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Protein

MAP/microtubule affinity-regulating kinase 4

Gene

MARK4

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

Functioni

Serine/threonine-protein kinase (PubMed:15009667, PubMed:14594945, PubMed:23666762, PubMed:23184942). Phosphorylates the microtubule-associated protein MAPT (PubMed:14594945, PubMed:23666762). Also phosphorylates the microtubule-associated proteins MAP2 and MAP4 (PubMed:14594945). Involved in regulation of the microtubule network, causing reorganization of microtubules into bundles (PubMed:14594945, PubMed:25123532). Required for the initiation of axoneme extension during cilium assembly (PubMed:23400999). Regulates the centrosomal location of ODF2 and phosphorylates ODF2 in vitro (PubMed:23400999). Plays a role in cell cycle progression, specifically in the G1/S checkpoint (PubMed:25123532). Reduces neuronal cell survival (PubMed:15009667). Plays a role in energy homeostasis by regulating satiety and metabolic rate (By similarity). Promotes adipogenesis by activating JNK1 and inhibiting the p38MAPK pathway, and triggers apoptosis by activating the JNK1 pathway (By similarity). Phosphorylates mTORC1 complex member RPTOR and acts as a negative regulator of the mTORC1 complex, probably due to disruption of the interaction between phosphorylated RPTOR and the RRAGA/RRAGC heterodimer which is required for mTORC1 activation (PubMed:23184942).By similarity6 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.3 Publications

Cofactori

Mg2+1 Publication

Enzyme regulationi

Activated by phosphorylation on Thr-214.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei88 – 881ATPPROSITE-ProRule annotation
Active sitei181 – 1811Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi65 – 739ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • gamma-tubulin binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • tau-protein kinase activity Source: UniProtKB
  • ubiquitin binding Source: UniProtKB

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • cell projection organization Source: UniProtKB-KW
  • microtubule bundle formation Source: UniProtKB
  • microtubule cytoskeleton organization Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • nervous system development Source: UniProtKB
  • positive regulation of programmed cell death Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Cilium biogenesis/degradation, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-5620912. Anchoring of the basal body to the plasma membrane.
SignaLinkiQ96L34.
SIGNORiQ96L34.

Names & Taxonomyi

Protein namesi
Recommended name:
MAP/microtubule affinity-regulating kinase 4 (EC:2.7.11.13 Publications)
Alternative name(s):
MAP/microtubule affinity-regulating kinase-like 1
Gene namesi
Name:MARK4
Synonyms:KIAA1860, MARKL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:13538. MARK4.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • ciliary basal body Source: CACAO
  • cytosol Source: Reactome
  • microtubule cytoskeleton Source: UniProtKB
  • microtubule organizing center Source: UniProtKB
  • neuron projection Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi214 – 2141T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. 1 Publication
Mutagenesisi214 – 2141T → E: Mimicks phosphorylation state, leading to increased activity. Decreases mTORC1 activity. 2 Publications

Organism-specific databases

PharmGKBiPA30641.

Chemistry

ChEMBLiCHEMBL5754.
GuidetoPHARMACOLOGYi2100.

Polymorphism and mutation databases

BioMutaiMARK4.
DMDMi29840797.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 752752MAP/microtubule affinity-regulating kinase 4PRO_0000086307Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei214 – 2141Phosphothreonine; by LKB11 Publication
Modified residuei423 – 4231PhosphoserineBy similarity
Modified residuei543 – 5431PhosphoserineCombined sources

Post-translational modificationi

Ubiquitinated with 'Lys-29'- and 'Lys-33'-linked polyubiquitins which appear to impede LKB1-mediated phosphorylation. Deubiquitinated by USP9X.2 Publications
Phosphorylated at Thr-214 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39 (PubMed:14976552). Phosphorylated throughout the cell cycle (PubMed:25123532).2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96L34.
MaxQBiQ96L34.
PaxDbiQ96L34.
PeptideAtlasiQ96L34.
PRIDEiQ96L34.

PTM databases

iPTMnetiQ96L34.
PhosphoSiteiQ96L34.

Expressioni

Tissue specificityi

Ubiquitous. Isoform 2 is brain-specific (PubMed:11326310). Expressed at highest levels in brain and testis. Also expressed in heart, lung, liver, muscle, kidney and spleen (PubMed:14594945).2 Publications

Developmental stagei

Expressed at all stages of the mitotic cell cycle.1 Publication

Gene expression databases

BgeeiQ96L34.
CleanExiHS_MARK4.
ExpressionAtlasiQ96L34. baseline and differential.
GenevisibleiQ96L34. HS.

Organism-specific databases

HPAiHPA039186.

Interactioni

Subunit structurei

Interacts with gamma-tubulin (PubMed:14594945). Interacts with ODF2 (PubMed:23400999). Interacts with USP9X (PubMed:18254724).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC42P609532EBI-302319,EBI-81752
PARD6GQ9BYG42EBI-302319,EBI-295417
PNMA1Q8ND902EBI-302319,EBI-302345
PRKCIP417432EBI-302319,EBI-286199
STK11Q158312EBI-302319,EBI-306838
TUBG1P232584EBI-302319,EBI-302589
YWHAHQ049176EBI-302319,EBI-306940

GO - Molecular functioni

  • gamma-tubulin binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi121760. 50 interactions.
IntActiQ96L34. 29 interactions.
MINTiMINT-6425023.
STRINGi9606.ENSP00000262891.

Chemistry

BindingDBiQ96L34.

Structurei

Secondary structure

1
752
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi59 – 679Combined sources
Beta strandi69 – 7810Combined sources
Turni79 – 813Combined sources
Beta strandi84 – 918Combined sources
Helixi92 – 943Combined sources
Helixi97 – 11115Combined sources
Beta strandi121 – 1266Combined sources
Beta strandi128 – 1358Combined sources
Helixi143 – 1508Combined sources
Helixi155 – 17420Combined sources
Beta strandi186 – 1894Combined sources
Beta strandi195 – 1973Combined sources
Turni219 – 2213Combined sources
Helixi224 – 2285Combined sources
Helixi235 – 25117Combined sources
Helixi261 – 27010Combined sources
Helixi281 – 29010Combined sources
Turni295 – 2973Combined sources
Helixi301 – 3044Combined sources
Helixi308 – 3114Combined sources
Helixi332 – 3398Combined sources
Turni340 – 3423Combined sources
Helixi345 – 3528Combined sources
Turni353 – 3553Combined sources
Helixi359 – 3668Combined sources
Turni367 – 3693Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5ES1X-ray2.80A44-370[»]
ProteinModelPortaliQ96L34.
SMRiQ96L34. Positions 11-369, 653-752.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini59 – 310252Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini324 – 36845UBAPROSITE-ProRule annotationAdd
BLAST
Domaini703 – 75250KA1PROSITE-ProRule annotationAdd
BLAST

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.
HOGENOMiHOG000233025.
HOVERGENiHBG052453.
InParanoidiQ96L34.
KOiK08798.
OMAiLAHEATP.
OrthoDBiEOG79CXXX.
PhylomeDBiQ96L34.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96L34-1) [UniParc]FASTAAdd to basket

Also known as: MARK4L

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
MSSRTVLAPG NDRNSDTHGT LGSGRSSDKG PSWSSRSLGA RCRNSIASCP
60 70 80 90 100
EEQPHVGNYR LLRTIGKGNF AKVKLARHIL TGREVAIKII DKTQLNPSSL
110 120 130 140 150
QKLFREVRIM KGLNHPNIVK LFEVIETEKT LYLVMEYASA GEVFDYLVSH
160 170 180 190 200
GRMKEKEARA KFRQIVSAVH YCHQKNIVHR DLKAENLLLD AEANIKIADF
210 220 230 240 250
GFSNEFTLGS KLDTFCGSPP YAAPELFQGK KYDGPEVDIW SLGVILYTLV
260 270 280 290 300
SGSLPFDGHN LKELRERVLR GKYRVPFYMS TDCESILRRF LVLNPAKRCT
310 320 330 340 350
LEQIMKDKWI NIGYEGEELK PYTEPEEDFG DTKRIEVMVG MGYTREEIKE
360 370 380 390 400
SLTSQKYNEV TATYLLLGRK TEEGGDRGAP GLALARVRAP SDTTNGTSSS
410 420 430 440 450
KGTSHSKGQR SSSSTYHRQR RHSDFCGPSP APLHPKRSPT STGEAELKEE
460 470 480 490 500
RLPGRKASCS TAGSGSRGLP PSSPMVSSAH NPNKAEIPER RKDSTSTPNN
510 520 530 540 550
LPPSMMTRRN TYVCTERPGA ERPSLLPNGK ENSSGTPRVP PASPSSHSLA
560 570 580 590 600
PPSGERSRLA RGSTIRSTFH GGQVRDRRAG GGGGGGVQNG PPASPTLAHE
610 620 630 640 650
AAPLPAGRPR PTTNLFTKLT SKLTRRVADE PERIGGPEVT SCHLPWDQTE
660 670 680 690 700
TAPRLLRFPW SVKLTSSRPP EALMAALRQA TAAARCRCRQ PQPFLLACLH
710 720 730 740 750
GGAGGPEPLS HFEVEVCQLP RPGLRGVLFR RVAGTALAFR TLVTRISNDL

EL
Length:752
Mass (Da):82,520
Last modified:December 1, 2001 - v1
Checksum:i4B430FFD2B150E7A
GO
Isoform 2 (identifier: Q96L34-2) [UniParc]FASTAAdd to basket

Also known as: MARKL1S, MARK4S

The sequence of this isoform differs from the canonical sequence as follows:
     628-752: ADEPERIGGP...VTRISNDLEL → TLDPSKRQNS...PPGCSDSPGV

Show »
Length:688
Mass (Da):75,321
Checksum:iA49143B34FDDD086
GO

Sequence cautioni

The sequence BAB47489.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB55238.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701F → S in BAB39380 (PubMed:11326310).Curated
Sequence conflicti70 – 701F → S in BAC03375 (PubMed:11326310).Curated
Sequence conflicti518 – 5181P → L in BAB55238 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti377 – 3771R → Q.1 Publication
Corresponds to variant rs35070611 [ dbSNP | Ensembl ].
VAR_040766
Natural varianti418 – 4181R → C in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
Corresponds to variant rs780763668 [ dbSNP | Ensembl ].
VAR_040767

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei628 – 752125ADEPE…NDLEL → TLDPSKRQNSNRCVSGASLP QGSKIRSQTNLRESGDLRSQ VAIYLGIKRKPPPGCSDSPG V in isoform 2. 2 PublicationsVSP_004946Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049127 mRNA. Translation: BAB39380.1.
AB088047 mRNA. Translation: BAC03375.1.
AY057448 mRNA. Translation: AAL23683.1.
AX305105 mRNA. No translation available.
AX305106 mRNA. No translation available.
AY120867 mRNA. Translation: AAM55491.1.
AB058763 mRNA. Translation: BAB47489.1. Different initiation.
AK027619 mRNA. Translation: BAB55238.1. Different initiation.
AK075272 mRNA. Translation: BAC11510.1.
CCDSiCCDS12658.1. [Q96L34-2]
CCDS56097.1. [Q96L34-1]
RefSeqiNP_001186796.1. NM_001199867.1. [Q96L34-1]
NP_113605.2. NM_031417.3. [Q96L34-2]
UniGeneiHs.34314.

Genome annotation databases

EnsembliENST00000262891; ENSP00000262891; ENSG00000007047. [Q96L34-1]
ENST00000300843; ENSP00000300843; ENSG00000007047. [Q96L34-2]
GeneIDi57787.
KEGGihsa:57787.
UCSCiuc002pba.3. human. [Q96L34-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049127 mRNA. Translation: BAB39380.1.
AB088047 mRNA. Translation: BAC03375.1.
AY057448 mRNA. Translation: AAL23683.1.
AX305105 mRNA. No translation available.
AX305106 mRNA. No translation available.
AY120867 mRNA. Translation: AAM55491.1.
AB058763 mRNA. Translation: BAB47489.1. Different initiation.
AK027619 mRNA. Translation: BAB55238.1. Different initiation.
AK075272 mRNA. Translation: BAC11510.1.
CCDSiCCDS12658.1. [Q96L34-2]
CCDS56097.1. [Q96L34-1]
RefSeqiNP_001186796.1. NM_001199867.1. [Q96L34-1]
NP_113605.2. NM_031417.3. [Q96L34-2]
UniGeneiHs.34314.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5ES1X-ray2.80A44-370[»]
ProteinModelPortaliQ96L34.
SMRiQ96L34. Positions 11-369, 653-752.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121760. 50 interactions.
IntActiQ96L34. 29 interactions.
MINTiMINT-6425023.
STRINGi9606.ENSP00000262891.

Chemistry

BindingDBiQ96L34.
ChEMBLiCHEMBL5754.
GuidetoPHARMACOLOGYi2100.

PTM databases

iPTMnetiQ96L34.
PhosphoSiteiQ96L34.

Polymorphism and mutation databases

BioMutaiMARK4.
DMDMi29840797.

Proteomic databases

EPDiQ96L34.
MaxQBiQ96L34.
PaxDbiQ96L34.
PeptideAtlasiQ96L34.
PRIDEiQ96L34.

Protocols and materials databases

DNASUi57787.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262891; ENSP00000262891; ENSG00000007047. [Q96L34-1]
ENST00000300843; ENSP00000300843; ENSG00000007047. [Q96L34-2]
GeneIDi57787.
KEGGihsa:57787.
UCSCiuc002pba.3. human. [Q96L34-1]

Organism-specific databases

CTDi57787.
GeneCardsiMARK4.
HGNCiHGNC:13538. MARK4.
HPAiHPA039186.
MIMi606495. gene.
neXtProtiNX_Q96L34.
PharmGKBiPA30641.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0586. Eukaryota.
ENOG410XNQ0. LUCA.
GeneTreeiENSGT00790000122947.
HOGENOMiHOG000233025.
HOVERGENiHBG052453.
InParanoidiQ96L34.
KOiK08798.
OMAiLAHEATP.
OrthoDBiEOG79CXXX.
PhylomeDBiQ96L34.
TreeFamiTF315213.

Enzyme and pathway databases

ReactomeiR-HSA-5620912. Anchoring of the basal body to the plasma membrane.
SignaLinkiQ96L34.
SIGNORiQ96L34.

Miscellaneous databases

GeneWikiiMARK4.
GenomeRNAii57787.
PROiQ96L34.
SOURCEiSearch...

Gene expression databases

BgeeiQ96L34.
CleanExiHS_MARK4.
ExpressionAtlasiQ96L34. baseline and differential.
GenevisibleiQ96L34. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a novel human gene, MARKL1, homologous to MARK3 and its involvement in hepatocellular carcinogenesis."
    Kato T., Satoh S., Okabe H., Kitahara O., Ono K., Kihara C., Tanaka T., Tsunoda T., Yamaoka Y., Nakamura Y., Furukawa Y.
    Neoplasia 3:4-9(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "MARK4 is a novel microtubule-associated proteins/microtubule affinity-regulating kinase that binds to the cellular microtubule network and to centrosomes."
    Trinczek B., Brajenovic M., Ebneth A., Drewes G.
    J. Biol. Chem. 279:5915-5923(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH GAMMA-TUBULIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "Identification of regulated genes during permanent focal cerebral ischaemia: characterization of the protein kinase 9b5/MARKL1/MARK4."
    Schneider A., Laage R., von Ahsen O., Fischer A., Rossner M., Scheek S., Grunewald S., Kuner R., Weber D., Kruger C., Klaussner B., Gotz B., Hiemisch H., Newrzella D., Martin-Villalba A., Bach A., Schwaninger M.
    J. Neurochem. 88:1114-1126(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC ACTIVITY.
  4. "Neural progenitor-restricted isoform of MARKL1 gene is upregulated by 19q13 amplification in human glioblastoma."
    Beghini A., Magnani I., Roversi G., Piepoli T., DiTerlizzi S., Pollo B., Conti A.M.F., Cowell J.K., Finocchiaro G., Larizza L.
    Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  5. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
    DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Thyroid.
  7. "LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1."
    Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A., Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G., Alessi D.R.
    EMBO J. 23:833-843(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PHOSPHORYLATION AT THR-214, MUTAGENESIS OF THR-214.
  8. "Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains."
    Al-Hakim A.K., Zagorska A., Chapman L., Deak M., Peggie M., Alessi D.R.
    Biochem. J. 411:249-260(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP9X, INTERACTION WITH USP9X.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Microtubule-associated protein/microtubule affinity-regulating kinase 4 (MARK4) is a negative regulator of the mammalian target of rapamycin complex 1 (mTORC1)."
    Li L., Guan K.L.
    J. Biol. Chem. 288:703-708(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF THR-214.
  11. "The microtubule affinity regulating kinase MARK4 promotes axoneme extension during early ciliogenesis."
    Kuhns S., Schmidt K.N., Reymann J., Gilbert D.F., Neuner A., Hub B., Carvalho R., Wiedemann P., Zentgraf H., Erfle H., Klingmuller U., Boutros M., Pereira G.
    J. Cell Biol. 200:505-522(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ODF2, SUBCELLULAR LOCATION.
  12. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  13. "Role of individual MARK isoforms in phosphorylation of tau at Ser262 in Alzheimer's disease."
    Gu G.J., Lund H., Wu D., Blokzijl A., Classon C., von Euler G., Landegren U., Sunnemark D., Kamali-Moghaddam M.
    NeuroMolecular Med. 15:458-469(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. "Microtubule-associated protein/microtubule affinity-regulating kinase 4 (MARK4) plays a role in cell cycle progression and cytoskeletal dynamics."
    Rovina D., Fontana L., Monti L., Novielli C., Panini N., Sirchia S.M., Erba E., Magnani I., Larizza L.
    Eur. J. Cell Biol. 93:355-365(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, PHOSPHORYLATION.
  15. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-377 AND CYS-418.

Entry informationi

Entry nameiMARK4_HUMAN
AccessioniPrimary (citable) accession number: Q96L34
Secondary accession number(s): Q8NG37
, Q96JG7, Q96SQ2, Q9BYD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 156 of the entry and version 1 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 19
    Human chromosome 19: 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.