Q03141 (MARK3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Mark3
Synonyms:	Emk2, Mpk10

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	753 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by phosphorylation on Thr-211. Inhibited by phosphorylation on Thr-564 By similarity.
Subcellular location	Cell membrane; Peripheral membrane protein By similarity.
Post-translational modification	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.
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 AAH26445.1 differs from that shown. Reason: Erroneous initiation. The sequence BAC35922.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q03141-1)

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: Q03141-2)

Also known as: ELKL motif kinase 2 short form;

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

Isoform 3 (identifier: Q03141-3)

Also known as: ELKL motif kinase 2 long form;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 753

753

MAP/microtubule affinity-regulating kinase 3

PRO_0000086305

Regions

Domain

56 – 307

252

Protein kinase

Domain

326 – 365

40

UBA

Domain

695 – 744

50

KA1

Nucleotide binding

62 – 70

9

ATP By similarity

Compositional bias

374 – 412

39

Ser-rich

Sites

Active site

178

1

Proton acceptor By similarity

Binding site

85

1

ATP By similarity

Amino acid modifications

Modified residue

42

1

Phosphoserine By similarity

Modified residue

211

1

Phosphothreonine; by LKB1 By similarity

Modified residue

383

1

Phosphoserine By similarity

Modified residue

400

1

Phosphoserine By similarity

Modified residue

469

1

Phosphoserine By similarity

Modified residue

549

1

Phosphothreonine By similarity

Modified residue

564

1

Phosphothreonine; by PKC/PRKCZ By similarity

Modified residue

598

1

Phosphoserine By similarity

Modified residue

643

1

Phosphoserine By similarity

Natural variations

Alternative sequence

615 – 638

24

Missing in isoform 2.

VSP_016140

Alternative sequence

615 – 623

9

Missing in isoform 3.

VSP_016141

Experimental info

Sequence conflict

333

1

D → V in BAC35922. Ref.2

Sequence conflict

496

1

N → S in AAF64456. Ref.1

Sequence conflict

511

1

S → G in BAC35922. Ref.2

Sequence conflict

684

1

D → G in BAC35922. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

753

Helix Strand Turn

Details...

Helix

672 – 685

14

Beta strand

689 – 692

4

Beta strand

698 – 702

5

Beta strand

704 – 706

3

Helix

707 – 709

3

Beta strand

711 – 719

9

Beta strand

721 – 735

15

Helix

737 – 750

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 8, 2005. Version 2. Checksum: B597BDD0398617CF	FASTA	753	84,390
	10 20 30 40 50 60 MSTRTPLPTV NERDTENHIS HGDGRQEVTS RTGRSGARCR NSIASCADEQ PHIGNYRLLK 70 80 90 100 110 120 TIGKGNFAKV KLARHILTGR EVAIKIIDKT QLNPTSLQKL FREVRIMKIL NHPNIVKLFE 130 140 150 160 170 180 VIETEKTLYL IMEYASGGEV FDYLVAHGRM KEKEARAKFR QIVSAVQYCH QKRIVHRDLK 190 200 210 220 230 240 AENLLLDADM NIKIADFGFS NEFTVGSKLD TFCGSPPYAA PELFQGKKYD GPEVDVWSLG 250 260 270 280 290 300 VILYTLVSGS LPFDGQNLKE LRERVLRGKY RIPFYMSTDC ENLLKRFLVL NPVKRGTLEQ 310 320 330 340 350 360 IMKDRWINAG HEEDELKPFV EPELDISDQK RIDIMVGMGY SQEEIQESLS KMKYDEITAT 370 380 390 400 410 420 YLLLGRKSAE LDASDSSSSS NLSLAKVRPN SDLSNSTGQS PHHKGQRSVS SSQKQRRYSD 430 440 450 460 470 480 HAGPAIPSVV AYPKRSQTST ADSDLKEDGI PSRKSSSSAV GGKGIAPASP MLGNAGNPNK 490 500 510 520 530 540 ADIPERKKSP AVPSSNTASG GMTRRNTYVC SERCAADRHS VIQNGKENSA IPDERTPVAS 550 560 570 580 590 600 THSISSATTP DRIRFPRGTA SRSTFHGQPR ERRTATYNGP PASPSLSHEA TPLSQTRSRG 610 620 630 640 650 660 STNLFSKLTS KLTRRNMSFR FIKRLPTEYE RNGRYEGSSR NVSSEQKDEN REAKPRSLRF 670 680 690 700 710 720 TWSMKTTSSM DPSDMMREIR KVLDANNCDY EQRERFLLFC VHGDGHAENL VQWEMEVCKL 730 740 750 PRLSLNGVRF KRISGTSIAF KNIASKIANE LKL
	Isoform 2 (ELKL motif kinase 2 short form) [UniParc]. Checksum: D76FBB9A27ED19C9	FASTA	729	81,400
	10 20 30 40 50 60 MSTRTPLPTV NERDTENHIS HGDGRQEVTS RTGRSGARCR NSIASCADEQ PHIGNYRLLK 70 80 90 100 110 120 TIGKGNFAKV KLARHILTGR EVAIKIIDKT QLNPTSLQKL FREVRIMKIL NHPNIVKLFE 130 140 150 160 170 180 VIETEKTLYL IMEYASGGEV FDYLVAHGRM KEKEARAKFR QIVSAVQYCH QKRIVHRDLK 190 200 210 220 230 240 AENLLLDADM NIKIADFGFS NEFTVGSKLD TFCGSPPYAA PELFQGKKYD GPEVDVWSLG 250 260 270 280 290 300 VILYTLVSGS LPFDGQNLKE LRERVLRGKY RIPFYMSTDC ENLLKRFLVL NPVKRGTLEQ 310 320 330 340 350 360 IMKDRWINAG HEEDELKPFV EPELDISDQK RIDIMVGMGY SQEEIQESLS KMKYDEITAT 370 380 390 400 410 420 YLLLGRKSAE LDASDSSSSS NLSLAKVRPN SDLSNSTGQS PHHKGQRSVS SSQKQRRYSD 430 440 450 460 470 480 HAGPAIPSVV AYPKRSQTST ADSDLKEDGI PSRKSSSSAV GGKGIAPASP MLGNAGNPNK 490 500 510 520 530 540 ADIPERKKSP AVPSSNTASG GMTRRNTYVC SERCAADRHS VIQNGKENSA IPDERTPVAS 550 560 570 580 590 600 THSISSATTP DRIRFPRGTA SRSTFHGQPR ERRTATYNGP PASPSLSHEA TPLSQTRSRG 610 620 630 640 650 660 STNLFSKLTS KLTRSRNVSS EQKDENREAK PRSLRFTWSM KTTSSMDPSD MMREIRKVLD 670 680 690 700 710 720 ANNCDYEQRE RFLLFCVHGD GHAENLVQWE MEVCKLPRLS LNGVRFKRIS GTSIAFKNIA SKIANELKL
	Isoform 3 (ELKL motif kinase 2 long form) [UniParc]. Checksum: 2CCA8FA8AEE20360	FASTA	744	83,209
	10 20 30 40 50 60 MSTRTPLPTV NERDTENHIS HGDGRQEVTS RTGRSGARCR NSIASCADEQ PHIGNYRLLK 70 80 90 100 110 120 TIGKGNFAKV KLARHILTGR EVAIKIIDKT QLNPTSLQKL FREVRIMKIL NHPNIVKLFE 130 140 150 160 170 180 VIETEKTLYL IMEYASGGEV FDYLVAHGRM KEKEARAKFR QIVSAVQYCH QKRIVHRDLK 190 200 210 220 230 240 AENLLLDADM NIKIADFGFS NEFTVGSKLD TFCGSPPYAA PELFQGKKYD GPEVDVWSLG 250 260 270 280 290 300 VILYTLVSGS LPFDGQNLKE LRERVLRGKY RIPFYMSTDC ENLLKRFLVL NPVKRGTLEQ 310 320 330 340 350 360 IMKDRWINAG HEEDELKPFV EPELDISDQK RIDIMVGMGY SQEEIQESLS KMKYDEITAT 370 380 390 400 410 420 YLLLGRKSAE LDASDSSSSS NLSLAKVRPN SDLSNSTGQS PHHKGQRSVS SSQKQRRYSD 430 440 450 460 470 480 HAGPAIPSVV AYPKRSQTST ADSDLKEDGI PSRKSSSSAV GGKGIAPASP MLGNAGNPNK 490 500 510 520 530 540 ADIPERKKSP AVPSSNTASG GMTRRNTYVC SERCAADRHS VIQNGKENSA IPDERTPVAS 550 560 570 580 590 600 THSISSATTP DRIRFPRGTA SRSTFHGQPR ERRTATYNGP PASPSLSHEA TPLSQTRSRG 610 620 630 640 650 660 STNLFSKLTS KLTRRLPTEY ERNGRYEGSS RNVSSEQKDE NREAKPRSLR FTWSMKTTSS 670 680 690 700 710 720 MDPSDMMREI RKVLDANNCD YEQRERFLLF CVHGDGHAEN LVQWEMEVCK LPRLSLNGVR 730 740 FKRISGTSIA FKNIASKIAN ELKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00279494.
IPI00312620.
IPI00625061.

PIR

S30496.

RefSeq

NP_067491.2. NM_021516.4.
NP_073712.2. NM_022801.4.

UniGene

Mm.260504.
Mm.420865.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UL7	NMR	-	A	659-753	[»]
1V5S	NMR	-	A	674-753	[»]

ProteinModelPortal

Q03141.

SMR

Q03141. Positions 1-366, 657-753.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q03141. 1 interaction.

PTM databases

PhosphoSite

Q03141.

Proteomic databases

PaxDb

Q03141.

PRIDE

Q03141.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000075281; ENSMUSP00000074757; ENSMUSG00000007411.
ENSMUST00000084953; ENSMUSP00000082017; ENSMUSG00000007411.

GeneID

17169.

KEGG

mmu:17169.

UCSC

uc007pdk.2. mouse.
uc007pdl.2. mouse.
uc007pdm.2. mouse.

Organism-specific databases

CTD

4140.

MGI

MGI:1341865. Mark3.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00690000101885.

HOGENOM

HOG000233025.

HOVERGEN

HBG052453.

InParanoid

Q03141.

KO

K08798.

OMA

PPVVAYP.

OrthoDB

EOG4QFWCQ.

Gene expression databases

ArrayExpress

Q03141.

Bgee

Q03141.

CleanEx

MM_MARK3.

Genevestigator

Q03141.

GermOnline

ENSMUSG00000007411. 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

ChiTaRS

MARK3. mouse.

EvolutionaryTrace

Q03141.

NextBio

291458.

SOURCE

Search...

Entry information

Entry name

MARK3_MOUSE

Accession

Primary (citable) accession number: Q03141
Secondary accession number(s): Q3TM40 , Q3V1U3, Q8C6G9, Q8R375, Q9JKE4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	November 8, 2005
Last modified:	May 1, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program