Q05512 (MARK2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Mark2
Synonyms:	Emk

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	776 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. ATP + [tau protein] = ADP + [tau protein] phosphate.
Cofactor	Magnesium By similarity.
Enzyme regulation	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.
Subunit structure	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.
Subcellular location	Cell membrane; Peripheral membrane protein 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.
Tissue specificity	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. Ref.4
Domain	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. The KA1 domain mediates binding to phospholipids and targeting to membranes By similarity.
Post-translational modification	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.
Disruption phenotype	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. Ref.4 Ref.5 Ref.9
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily. Contains 1 KA1 (kinase-associated) domain. Contains 1 protein kinase domain. Contains 1 UBA domain.
Sequence caution	The sequence BAC32312.1 differs from that shown. Reason: Frameshift at position 772.

Ontologies

Keywords
Biological process	Differentiation Wnt signaling pathway
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Lipid-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW establishment of cell polarity Inferred from sequence or structural similarity. Source: UniProtKB establishment or maintenance of epithelial cell apical/basal polarity Inferred from sequence or structural similarity. Source: UniProtKB intracellular protein kinase cascade Inferred from sequence or structural similarity. Source: UniProtKB neuron migration Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of neuron projection development Inferred from sequence or structural similarity. Source: UniProtKB protein autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of axonogenesis Inferred from sequence or structural similarity. Source: UniProtKB regulation of cytoskeleton organization Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	basal cortex Inferred from direct assay PubMed 15950600. Source: MGI membrane Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from direct assay PubMed 15950600. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB lipid binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from sequence or structural similarity. Source: UniProtKB protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB tau-protein kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q05512-1)

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.

Isoform 2 (identifier: Q05512-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: Q05512-3)

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

Note: No experimental confirmation available.

Isoform 4 (identifier: Q05512-4)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 776	776	Serine/threonine-protein kinase MARK2		PRO_0000086302
Regions
	Domain	53 – 304	252	Protein kinase
	Domain	323 – 362	40	UBA
	Domain	727 – 776	50	KA1
	Nucleotide binding	59 – 67	9	ATP By similarity
Sites
	Active site	175	1	Proton acceptor By similarity
	Binding site	82	1	ATP By similarity
Amino acid modifications
	Modified residue	40	1	Phosphoserine Ref.10
	Modified residue	58	1	Phosphothreonine; by autocatalysis By similarity
	Modified residue	91	1	Phosphoserine; by CaMK1 By similarity
	Modified residue	92	1	Phosphoserine; by CaMK1 By similarity
	Modified residue	93	1	Phosphoserine; by CaMK1 By similarity
	Modified residue	208	1	Phosphothreonine; by LKB1 and TAOK1 Ref.7 Ref.8
	Modified residue	212	1	Phosphoserine; by GSK3-beta By similarity
	Modified residue	274	1	Phosphoserine; by autocatalysis By similarity
	Modified residue	275	1	Phosphothreonine; by autocatalysis By similarity
	Modified residue	294	1	Phosphothreonine; by CaMK1 By similarity
	Modified residue	409	1	Phosphoserine By similarity
	Modified residue	453	1	Phosphoserine Ref.7 Ref.11
	Modified residue	483	1	Phosphoserine Ref.6 Ref.10
	Modified residue	490	1	Phosphoserine By similarity
	Modified residue	566	1	Phosphoserine By similarity
	Modified residue	568	1	Phosphoserine Ref.8
	Modified residue	592	1	Phosphoserine Ref.10
	Modified residue	593	1	Phosphothreonine; by PKC/PRKCZ By similarity
	Modified residue	616	1	Phosphoserine By similarity
	Modified residue	710	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	321 – 339	19	PDYKD…MGYTR → LTTGPRDRVDGVNGLHT in isoform 2.		VSP_013341
	Alternative sequence	502 – 555	54	Missing in isoform 3 and isoform 4.		VSP_013342
	Alternative sequence	640	1	V → VRRNLSFRFA in isoform 4.		VSP_022597
Experimental info
	Sequence conflict	161 – 162	2	SA → LH in CAA50040. Ref.1
	Sequence conflict	368	1	L → P in CAA50040. Ref.1
	Sequence conflict	760	1	S → Y in BAC32312. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 533C8DE0B5EC507E	FASTA	776	86,306
	10 20 30 40 50 60 MSSARTPLPT LNERDTEQPT LGHLDSKPSS KSNMLRGRNS ATSADEQPHI GNYRLLKTIG 70 80 90 100 110 120 KGNFAKVKLA RHILTGKEVA VKIIDKTQLN SSSLQKLFRE VRIMKVLNHP NIVKLFEVIE 130 140 150 160 170 180 TEKTLYLVME YASGGEVFDY LVAHGRMKEK EARAKFRQIV SAVQYCHQKF IVHRDLKAEN 190 200 210 220 230 240 LLLDADMNIK IADFGFSNEF TFGNKLDTFC GSPPYAAPEL FQGKKIDGPE VDVWSLGVIL 250 260 270 280 290 300 YTLVSGSLPF DGQNLKELRE RVLRGKYRIP FYMSTDCENL LKKFLILNPS KRGTLEQIMK 310 320 330 340 350 360 DRWMNVGHED DELKPYVEPL PDYKDPRRTE LMVSMGYTRE EIQDSLVGQR YNEVMATYLL 370 380 390 400 410 420 LGYKSSELEG DTITLKPRPS ADLTNSSAPS PSHKVQRSVS ANPKQRRSSD QAVPAIPTSN 430 440 450 460 470 480 SYSKKTQSNN AENKRPEEET GRKASSTAKV PASPLPGLDR KKTTPAPSTN SVLSTSTNRS 490 500 510 520 530 540 RNSPLLDRAS LGQASIQNGK DSLTMPGSRA STASASAAVS AARPRQHQKS MSASVHPNKA 550 560 570 580 590 600 SGLPPTESNC EVPRPSTAPQ RVPVASPSAH NISSSSGAPD RTNFPRGVSS RSTFHAGQLR 610 620 630 640 650 660 QVRDQQNLPY GVTPASPSGH SQGRRGASGS IFSKFTSKFV RRNLNEPESK DRVETLRPHV 670 680 690 700 710 720 VGSGGTDKDK EEFREAKPRS LRFTWSMKTT SSMEPNEMMR EIRKVLDANS CQSELHERYM 730 740 750 760 770 LLCVHGTPGH ENFVQWEMEV CKLPRLSLNG VRFKRISGTS MAFKNIASKI ANELKL
	Isoform 2 [UniParc]. Checksum: A16080EE5F864414	FASTA	774	85,798
	10 20 30 40 50 60 MSSARTPLPT LNERDTEQPT LGHLDSKPSS KSNMLRGRNS ATSADEQPHI GNYRLLKTIG 70 80 90 100 110 120 KGNFAKVKLA RHILTGKEVA VKIIDKTQLN SSSLQKLFRE VRIMKVLNHP NIVKLFEVIE 130 140 150 160 170 180 TEKTLYLVME YASGGEVFDY LVAHGRMKEK EARAKFRQIV SAVQYCHQKF IVHRDLKAEN 190 200 210 220 230 240 LLLDADMNIK IADFGFSNEF TFGNKLDTFC GSPPYAAPEL FQGKKIDGPE VDVWSLGVIL 250 260 270 280 290 300 YTLVSGSLPF DGQNLKELRE RVLRGKYRIP FYMSTDCENL LKKFLILNPS KRGTLEQIMK 310 320 330 340 350 360 DRWMNVGHED DELKPYVEPL LTTGPRDRVD GVNGLHTEEI QDSLVGQRYN EVMATYLLLG 370 380 390 400 410 420 YKSSELEGDT ITLKPRPSAD LTNSSAPSPS HKVQRSVSAN PKQRRSSDQA VPAIPTSNSY 430 440 450 460 470 480 SKKTQSNNAE NKRPEEETGR KASSTAKVPA SPLPGLDRKK TTPAPSTNSV LSTSTNRSRN 490 500 510 520 530 540 SPLLDRASLG QASIQNGKDS LTMPGSRAST ASASAAVSAA RPRQHQKSMS ASVHPNKASG 550 560 570 580 590 600 LPPTESNCEV PRPSTAPQRV PVASPSAHNI SSSSGAPDRT NFPRGVSSRS TFHAGQLRQV 610 620 630 640 650 660 RDQQNLPYGV TPASPSGHSQ GRRGASGSIF SKFTSKFVRR NLNEPESKDR VETLRPHVVG 670 680 690 700 710 720 SGGTDKDKEE FREAKPRSLR FTWSMKTTSS MEPNEMMREI RKVLDANSCQ SELHERYMLL 730 740 750 760 770 CVHGTPGHEN FVQWEMEVCK LPRLSLNGVR FKRISGTSMA FKNIASKIAN ELKL
	Isoform 3 [UniParc]. Checksum: A5FF894FBA51F656	FASTA	722	80,824
	10 20 30 40 50 60 MSSARTPLPT LNERDTEQPT LGHLDSKPSS KSNMLRGRNS ATSADEQPHI GNYRLLKTIG 70 80 90 100 110 120 KGNFAKVKLA RHILTGKEVA VKIIDKTQLN SSSLQKLFRE VRIMKVLNHP NIVKLFEVIE 130 140 150 160 170 180 TEKTLYLVME YASGGEVFDY LVAHGRMKEK EARAKFRQIV SAVQYCHQKF IVHRDLKAEN 190 200 210 220 230 240 LLLDADMNIK IADFGFSNEF TFGNKLDTFC GSPPYAAPEL FQGKKIDGPE VDVWSLGVIL 250 260 270 280 290 300 YTLVSGSLPF DGQNLKELRE RVLRGKYRIP FYMSTDCENL LKKFLILNPS KRGTLEQIMK 310 320 330 340 350 360 DRWMNVGHED DELKPYVEPL PDYKDPRRTE LMVSMGYTRE EIQDSLVGQR YNEVMATYLL 370 380 390 400 410 420 LGYKSSELEG DTITLKPRPS ADLTNSSAPS PSHKVQRSVS ANPKQRRSSD QAVPAIPTSN 430 440 450 460 470 480 SYSKKTQSNN AENKRPEEET GRKASSTAKV PASPLPGLDR KKTTPAPSTN SVLSTSTNRS 490 500 510 520 530 540 RNSPLLDRAS LGQASIQNGK DSTAPQRVPV ASPSAHNISS SSGAPDRTNF PRGVSSRSTF 550 560 570 580 590 600 HAGQLRQVRD QQNLPYGVTP ASPSGHSQGR RGASGSIFSK FTSKFVRRNL NEPESKDRVE 610 620 630 640 650 660 TLRPHVVGSG GTDKDKEEFR EAKPRSLRFT WSMKTTSSME PNEMMREIRK VLDANSCQSE 670 680 690 700 710 720 LHERYMLLCV HGTPGHENFV QWEMEVCKLP RLSLNGVRFK RISGTSMAFK NIASKIANEL KL
	Isoform 4 [UniParc]. Checksum: AC87AD0A923FB943	FASTA	731	81,972
	10 20 30 40 50 60 MSSARTPLPT LNERDTEQPT LGHLDSKPSS KSNMLRGRNS ATSADEQPHI GNYRLLKTIG 70 80 90 100 110 120 KGNFAKVKLA RHILTGKEVA VKIIDKTQLN SSSLQKLFRE VRIMKVLNHP NIVKLFEVIE 130 140 150 160 170 180 TEKTLYLVME YASGGEVFDY LVAHGRMKEK EARAKFRQIV SAVQYCHQKF IVHRDLKAEN 190 200 210 220 230 240 LLLDADMNIK IADFGFSNEF TFGNKLDTFC GSPPYAAPEL FQGKKIDGPE VDVWSLGVIL 250 260 270 280 290 300 YTLVSGSLPF DGQNLKELRE RVLRGKYRIP FYMSTDCENL LKKFLILNPS KRGTLEQIMK 310 320 330 340 350 360 DRWMNVGHED DELKPYVEPL PDYKDPRRTE LMVSMGYTRE EIQDSLVGQR YNEVMATYLL 370 380 390 400 410 420 LGYKSSELEG DTITLKPRPS ADLTNSSAPS PSHKVQRSVS ANPKQRRSSD QAVPAIPTSN 430 440 450 460 470 480 SYSKKTQSNN AENKRPEEET GRKASSTAKV PASPLPGLDR KKTTPAPSTN SVLSTSTNRS 490 500 510 520 530 540 RNSPLLDRAS LGQASIQNGK DSTAPQRVPV ASPSAHNISS SSGAPDRTNF PRGVSSRSTF 550 560 570 580 590 600 HAGQLRQVRD QQNLPYGVTP ASPSGHSQGR RGASGSIFSK FTSKFVRRNL SFRFARRNLN 610 620 630 640 650 660 EPESKDRVET LRPHVVGSGG TDKDKEEFRE AKPRSLRFTW SMKTTSSMEP NEMMREIRKV 670 680 690 700 710 720 LDANSCQSEL HERYMLLCVH GTPGHENFVQ WEMEVCKLPR LSLNGVRFKR ISGTSMAFKN 730 IASKIANELK L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, MASS SPECTROMETRY. Tissue: Brain.
[7]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-208 AND SER-453, MASS SPECTROMETRY. Tissue: Brain cortex.
[8]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-208 AND SER-568, MASS SPECTROMETRY. Tissue: Liver.
[9]	"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.
[10]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-483 AND SER-592, MASS SPECTROMETRY. Tissue: Melanoma.
[11]	"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, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X70764 mRNA. Translation: CAA50040.1. AK045329 mRNA. Translation: BAC32312.1. Frameshift. AK172444 mRNA. Translation: BAE43007.1. BC058556 mRNA. Translation: AAH58556.1.
IPI	IPI00111754. IPI00554855. IPI00554871. IPI00762727.
PIR	I48609.
RefSeq	NP_001073857.1. NM_001080388.1. NP_001073858.1. NM_001080389.1. NP_001073859.1. NM_001080390.1. NP_031954.2. NM_007928.2.
UniGene	Mm.258986.
3D structure databases
ProteinModelPortal	Q05512.
SMR	Q05512. Positions 13-363, 677-776.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q05512. 3 interactions.
PTM databases
PhosphoSite	Q05512.
Proteomic databases
PaxDb	Q05512.
PRIDE	Q05512.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000032557; ENSMUSP00000032557; ENSMUSG00000024969. ENSMUST00000164205; ENSMUSP00000127827; ENSMUSG00000024969.
GeneID	13728.
KEGG	mmu:13728.
UCSC	uc008gkr.1. mouse. uc008gks.1. mouse. uc008gkt.1. mouse.
Organism-specific databases
CTD	2011.
MGI	MGI:99638. Mark2.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00690000101885.
HOGENOM	HOG000233025.
HOVERGEN	HBG052453.
InParanoid	Q05512.
KO	K08798.
OrthoDB	EOG4C2H8X.
Gene expression databases
ArrayExpress	Q05512.
Bgee	Q05512.
CleanEx	MM_MARK2.
Genevestigator	Q05512.
GermOnline	ENSMUSG00000024969. Mus musculus.
Family and domain databases
InterPro	IPR001772. KA1_dom. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_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]
Pfam	PF02149. KA1. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. SM00165. UBA. 1 hit. [Graphical view]
SUPFAM	SSF103243. Kinase-assoc_KA1. 1 hit. SSF56112. Kinase_like. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
NextBio	284516.
SOURCE	Search...

Entry information

Entry name

MARK2_MOUSE

Accession

Primary (citable) accession number: Q05512
Secondary accession number(s): Q3T9L3, Q6PDR4, Q8BR95

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 134 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program