Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q05512

- MARK2_MOUSE

UniProt

Q05512 - MARK2_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Serine/threonine-protein kinase MARK2

Gene

Mark2

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4, MAPT/TAU and RAB11FIP2. 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 dishevelled 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 (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.
ATP + [tau protein] = ADP + [tau protein] phosphate.

Cofactori

Magnesium.By similarity

Enzyme regulationi

Inhibited by PAK7/PAK5; inhibition is independent of the kinase activity of PAK7/PAK5. Activated by phosphorylation on Thr-208. Inhibited by phosphorylation at Ser-212 and Thr-593. Inhibited by hymenialdisine (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei82 – 821ATPPROSITE-ProRule annotation
Active sitei175 – 1751Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi59 – 679ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. lipid binding Source: UniProtKB-KW
  3. magnesium ion binding Source: UniProtKB
  4. protein serine/threonine kinase activity Source: UniProtKB
  5. tau-protein kinase activity Source: UniProtKB

GO - Biological processi

  1. establishment of cell polarity Source: UniProtKB
  2. establishment or maintenance of epithelial cell apical/basal polarity Source: UniProtKB
  3. intracellular signal transduction Source: UniProtKB
  4. neuron migration Source: UniProtKB
  5. positive regulation of neuron projection development Source: UniProtKB
  6. protein autophosphorylation Source: UniProtKB
  7. protein phosphorylation Source: UniProtKB
  8. regulation of axonogenesis Source: UniProtKB
  9. regulation of cytoskeleton organization Source: UniProtKB
  10. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Differentiation, Wnt signaling pathway

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase MARK2 (EC:2.7.11.1, EC:2.7.11.26)
Alternative name(s):
ELKL motif kinase 1
Short name:
EMK-1
MAP/microtubule affinity-regulating kinase 2
PAR1 homolog
PAR1 homolog b
Short name:
Par-1b
Short name:
mPar-1b
Gene namesi
Name:Mark2
Synonyms:Emk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:99638. Mark2.

Subcellular locationi

Cell membrane By similarity; Peripheral membrane protein By similarity. Lateral cell membrane By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasm By similarity
Note: Phosphorylation at Thr-593 by PRKCZ/aPKC and subsequent interaction with 14-3-3 protein YWHAZ promotes relocation from the cell membrane to the cytoplasm.By similarity

GO - Cellular componenti

  1. actin filament Source: UniProtKB
  2. basal cortex Source: MGI
  3. lateral plasma membrane Source: UniProtKB
  4. membrane Source: UniProtKB
  5. microtubule bundle Source: UniProtKB
  6. nucleus Source: MGI
  7. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice have no embryonic defect and are viable. They do not display obvious neuronal phenotype, possibly due to genetic redundancy with Mark1, Mark3 and Mark4. They however show an overall proportionate dwarfism and a peculiar hypofertility: homozygotes are not fertile when intercrossed, but are fertile in other types of crosses. They also show immune-cell dysfunction. As mice age, they develop splenomegaly, lymphadenopathy, membranoproliferative glomerulonephritis, and lymphocytic infiltrates in the lungs, parotid glands and kidneys. Moreover, mice are lean, insulin hypersensitive, resistant to high-fat-diet-induced weight gain, and hypermetabolic.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 776776Serine/threonine-protein kinase MARK2PRO_0000086302Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401PhosphoserineBy similarity
Modified residuei58 – 581Phosphothreonine; by autocatalysisBy similarity
Modified residuei91 – 911Phosphoserine; by CaMK1By similarity
Modified residuei92 – 921Phosphoserine; by CaMK1By similarity
Modified residuei93 – 931Phosphoserine; by CaMK1By similarity
Modified residuei208 – 2081Phosphothreonine; by LKB1 and TAOK1
Modified residuei212 – 2121Phosphoserine; by GSK3-betaBy similarity
Modified residuei274 – 2741Phosphoserine; by autocatalysisBy similarity
Modified residuei275 – 2751Phosphothreonine; by autocatalysisBy similarity
Modified residuei294 – 2941Phosphothreonine; by CaMK1By similarity
Modified residuei409 – 4091PhosphoserineBy similarity
Modified residuei453 – 4531Phosphoserine1 Publication
Modified residuei483 – 4831PhosphoserineBy similarity
Modified residuei490 – 4901PhosphoserineBy similarity
Modified residuei566 – 5661PhosphoserineBy similarity
Modified residuei593 – 5931Phosphothreonine; by PKC/PRKCZBy similarity
Modified residuei616 – 6161PhosphoserineBy similarity
Modified residuei710 – 7101PhosphoserineBy similarity

Post-translational modificationi

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-593 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 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ05512.
PaxDbiQ05512.
PRIDEiQ05512.

PTM databases

PhosphoSiteiQ05512.

Expressioni

Tissue specificityi

Highly expressed in adult kidney and testis, lower levels in heart, brain, spleen, lung and liver. Expressed in the head and neural fold in 8 dpc embryos, the limb buds, telencephalic vesicles, eyes, branchial archs and heart at 11.5 dpc, the ectoderm at 13 dpc and epiderm, hair and whisker follicles at 15 dpc.1 Publication

Gene expression databases

BgeeiQ05512.
CleanExiMM_MARK2.
ExpressionAtlasiQ05512. baseline and differential.
GenevestigatoriQ05512.

Interactioni

Subunit structurei

Homodimer. Interacts with PAK7/PAK5; leading to inhibit the protein kinase activity (By similarity). Interacts (when phosphorylated at Thr-593) with YWHAZ. Interacts with PAK7/PAK5 (By similarity). Interacts with MTCL1; the interaction is direct and increases MARK2 microtubule-binding ability (By similarity).By similarity

Protein-protein interaction databases

BioGridi199437. 7 interactions.
IntActiQ05512. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ05512.
SMRiQ05512. Positions 13-363, 677-776.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 304252Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini323 – 36240UBAPROSITE-ProRule annotationAdd
BLAST
Domaini727 – 77650KA1PROSITE-ProRule annotationAdd
BLAST

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.By similarity

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

eggNOGiCOG0515.
GeneTreeiENSGT00760000118892.
HOGENOMiHOG000233025.
HOVERGENiHBG052453.
InParanoidiQ05512.
KOiK08798.
OrthoDBiEOG79CXXX.
PhylomeDBiQ05512.

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.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q05512-1) [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
MSSARTPLPT LNERDTEQPT LGHLDSKPSS KSNMLRGRNS ATSADEQPHI
60 70 80 90 100
GNYRLLKTIG KGNFAKVKLA RHILTGKEVA VKIIDKTQLN SSSLQKLFRE
110 120 130 140 150
VRIMKVLNHP NIVKLFEVIE TEKTLYLVME YASGGEVFDY LVAHGRMKEK
160 170 180 190 200
EARAKFRQIV SAVQYCHQKF IVHRDLKAEN LLLDADMNIK IADFGFSNEF
210 220 230 240 250
TFGNKLDTFC GSPPYAAPEL FQGKKIDGPE VDVWSLGVIL YTLVSGSLPF
260 270 280 290 300
DGQNLKELRE RVLRGKYRIP FYMSTDCENL LKKFLILNPS KRGTLEQIMK
310 320 330 340 350
DRWMNVGHED DELKPYVEPL PDYKDPRRTE LMVSMGYTRE EIQDSLVGQR
360 370 380 390 400
YNEVMATYLL LGYKSSELEG DTITLKPRPS ADLTNSSAPS PSHKVQRSVS
410 420 430 440 450
ANPKQRRSSD QAVPAIPTSN SYSKKTQSNN AENKRPEEET GRKASSTAKV
460 470 480 490 500
PASPLPGLDR KKTTPAPSTN SVLSTSTNRS RNSPLLDRAS LGQASIQNGK
510 520 530 540 550
DSLTMPGSRA STASASAAVS AARPRQHQKS MSASVHPNKA SGLPPTESNC
560 570 580 590 600
EVPRPSTAPQ RVPVASPSAH NISSSSGAPD RTNFPRGVSS RSTFHAGQLR
610 620 630 640 650
QVRDQQNLPY GVTPASPSGH SQGRRGASGS IFSKFTSKFV RRNLNEPESK
660 670 680 690 700
DRVETLRPHV VGSGGTDKDK EEFREAKPRS LRFTWSMKTT SSMEPNEMMR
710 720 730 740 750
EIRKVLDANS CQSELHERYM LLCVHGTPGH ENFVQWEMEV CKLPRLSLNG
760 770
VRFKRISGTS MAFKNIASKI ANELKL
Length:776
Mass (Da):86,306
Last modified:January 23, 2007 - v3
Checksum:i533C8DE0B5EC507E
GO
Isoform 2 (identifier: Q05512-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     321-339: PDYKDPRRTELMVSMGYTR → LTTGPRDRVDGVNGLHT

Note: No experimental confirmation available.

Show »
Length:774
Mass (Da):85,798
Checksum:iA16080EE5F864414
GO
Isoform 3 (identifier: Q05512-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     502-555: Missing.

Note: No experimental confirmation available.

Show »
Length:722
Mass (Da):80,824
Checksum:iA5FF894FBA51F656
GO
Isoform 4 (identifier: Q05512-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     502-555: Missing.
     640-640: V → VRRNLSFRFA

Note: No experimental confirmation available.

Show »
Length:731
Mass (Da):81,972
Checksum:iAC87AD0A923FB943
GO

Sequence cautioni

The sequence BAC32312.1 differs from that shown. Reason: Frameshift at position 772.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti161 – 1622SA → LH in CAA50040. (PubMed:8358177)Curated
Sequence conflicti368 – 3681L → P in CAA50040. (PubMed:8358177)Curated
Sequence conflicti760 – 7601S → Y in BAC32312. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei321 – 33919PDYKD…MGYTR → LTTGPRDRVDGVNGLHT in isoform 2. 1 PublicationVSP_013341Add
BLAST
Alternative sequencei502 – 55554Missing in isoform 3 and isoform 4. 2 PublicationsVSP_013342Add
BLAST
Alternative sequencei640 – 6401V → VRRNLSFRFA in isoform 4. 1 PublicationVSP_022597

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X70764 mRNA. Translation: CAA50040.1.
AK045329 mRNA. Translation: BAC32312.1. Frameshift.
AK172444 mRNA. Translation: BAE43007.1.
BC058556 mRNA. Translation: AAH58556.1.
CCDSiCCDS37903.1. [Q05512-4]
CCDS37904.1. [Q05512-1]
CCDS50378.1. [Q05512-3]
PIRiI48609.
RefSeqiNP_001073857.1. NM_001080388.2.
NP_001073858.1. NM_001080389.2.
NP_001073859.1. NM_001080390.2.
NP_031954.2. NM_007928.3.
UniGeneiMm.258986.

Genome annotation databases

EnsembliENSMUST00000032557; ENSMUSP00000032557; ENSMUSG00000024969.
ENSMUST00000164205; ENSMUSP00000127827; ENSMUSG00000024969.
GeneIDi13728.
KEGGimmu:13728.
UCSCiuc008gks.1. mouse. [Q05512-4]
uc008gkt.1. mouse. [Q05512-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X70764 mRNA. Translation: CAA50040.1 .
AK045329 mRNA. Translation: BAC32312.1 . Frameshift.
AK172444 mRNA. Translation: BAE43007.1 .
BC058556 mRNA. Translation: AAH58556.1 .
CCDSi CCDS37903.1. [Q05512-4 ]
CCDS37904.1. [Q05512-1 ]
CCDS50378.1. [Q05512-3 ]
PIRi I48609.
RefSeqi NP_001073857.1. NM_001080388.2.
NP_001073858.1. NM_001080389.2.
NP_001073859.1. NM_001080390.2.
NP_031954.2. NM_007928.3.
UniGenei Mm.258986.

3D structure databases

ProteinModelPortali Q05512.
SMRi Q05512. Positions 13-363, 677-776.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199437. 7 interactions.
IntActi Q05512. 3 interactions.

PTM databases

PhosphoSitei Q05512.

Proteomic databases

MaxQBi Q05512.
PaxDbi Q05512.
PRIDEi Q05512.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000032557 ; ENSMUSP00000032557 ; ENSMUSG00000024969 .
ENSMUST00000164205 ; ENSMUSP00000127827 ; ENSMUSG00000024969 .
GeneIDi 13728.
KEGGi mmu:13728.
UCSCi uc008gks.1. mouse. [Q05512-4 ]
uc008gkt.1. mouse. [Q05512-3 ]

Organism-specific databases

CTDi 2011.
MGIi MGI:99638. Mark2.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118892.
HOGENOMi HOG000233025.
HOVERGENi HBG052453.
InParanoidi Q05512.
KOi K08798.
OrthoDBi EOG79CXXX.
PhylomeDBi Q05512.

Miscellaneous databases

NextBioi 284516.
PROi Q05512.
SOURCEi Search...

Gene expression databases

Bgeei Q05512.
CleanExi MM_MARK2.
ExpressionAtlasi Q05512. baseline and differential.
Genevestigatori Q05512.

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.
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. "Emk, a protein kinase with homologs in yeast maps to mouse chromosome 19."
    Inglis J.D., Lee M., Hill R.E.
    Mamm. Genome 4:401-403(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Embryo.
  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 AND 4).
    Strain: NOD.
    Tissue: Spleen.
  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] (ISOFORM 3).
    Strain: 129.
    Tissue: Mammary gland.
  4. "EMK protein kinase-null mice: dwarfism and hypofertility associated with alterations in the somatotrope and prolactin pathways."
    Bessone S., Vidal F., Le Bouc Y., Epelbaum J., Bluet-Pajot M.T., Darmon M.
    Dev. Biol. 214:87-101(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  5. "Immune system dysfunction and autoimmune disease in mice lacking Emk (Par-1) protein kinase."
    Hurov J.B., Stappenbeck T.S., Zmasek C.M., White L.S., Ranganath S.H., Russell J.H., Chan A.C., Murphy K.M., Piwnica-Worms H.
    Mol. Cell. Biol. 21:3206-3219(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Loss of the Par-1b/MARK2 polarity kinase leads to increased metabolic rate, decreased adiposity, and insulin hypersensitivity in vivo."
    Hurov J.B., Huang M., White L.S., Lennerz J., Choi C.S., Cho Y.R., Kim H.J., Prior J.L., Piwnica-Worms D., Cantley L.C., Kim J.K., Shulman G.I., Piwnica-Worms H.
    Proc. Natl. Acad. Sci. U.S.A. 104:5680-5685(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  8. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMARK2_MOUSE
AccessioniPrimary (citable) accession number: Q05512
Secondary accession number(s): Q3T9L3, Q6PDR4, Q8BR95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3