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P27448 (MARK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length753 AA.
Sequence statusComplete.
Protein existenceEvidence 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.12

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activated by phosphorylation on Thr-211. Inhibited by phosphorylation on Thr-564. Ref.11

Subcellular location

Cell membrane; Peripheral membrane protein Ref.18.

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.10 Ref.11

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 componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentplasma membrane

Inferred from direct assay Ref.18. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine kinase activity

Inferred from direct assay Ref.12. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 7 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.
Note: Contains a phosphoserine at position 384.
Isoform 6 (identifier: P27448-7)

The sequence of this isoform differs from the canonical sequence as follows:
     161-161: Q → QGCQAGQTIKVQVSFDLLSLMFTF
     371-386: Missing.
Note: Contains a phosphoserine at position 407.
Isoform 7 (identifier: P27448-8)

The sequence of this isoform differs from the canonical sequence as follows:
     179-257: Missing.
     624-638: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 753753MAP/microtubule affinity-regulating kinase 3
PRO_0000086304

Regions

Domain56 – 307252Protein kinase
Domain326 – 36540UBA
Domain704 – 75350KA1
Nucleotide binding62 – 709ATP By similarity

Sites

Active site1781Proton acceptor By similarity
Binding site851ATP By similarity

Amino acid modifications

Modified residue421Phosphoserine Ref.16
Modified residue2111Phosphothreonine; by LKB1 Ref.11
Modified residue3831Phosphoserine Ref.14 Ref.16
Modified residue4001Phosphoserine Ref.14
Modified residue4691Phosphoserine Ref.14 Ref.16 Ref.20
Modified residue5491Phosphothreonine Ref.13 Ref.14
Modified residue5641Phosphothreonine; by PKC/PRKCZ By similarity
Modified residue5981Phosphoserine Ref.14
Modified residue6431Phosphoserine Ref.14 Ref.16

Natural variations

Alternative sequence1611Q → QGCQAGQTIKVQVSFDLLSL MFTF in isoform 2 and isoform 6.
VSP_041582
Alternative sequence179 – 25779Missing in isoform 7.
VSP_043197
Alternative sequence371 – 38616Missing in isoform 5 and isoform 6.
VSP_004943
Alternative sequence615 – 63824Missing in isoform 2, isoform 3 and isoform 5.
VSP_004944
Alternative sequence615 – 6239Missing in isoform 4.
VSP_004945
Alternative sequence624 – 63815Missing in isoform 7.
VSP_043198
Natural variant4291V → A. Ref.21
VAR_040765
Natural variant4431S → G. Ref.1 Ref.2 Ref.21
Corresponds to variant rs56305318 [ dbSNP | Ensembl ].
VAR_046763

Experimental info

Mutagenesis2111T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. Ref.11
Sequence conflict1251E → Q in AAA59991. Ref.5
Sequence conflict1391E → K in AAL69982. Ref.4
Sequence conflict1391E → K in AAA59991. Ref.5
Sequence conflict1491R → K in AAD48007. Ref.2
Sequence conflict4101F → S in AAC15093. Ref.1
Sequence conflict4101F → S in AAD48007. Ref.2
Sequence conflict4101F → S in AAK82367. Ref.3
Sequence conflict4101F → S in AAL69982. Ref.4
Sequence conflict4101F → S in AAA59991. Ref.5
Sequence conflict4101F → S in AAH24773. Ref.7
Sequence conflict4101F → S in AAD51631. Ref.8
Sequence conflict4251A → G in AAA59991. Ref.5
Sequence conflict4561S → T in AAA59991. Ref.5
Sequence conflict5161A → D in AAA59991. Ref.5
Sequence conflict6031N → T in AAA59991. Ref.5
Sequence conflict6451E → K in AAA59991. Ref.5

Secondary structure

1 .................................................... 753
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: 0CA50C58A4A49D93

FASTA75384,489
        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

« Hide

Isoform 2 (CTAK75a) [UniParc].

Checksum: 0306682A37C313D7
Show »

FASTA75284,015
Isoform 3 [UniParc].

Checksum: 4DF13ABB00F2305D
Show »

FASTA72981,499
Isoform 4 [UniParc].

Checksum: EDDC40EDF509566E
Show »

FASTA74483,308
Isoform 5 (p58) [UniParc].

Checksum: 32B5C41C16F5F080
Show »

FASTA71379,936
Isoform 6 [UniParc].

Checksum: 4CBABE5452A1A22F
Show »

FASTA76085,441
Isoform 7 [UniParc].

Checksum: BBF32F62ABACEF9B
Show »

FASTA65974,151

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
Tissue: Neuroblastoma.
[7]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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).
Tissue: Cervix.
[9]"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.
[10]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-564.
[11]"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] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, PHOSPHORYLATION AT THR-211, MUTAGENESIS OF THR-211.
[12]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-549, 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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-400; SER-469; THR-549; SER-598 AND SER-643, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384 (ISOFORM 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 (ISOFORM 6), MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-383; SER-469 AND SER-643, MASS SPECTROMETRY.
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469, MASS SPECTROMETRY.
[21]"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. expand/collapse author list , 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] [Europe PMC] [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.
BX161395 mRNA. Translation: CAD61882.1.
AL133367 Genomic DNA. No translation available.
BC024773 mRNA. Translation: AAH24773.1.
AF170723 mRNA. Translation: AAD51631.1.
IPIIPI00183118.
IPI00220505.
IPI00220506.
IPI00220507.
IPI00220508.
IPI00220509.
IPI00827718.
PIRS27966.
RefSeqNP_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.
UniGeneHs.35828.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QNJX-ray2.70A/B48-370[»]
3FE3X-ray1.90A/B41-367[»]
ProteinModelPortalP27448.
SMRP27448. Positions 18-366, 657-753.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-34637N.
IntActP27448. 34 interactions.
MINTMINT-272697.
STRING9606.ENSP00000411397.

PTM databases

PhosphoSiteP27448.

Polymorphism databases

DMDM281185502.

Proteomic databases

PaxDbP27448.
PRIDEP27448.

Protocols and materials databases

DNASU4140.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216288; ENSP00000216288; ENSG00000075413.
ENST00000303622; ENSP00000303698; ENSG00000075413.
ENST00000416682; ENSP00000408092; ENSG00000075413.
ENST00000429436; ENSP00000411397; ENSG00000075413.
ENST00000440884; ENSP00000402104; ENSG00000075413.
ENST00000553942; ENSP00000450772; ENSG00000075413.
GeneID4140.
KEGGhsa:4140.
UCSCuc001ymw.4. human.
uc001ymx.4. human.
uc001ymy.4. human.
uc001ymz.4. human.
uc001yna.4. human.
uc010awp.3. human.
uc010tyb.2. human.

Organism-specific databases

CTD4140.
GeneCardsGC14P103851.
HGNCHGNC:6897. MARK3.
HPAHPA024652.
MIM602678. gene.
neXtProtNX_P27448.
PharmGKBPA30640.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233025.
HOVERGENHBG052453.
InParanoidP27448.
KOK08798.

Enzyme and pathway databases

SignaLinkP27448.

Gene expression databases

ArrayExpressP27448.
BgeeP27448.
CleanExHS_MARK3.
GenevestigatorP27448.
GermOnlineENSG00000075413. Homo sapiens.

Family and domain databases

InterProIPR001772. 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]
PfamPF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]
SUPFAMSSF103243. Kinase-assoc_KA1. 1 hit.
SSF56112. Kinase_like. 1 hit.
PROSITEPS50032. 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]
ProtoNetSearch...

Other

ChEMBLCHEMBL5600.
ChiTaRSMARK3. human.
EvolutionaryTraceP27448.
GenomeRNAi4140.
NextBio16260.
SOURCESearch...

Entry information

Entry nameMARK3_HUMAN
AccessionPrimary (citable) accession number: P27448
Secondary accession number(s): O60219 expand/collapse secondary AC list , Q86TT8, Q8TB41, Q8WX83, Q96RG1, Q9UMY9, Q9UN34
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 27, 2011
Last modified: May 29, 2013
This is version 139 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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