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Protein

Mitogen-activated protein kinase kinase kinase MLK4

Gene

MLK4

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

Functioni

Negative regulator of TLR4 signaling. Does not activate JNK1/MAPK8 pathway, p38/MAPK14, nor ERK2/MAPK1 pathways.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.Curated

Cofactori

Mg2+By similarity

Enzyme regulationi

Homodimerization via the leucine zipper domains is required for autophosphorylation and subsequent activation.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei151 – 1511ATPPROSITE-ProRule annotationBy similarity
Active sitei263 – 2631Proton acceptorPROSITE-ProRule annotationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi130 – 1389ATPPROSITE-ProRule annotationBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase kinase kinase activity Source: UniProtKB-EC
  3. protein homodimerization activity Source: UniProtKB
  4. protein tyrosine kinase activity Source: InterPro

GO - Biological processi

  1. activation of JUN kinase activity Source: UniProtKB
  2. protein autophosphorylation Source: UniProtKB
  3. protein phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase kinase kinase MLK4 (EC:2.7.11.25)
Alternative name(s):
Mixed lineage kinase 4
Gene namesi
Name:MLK41 Publication
Synonyms:KIAA1804Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Unplaced

Pathology & Biotechi

Polymorphism and mutation databases

BioMutaiMLK4.
DMDMi71153820.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10361036Mitogen-activated protein kinase kinase kinase MLK4PRO_0000086268Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei299 – 2991Phosphothreonine; by autocatalysisBy similarity
Modified residuei303 – 3031Phosphoserine; by autocatalysis and MAP4K1By similarity
Modified residuei528 – 5281Phosphoserine3 Publications

Post-translational modificationi

Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ5TCX8.
PaxDbiQ5TCX8.
PRIDEiQ5TCX8.

PTM databases

PhosphoSiteiQ5TCX8.

Expressioni

Gene expression databases

BgeeiQ5TCX8.
ExpressionAtlasiQ5TCX8. baseline and differential.
GenevestigatoriQ5TCX8.

Organism-specific databases

HPAiHPA007636.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with TLR4.By similarity1 Publication

Protein-protein interaction databases

BioGridi124089. 3 interactions.
IntActiQ5TCX8. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ5TCX8.
SMRiQ5TCX8. Positions 42-99, 117-473.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 10265SH3PROSITE-ProRule annotationAdd
BLAST
Domaini124 – 401278Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni425 – 44622Leucine-zipper 1Add
BLAST
Regioni460 – 48122Leucine-zipper 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi15 – 3723Ser-richSequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118807.
HOVERGENiHBG067662.
InParanoidiQ5TCX8.
KOiK17534.
OMAiCEEPKLS.
PhylomeDBiQ5TCX8.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR016231. MLK1/MLK2/MLK4.
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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 11 Publication (identifier: Q5TCX8-1) [UniParc]FASTAAdd to basket

Also known as: MLK4beta

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.

« Hide

        10         20         30         40         50
MALRGAAGAT DTPVSSAGGA PGGSASSSST SSGGSASAGA GLWAALYDYE
60 70 80 90 100
ARGEDELSLR RGQLVEVLSQ DAAVSGDEGW WAGQVQRRLG IFPANYVAPC
110 120 130 140 150
RPAASPAPPP SRPSSPVHVA FERLELKELI GAGGFGQVYR ATWQGQEVAV
160 170 180 190 200
KAARQDPEQD AAAAAESVRR EARLFAMLRH PNIIELRGVC LQQPHLCLVL
210 220 230 240 250
EFARGGALNR ALAAANAAPD PRAPGPRRAR RIPPHVLVNW AVQIARGMLY
260 270 280 290 300
LHEEAFVPIL HRDLKSSNIL LLEKIEHDDI CNKTLKITDF GLAREWHRTT
310 320 330 340 350
KMSTAGTYAW MAPEVIKSSL FSKGSDIWSY GVLLWELLTG EVPYRGIDGL
360 370 380 390 400
AVAYGVAVNK LTLPIPSTCP EPFAKLMKEC WQQDPHIRPS FALILEQLTA
410 420 430 440 450
IEGAVMTEMP QESFHSMQDD WKLEIQQMFD ELRTKEKELR SREEELTRAA
460 470 480 490 500
LQQKSQEELL KRREQQLAER EIDVLERELN ILIFQLNQEK PKVKKRKGKF
510 520 530 540 550
KRSRLKLKDG HRISLPSDFQ HKITVQASPN LDKRRSLNSS SSSPPSSPTM
560 570 580 590 600
MPRLRAIQLT SDESNKTWGR NTVFRQEEFE DVKRNFKKKG CTWGPNSIQM
610 620 630 640 650
KDRTDCKERI RPLSDGNSPW STILIKNQKT MPLASLFVDQ PGSCEEPKLS
660 670 680 690 700
PDGLEHRKPK QIKLPSQAYI DLPLGKDAQR ENPAEAESWE EAASANAATV
710 720 730 740 750
SIEMTPTNSL SRSPQRKKTE SALYGCTVLL ASVALGLDLR ELHKAQAAEE
760 770 780 790 800
PLPKEEKKKR EGIFQRASKS RRSASPPTSL PSTCGEASSP PSLPLSSALG
810 820 830 840 850
ILSTPSFSTK CLLQMDSEDP LVDSAPVTCD SEMLTPDFCP TAPGSGREPA
860 870 880 890 900
LMPRLDTDCS VSRNLPSSFL QQTCGNVPYC ASSKHRPSHH RRTMSDGNPT
910 920 930 940 950
PTGATIISAT GASALPLCPS PAPHSHLPRE VSPKKHSTVH IVPQRRPASL
960 970 980 990 1000
RSRSDLPQAY PQTAVSQLAQ TACVVGRPGP HPTQFLAAKE RTKSHVPSLL
1010 1020 1030
DADVEGQSRD YTVPLCRMRS KTSRPSIYEL EKEFLS
Length:1,036
Mass (Da):113,957
Last modified:December 21, 2004 - v1
Checksum:i2520984802143069
GO
Isoform 21 Publication (identifier: Q5TCX8-2) [UniParc]FASTAAdd to basket

Also known as: MLK4alpha

The sequence of this isoform differs from the canonical sequence as follows:
     559-570: LTSDESNKTWGR → CELSALPRGLLC
     571-1036: Missing.

Show »
Length:570
Mass (Da):63,040
Checksum:i7D8A39D60DBA84F9
GO
Isoform 3 (identifier: Q5TCX8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-554: Missing.
     555-559: RAIQL → MFFLVT

Note: No experimental confirmation available.Curated

Show »
Length:483
Mass (Da):52,817
Checksum:iB38F2AB9CBA7A614
GO

Sequence cautioni

The sequence BAB47433.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti274 – 2741K → E in CAC84639 (Ref. 1) Curated
Sequence conflicti274 – 2741K → E in CAC84640 (Ref. 1) Curated
Sequence conflicti330 – 3301Y → C in CAC84639 (Ref. 1) Curated
Sequence conflicti330 – 3301Y → C in CAC84640 (Ref. 1) Curated
Sequence conflicti687 – 6871E → G in CAC84640 (Ref. 1) Curated
Sequence conflicti701 – 7011S → T in CAC84640 (Ref. 1) Curated
Sequence conflicti705 – 7051T → A in CAC84640 (Ref. 1) Curated
Sequence conflicti781 – 7811P → S in CAC84640 (Ref. 1) Curated
Sequence conflicti872 – 8721Q → R in CAC84640 (Ref. 1) Curated
Sequence conflicti1002 – 10021A → V in CAC84640 (Ref. 1) Curated
Sequence conflicti1016 – 10161C → G in CAC84640 (Ref. 1) Curated
Isoform 21 Publication (identifier: Q5TCX8-2)
Sequence conflicti566 – 5661R → P in CAC84639 (Ref. 1) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti420 – 4201D → N.1 Publication
Corresponds to variant rs35465006 [ dbSNP | Ensembl ].
VAR_040729
Natural varianti563 – 5631E → D.1 Publication
Corresponds to variant rs35758282 [ dbSNP | Ensembl ].
VAR_040730
Natural varianti597 – 5971S → F.1 Publication
Corresponds to variant rs34984140 [ dbSNP | Ensembl ].
VAR_040731
Natural varianti728 – 7281V → I.1 Publication
Corresponds to variant rs3795375 [ dbSNP | Ensembl ].
VAR_040732
Natural varianti741 – 7411E → D.1 Publication
Corresponds to variant rs3795374 [ dbSNP | Ensembl ].
VAR_040733
Natural varianti784 – 7841C → G.1 Publication
Corresponds to variant rs963981 [ dbSNP | Ensembl ].
VAR_040734
Natural varianti892 – 8921R → W.1 Publication
Corresponds to variant rs55681416 [ dbSNP | Ensembl ].
VAR_040735
Natural varianti900 – 9001T → I.1 Publication
Corresponds to variant rs34499091 [ dbSNP | Ensembl ].
VAR_040736
Natural varianti977 – 9771R → C.1 Publication
Corresponds to variant rs56065162 [ dbSNP | Ensembl ].
VAR_040737
Natural varianti982 – 9821P → L.1 Publication
Corresponds to variant rs34794284 [ dbSNP | Ensembl ].
VAR_040738

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 554554Missing in isoform 3. 1 PublicationVSP_051731Add
BLAST
Alternative sequencei555 – 5595RAIQL → MFFLVT in isoform 3. 1 PublicationVSP_051732
Alternative sequencei559 – 57012LTSDE…KTWGR → CELSALPRGLLC in isoform 2. 1 PublicationVSP_051733Add
BLAST
Alternative sequencei571 – 1036466Missing in isoform 2. 1 PublicationVSP_051734Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ311797 mRNA. Translation: CAC84639.1.
AJ311798 mRNA. Translation: CAC84640.1.
AB058707 mRNA. Translation: BAB47433.1. Different initiation.
AL133380 Genomic DNA. Translation: CAI23045.1.
AL133380 Genomic DNA. Translation: CAI23046.1.
AL133380 Genomic DNA. Translation: CAI23047.1.
CH471098 Genomic DNA. Translation: EAW69988.1.
BC136648 mRNA. Translation: AAI36649.1.
BC136649 mRNA. Translation: AAI36650.1.
CCDSiCCDS1598.1. [Q5TCX8-1]
RefSeqiNP_115811.2. NM_032435.2. [Q5TCX8-1]
UniGeneiHs.547779.

Genome annotation databases

GeneIDi84451.
KEGGihsa:84451.
UCSCiuc001hvs.1. human. [Q5TCX8-2]
uc001hvt.4. human. [Q5TCX8-1]
uc001hvu.4. human. [Q5TCX8-3]

Polymorphism and mutation databases

BioMutaiMLK4.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ311797 mRNA. Translation: CAC84639.1.
AJ311798 mRNA. Translation: CAC84640.1.
AB058707 mRNA. Translation: BAB47433.1. Different initiation.
AL133380 Genomic DNA. Translation: CAI23045.1.
AL133380 Genomic DNA. Translation: CAI23046.1.
AL133380 Genomic DNA. Translation: CAI23047.1.
CH471098 Genomic DNA. Translation: EAW69988.1.
BC136648 mRNA. Translation: AAI36649.1.
BC136649 mRNA. Translation: AAI36650.1.
CCDSiCCDS1598.1. [Q5TCX8-1]
RefSeqiNP_115811.2. NM_032435.2. [Q5TCX8-1]
UniGeneiHs.547779.

3D structure databases

ProteinModelPortaliQ5TCX8.
SMRiQ5TCX8. Positions 42-99, 117-473.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124089. 3 interactions.
IntActiQ5TCX8. 2 interactions.

PTM databases

PhosphoSiteiQ5TCX8.

Polymorphism and mutation databases

BioMutaiMLK4.
DMDMi71153820.

Proteomic databases

MaxQBiQ5TCX8.
PaxDbiQ5TCX8.
PRIDEiQ5TCX8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi84451.
KEGGihsa:84451.
UCSCiuc001hvs.1. human. [Q5TCX8-2]
uc001hvt.4. human. [Q5TCX8-1]
uc001hvu.4. human. [Q5TCX8-3]

Organism-specific databases

CTDi84451.
GeneCardsiGC01P233463.
H-InvDBHIX0001705.
HPAiHPA007636.
MIMi614793. gene.
neXtProtiNX_Q5TCX8.
HUGEiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118807.
HOVERGENiHBG067662.
InParanoidiQ5TCX8.
KOiK17534.
OMAiCEEPKLS.
PhylomeDBiQ5TCX8.

Miscellaneous databases

ChiTaRSiKIAA1804. human.
GenomeRNAii84451.
NextBioi74235.
PROiQ5TCX8.
SOURCEiSearch...

Gene expression databases

BgeeiQ5TCX8.
ExpressionAtlasiQ5TCX8. baseline and differential.
GenevestigatoriQ5TCX8.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR016231. MLK1/MLK2/MLK4.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "MLK4, a new member of mixed lineage kinases."
    Kvasha S., Protopopov A., Rynditch A., Zabarovsky E., Kashuba V.
    Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: HeartImported.
  2. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
    DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: BrainImported.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 1).
  6. "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-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "MLK4 has negative effect on TLR4 signaling."
    Seit-Nebi A., Cheng W., Xu H., Han J.
    Cell. Mol. Immunol. 9:27-33(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TLR4.
  11. "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] ASN-420; ASP-563; PHE-597; ILE-728; ASP-741; GLY-784; TRP-892; ILE-900; CYS-977 AND LEU-982.

Entry informationi

Entry nameiM3KL4_HUMAN
AccessioniPrimary (citable) accession number: Q5TCX8
Secondary accession number(s): B2RN34
, Q5TCX7, Q5TCX9, Q8WWN1, Q8WWN2, Q96JM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: December 21, 2004
Last modified: April 29, 2015
This is version 109 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 1
    Human chromosome 1: 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.