P27448 (MARK3_HUMAN) 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):
C-TAK1
Short name=cTAK1
Cdc25C-associated protein kinase 1
ELKL motif kinase 2
Short name=EMK-2
Protein kinase STK10
Ser/Thr protein kinase PAR-1
Short name=Par-1a
Serine/threonine-protein kinase p78

Gene names

Name:	MARK3
Synonyms:	CTAK1, EMK2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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 on 'Ser-216'. 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. Ref.11
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by phosphorylation on Thr-211. Inhibited by phosphorylation on Thr-564. Ref.10
Subcellular location	Cell membrane; Peripheral membrane protein Ref.17.
Tissue specificity	Ubiquitous.
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. Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16
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.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
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 direct assay Ref.17. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.11. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.11. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ASB13	Q8WXK3	2	EBI-707595,EBI-707573
TCEA2	Q15560	2	EBI-707595,EBI-710310

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P27448-5)

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: P27448-2)

Also known as: CTAK75a;

The sequence of this isoform differs from the canonical sequence as follows:
     161-161: Q → QGCQAGQTIKVQVSFDLLSLMFTF
     615-638: Missing.

Isoform 3 (identifier: P27448-3)

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

Isoform 4 (identifier: P27448-4)

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

Isoform 5 (identifier: P27448-6)

Also known as: p58;

The sequence of this isoform differs from the canonical sequence as follows:
     371-386: Missing.
     615-638: Missing.

Isoform 6 (identifier: P27448-7)

The sequence of this isoform differs from the canonical sequence as follows:
     161-161: Q → QGCQAGQTIKVQVSFDLLSLMFTF
     371-386: 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_0000086304

Regions

Domain

56 – 307

252

Protein kinase

Domain

326 – 365

40

UBA

Domain

704 – 753

50

KA1

Nucleotide binding

62 – 70

9

ATP By similarity

Sites

Active site

178

1

Proton acceptor By similarity

Binding site

85

1

ATP By similarity

Amino acid modifications

Modified residue

2

1

Phosphoserine Ref.16

Modified residue

3

1

Phosphothreonine Ref.16

Modified residue

42

1

Phosphoserine Ref.16

Modified residue

61

1

Phosphothreonine Ref.14 Ref.16

Modified residue

211

1

Phosphothreonine; by LKB1 Ref.10 Ref.12 Ref.16

Modified residue

340

1

Phosphotyrosine Ref.16

Modified residue

341

1

Phosphoserine Ref.16

Modified residue

374

1

Phosphoserine Ref.16

Modified residue

376

1

Phosphoserine Ref.16

Modified residue

377

1

Phosphoserine Ref.16

Modified residue

378

1

Phosphoserine Ref.16

Modified residue

379

1

Phosphoserine Ref.16

Modified residue

380

1

Phosphoserine Ref.14 Ref.15 Ref.16

Modified residue

383

1

Phosphoserine Ref.14 Ref.16

Modified residue

397

1

Phosphothreonine Ref.16

Modified residue

400

1

Phosphoserine Ref.14 Ref.16

Modified residue

418

1

Phosphotyrosine Ref.16

Modified residue

419

1

Phosphoserine Ref.12 Ref.14 Ref.16

Modified residue

436

1

Phosphoserine Ref.16

Modified residue

438

1

Phosphothreonine Ref.16

Modified residue

455

1

Phosphoserine Ref.14

Modified residue

456

1

Phosphoserine Ref.16

Modified residue

469

1

Phosphoserine Ref.12 Ref.14 Ref.15 Ref.16

Modified residue

476

1

Phosphoserine Ref.14

Modified residue

494

1

Phosphoserine Ref.16

Modified residue

499

1

Phosphoserine Ref.16

Modified residue

536

1

Phosphothreonine Ref.14

Modified residue

540

1

Phosphoserine Ref.13 Ref.16

Modified residue

541

1

Phosphothreonine Ref.16

Modified residue

543

1

Phosphoserine Ref.13 Ref.16

Modified residue

545

1

Phosphoserine Ref.16

Modified residue

549

1

Phosphothreonine Ref.13 Ref.14

Modified residue

564

1

Phosphothreonine; by PKC/PRKCZ By similarity

Modified residue

583

1

Phosphoserine Ref.14 Ref.15 Ref.16

Modified residue

585

1

Phosphoserine Ref.15 Ref.16

Modified residue

587

1

Phosphoserine Ref.14 Ref.16

Modified residue

591

1

Phosphothreonine Ref.13

Modified residue

598

1

Phosphoserine Ref.14 Ref.16

Modified residue

601

1

Phosphoserine Ref.12 Ref.16

Modified residue

639

1

Phosphoserine Ref.16

Modified residue

643

1

Phosphoserine Ref.14 Ref.16

Natural variations

Alternative sequence

161

1

Q → QGCQAGQTIKVQVSFDLLSL MFTF in isoform 2 and isoform 6.

VSP_041582

Alternative sequence

371 – 386

16

Missing in isoform 5 and isoform 6.

VSP_004943

Alternative sequence

615 – 638

24

Missing in isoform 2, isoform 3 and isoform 5.

VSP_004944

Alternative sequence

615 – 623

9

Missing in isoform 4.

VSP_004945

Natural variant

429

1

V → A. Ref.18

VAR_040765

Natural variant

443

1

S → G. Ref.1 Ref.2 Ref.18
Corresponds to variant rs56305318 [ dbSNP | Ensembl ].

VAR_046763

Experimental info

Mutagenesis

211

1

T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. Ref.10

Sequence conflict

125

1

E → Q in AAA59991. Ref.5

Sequence conflict

139

1

E → K in AAL69982. Ref.4

Sequence conflict

139

1

E → K in AAA59991. Ref.5

Sequence conflict

149

1

R → K in AAD48007. Ref.2

Sequence conflict

410

1

F → S in AAC15093. Ref.1

Sequence conflict

410

1

F → S in AAD48007. Ref.2

Sequence conflict

410

1

F → S in AAK82367. Ref.3

Sequence conflict

410

1

F → S in AAL69982. Ref.4

Sequence conflict

410

1

F → S in AAA59991. Ref.5

Sequence conflict

410

1

F → S in AAH24773. Ref.7

Sequence conflict

410

1

F → S in AAD51631. Ref.8

Sequence conflict

425

1

A → G in AAA59991. Ref.5

Sequence conflict

456

1

S → T in AAA59991. Ref.5

Sequence conflict

516

1

A → D in AAA59991. Ref.5

Sequence conflict

603

1

N → T in AAA59991. Ref.5

Sequence conflict

645

1

E → K in AAA59991. Ref.5

Secondary structure

1

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753

Helix Strand Turn

Details...

Beta strand

56 – 61

6

Beta strand

68 – 76

9

Beta strand

81 – 88

8

Helix

89 – 91

3

Helix

94 – 109

16

Beta strand

118 – 123

6

Beta strand

125 – 132

8

Helix

140 – 146

7

Helix

152 – 161

10

Helix

162 – 171

10

Helix

181 – 183

3

Beta strand

184 – 186

3

Beta strand

192 – 194

3

Helix

201 – 203

3

Turn

209 – 212

4

Helix

216 – 218

3

Helix

221 – 224

4

Helix

233 – 238

6

Helix

242 – 248

7

Helix

258 – 266

9

Helix

278 – 287

10

Turn

292 – 294

3

Helix

298 – 301

4

Turn

305 – 308

4

Helix

329 – 335

7

Helix

342 – 350

9

Helix

356 – 363

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 4. Checksum: 0CA50C58A4A49D93	FASTA	753	84,489
	10 20 30 40 50 60 MSTRTPLPTV NERDTENHTS HGDGRQEVTS RTSRSGARCR NSIASCADEQ PHIGNYRLLK 70 80 90 100 110 120 TIGKGNFAKV KLARHILTGR EVAIKIIDKT QLNPTSLQKL FREVRIMKIL NHPNIVKLFE 130 140 150 160 170 180 VIETEKTLYL IMEYASGGEV FDYLVAHGRM KEKEARSKFR QIVSAVQYCH QKRIVHRDLK 190 200 210 220 230 240 AENLLLDADM NIKIADFGFS NEFTVGGKLD TFCGSPPYAA PELFQGKKYD GPEVDVWSLG 250 260 270 280 290 300 VILYTLVSGS LPFDGQNLKE LRERVLRGKY RIPFYMSTDC ENLLKRFLVL NPIKRGTLEQ 310 320 330 340 350 360 IMKDRWINAG HEEDELKPFV EPELDISDQK RIDIMVGMGY SQEEIQESLS KMKYDEITAT 370 380 390 400 410 420 YLLLGRKSSE LDASDSSSSS NLSLAKVRPS SDLNNSTGQS PHHKVQRSVF SSQKQRRYSD 430 440 450 460 470 480 HAGPAIPSVV AYPKRSQTST ADSDLKEDGI SSRKSSGSAV GGKGIAPASP MLGNASNPNK 490 500 510 520 530 540 ADIPERKKSS TVPSSNTASG GMTRRNTYVC SERTTADRHS VIQNGKENST IPDQRTPVAS 550 560 570 580 590 600 THSISSAATP DRIRFPRGTA SRSTFHGQPR ERRTATYNGP PASPSLSHEA TPLSQTRSRG 610 620 630 640 650 660 STNLFSKLTS KLTRRNMSFR FIKRLPTEYE RNGRYEGSSR NVSAEQKDEN KEAKPRSLRF 670 680 690 700 710 720 TWSMKTTSSM DPGDMMREIR KVLDANNCDY EQRERFLLFC VHGDGHAENL VQWEMEVCKL 730 740 750 PRLSLNGVRF KRISGTSIAF KNIASKIANE LKL
	Isoform 2 (CTAK75a) [UniParc]. Checksum: 0306682A37C313D7	FASTA	752	84,015
	10 20 30 40 50 60 MSTRTPLPTV NERDTENHTS HGDGRQEVTS RTSRSGARCR NSIASCADEQ PHIGNYRLLK 70 80 90 100 110 120 TIGKGNFAKV KLARHILTGR EVAIKIIDKT QLNPTSLQKL FREVRIMKIL NHPNIVKLFE 130 140 150 160 170 180 VIETEKTLYL IMEYASGGEV FDYLVAHGRM KEKEARSKFR QGCQAGQTIK VQVSFDLLSL 190 200 210 220 230 240 MFTFIVSAVQ YCHQKRIVHR DLKAENLLLD ADMNIKIADF GFSNEFTVGG KLDTFCGSPP 250 260 270 280 290 300 YAAPELFQGK KYDGPEVDVW SLGVILYTLV SGSLPFDGQN LKELRERVLR GKYRIPFYMS 310 320 330 340 350 360 TDCENLLKRF LVLNPIKRGT LEQIMKDRWI NAGHEEDELK PFVEPELDIS DQKRIDIMVG 370 380 390 400 410 420 MGYSQEEIQE SLSKMKYDEI TATYLLLGRK SSELDASDSS SSSNLSLAKV RPSSDLNNST 430 440 450 460 470 480 GQSPHHKVQR SVFSSQKQRR YSDHAGPAIP SVVAYPKRSQ TSTADSDLKE DGISSRKSSG 490 500 510 520 530 540 SAVGGKGIAP ASPMLGNASN PNKADIPERK KSSTVPSSNT ASGGMTRRNT YVCSERTTAD 550 560 570 580 590 600 RHSVIQNGKE NSTIPDQRTP VASTHSISSA ATPDRIRFPR GTASRSTFHG QPRERRTATY 610 620 630 640 650 660 NGPPASPSLS HEATPLSQTR SRGSTNLFSK LTSKLTRSRN VSAEQKDENK EAKPRSLRFT 670 680 690 700 710 720 WSMKTTSSMD PGDMMREIRK VLDANNCDYE QRERFLLFCV HGDGHAENLV QWEMEVCKLP 730 740 750 RLSLNGVRFK RISGTSIAFK NIASKIANEL KL
	Isoform 3 [UniParc]. Checksum: 4DF13ABB00F2305D	FASTA	729	81,499
	10 20 30 40 50 60 MSTRTPLPTV NERDTENHTS HGDGRQEVTS RTSRSGARCR NSIASCADEQ PHIGNYRLLK 70 80 90 100 110 120 TIGKGNFAKV KLARHILTGR EVAIKIIDKT QLNPTSLQKL FREVRIMKIL NHPNIVKLFE 130 140 150 160 170 180 VIETEKTLYL IMEYASGGEV FDYLVAHGRM KEKEARSKFR QIVSAVQYCH QKRIVHRDLK 190 200 210 220 230 240 AENLLLDADM NIKIADFGFS NEFTVGGKLD TFCGSPPYAA PELFQGKKYD GPEVDVWSLG 250 260 270 280 290 300 VILYTLVSGS LPFDGQNLKE LRERVLRGKY RIPFYMSTDC ENLLKRFLVL NPIKRGTLEQ 310 320 330 340 350 360 IMKDRWINAG HEEDELKPFV EPELDISDQK RIDIMVGMGY SQEEIQESLS KMKYDEITAT 370 380 390 400 410 420 YLLLGRKSSE LDASDSSSSS NLSLAKVRPS SDLNNSTGQS PHHKVQRSVF SSQKQRRYSD 430 440 450 460 470 480 HAGPAIPSVV AYPKRSQTST ADSDLKEDGI SSRKSSGSAV GGKGIAPASP MLGNASNPNK 490 500 510 520 530 540 ADIPERKKSS TVPSSNTASG GMTRRNTYVC SERTTADRHS VIQNGKENST IPDQRTPVAS 550 560 570 580 590 600 THSISSAATP DRIRFPRGTA SRSTFHGQPR ERRTATYNGP PASPSLSHEA TPLSQTRSRG 610 620 630 640 650 660 STNLFSKLTS KLTRSRNVSA EQKDENKEAK PRSLRFTWSM KTTSSMDPGD MMREIRKVLD 670 680 690 700 710 720 ANNCDYEQRE RFLLFCVHGD GHAENLVQWE MEVCKLPRLS LNGVRFKRIS GTSIAFKNIA SKIANELKL
	Isoform 4 [UniParc]. Checksum: EDDC40EDF509566E	FASTA	744	83,308
	10 20 30 40 50 60 MSTRTPLPTV NERDTENHTS HGDGRQEVTS RTSRSGARCR NSIASCADEQ PHIGNYRLLK 70 80 90 100 110 120 TIGKGNFAKV KLARHILTGR EVAIKIIDKT QLNPTSLQKL FREVRIMKIL NHPNIVKLFE 130 140 150 160 170 180 VIETEKTLYL IMEYASGGEV FDYLVAHGRM KEKEARSKFR QIVSAVQYCH QKRIVHRDLK 190 200 210 220 230 240 AENLLLDADM NIKIADFGFS NEFTVGGKLD TFCGSPPYAA PELFQGKKYD GPEVDVWSLG 250 260 270 280 290 300 VILYTLVSGS LPFDGQNLKE LRERVLRGKY RIPFYMSTDC ENLLKRFLVL NPIKRGTLEQ 310 320 330 340 350 360 IMKDRWINAG HEEDELKPFV EPELDISDQK RIDIMVGMGY SQEEIQESLS KMKYDEITAT 370 380 390 400 410 420 YLLLGRKSSE LDASDSSSSS NLSLAKVRPS SDLNNSTGQS PHHKVQRSVF SSQKQRRYSD 430 440 450 460 470 480 HAGPAIPSVV AYPKRSQTST ADSDLKEDGI SSRKSSGSAV GGKGIAPASP MLGNASNPNK 490 500 510 520 530 540 ADIPERKKSS TVPSSNTASG GMTRRNTYVC SERTTADRHS VIQNGKENST IPDQRTPVAS 550 560 570 580 590 600 THSISSAATP DRIRFPRGTA SRSTFHGQPR ERRTATYNGP PASPSLSHEA TPLSQTRSRG 610 620 630 640 650 660 STNLFSKLTS KLTRRLPTEY ERNGRYEGSS RNVSAEQKDE NKEAKPRSLR FTWSMKTTSS 670 680 690 700 710 720 MDPGDMMREI RKVLDANNCD YEQRERFLLF CVHGDGHAEN LVQWEMEVCK LPRLSLNGVR 730 740 FKRISGTSIA FKNIASKIAN ELKL
	Isoform 5 (p58) [UniParc]. Checksum: 32B5C41C16F5F080	FASTA	713	79,936
	10 20 30 40 50 60 MSTRTPLPTV NERDTENHTS HGDGRQEVTS RTSRSGARCR NSIASCADEQ PHIGNYRLLK 70 80 90 100 110 120 TIGKGNFAKV KLARHILTGR EVAIKIIDKT QLNPTSLQKL FREVRIMKIL NHPNIVKLFE 130 140 150 160 170 180 VIETEKTLYL IMEYASGGEV FDYLVAHGRM KEKEARSKFR QIVSAVQYCH QKRIVHRDLK 190 200 210 220 230 240 AENLLLDADM NIKIADFGFS NEFTVGGKLD TFCGSPPYAA PELFQGKKYD GPEVDVWSLG 250 260 270 280 290 300 VILYTLVSGS LPFDGQNLKE LRERVLRGKY RIPFYMSTDC ENLLKRFLVL NPIKRGTLEQ 310 320 330 340 350 360 IMKDRWINAG HEEDELKPFV EPELDISDQK RIDIMVGMGY SQEEIQESLS KMKYDEITAT 370 380 390 400 410 420 YLLLGRKSSE VRPSSDLNNS TGQSPHHKVQ RSVFSSQKQR RYSDHAGPAI PSVVAYPKRS 430 440 450 460 470 480 QTSTADSDLK EDGISSRKSS GSAVGGKGIA PASPMLGNAS NPNKADIPER KKSSTVPSSN 490 500 510 520 530 540 TASGGMTRRN TYVCSERTTA DRHSVIQNGK ENSTIPDQRT PVASTHSISS AATPDRIRFP 550 560 570 580 590 600 RGTASRSTFH GQPRERRTAT YNGPPASPSL SHEATPLSQT RSRGSTNLFS KLTSKLTRSR 610 620 630 640 650 660 NVSAEQKDEN KEAKPRSLRF TWSMKTTSSM DPGDMMREIR KVLDANNCDY EQRERFLLFC 670 680 690 700 710 VHGDGHAENL VQWEMEVCKL PRLSLNGVRF KRISGTSIAF KNIASKIANE LKL
	Isoform 6 [UniParc]. Checksum: 4CBABE5452A1A22F	FASTA	760	85,441
	10 20 30 40 50 60 MSTRTPLPTV NERDTENHTS HGDGRQEVTS RTSRSGARCR NSIASCADEQ PHIGNYRLLK 70 80 90 100 110 120 TIGKGNFAKV KLARHILTGR EVAIKIIDKT QLNPTSLQKL FREVRIMKIL NHPNIVKLFE 130 140 150 160 170 180 VIETEKTLYL IMEYASGGEV FDYLVAHGRM KEKEARSKFR QGCQAGQTIK VQVSFDLLSL 190 200 210 220 230 240 MFTFIVSAVQ YCHQKRIVHR DLKAENLLLD ADMNIKIADF GFSNEFTVGG KLDTFCGSPP 250 260 270 280 290 300 YAAPELFQGK KYDGPEVDVW SLGVILYTLV SGSLPFDGQN LKELRERVLR GKYRIPFYMS 310 320 330 340 350 360 TDCENLLKRF LVLNPIKRGT LEQIMKDRWI NAGHEEDELK PFVEPELDIS DQKRIDIMVG 370 380 390 400 410 420 MGYSQEEIQE SLSKMKYDEI TATYLLLGRK SSEVRPSSDL NNSTGQSPHH KVQRSVFSSQ 430 440 450 460 470 480 KQRRYSDHAG PAIPSVVAYP KRSQTSTADS DLKEDGISSR KSSGSAVGGK GIAPASPMLG 490 500 510 520 530 540 NASNPNKADI PERKKSSTVP SSNTASGGMT RRNTYVCSER TTADRHSVIQ NGKENSTIPD 550 560 570 580 590 600 QRTPVASTHS ISSAATPDRI RFPRGTASRS TFHGQPRERR TATYNGPPAS PSLSHEATPL 610 620 630 640 650 660 SQTRSRGSTN LFSKLTSKLT RRNMSFRFIK RLPTEYERNG RYEGSSRNVS AEQKDENKEA 670 680 690 700 710 720 KPRSLRFTWS MKTTSSMDPG DMMREIRKVL DANNCDYEQR ERFLLFCVHG DGHAENLVQW 730 740 750 760 EMEVCKLPRL SLNGVRFKRI SGTSIAFKNI ASKIANELKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"C-TAK1 protein kinase phosphorylates human Cdc25C on serine 216 and promotes 14-3-3 protein binding." Peng C.Y., Graves P.R., Ogg S., Thoma R.S., Byrnes M.J. III, Wu Z., Stephenson M.T., Piwnica-Worms H. Cell Growth Differ. 9:197-208(1998) [PubMed: 9543386] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT GLY-443. Tissue: Cervix carcinoma.
[2]	"Human serine/threonine protein kinase cTAK1/Kp78/Mark3: Identification of a novel splice variant and a larger 5'UTR." Waggoner S.N., Stephen R., Farrar W.L., Howard O.M.Z. Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT GLY-443. Tissue: Monocyte.
[3]	"PAR-1 is a Dishevelled-associated kinase and a positive regulator of Wnt signalling." Sun T.-Q., Lu B., Feng J.-J., Reinhard C., Jan Y.N., Fantl W.J., Williams L.T. Nat. Cell Biol. 3:628-636(2001) [PubMed: 11433294] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[4]	"Characterization of an alternatively spliced form of MARK3 from human brain." Drewes G. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	Maheshwari K.K., Som S., Parsa I. Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). Tissue: Pancreas.
[6]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed: 12508121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Cervix.
[8]	"Homo sapiens mRNA partial sequence for a protein kinase, STK10, similar to p78/C-TAK1." Reynolds C.H., Patel U.A., Anderton B.H. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 300-752 (ISOFORM 6). Tissue: Urinary bladder.
[9]	"Atypical PKC phosphorylates PAR-1 kinases to regulate localization and activity." Hurov J.B., Watkins J.L., Piwnica-Worms H. Curr. Biol. 14:736-741(2004) [PubMed: 15084291] [Abstract] Cited for: PHOSPHORYLATION AT THR-564.
[10]	"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: 14976552] [Abstract] Cited for: ENZYME REGULATION, PHOSPHORYLATION AT THR-211, MUTAGENESIS OF THR-211.
[11]	"New role for hPar-1 kinases EMK and C-TAK1 in regulating localization and activity of class IIa histone deacetylases." Dequiedt F., Martin M., Von Blume J., Vertommen D., Lecomte E., Mari N., Heinen M.F., Bachmann M., Twizere J.C., Huang M.C., Rider M.H., Piwnica-Worms H., Seufferlein T., Kettmann R. Mol. Cell. Biol. 26:7086-7102(2006) [PubMed: 16980613] [Abstract] Cited for: FUNCTION.
[12]	"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H. Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-211; SER-419; SER-469 AND SER-601, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540; SER-543; THR-549 AND THR-591, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-61; SER-380; SER-383; SER-400; SER-419; SER-455; SER-469; SER-476; THR-536; THR-549; SER-583; SER-587; SER-598 AND SER-643, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-469; SER-583 AND SER-585, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-3; SER-42; THR-61; THR-211; TYR-340; SER-341; SER-374; SER-376; SER-377; SER-378; SER-379; SER-380; SER-383; THR-397; SER-400; TYR-418; SER-419; SER-436; THR-438; SER-456; SER-469; SER-494; SER-499; SER-540; THR-541; SER-543; SER-545; SER-583; SER-585; SER-587; SER-598; SER-601; SER-639 AND SER-643, MASS SPECTROMETRY.
[17]	"Kinase associated-1 domains drive MARK/PAR1 kinases to membrane targets by binding acidic phospholipids." Moravcevic K., Mendrola J.M., Schmitz K.R., Wang Y.H., Slochower D., Janmey P.A., Lemmon M.A. Cell 143:966-977(2010) [PubMed: 21145462] [Abstract] Cited for: SUBCELLULAR LOCATION.
[18]	"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: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-429 AND GLY-443.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U64205 mRNA. Translation: AAC15093.1.
AF159295 mRNA. Translation: AAD48007.1.
AF387637 mRNA. Translation: AAK82367.1.
AF465413 mRNA. Translation: AAL69982.1.
M80359 mRNA. Translation: AAA59991.1.
AL133367 Genomic DNA. No translation available.
BC024773 mRNA. Translation: AAH24773.1.
AF170723 mRNA. Translation: AAD51631.1.

IPI

IPI00183118.
IPI00220505.
IPI00220506.
IPI00220507.
IPI00220508.
IPI00220509.

PIR

S27966.

RefSeq

NP_001122390.1. NM_001128918.1.
NP_001122391.1. NM_001128919.1.
NP_001122392.1. NM_001128920.1.
NP_001122393.1. NM_001128921.1.
NP_002367.4. NM_002376.5.

UniGene

Hs.35828.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QNJ	X-ray	2.70	A/B	48-370	[»]
3FE3	X-ray	1.90	A/B	41-367	[»]

ProteinModelPortal

P27448.

SMR

P27448. Positions 50-366, 657-753.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34637N.

IntAct

P27448. 32 interactions.

MINT

MINT-272697.

STRING

P27448.

PTM databases

PhosphoSite

P27448.

Polymorphism databases

DMDM

281185502.

Proteomic databases

PRIDE

P27448.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000335102; ENSP00000335347; ENSG00000075413.

GeneID

4140.

KEGG

hsa:4140.

UCSC

uc001ymw.2. human.
uc001ymx.2. human.
uc001yna.2. human.
uc010awp.1. human.

Organism-specific databases

CTD

4140.

GeneCards

GC14P103851.

HGNC

HGNC:6897. MARK3.

HPA

HPA024652.

MIM

602678. gene.

neXtProt

NX_P27448.

PharmGKB

PA30640.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG08718.

HOVERGEN

HBG052453.

InParanoid

P27448.

OMA

DGIPSRK.

PhylomeDB

P27448.

Gene expression databases

ArrayExpress

P27448.

Bgee

P27448.

CleanEx

HS_MARK3.

Genevestigator

P27448.

GermOnline

ENSG00000075413. Homo sapiens.

Family and domain databases

InterPro

IPR001772. Kinase-assoc_KA1.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_kinase-like_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR002290. Ser/Thr_kinase_dom.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view]

Gene3D

G3DSA:3.30.310.80. Kinase-assoc_KA1. 1 hit.

KO

K08798.

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

SOURCE

Search...

Entry information

Entry name

MARK3_HUMAN

Accession

Primary (citable) accession number: P27448
Secondary accession number(s): O60219 , Q8TB41, Q8WX83, Q96RG1, Q9UMY9, Q9UN34

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	July 27, 2011
Last modified:	January 25, 2012
This is version 126 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.