65789.1. [Q9P0L2-3]
RefSeqiNP_001273057.1. NM_001286128.1. [Q9P0L2-3]
NP_061120.3. NM_018650.4. [Q9P0L2-1]
UniGeneiHs.497806.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HAKX-ray2.60A/B/C/D/E/F/G/H45-371[»]
3OSEX-ray1.70A683-795[»]
ProteinModelPortaliQ9P0L2.
SMRiQ9P0L2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110309. 16 interactors.
DIPiDIP-39777N.
IntActiQ9P0L2. 10 interactors.
MINTiMINT-3975018.
STRINGi9606.ENSP00000355884.

Chemistry databases

BindingDBiQ9P0L2.
ChEMBLiCHEMBL5940.
GuidetoPHARMACOLOGYi2097.

PTM databases

iPTMnetiQ9P0L2.
PhosphoSitePlusiQ9P0L2.

Polymorphism and mutation databases

BioMutaiMARK1.
DMDMi124056494.

Proteomic databases

EPDiQ9P0L2.
MaxQBiQ9P0L2.
PaxDbiQ9P0L2.
PeptideAtlasiQ9P0L2.
PRIDEiQ9P0L2.

Protocols and materials databases

DNASUi4139.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366917; ENSP00000355884; ENSG00000116141. [Q9P0L2-1]
ENST00000366918; ENSP00000355885; ENSG00000116141. [Q9P0L2-3]
GeneIDi4139.
KEGGihsa:4139.
UCSCiuc001hmm.6. human. [Q9P0L2-1]

Organism-specific databases

CTDi4139.
DisGeNETi4139.
GeneCardsiMARK1.
HGNCiHGNC:6896. MARK1.
HPAiHPA007421.
HPA008061.
MIMi606511. gene.
neXtProtiNX_Q9P0L2.
OpenTargetsiENSG00000116141.
PharmGKBiPA30639.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0586. Eukaryota.
ENOG410XNQ0. LUCA.
GeneTreeiENSGT00790000122947.
HOVERGENiHBG052453.
InParanoidiQ9P0L2.
KOiK08798.
PhylomeDBiQ9P0L2.
TreeFamiTF315213.

Enzyme and pathway databases

BioCyciZFISH:HS03987-MONOMER.
SignaLinkiQ9P0L2.
SIGNORiQ9P0L2.

Miscellaneous databases

ChiTaRSiMARK1. human.
EvolutionaryTraceiQ9P0L2.
GeneWikiiMARK1.
GenomeRNAii4139.
PROiQ9P0L2.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000116141.
CleanExiHS_MARK1.
ExpressionAtlasiQ9P0L2. baseline and differential.
GenevisibleiQ9P0L2. 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.
IPR033627. MARK1.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR015940. UBA.
[Graphical view]
PANTHERiPTHR24346. PTHR24346. 1 hit.
PTHR24346:SF21. PTHR24346:SF21. 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 nameiMARK1_HUMAN
AccessioniPrimary (citable) accession number: Q9P0L2
Secondary accession number(s): D3DTB0
, D3DTB1, Q2HIY1, Q5VTF9, Q5VTG0, Q96SW9, Q9P251
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 149 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

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 (PubMed:11089574).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. 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.