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Q03141

- MARK3_MOUSE

UniProt

Q03141 - MARK3_MOUSE

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Protein

MAP/microtubule affinity-regulating kinase 3

Gene
Mark3, Emk2, Mpk10
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the specific phosphorylation of microtubule-associated proteins for tau, MAP2 and MAP4. Phosphorylates CDC25C. 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 By similarity.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by phosphorylation on Thr-211. Inhibited by phosphorylation on Thr-564 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei85 – 851ATP By similarity
Active sitei178 – 1781Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi62 – 709ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine kinase activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
MAP/microtubule affinity-regulating kinase 3 (EC:2.7.11.1)
Alternative name(s):
ELKL motif kinase 2
Short name:
EMK-2
MPK-10
Gene namesi
Name:Mark3
Synonyms:Emk2, Mpk10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:1341865. Mark3.

Subcellular locationi

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 753753MAP/microtubule affinity-regulating kinase 3PRO_0000086305Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421Phosphoserine By similarity
Modified residuei211 – 2111Phosphothreonine; by LKB1 By similarity
Modified residuei383 – 3831Phosphoserine By similarity
Modified residuei400 – 4001Phosphoserine By similarity
Modified residuei469 – 4691Phosphoserine By similarity
Modified residuei549 – 5491Phosphothreonine By similarity
Modified residuei564 – 5641Phosphothreonine; by PKC/PRKCZ By similarity
Modified residuei598 – 5981Phosphoserine By similarity
Modified residuei643 – 6431Phosphoserine By similarity

Post-translational modificationi

Phosphorylated at Thr-211 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Phosphorylation at Thr-564 by PRKCZ/aPKC inhibits the kinase activity By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ03141.
PRIDEiQ03141.

PTM databases

PhosphoSiteiQ03141.

Expressioni

Gene expression databases

ArrayExpressiQ03141.
BgeeiQ03141.
CleanExiMM_MARK3.
GenevestigatoriQ03141.

Interactioni

Protein-protein interaction databases

BioGridi201312. 6 interactions.
IntActiQ03141. 1 interaction.

Structurei

Secondary structure

1
753
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi672 – 68514
Beta strandi689 – 6924
Beta strandi698 – 7025
Beta strandi704 – 7063
Helixi707 – 7093
Beta strandi711 – 7199
Beta strandi721 – 73515
Helixi737 – 75014

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UL7NMR-A659-753[»]
1V5SNMR-A674-753[»]
ProteinModelPortaliQ03141.
SMRiQ03141. Positions 1-366, 657-753.

Miscellaneous databases

EvolutionaryTraceiQ03141.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 307252Protein kinaseAdd
BLAST
Domaini326 – 36540UBAAdd
BLAST
Domaini695 – 74450KA1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi374 – 41239Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 UBA domain.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00730000110535.
HOGENOMiHOG000233025.
HOVERGENiHBG052453.
InParanoidiQ03141.
KOiK08798.
OMAiTFHGQLR.
OrthoDBiEOG79CXXX.
PhylomeDBiQ03141.
TreeFamiTF315213.

Family and domain databases

Gene3Di3.30.310.80. 1 hit.
InterProiIPR028375. KA1/Ssp2_C.
IPR001772. KA1_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view]
PfamiPF02149. KA1. 1 hit.
PF00069. Pkinase. 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. Align

Isoform 1 (identifier: Q03141-1) [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

MSTRTPLPTV NERDTENHIS HGDGRQEVTS RTGRSGARCR NSIASCADEQ    50
PHIGNYRLLK TIGKGNFAKV KLARHILTGR EVAIKIIDKT QLNPTSLQKL 100
FREVRIMKIL NHPNIVKLFE VIETEKTLYL IMEYASGGEV FDYLVAHGRM 150
KEKEARAKFR QIVSAVQYCH QKRIVHRDLK AENLLLDADM NIKIADFGFS 200
NEFTVGSKLD TFCGSPPYAA PELFQGKKYD GPEVDVWSLG VILYTLVSGS 250
LPFDGQNLKE LRERVLRGKY RIPFYMSTDC ENLLKRFLVL NPVKRGTLEQ 300
IMKDRWINAG HEEDELKPFV EPELDISDQK RIDIMVGMGY SQEEIQESLS 350
KMKYDEITAT YLLLGRKSAE LDASDSSSSS NLSLAKVRPN SDLSNSTGQS 400
PHHKGQRSVS SSQKQRRYSD HAGPAIPSVV AYPKRSQTST ADSDLKEDGI 450
PSRKSSSSAV GGKGIAPASP MLGNAGNPNK ADIPERKKSP AVPSSNTASG 500
GMTRRNTYVC SERCAADRHS VIQNGKENSA IPDERTPVAS THSISSATTP 550
DRIRFPRGTA SRSTFHGQPR ERRTATYNGP PASPSLSHEA TPLSQTRSRG 600
STNLFSKLTS KLTRRNMSFR FIKRLPTEYE RNGRYEGSSR NVSSEQKDEN 650
REAKPRSLRF TWSMKTTSSM DPSDMMREIR KVLDANNCDY EQRERFLLFC 700
VHGDGHAENL VQWEMEVCKL PRLSLNGVRF KRISGTSIAF KNIASKIANE 750
LKL 753
Length:753
Mass (Da):84,390
Last modified:November 8, 2005 - v2
Checksum:iB597BDD0398617CF
GO
Isoform 2 (identifier: Q03141-2) [UniParc]FASTAAdd to Basket

Also known as: ELKL motif kinase 2 short form

The sequence of this isoform differs from the canonical sequence as follows:
     615-638: Missing.

Show »
Length:729
Mass (Da):81,400
Checksum:iD76FBB9A27ED19C9
GO
Isoform 3 (identifier: Q03141-3) [UniParc]FASTAAdd to Basket

Also known as: ELKL motif kinase 2 long form

The sequence of this isoform differs from the canonical sequence as follows:
     615-623: Missing.

Show »
Length:744
Mass (Da):83,209
Checksum:i2CCA8FA8AEE20360
GO

Sequence cautioni

The sequence AAH26445.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAC35922.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei615 – 63824Missing in isoform 2. VSP_016140Add
BLAST
Alternative sequencei615 – 6239Missing in isoform 3. VSP_016141

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti333 – 3331D → V in BAC35922. 1 Publication
Sequence conflicti496 – 4961N → S in AAF64456. 1 Publication
Sequence conflicti511 – 5111S → G in BAC35922. 1 Publication
Sequence conflicti684 – 6841D → G in BAC35922. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF240783 mRNA. Translation: AAF64456.1.
AK075742 mRNA. Translation: BAC35922.1. Different initiation.
AK132247 mRNA. Translation: BAE21056.1.
AK166157 mRNA. Translation: BAE38602.1.
BC026445 mRNA. Translation: AAH26445.1. Different initiation.
X57244 mRNA. Translation: CAA40520.1.
CCDSiCCDS26181.1. [Q03141-3]
CCDS26182.1. [Q03141-2]
PIRiS30496.
RefSeqiNP_067491.2. NM_021516.4. [Q03141-3]
NP_073712.2. NM_022801.4. [Q03141-2]
XP_006515578.1. XM_006515515.1. [Q03141-1]
UniGeneiMm.260504.
Mm.420865.

Genome annotation databases

EnsembliENSMUST00000075281; ENSMUSP00000074757; ENSMUSG00000007411. [Q03141-2]
ENSMUST00000084953; ENSMUSP00000082017; ENSMUSG00000007411. [Q03141-3]
GeneIDi17169.
KEGGimmu:17169.
UCSCiuc007pdk.2. mouse. [Q03141-3]
uc007pdl.2. mouse. [Q03141-2]
uc007pdm.2. mouse. [Q03141-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF240783 mRNA. Translation: AAF64456.1 .
AK075742 mRNA. Translation: BAC35922.1 . Different initiation.
AK132247 mRNA. Translation: BAE21056.1 .
AK166157 mRNA. Translation: BAE38602.1 .
BC026445 mRNA. Translation: AAH26445.1 . Different initiation.
X57244 mRNA. Translation: CAA40520.1 .
CCDSi CCDS26181.1. [Q03141-3 ]
CCDS26182.1. [Q03141-2 ]
PIRi S30496.
RefSeqi NP_067491.2. NM_021516.4. [Q03141-3 ]
NP_073712.2. NM_022801.4. [Q03141-2 ]
XP_006515578.1. XM_006515515.1. [Q03141-1 ]
UniGenei Mm.260504.
Mm.420865.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UL7 NMR - A 659-753 [» ]
1V5S NMR - A 674-753 [» ]
ProteinModelPortali Q03141.
SMRi Q03141. Positions 1-366, 657-753.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201312. 6 interactions.
IntActi Q03141. 1 interaction.

PTM databases

PhosphoSitei Q03141.

Proteomic databases

PaxDbi Q03141.
PRIDEi Q03141.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000075281 ; ENSMUSP00000074757 ; ENSMUSG00000007411 . [Q03141-2 ]
ENSMUST00000084953 ; ENSMUSP00000082017 ; ENSMUSG00000007411 . [Q03141-3 ]
GeneIDi 17169.
KEGGi mmu:17169.
UCSCi uc007pdk.2. mouse. [Q03141-3 ]
uc007pdl.2. mouse. [Q03141-2 ]
uc007pdm.2. mouse. [Q03141-1 ]

Organism-specific databases

CTDi 4140.
MGIi MGI:1341865. Mark3.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00730000110535.
HOGENOMi HOG000233025.
HOVERGENi HBG052453.
InParanoidi Q03141.
KOi K08798.
OMAi TFHGQLR.
OrthoDBi EOG79CXXX.
PhylomeDBi Q03141.
TreeFami TF315213.

Miscellaneous databases

ChiTaRSi MARK3. mouse.
EvolutionaryTracei Q03141.
NextBioi 291458.
PROi Q03141.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q03141.
Bgeei Q03141.
CleanExi MM_MARK3.
Genevestigatori Q03141.

Family and domain databases

Gene3Di 3.30.310.80. 1 hit.
InterProi IPR028375. KA1/Ssp2_C.
IPR001772. KA1_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view ]
Pfami PF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view ]
SUPFAMi SSF103243. SSF103243. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS50032. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse EMK2 (ELKL motif kinase 2)."
    Darmon Y., Tornier C., Bessone S., Le Morvan V.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Embryo, Lung and Placenta.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 168-753 (ISOFORM 2).
    Strain: FVB/N.
    Tissue: Mammary gland.
  4. "An Eph-related receptor protein tyrosine kinase gene segmentally expressed in the developing mouse hindbrain."
    Gilardi-Hebenstreit P., Nieto M.A., Frain M., Mattei M.-G., Chestier A., Wilkinson D.G., Charnay P.
    Oncogene 7:2499-2506(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 180-234.
    Strain: C57BL/6.
    Tissue: Embryonic brain.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Solution structure of the kinase-associated domain 1 of mouse microtubule-associated protein/microtubule affinity-regulating kinase 3."
    Tochio N., Koshiba S., Kobayashi N., Inoue M., Yabuki T., Aoki M., Seki E., Matsuda T., Tomo Y., Motoda Y., Kobayashi A., Tanaka A., Hayashizaki Y., Terada T., Shirouzu M., Kigawa T., Yokoyama S.
    Protein Sci. 15:2534-2543(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 659-753.

Entry informationi

Entry nameiMARK3_MOUSE
AccessioniPrimary (citable) accession number: Q03141
Secondary accession number(s): Q3TM40
, Q3V1U3, Q8C6G9, Q8R375, Q9JKE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 8, 2005
Last modified: July 9, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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