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Q8NB16 (MLKL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
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:
Mixed lineage kinase domain-like protein

Short name=hMLKL
Gene names
Name:MLKL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.11 Ref.12 Ref.13

Enzyme regulation

Inhibited by necrosulfonamide, a specific inhibitor of necroptosis that targets Cys-86. Ref.10

Subunit structure

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. Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

Cytoplasm. Cell membrane. Note: Localizes to the cytoplasm and translocates to the plasma membrane on necroptosis induction. Ref.13

Domain

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.

The coiled coil region 2 is responsible for homotrimerization (Ref.13).

Post-translational modification

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

Miscellaneous

Interaction with RIPK3 is species specific: human MLKL only interacts with human RIPK3 and not mouse RIPK3 (Ref.10).

Sequence similarities

Belongs to the protein kinase superfamily.

Contains 1 protein kinase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RIPK3Q9Y57210EBI-1055040,EBI-298250

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 Ref.2 (identifier: Q8NB16-1)

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 Ref.4 (identifier: Q8NB16-2)

The sequence of this isoform differs from the canonical sequence as follows:
     179-205: YLPPKCMQEIPQEQIKEIKKEQLSGSP → SLESSSGKSPLEISRFKVKNVKTGSAS
     206-413: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 471471Mixed lineage kinase domain-like protein
PRO_0000248239

Regions

Domain194 – 469276Protein kinase
Nucleotide binding209 – 2179ATP By similarity
Coiled coil55 – 8430 Potential
Coiled coil139 – 18042 Potential

Sites

Binding site2301ATP Probable
Site861Target of necrosulfonamide inhibitor

Amino acid modifications

Modified residue1251Phosphoserine Ref.5 Ref.6
Modified residue3571Phosphothreonine; by RIPK3 Ref.10
Modified residue3581Phosphoserine; by RIPK3 Ref.10
Modified residue3601Phosphoserine; by RIPK3 By similarity

Natural variations

Alternative sequence179 – 20527YLPPK…LSGSP → SLESSSGKSPLEISRFKVKN VKTGSAS in isoform 2. Ref.4
VSP_052133
Alternative sequence206 – 413208Missing in isoform 2. Ref.4
VSP_052134
Natural variant521S → T. Ref.16
Corresponds to variant rs34251827 [ dbSNP | Ensembl ].
VAR_041350
Natural variant1001D → E. Ref.16
Corresponds to variant rs33987771 [ dbSNP | Ensembl ].
VAR_041351
Natural variant1321S → P. Ref.16
Corresponds to variant rs35589326 [ dbSNP | Ensembl ].
VAR_041352
Natural variant1461R → Q. Ref.16
Corresponds to variant rs34515646 [ dbSNP | Ensembl ].
VAR_041353
Natural variant1691M → L. Ref.16
Corresponds to variant rs55929310 [ dbSNP | Ensembl ].
VAR_041354
Natural variant2911L → P in a gastric adenocarcinoma sample; somatic mutation. Ref.16
VAR_041355
Natural variant3641T → M. Ref.16
Corresponds to variant rs34389205 [ dbSNP | Ensembl ].
VAR_041356
Natural variant3981F → I in a gastric adenocarcinoma sample; somatic mutation. Ref.16
VAR_041357
Natural variant4211R → H. Ref.16
Corresponds to variant rs55987292 [ dbSNP | Ensembl ].
VAR_041358

Experimental info

Mutagenesis581L → G: Does not affect formation of homotrimers, while translocation to the plasma membrane on necroptosis induction is impaired; when associated with G-76. Ref.13
Mutagenesis761I → G: Does not affect formation of homotrimers, while translocation to the plasma membrane on necroptosis induction is impaired; when associated with G-58. Ref.13
Mutagenesis861C → S: Abolishes binding to necrosulfonamide inhibitor. Ref.10
Mutagenesis1621L → G: Impairs formation of homotrimers and translocation to the plasma membrane on necroptosis induction; when associated with G-165. Ref.13
Mutagenesis1651L → G: Impairs formation of homotrimers and translocation to the plasma membrane on necroptosis induction; when associated with G-162. Ref.13
Mutagenesis2301K → M: Abolishes ATP-binding. Ref.14
Mutagenesis3311K → N: Impairs ATP-binding. Ref.14
Mutagenesis3511E → K: Binds ATP with an enhanced affinity. Ref.14
Mutagenesis357 – 3582TS → ED: Mimics phosphorylation state; acts as a dominant-negative mutant that impairs necroptosis. Ref.10
Mutagenesis3571T → A: No effect. Abolishes ability to mediate necroptosis; when associated with A-358. Ref.10
Mutagenesis3581S → A: No effect. Abolishes ability to mediate necroptosis; when associated with A-357. Ref.10

Secondary structure

........................................... 471
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 2002. Version 1.
Checksum: 005E7F7AB6D20649

FASTA47154,479
        10         20         30         40         50         60 
MENLKHIITL GQVIHKRCEE MKYCKKQCRR LGHRVLGLIK PLEMLQDQGK RSVPSEKLTT 

        70         80         90        100        110        120 
AMNRFKAALE EANGEIEKFS NRSNICRFLT ASQDKILFKD VNRKLSDVWK ELSLLLQVEQ 

       130        140        150        160        170        180 
RMPVSPISQG ASWAQEDQQD ADEDRRAFQM LRRDNEKIEA SLRRLEINMK EIKETLRQYL 

       190        200        210        220        230        240 
PPKCMQEIPQ EQIKEIKKEQ LSGSPWILLR ENEVSTLYKG EYHRAPVAIK VFKKLQAGSI 

       250        260        270        280        290        300 
AIVRQTFNKE IKTMKKFESP NILRIFGICI DETVTPPQFS IVMEYCELGT LRELLDREKD 

       310        320        330        340        350        360 
LTLGKRMVLV LGAARGLYRL HHSEAPELHG KIRSSNFLVT QGYQVKLAGF ELRKTQTSMS 

       370        380        390        400        410        420 
LGTTREKTDR VKSTAYLSPQ ELEDVFYQYD VKSEIYSFGI VLWEIATGDI PFQGCNSEKI 

       430        440        450        460        470 
RKLVAVKRQQ EPLGEDCPSE LREIIDECRA HDPSVRPSVD EILKKLSTFS K 

« Hide

Isoform 2 [UniParc].

Checksum: 183FD0023D8A1EC3
Show »

FASTA26330,279

References

« Hide 'large scale' references
[1]"The protein kinase complement of the human genome."
Manning G., Whyte D.B., Martinez R., Hunter T., Sudarsanam S.
Science 298:1912-1934(2002) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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: Chondrocyte.
[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. expand/collapse author list , 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: Leukocyte.
[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]"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: 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]"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].
[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. 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] THR-52; GLU-100; PRO-132; GLN-146; LEU-169; PRO-291; MET-364; ILE-398 AND HIS-421.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK091708 mRNA. Translation: BAC03728.1.
AC109599 Genomic DNA. No translation available.
BC028141 mRNA. Translation: AAH28141.1.
RefSeqNP_001135969.1. NM_001142497.1.
NP_689862.1. NM_152649.2.
XP_005255891.1. XM_005255834.1.
UniGeneHs.119878.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4M67X-ray1.90A179-471[»]
4MWIX-ray1.70A189-471[»]
ProteinModelPortalQ8NB16.
SMRQ8NB16. Positions 2-469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128244. 7 interactions.
IntActQ8NB16. 7 interactions.
MINTMINT-1033261.
STRING9606.ENSP00000308351.

Chemistry

ChEMBLCHEMBL1938217.

PTM databases

PhosphoSiteQ8NB16.

Polymorphism databases

DMDM74762545.

Proteomic databases

PaxDbQ8NB16.
PRIDEQ8NB16.

Protocols and materials databases

DNASU197259.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306247; ENSP00000303118; ENSG00000168404. [Q8NB16-2]
ENST00000308807; ENSP00000308351; ENSG00000168404. [Q8NB16-1]
GeneID197259.
KEGGhsa:197259.
UCSCuc002fdb.2. human. [Q8NB16-1]
uc002fdc.2. human. [Q8NB16-2]

Organism-specific databases

CTD197259.
GeneCardsGC16M074705.
HGNCHGNC:26617. MLKL.
HPAHPA010535.
HPA046756.
MIM615153. gene.
neXtProtNX_Q8NB16.
PharmGKBPA142671349.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000113601.
HOVERGENHBG056156.
InParanoidQ8NB16.
KOK08849.
OMASIVMEYC.
OrthoDBEOG7P5T0V.
PhylomeDBQ8NB16.
TreeFamTF328453.

Gene expression databases

ArrayExpressQ8NB16.
BgeeQ8NB16.
CleanExHS_MLKL.
GenevestigatorQ8NB16.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMLKL. human.
GenomeRNAi197259.
NextBio89630.
PROQ8NB16.
SOURCESearch...

Entry information

Entry nameMLKL_HUMAN
AccessionPrimary (citable) accession number: Q8NB16
Secondary accession number(s): A6NCE4, Q8N6V0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 102 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM