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Q16659

- MK06_HUMAN

UniProt

Q16659 - MK06_HUMAN

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Protein

Mitogen-activated protein kinase 6

Gene

MAPK6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Atypical MAPK protein. Phosphorylates microtubule-associated protein 2 (MAP2) and MAPKAPK5. The precise role of the complex formed with MAPKAPK5 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPKAPK5, ERK3/MAPK6 is phosphorylated at Ser-189 and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6. May promote entry in the cell cycle (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.By similarity

Enzyme regulationi

Activated by phosphorylation at Ser-189.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491ATPPROSITE-ProRule annotation
Active sitei152 – 1521Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 349ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase activity Source: UniProtKB
  3. protein serine/threonine kinase activity Source: ProtInc

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. MAPK cascade Source: GOC
  3. protein phosphorylation Source: UniProtKB
  4. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.24. 2681.
SignaLinkiQ16659.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 6 (EC:2.7.11.24)
Short name:
MAP kinase 6
Short name:
MAPK 6
Alternative name(s):
Extracellular signal-regulated kinase 3
Short name:
ERK-3
MAP kinase isoform p97
Short name:
p97-MAPK
Gene namesi
Name:MAPK6
Synonyms:ERK3, PRKM6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:6879. MAPK6.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity
Note: Translocates to the cytoplasm following interaction with MAPKAPK5.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30624.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 721721Mitogen-activated protein kinase 6PRO_0000186257Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki1 – 1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei189 – 1891Phosphoserine; by PAK1, PAK2 and PAK33 Publications

Post-translational modificationi

Phosphorylated at Ser-189 by PAK1, PAK2 and PAK3 resulting in catalytic activation. Phosphorylated by MAPKAPK5 at other sites.3 Publications
Ubiquitination at Met-1 leads to degradation by the proteasome pathway.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ16659.
PaxDbiQ16659.
PRIDEiQ16659.

PTM databases

PhosphoSiteiQ16659.

Expressioni

Tissue specificityi

Highest expression in the skeletal muscle, followed by the brain. Also found in heart, placenta, lung, liver, pancreas, kidney and skin fibroblasts.

Gene expression databases

BgeeiQ16659.
CleanExiHS_MAPK6.
GenevestigatoriQ16659.

Organism-specific databases

HPAiCAB005184.
HPA030262.
HPA047825.

Interactioni

Subunit structurei

Heterodimer with ERK4/MAPK4. Interacts with (via FRIEDE motif) MAPKAPK5 (By similarity). Interacts with UBE3A; this interaction may be indirect and mediated by HERC2, possibly via HERC2 interaction with NEURL4.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPKAPK5Q8IW413EBI-1384105,EBI-1201460
vifP125042EBI-1384105,EBI-779991From a different organism.

Protein-protein interaction databases

BioGridi111583. 176 interactions.
IntActiQ16659. 173 interactions.
MINTiMINT-8247530.
STRINGi9606.ENSP00000261845.

Structurei

Secondary structure

1
721
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 163
Turni17 – 193
Beta strandi20 – 256
Beta strandi34 – 396
Turni40 – 423
Beta strandi45 – 528
Helixi56 – 7015
Beta strandi80 – 845
Beta strandi102 – 1098
Beta strandi112 – 1143
Helixi115 – 1195
Helixi126 – 14520
Helixi155 – 1573
Beta strandi158 – 1614
Turni162 – 1654
Beta strandi166 – 1694
Helixi190 – 1923
Helixi200 – 2045
Helixi211 – 22717
Helixi237 – 24711
Helixi253 – 2608
Helixi265 – 2706
Helixi278 – 2814
Helixi287 – 2948
Helixi301 – 3033
Helixi307 – 3115
Helixi314 – 3174

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I6LX-ray2.25A/B9-327[»]
ProteinModelPortaliQ16659.
SMRiQ16659. Positions 13-358.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16659.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 316297Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi189 – 1913SEG motif
Motifi332 – 3376FRIEDE motif

Domaini

In contrast to classical MAPKs, the TXY motif within the activation loop is replaced by the SEG motif, whose phosphorylation activates the MAP kinases.By similarity

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074298.
HOGENOMiHOG000233020.
HOVERGENiHBG104376.
InParanoidiQ16659.
KOiK06855.
OMAiEHDWPIH.
OrthoDBiEOG780RKS.
PhylomeDBiQ16659.
TreeFamiTF105098.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR008350. MAPK_ERK3/4.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01771. ERK3ERK4MAPK.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q16659-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEKFESLMN IHGFDLGSRY MDLKPLGCGG NGLVFSAVDN DCDKRVAIKK
60 70 80 90 100
IVLTDPQSVK HALREIKIIR RLDHDNIVKV FEILGPSGSQ LTDDVGSLTE
110 120 130 140 150
LNSVYIVQEY METDLANVLE QGPLLEEHAR LFMYQLLRGL KYIHSANVLH
160 170 180 190 200
RDLKPANLFI NTEDLVLKIG DFGLARIMDP HYSHKGHLSE GLVTKWYRSP
210 220 230 240 250
RLLLSPNNYT KAIDMWAAGC IFAEMLTGKT LFAGAHELEQ MQLILESIPV
260 270 280 290 300
VHEEDRQELL SVIPVYIRND MTEPHKPLTQ LLPGISREAL DFLEQILTFS
310 320 330 340 350
PMDRLTAEEA LSHPYMSIYS FPMDEPISSH PFHIEDEVDD ILLMDETHSH
360 370 380 390 400
IYNWERYHDC QFSEHDWPVH NNFDIDEVQL DPRALSDVTD EEEVQVDPRK
410 420 430 440 450
YLDGDREKYL EDPAFDTNYS TEPCWQYSDH HENKYCDLEC SHTCNYKTRS
460 470 480 490 500
SSYLDNLVWR ESEVNHYYEP KLIIDLSNWK EQSKEKSDKK GKSKCERNGL
510 520 530 540 550
VKAQIALEEA SQQLAGKERE KNQGFDFDSF IAGTIQLSSQ HEPTDVVDKL
560 570 580 590 600
NDLNSSVSQL ELKSLISKSV SQEKQEKGMA NLAQLEALYQ SSWDSQFVSG
610 620 630 640 650
GEDCFFINQF CEVRKDEQVE KENTYTSYLD KFFSRKEDTE MLETEPVEDG
660 670 680 690 700
KLGERGHEEG FLNNSGEFLF NKQLESIGIP QFHSPVGSPL KSIQATLTPS
710 720
AMKSSPQIPH QTYSSILKHL N
Length:721
Mass (Da):82,681
Last modified:November 1, 1996 - v1
Checksum:iDAA3AAA9B98BB31F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti229 – 2291K → R in BAG36392. (PubMed:14702039)Curated
Sequence conflicti527 – 5271F → L in BAG70115. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti290 – 2901L → V.2 Publications
Corresponds to variant rs35697691 [ dbSNP | Ensembl ].
VAR_042256

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80692 mRNA. Translation: CAA56709.1.
L77964 mRNA. Translation: AAA98769.1.
AF420474 mRNA. Translation: AAL17605.1.
AK313633 mRNA. Translation: BAG36392.1.
CR749401 mRNA. Translation: CAH18246.1.
AB451301 mRNA. Translation: BAG70115.1.
BC035492 mRNA. Translation: AAH35492.1.
CCDSiCCDS10147.1.
PIRiA56352.
RefSeqiNP_002739.1. NM_002748.3.
XP_005254593.1. XM_005254536.2.
XP_005254594.1. XM_005254537.1.
XP_005254595.1. XM_005254538.1.
XP_005254596.1. XM_005254539.2.
UniGeneiHs.411847.

Genome annotation databases

EnsembliENST00000261845; ENSP00000261845; ENSG00000069956.
GeneIDi5597.
KEGGihsa:5597.
UCSCiuc002abp.3. human.

Polymorphism databases

DMDMi2499596.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80692 mRNA. Translation: CAA56709.1 .
L77964 mRNA. Translation: AAA98769.1 .
AF420474 mRNA. Translation: AAL17605.1 .
AK313633 mRNA. Translation: BAG36392.1 .
CR749401 mRNA. Translation: CAH18246.1 .
AB451301 mRNA. Translation: BAG70115.1 .
BC035492 mRNA. Translation: AAH35492.1 .
CCDSi CCDS10147.1.
PIRi A56352.
RefSeqi NP_002739.1. NM_002748.3.
XP_005254593.1. XM_005254536.2.
XP_005254594.1. XM_005254537.1.
XP_005254595.1. XM_005254538.1.
XP_005254596.1. XM_005254539.2.
UniGenei Hs.411847.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2I6L X-ray 2.25 A/B 9-327 [» ]
ProteinModelPortali Q16659.
SMRi Q16659. Positions 13-358.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111583. 176 interactions.
IntActi Q16659. 173 interactions.
MINTi MINT-8247530.
STRINGi 9606.ENSP00000261845.

Chemistry

BindingDBi Q16659.
ChEMBLi CHEMBL5121.
GuidetoPHARMACOLOGYi 2092.

PTM databases

PhosphoSitei Q16659.

Polymorphism databases

DMDMi 2499596.

Proteomic databases

MaxQBi Q16659.
PaxDbi Q16659.
PRIDEi Q16659.

Protocols and materials databases

DNASUi 5597.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261845 ; ENSP00000261845 ; ENSG00000069956 .
GeneIDi 5597.
KEGGi hsa:5597.
UCSCi uc002abp.3. human.

Organism-specific databases

CTDi 5597.
GeneCardsi GC15P052311.
HGNCi HGNC:6879. MAPK6.
HPAi CAB005184.
HPA030262.
HPA047825.
MIMi 602904. gene.
neXtProti NX_Q16659.
PharmGKBi PA30624.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074298.
HOGENOMi HOG000233020.
HOVERGENi HBG104376.
InParanoidi Q16659.
KOi K06855.
OMAi EHDWPIH.
OrthoDBi EOG780RKS.
PhylomeDBi Q16659.
TreeFami TF105098.

Enzyme and pathway databases

BRENDAi 2.7.11.24. 2681.
SignaLinki Q16659.

Miscellaneous databases

EvolutionaryTracei Q16659.
GeneWikii MAPK6.
GenomeRNAii 5597.
NextBioi 21724.
PROi Q16659.
SOURCEi Search...

Gene expression databases

Bgeei Q16659.
CleanExi HS_MAPK6.
Genevestigatori Q16659.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR008350. MAPK_ERK3/4.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR01771. ERK3ERK4MAPK.
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of p97MAPK, a novel human homolog of rat ERK-3."
    Zhu A.X., Zhao Y., Moller D.E., Flier J.S.
    Mol. Cell. Biol. 14:8202-8211(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal skeletal muscle.
  2. "Primary structure, expression and chromosomal locus of a human homolog of rat ERK3."
    Meloche S., Beatty B.G., Pellerin J.
    Oncogene 13:1575-1579(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Smooth muscle.
  3. "ERK-3 cDNA clone isolated from human oral cancer."
    Saranath D., Mahale A., Rai R., Dedhia P.
    Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Oral cancer.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Trachea.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Esophageal carcinoma.
  6. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-290.
    Tissue: Placenta.
  8. "N-Terminal ubiquitination of extracellular signal-regulated kinase 3 and p21 directs their degradation by the proteasome."
    Coulombe P., Rodier G., Bonneil E., Thibault P., Meloche S.
    Mol. Cell. Biol. 24:6140-6150(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT MET-1.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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.
  12. "Activation loop phosphorylation of ERK3/ERK4 by group I p21-activated kinases (PAKs) defines a novel PAK-ERK3/4-MAPK-activated protein kinase 5 signaling pathway."
    Deleris P., Trost M., Topisirovic I., Tanguay P.L., Borden K.L., Thibault P., Meloche S.
    J. Biol. Chem. 286:6470-6478(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-189.
  13. "Identification and proteomic analysis of distinct UBE3A/E6AP protein complexes."
    Martinez-Noel G., Galligan J.T., Sowa M.E., Arndt V., Overton T.M., Harper J.W., Howley P.M.
    Mol. Cell. Biol. 32:3095-3106(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBE3A AND NEURL4.
  14. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-290.

Entry informationi

Entry nameiMK06_HUMAN
AccessioniPrimary (citable) accession number: Q16659
Secondary accession number(s): B2R945
, B5BU65, Q68DH4, Q8IYN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3