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Q8NB16

- MLKL_HUMAN

UniProt

Q8NB16 - MLKL_HUMAN

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Protein

Mixed lineage kinase domain-like protein

Gene

MLKL

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

Functioni

Pseudokinase that plays a key role in TNF-induced necroptosis, a programmed cell death process. Activated following phosphorylation by RIPK3, leading to homotrimerization, localization to the plasma membrane and execution of programmed necrosis characterized by calcium influx and plasma membrane damage. Does not have protein kinase activity.4 Publications

Enzyme regulationi

Inhibited by necrosulfonamide, a specific inhibitor of necroptosis that targets Cys-86.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei86 – 861Target of necrosulfonamide inhibitor
Binding sitei230 – 2301ATPCurated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi209 – 2179ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. protein complex binding Source: UniProtKB
  3. transferase activity, transferring phosphorus-containing groups Source: InterPro

GO - Biological processi

  1. necroptotic process Source: UniProtKB
  2. protein homotrimerization Source: UniProtKB
  3. protein phosphorylation Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Necrosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mixed lineage kinase domain-like protein
Short name:
hMLKL
Gene namesi
Name:MLKLImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:26617. MLKL.

Subcellular locationi

Cytoplasm 1 Publication. Cell membrane 1 Publication
Note: Localizes to the cytoplasm and translocates to the plasma membrane on necroptosis induction.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581L → G: Does not affect formation of homotrimers, while translocation to the plasma membrane on necroptosis induction is impaired; when associated with G-76. 1 Publication
Mutagenesisi76 – 761I → G: Does not affect formation of homotrimers, while translocation to the plasma membrane on necroptosis induction is impaired; when associated with G-58. 1 Publication
Mutagenesisi86 – 861C → S: Abolishes binding to necrosulfonamide inhibitor. 1 Publication
Mutagenesisi162 – 1621L → G: Impairs formation of homotrimers and translocation to the plasma membrane on necroptosis induction; when associated with G-165. 1 Publication
Mutagenesisi165 – 1651L → G: Impairs formation of homotrimers and translocation to the plasma membrane on necroptosis induction; when associated with G-162. 1 Publication
Mutagenesisi230 – 2301K → M: Abolishes ATP-binding. 1 Publication
Mutagenesisi331 – 3311K → N: Impairs ATP-binding. 1 Publication
Mutagenesisi351 – 3511E → K: Binds ATP with an enhanced affinity. 1 Publication
Mutagenesisi357 – 3582TS → ED: Mimics phosphorylation state; acts as a dominant-negative mutant that impairs necroptosis.
Mutagenesisi357 – 3571T → A: No effect. Abolishes ability to mediate necroptosis; when associated with A-358. 1 Publication
Mutagenesisi358 – 3581S → A: No effect. Abolishes ability to mediate necroptosis; when associated with A-357. 1 Publication

Organism-specific databases

PharmGKBiPA142671349.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 471471Mixed lineage kinase domain-like proteinPRO_0000248239Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei125 – 1251Phosphoserine2 Publications
Modified residuei357 – 3571Phosphothreonine; by RIPK31 Publication
Modified residuei358 – 3581Phosphoserine; by RIPK31 Publication
Modified residuei360 – 3601Phosphoserine; by RIPK3By similarity

Post-translational modificationi

Phosphorylation by RIPK3 induces a conformational switch that is required for necroptosis. It also induces homotrimerization and localization to the plasma membrane.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8NB16.
PaxDbiQ8NB16.
PRIDEiQ8NB16.

PTM databases

PhosphoSiteiQ8NB16.

Expressioni

Gene expression databases

BgeeiQ8NB16.
CleanExiHS_MLKL.
ExpressionAtlasiQ8NB16. baseline and differential.
GenevestigatoriQ8NB16.

Organism-specific databases

HPAiHPA010535.
HPA046756.

Interactioni

Subunit structurei

Homotrimer; forms homotrimers on necroptosis induction. Interacts with RIPK3; the interaction is direct. Upon TNF-induced necrosis, forms in complex with PGAM5, RIPK1 and RIPK3. Within this complex, may play a role in the proper targeting of RIPK1/RIPK3 to its downstream effector PGAM5.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RIPK3Q9Y57210EBI-1055040,EBI-298250

Protein-protein interaction databases

BioGridi128244. 7 interactions.
DIPiDIP-41782N.
IntActiQ8NB16. 7 interactions.
MINTiMINT-1033261.
STRINGi9606.ENSP00000308351.

Structurei

Secondary structure

1
471
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi198 – 2014
Beta strandi207 – 2115
Beta strandi213 – 22210
Beta strandi225 – 2328
Helixi240 – 25617
Beta strandi265 – 2717
Beta strandi274 – 2763
Beta strandi278 – 2847
Helixi291 – 2977
Helixi303 – 32220
Beta strandi323 – 3253
Helixi334 – 3363
Beta strandi337 – 3393
Beta strandi345 – 3473
Helixi373 – 3764
Helixi379 – 3835
Helixi391 – 40717
Turni411 – 4144
Helixi417 – 4259
Helixi439 – 44810
Helixi453 – 4553
Helixi459 – 4679

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4M67X-ray1.90A179-471[»]
4MWIX-ray1.70A183-471[»]
ProteinModelPortaliQ8NB16.
SMRiQ8NB16. Positions 2-470.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini194 – 469276Protein kinasePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili55 – 8430Sequence AnalysisAdd
BLAST
Coiled coili139 – 18042Sequence AnalysisAdd
BLAST

Domaini

The protein kinase domain is catalytically inactive but contains an unusual pseudoactive site with an interaction between Lys-230 and Gln-356 residues. Upon phosphorylation by RIPK3, undergoes an active conformation By similarity.By similarity
The coiled coil region 2 is responsible for homotrimerization.1 Publication

Sequence similaritiesi

Belongs to the protein kinase superfamily.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00390000016453.
HOGENOMiHOG000113601.
HOVERGENiHBG056156.
InParanoidiQ8NB16.
KOiK08849.
OMAiICIDETV.
OrthoDBiEOG7P5T0V.
PhylomeDBiQ8NB16.
TreeFamiTF328453.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 12 Publications (identifier: Q8NB16-1) [UniParc]FASTAAdd to Basket

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
MENLKHIITL GQVIHKRCEE MKYCKKQCRR LGHRVLGLIK PLEMLQDQGK
60 70 80 90 100
RSVPSEKLTT AMNRFKAALE EANGEIEKFS NRSNICRFLT ASQDKILFKD
110 120 130 140 150
VNRKLSDVWK ELSLLLQVEQ RMPVSPISQG ASWAQEDQQD ADEDRRAFQM
160 170 180 190 200
LRRDNEKIEA SLRRLEINMK EIKETLRQYL PPKCMQEIPQ EQIKEIKKEQ
210 220 230 240 250
LSGSPWILLR ENEVSTLYKG EYHRAPVAIK VFKKLQAGSI AIVRQTFNKE
260 270 280 290 300
IKTMKKFESP NILRIFGICI DETVTPPQFS IVMEYCELGT LRELLDREKD
310 320 330 340 350
LTLGKRMVLV LGAARGLYRL HHSEAPELHG KIRSSNFLVT QGYQVKLAGF
360 370 380 390 400
ELRKTQTSMS LGTTREKTDR VKSTAYLSPQ ELEDVFYQYD VKSEIYSFGI
410 420 430 440 450
VLWEIATGDI PFQGCNSEKI RKLVAVKRQQ EPLGEDCPSE LREIIDECRA
460 470
HDPSVRPSVD EILKKLSTFS K
Length:471
Mass (Da):54,479
Last modified:October 1, 2002 - v1
Checksum:i005E7F7AB6D20649
GO
Isoform 21 Publication (identifier: Q8NB16-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     179-205: YLPPKCMQEIPQEQIKEIKKEQLSGSP → SLESSSGKSPLEISRFKVKNVKTGSAS
     206-413: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:263
Mass (Da):30,279
Checksum:i183FD0023D8A1EC3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521S → T.1 Publication
Corresponds to variant rs34251827 [ dbSNP | Ensembl ].
VAR_041350
Natural varianti100 – 1001D → E.1 Publication
Corresponds to variant rs33987771 [ dbSNP | Ensembl ].
VAR_041351
Natural varianti132 – 1321S → P.1 Publication
Corresponds to variant rs35589326 [ dbSNP | Ensembl ].
VAR_041352
Natural varianti146 – 1461R → Q.1 Publication
Corresponds to variant rs34515646 [ dbSNP | Ensembl ].
VAR_041353
Natural varianti169 – 1691M → L.1 Publication
Corresponds to variant rs55929310 [ dbSNP | Ensembl ].
VAR_041354
Natural varianti291 – 2911L → P in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041355
Natural varianti364 – 3641T → M.1 Publication
Corresponds to variant rs34389205 [ dbSNP | Ensembl ].
VAR_041356
Natural varianti398 – 3981F → I in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041357
Natural varianti421 – 4211R → H.1 Publication
Corresponds to variant rs55987292 [ dbSNP | Ensembl ].
VAR_041358

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei179 – 20527YLPPK…LSGSP → SLESSSGKSPLEISRFKVKN VKTGSAS in isoform 2. 1 PublicationVSP_052133Add
BLAST
Alternative sequencei206 – 413208Missing in isoform 2. 1 PublicationVSP_052134Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK091708 mRNA. Translation: BAC03728.1.
AC109599 Genomic DNA. No translation available.
BC028141 mRNA. Translation: AAH28141.1.
CCDSiCCDS32487.1. [Q8NB16-1]
CCDS45528.1. [Q8NB16-2]
RefSeqiNP_001135969.1. NM_001142497.1. [Q8NB16-2]
NP_689862.1. NM_152649.2. [Q8NB16-1]
XP_005255891.1. XM_005255834.1. [Q8NB16-1]
UniGeneiHs.119878.

Genome annotation databases

EnsembliENST00000306247; ENSP00000303118; ENSG00000168404. [Q8NB16-2]
ENST00000308807; ENSP00000308351; ENSG00000168404. [Q8NB16-1]
GeneIDi197259.
KEGGihsa:197259.
UCSCiuc002fdb.2. human. [Q8NB16-1]
uc002fdc.2. human. [Q8NB16-2]

Polymorphism databases

DMDMi74762545.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK091708 mRNA. Translation: BAC03728.1 .
AC109599 Genomic DNA. No translation available.
BC028141 mRNA. Translation: AAH28141.1 .
CCDSi CCDS32487.1. [Q8NB16-1 ]
CCDS45528.1. [Q8NB16-2 ]
RefSeqi NP_001135969.1. NM_001142497.1. [Q8NB16-2 ]
NP_689862.1. NM_152649.2. [Q8NB16-1 ]
XP_005255891.1. XM_005255834.1. [Q8NB16-1 ]
UniGenei Hs.119878.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4M67 X-ray 1.90 A 179-471 [» ]
4MWI X-ray 1.70 A 183-471 [» ]
ProteinModelPortali Q8NB16.
SMRi Q8NB16. Positions 2-470.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 128244. 7 interactions.
DIPi DIP-41782N.
IntActi Q8NB16. 7 interactions.
MINTi MINT-1033261.
STRINGi 9606.ENSP00000308351.

Chemistry

ChEMBLi CHEMBL1938217.

PTM databases

PhosphoSitei Q8NB16.

Polymorphism databases

DMDMi 74762545.

Proteomic databases

MaxQBi Q8NB16.
PaxDbi Q8NB16.
PRIDEi Q8NB16.

Protocols and materials databases

DNASUi 197259.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000306247 ; ENSP00000303118 ; ENSG00000168404 . [Q8NB16-2 ]
ENST00000308807 ; ENSP00000308351 ; ENSG00000168404 . [Q8NB16-1 ]
GeneIDi 197259.
KEGGi hsa:197259.
UCSCi uc002fdb.2. human. [Q8NB16-1 ]
uc002fdc.2. human. [Q8NB16-2 ]

Organism-specific databases

CTDi 197259.
GeneCardsi GC16M074705.
HGNCi HGNC:26617. MLKL.
HPAi HPA010535.
HPA046756.
MIMi 615153. gene.
neXtProti NX_Q8NB16.
PharmGKBi PA142671349.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00390000016453.
HOGENOMi HOG000113601.
HOVERGENi HBG056156.
InParanoidi Q8NB16.
KOi K08849.
OMAi ICIDETV.
OrthoDBi EOG7P5T0V.
PhylomeDBi Q8NB16.
TreeFami TF328453.

Miscellaneous databases

ChiTaRSi MLKL. human.
GenomeRNAii 197259.
NextBioi 89630.
PROi Q8NB16.
SOURCEi Search...

Gene expression databases

Bgeei Q8NB16.
CleanExi HS_MLKL.
ExpressionAtlasi Q8NB16. baseline and differential.
Genevestigatori Q8NB16.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NOMENCLATURE.
  2. "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] (ISOFORM 1).
    Tissue: ChondrocyteImported.
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 2).
    Tissue: LeukocyteImported.
  5. "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-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase."
    Sun L., Wang H., Wang Z., He S., Chen S., Liao D., Wang L., Yan J., Liu W., Lei X., Wang X.
    Cell 148:213-227(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RIPK3, ENZYME REGULATION, PHOSPHORYLATION AT THR-357 AND SER-358, MUTAGENESIS OF CYS-86; THR-357 AND SER-358.
  11. "The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways."
    Wang Z., Jiang H., Chen S., Du F., Wang X.
    Cell 148:228-243(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN COMPLEX WITH PGAM5; RIPK1 AND RIPK3.
  12. "Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis."
    Zhao J., Jitkaew S., Cai Z., Choksi S., Li Q., Luo J., Liu Z.G.
    Proc. Natl. Acad. Sci. U.S.A. 109:5322-5327(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RIPK3.
  13. "Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis."
    Cai Z., Jitkaew S., Zhao J., Chiang H.C., Choksi S., Liu J., Ward Y., Wu L.G., Liu Z.G.
    Nat. Cell Biol. 16:55-65(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF LEU-58; ILE-76; LEU-162 AND LEU-165.
  14. "Insights into the evolution of divergent nucleotide-binding mechanisms among pseudokinases revealed by crystal structures of human and mouse MLKL."
    Murphy J.M., Lucet I.S., Hildebrand J.M., Tanzer M.C., Young S.N., Sharma P., Lessene G., Alexander W.S., Babon J.J., Silke J., Czabotar P.E.
    Biochem. J. 457:369-377(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 189-471, ATP-BINDING, MUTAGENESIS OF LYS-230; LYS-331 AND GLU-351.
  15. "Structural insights into RIP3-mediated necroptotic signaling."
    Xie T., Peng W., Yan C., Wu J., Gong X., Shi Y.
    Cell Rep. 5:70-78(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 179-471.
  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] THR-52; GLU-100; PRO-132; GLN-146; LEU-169; PRO-291; MET-364; ILE-398 AND HIS-421.

Entry informationi

Entry nameiMLKL_HUMAN
AccessioniPrimary (citable) accession number: Q8NB16
Secondary accession number(s): A6NCE4, Q8N6V0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: October 1, 2002
Last modified: October 29, 2014
This is version 107 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

Miscellaneous

Interaction with RIPK3 is species specific: human MLKL only interacts with human RIPK3 and not mouse RIPK3.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3