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Q16584

- M3K11_HUMAN

UniProt

Q16584 - M3K11_HUMAN

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Protein
Mitogen-activated protein kinase kinase kinase 11
Gene
MAP3K11, MLK3, PTK1, SPRK
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Activates the JUN N-terminal pathway. Required for serum-stimulated cell proliferation and for mitogen and cytokine activation of MAPK14 (p38), MAPK3 (ERK) and MAPK8 (JNK1) through phosphorylation and activation of MAP2K4/MKK4 and MAP2K7/MKK7. Plays a role in mitogen-stimulated phosphorylation and activation of BRAF, but does not phosphorylate BRAF directly. Influences microtubule organization during the cell cycle.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Magnesium By similarity.By similarity

Enzyme regulationi

Homodimerization via the leucine zipper domains is required for autophosphorylation and subsequent activation.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei144 – 1441ATP2 Publications
Active sitei241 – 2411Proton acceptor By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi123 – 1319ATP By similarityBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. JUN kinase kinase kinase activity Source: UniProtKB
  3. identical protein binding Source: UniProtKB
  4. mitogen-activated protein kinase kinase kinase binding Source: UniProtKB
  5. protein binding Source: IntAct
  6. protein homodimerization activity Source: UniProtKB
  7. protein kinase activity Source: ProtInc
  8. protein serine/threonine kinase activity Source: UniProtKB
  9. protein tyrosine kinase activity Source: InterPro

GO - Biological processi

  1. JNK cascade Source: ProtInc
  2. activation of JUN kinase activity Source: UniProtKB
  3. activation of MAPK activity Source: UniProtKB
  4. cell death Source: Ensembl
  5. cell proliferation Source: UniProtKB
  6. microtubule-based process Source: UniProtKB
  7. mitotic G1 phase Source: UniProtKB
  8. positive regulation of JNK cascade Source: UniProtKB
  9. positive regulation of JUN kinase activity Source: UniProtKB
  10. positive regulation of neuron apoptotic process Source: Ensembl
  11. protein autophosphorylation Source: UniProtKB
  12. protein phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ16584.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase kinase kinase 11 (EC:2.7.11.25)
Alternative name(s):
Mixed lineage kinase 3
Src-homology 3 domain-containing proline-rich kinase
Gene namesi
Name:MAP3K11
Synonyms:MLK3, PTK1, SPRK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:6850. MAP3K11.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
Note: Location is cell cycle dependent.1 Publication

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB-KW
  3. microtubule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi144 – 1441K → A: Greatly reduced autophosphorylation activity. 2 Publications
Mutagenesisi144 – 1441K → R: Loss of kinase activity. Prevents activation of SAPK and MAPK14. 2 Publications
Mutagenesisi164 – 1641E → A: Greatly reduced autophosphorylation activity. 1 Publication
Mutagenesisi277 – 2771T → A: Severely reduced autophosphorylation activity. Prevents phosphorylation of SAPK and MAPK14. 1 Publication
Mutagenesisi277 – 2771T → E: No effect on SAPK activation. 1 Publication
Mutagenesisi278 – 2781T → A: No effect on autophosphorylation activity or activation of SAPK and MAPK14. 1 Publication
Mutagenesisi281 – 2811S → A: Reduced autophosphorylation activity. Reduced activation of SAPK and MAPK14. 1 Publication
Mutagenesisi281 – 2811S → E: No effect on SAPK activation. 1 Publication

Organism-specific databases

PharmGKBiPA30594.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 847847Mitogen-activated protein kinase kinase kinase 11
PRO_0000086260Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111Phosphoserine1 Publication
Modified residuei277 – 2771Phosphothreonine; by autocatalysis1 Publication
Modified residuei281 – 2811Phosphoserine; by autocatalysis and MAP4K11 Publication
Modified residuei394 – 3941Phosphoserine1 Publication
Modified residuei507 – 5071Phosphoserine3 Publications
Modified residuei524 – 5241Phosphoserine1 Publication
Modified residuei548 – 5481Phosphoserine2 Publications
Modified residuei555 – 5551Phosphoserine1 Publication
Modified residuei556 – 5561Phosphoserine1 Publication
Modified residuei654 – 6541Phosphoserine1 Publication
Modified residuei693 – 6931Phosphoserine1 Publication
Modified residuei705 – 7051Phosphoserine3 Publications
Modified residuei708 – 7081Phosphothreonine1 Publication
Modified residuei724 – 7241Phosphoserine1 Publication
Modified residuei727 – 7271Phosphoserine1 Publication
Modified residuei740 – 7401Phosphoserine1 Publication
Modified residuei748 – 7481Phosphoserine2 Publications
Modified residuei758 – 7581Phosphoserine3 Publications
Modified residuei770 – 7701Phosphoserine1 Publication
Modified residuei789 – 7891Phosphoserine3 Publications
Modified residuei793 – 7931Phosphoserine5 Publications
Modified residuei815 – 8151Phosphoserine1 Publication

Post-translational modificationi

Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation. Thr-277 is likely to be the main autophosphorylation site. Phosphorylation of Ser-555 and Ser-556 is induced by CDC42.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ16584.
PaxDbiQ16584.
PRIDEiQ16584.

PTM databases

PhosphoSiteiQ16584.

Expressioni

Tissue specificityi

Expressed in a wide variety of normal and neoplastic tissues including fetal lung, liver, heart and kidney, and adult lung, liver, heart, kidney, placenta, skeletal muscle, pancreas and brain.2 Publications

Gene expression databases

ArrayExpressiQ16584.
BgeeiQ16584.
CleanExiHS_MAP3K11.
GenevestigatoriQ16584.

Organism-specific databases

HPAiCAB010165.

Interactioni

Subunit structurei

Homodimer; undergoes dimerization during activation. Interacts with MAP2K4/MKK4. Interacts with MAP2K7/MKK7 By similarity.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q99IB85EBI-49961,EBI-6927873From a different organism.
CDC42P609532EBI-49961,EBI-81752
Map4k1P702183EBI-49961,EBI-2906801From a different organism.
NF2P352404EBI-49961,EBI-1014472

Protein-protein interaction databases

BioGridi110442. 36 interactions.
IntActiQ16584. 14 interactions.
MINTiMINT-2836851.
STRINGi9606.ENSP00000309597.

Structurei

3D structure databases

ProteinModelPortaliQ16584.
SMRiQ16584. Positions 44-101, 114-465.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 10565SH3
Add
BLAST
Domaini117 – 379263Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni403 – 42422Leucine-zipper 1
Add
BLAST
Regioni438 – 45922Leucine-zipper 2
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi14 – 138125Gly-rich
Add
BLAST
Compositional biasi18 – 3013Poly-Gly
Add
BLAST
Compositional biasi426 – 51489Arg-rich
Add
BLAST
Compositional biasi599 – 825227Pro-rich
Add
BLAST

Sequence similaritiesi

Contains 1 SH3 domain.

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000060081.
HOVERGENiHBG067662.
InParanoidiQ16584.
KOiK04419.
OMAiAWGRQSP.
PhylomeDBiQ16584.
TreeFamiTF105118.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR016231. MAPKKK9/10/11.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR001452. SH3_domain.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PIRSFiPIRSF000556. MAPKKK9_11. 1 hit.
PRINTSiPR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q16584-1 [UniParc]FASTAAdd to Basket

« Hide

MEPLKSLFLK SPLGSWNGSG SGGGGGGGGG RPEGSPKAAG YANPVWTALF    50
DYEPSGQDEL ALRKGDRVEV LSRDAAISGD EGWWAGQVGG QVGIFPSNYV 100
SRGGGPPPCE VASFQELRLE EVIGIGGFGK VYRGSWRGEL VAVKAARQDP 150
DEDISVTAES VRQEARLFAM LAHPNIIALK AVCLEEPNLC LVMEYAAGGP 200
LSRALAGRRV PPHVLVNWAV QIARGMHYLH CEALVPVIHR DLKSNNILLL 250
QPIESDDMEH KTLKITDFGL AREWHKTTQM SAAGTYAWMA PEVIKASTFS 300
KGSDVWSFGV LLWELLTGEV PYRGIDCLAV AYGVAVNKLT LPIPSTCPEP 350
FAQLMADCWA QDPHRRPDFA SILQQLEALE AQVLREMPRD SFHSMQEGWK 400
REIQGLFDEL RAKEKELLSR EEELTRAARE QRSQAEQLRR REHLLAQWEL 450
EVFERELTLL LQQVDRERPH VRRRRGTFKR SKLRARDGGE RISMPLDFKH 500
RITVQASPGL DRRRNVFEVG PGDSPTFPRF RAIQLEPAEP GQAWGRQSPR 550
RLEDSSNGER RACWAWGPSS PKPGEAQNGR RRSRMDEATW YLDSDDSSPL 600
GSPSTPPALN GNPPRPSLEP EEPKRPVPAE RGSSSGTPKL IQRALLRGTA 650
LLASLGLGRD LQPPGGPGRE RGESPTTPPT PTPAPCPTEP PPSPLICFSL 700
KTPDSPPTPA PLLLDLGIPV GQRSAKSPRR EEEPRGGTVS PPPGTSRSAP 750
GTPGTPRSPP LGLISRPRPS PLRSRIDPWS FVSAGPRPSP LPSPQPAPRR 800
APWTLFPDSD PFWDSPPANP FQGGPQDCRA QTKDMGAQAP WVPEAGP 847
Length:847
Mass (Da):92,688
Last modified:November 1, 1996 - v1
Checksum:iAFB6E930EA281C15
GO

Sequence cautioni

The sequence BAD92892.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti151 – 1511D → V.1 Publication
Corresponds to variant rs34178129 [ dbSNP | Ensembl ].
VAR_040703
Natural varianti252 – 2521P → H.1 Publication
Corresponds to variant rs17855912 [ dbSNP | Ensembl ].
VAR_030604
Natural varianti282 – 2821A → G.1 Publication
Corresponds to variant rs34594252 [ dbSNP | Ensembl ].
VAR_040704

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti247 – 27226ILLLQ…FGLAR → SEFLGAWLGVAWLWYTPAPN LPLSLA in BAD92892. 1 Publication
Add
BLAST
Sequence conflicti791 – 7911L → P in BAD96501. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U07747 mRNA. Translation: AAA19647.1.
L32976 mRNA. Translation: AAA59859.1.
AB209655 mRNA. Translation: BAD92892.1. Different initiation.
AK222781 mRNA. Translation: BAD96501.1.
BC011263 mRNA. Translation: AAH11263.1.
BC064543 mRNA. Translation: AAH64543.1.
CCDSiCCDS8107.1.
PIRiA53800.
RefSeqiNP_002410.1. NM_002419.3.
UniGeneiHs.502872.

Genome annotation databases

EnsembliENST00000309100; ENSP00000309597; ENSG00000173327.
GeneIDi4296.
KEGGihsa:4296.
UCSCiuc001oew.3. human.

Polymorphism databases

DMDMi71153819.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U07747 mRNA. Translation: AAA19647.1 .
L32976 mRNA. Translation: AAA59859.1 .
AB209655 mRNA. Translation: BAD92892.1 . Different initiation.
AK222781 mRNA. Translation: BAD96501.1 .
BC011263 mRNA. Translation: AAH11263.1 .
BC064543 mRNA. Translation: AAH64543.1 .
CCDSi CCDS8107.1.
PIRi A53800.
RefSeqi NP_002410.1. NM_002419.3.
UniGenei Hs.502872.

3D structure databases

ProteinModelPortali Q16584.
SMRi Q16584. Positions 44-101, 114-465.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110442. 36 interactions.
IntActi Q16584. 14 interactions.
MINTi MINT-2836851.
STRINGi 9606.ENSP00000309597.

Chemistry

BindingDBi Q16584.
ChEMBLi CHEMBL2708.
GuidetoPHARMACOLOGYi 2071.

PTM databases

PhosphoSitei Q16584.

Polymorphism databases

DMDMi 71153819.

Proteomic databases

MaxQBi Q16584.
PaxDbi Q16584.
PRIDEi Q16584.

Protocols and materials databases

DNASUi 4296.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309100 ; ENSP00000309597 ; ENSG00000173327 .
GeneIDi 4296.
KEGGi hsa:4296.
UCSCi uc001oew.3. human.

Organism-specific databases

CTDi 4296.
GeneCardsi GC11M065365.
HGNCi HGNC:6850. MAP3K11.
HPAi CAB010165.
MIMi 600050. gene.
neXtProti NX_Q16584.
PharmGKBi PA30594.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000060081.
HOVERGENi HBG067662.
InParanoidi Q16584.
KOi K04419.
OMAi AWGRQSP.
PhylomeDBi Q16584.
TreeFami TF105118.

Enzyme and pathway databases

SignaLinki Q16584.

Miscellaneous databases

GeneWikii MAP3K11.
GenomeRNAii 4296.
NextBioi 16911.
PROi Q16584.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q16584.
Bgeei Q16584.
CleanExi HS_MAP3K11.
Genevestigatori Q16584.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR016231. MAPKKK9/10/11.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR001452. SH3_domain.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view ]
PIRSFi PIRSF000556. MAPKKK9_11. 1 hit.
PRINTSi PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of SPRK, a novel src-homology 3 domain-containing proline-rich kinase with serine/threonine kinase activity."
    Gallo K.A., Mark M.R., Scadden D.T., Wang Z., Gu Q., Godowski P.J.
    J. Biol. Chem. 269:15092-15100(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-144 AND GLU-164.
    Tissue: Megakaryocyte.
  2. "MLK-3: identification of a widely-expressed protein kinase bearing an SH3 domain and a leucine zipper-basic region domain."
    Ing Y.L., Leung I.W.L., Heng H.H.Q., Tsui L.-C., Lassam N.J.
    Oncogene 9:1745-1750(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Thymus.
  3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver and Spleen.
  4. "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 HIS-252.
    Tissue: Brain and Hippocampus.
  5. "MLK-3 activates the SAPK/JNK and p38/RK pathways via SEK1 and MKK3/6."
    Tibbles L.A., Ing Y.L., Kiefer F., Chan J., Iscove N., Woodgett J.R., Lassam N.J.
    EMBO J. 15:7026-7035(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP2K4/MKK4, FUNCTION IN PHOSPHORYLATION OF MAP2K4/MKK4.
  6. "Dimerization via tandem leucine zippers is essential for the activation of the mitogen-activated protein kinase kinase kinase, MLK-3."
    Leung I.W.L., Lassam N.J.
    J. Biol. Chem. 273:32408-32415(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, HOMODIMERIZATION.
  7. "The kinase activation loop is the key to mixed lineage kinase-3 activation via both autophosphorylation and hematopoietic progenitor kinase 1 phosphorylation."
    Leung I.W.L., Lassam N.J.
    J. Biol. Chem. 276:1961-1967(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PHOSPHORYLATION AT THR-277 AND SER-281, MUTAGENESIS OF LYS-144; THR-277; THR-278 AND SER-281.
  8. "Identification of in vivo phosphorylation sites of MLK3 by mass spectrometry and phosphopeptide mapping."
    Vacratsis P.O., Phinney B.S., Gage D.A., Gallo K.A.
    Biochemistry 41:5613-5624(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-524; SER-555; SER-556; SER-654; SER-705; SER-724; SER-727; SER-740; SER-758; SER-770 AND SER-793.
  9. "A new identity for MLK3 as an NIMA-related, cell cycle-regulated kinase that is localized near centrosomes and influences microtubule organization."
    Swenson K.I., Winkler K.E., Means A.R.
    Mol. Biol. Cell 14:156-172(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "MLK3 is required for mitogen activation of B-Raf, ERK and cell proliferation."
    Chadee D.N., Kyriakis J.M.
    Nat. Cell Biol. 6:770-776(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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-11; SER-507; SER-548; SER-705; THR-708; SER-748; SER-758; SER-793 AND SER-815, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-789 AND SER-793, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-507; SER-548; SER-693; SER-705; SER-748; SER-758; SER-789 AND SER-793, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-789 AND SER-793, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "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: VARIANTS [LARGE SCALE ANALYSIS] VAL-151 AND GLY-282.

Entry informationi

Entry nameiM3K11_HUMAN
AccessioniPrimary (citable) accession number: Q16584
Secondary accession number(s): Q53H00, Q59F06, Q6P2G4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: November 1, 1996
Last modified: July 9, 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi