Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9ESL4

- MLTK_MOUSE

UniProt

Q9ESL4 - MLTK_MOUSE

Protein

Mitogen-activated protein kinase kinase kinase MLT

Gene

Zak

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Stress-activated component of a protein kinase signal transduction cascade. Regulates the JNK and p38 pathways. Pro-apoptotic. Role in regulation of S and G2 cell cycle checkpoint by direct phosphorylation of CHEK2. Isoform 1, but not isoform 2, phosphorylates histone H3 at 'Ser-28'.1 Publication

    Catalytic activityi

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

    Cofactori

    Magnesium.1 Publication

    Enzyme regulationi

    Activated by phosphorylation by PKN1 and autophosphorylation on Thr-161 and Ser-165.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei45 – 451ATPBy similarityPROSITE-ProRule annotation
    Active sitei133 – 1331Proton acceptorBy similarityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi22 – 309ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. MAP kinase kinase kinase activity Source: MGI
    4. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. activation of JUN kinase activity Source: Ensembl
    2. activation of MAPKK activity Source: GOC
    3. cell cycle arrest Source: Ensembl
    4. cell cycle checkpoint Source: UniProtKB
    5. cytoskeleton organization Source: MGI
    6. DNA damage checkpoint Source: Ensembl
    7. intracellular signal transduction Source: UniProtKB
    8. positive regulation of apoptotic process Source: UniProtKB
    9. protein phosphorylation Source: UniProtKB
    10. response to radiation Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase kinase kinase MLT (EC:2.7.11.25)
    Alternative name(s):
    Leucine zipper- and sterile alpha motif kinase ZAK
    MLK-like mitogen-activated protein triple kinase
    Mixed lineage kinase-related kinase
    Short name:
    MLK-related kinase
    Short name:
    MRK
    Sterile alpha motif- and leucine zipper-containing kinase AZK
    Gene namesi
    Name:Zak
    Synonyms:Mltk
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:2443258. Zak.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Appears to shuttle between nucleus and cytoplasm.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi45 – 451K → M: Loss of kinase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 802802Mitogen-activated protein kinase kinase kinase MLTPRO_0000086339Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21PhosphoserineBy similarity
    Modified residuei3 – 31PhosphoserineBy similarity
    Modified residuei155 – 1551PhosphoserineBy similarity
    Modified residuei161 – 1611Phosphothreonine; by autocatalysisBy similarity
    Modified residuei165 – 1651Phosphoserine; by autocatalysisBy similarity
    Modified residuei264 – 2641PhosphoserineBy similarity
    Modified residuei275 – 2751PhosphoserineBy similarity
    Modified residuei302 – 3021PhosphoserineBy similarity
    Modified residuei326 – 3261PhosphoserineBy similarity
    Modified residuei328 – 3281PhosphothreonineBy similarity
    Modified residuei557 – 5571PhosphoserineBy similarity
    Modified residuei565 – 5651PhosphoserineBy similarity
    Modified residuei568 – 5681PhosphoserineBy similarity
    Modified residuei584 – 5841PhosphoserineBy similarity
    Modified residuei586 – 5861PhosphothreonineBy similarity
    Modified residuei591 – 5911PhosphoserineBy similarity
    Modified residuei593 – 5931PhosphoserineBy similarity
    Modified residuei599 – 5991PhosphoserineBy similarity
    Modified residuei628 – 6281PhosphothreonineBy similarity
    Modified residuei634 – 6341PhosphoserineBy similarity
    Modified residuei636 – 6361PhosphoserineBy similarity
    Modified residuei637 – 6371PhosphoserineBy similarity
    Modified residuei638 – 6381PhosphoserineBy similarity
    Modified residuei640 – 6401PhosphothreonineBy similarity
    Modified residuei649 – 6491PhosphoserineBy similarity
    Modified residuei661 – 6611PhosphoserineBy similarity
    Modified residuei667 – 6671PhosphoserineBy similarity
    Modified residuei668 – 6681PhosphoserineBy similarity
    Modified residuei687 – 6871PhosphoserineBy similarity
    Modified residuei690 – 6901PhosphoserineBy similarity
    Modified residuei691 – 6911PhosphoserineBy similarity
    Modified residuei727 – 7271PhosphoserineBy similarity
    Modified residuei733 – 7331PhosphoserineBy similarity
    Modified residuei756 – 7561PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9ESL4.
    PaxDbiQ9ESL4.
    PRIDEiQ9ESL4.

    PTM databases

    PhosphoSiteiQ9ESL4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9ESL4.
    BgeeiQ9ESL4.
    CleanExiMM_B230120H23RIK.
    GenevestigatoriQ9ESL4.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with PKN1 and ZNF33A By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ9ESL4. 1 interaction.
    MINTiMINT-4129310.
    STRINGi10090.ENSMUSP00000088334.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ESL4.
    SMRiQ9ESL4. Positions 9-325.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 277262Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini339 – 41072SAMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni287 – 30822Leucine-zipperAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117425.
    HOGENOMiHOG000231813.
    HOVERGENiHBG080445.
    InParanoidiQ9ESL4.
    KOiK04424.
    OMAiHRDSHET.
    OrthoDBiEOG7D85VN.
    PhylomeDBiQ9ESL4.
    TreeFamiTF106505.

    Family and domain databases

    Gene3Di1.10.150.50. 1 hit.
    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR021129. SAM_type1.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF07714. Pkinase_Tyr. 1 hit.
    PF00536. SAM_1. 1 hit.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00454. SAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50105. SAM_DOMAIN. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q9ESL4-1) [UniParc]FASTAAdd to Basket

    Also known as: Alpha

    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

    MSSLGASFVQ IKFDDLQFFE NCGGGSFGSV YRAKWISQDK EVAVKKLLKI    50
    EKEAEILSVL SHRNIIQFYG VILEPPNYGI VTEYASLGSL YDYINSNRSE 100
    EMDMEHIMTW ATDVAKGMHY LHMEAPVKVI HRDLKSRNVV IAADGVLKIC 150
    DFGASRFHNH TTHMSLVGTF PWMAPEVIQS LPVSETCDTY SYGVVLWEML 200
    TREVPFKGLE GLQVAWLVVE KNERLTIPSS CPRSFAELLH QCWEADAKKR 250
    PSFKQIISIL ESMSNDTNLP DQCNSFLHNK AEWRCEIEAT LERLKKLERD 300
    LSFKEQELKE RERRLKMWEQ KLTEQSNTPL LPSFEIGAWT EDDVYFWVQQ 350
    LVRKGESSVE MSGYASLFKE NNITGKRLLL LEEEDLKDMG IVSKGHIIHF 400
    KSAIEKLTHD YLNLFHFPPL IKDSGGEPEE NEEKIVNLEL VFGFHLKPGT 450
    GPQDCKWKMY MEMDGDEVAI TYIKDVTFNT SLPDAEILKM TKPPFVMEKW 500
    IVGIAEDQTV ECTVTYENDV RTPKLTKHVH SIQWDRTKPQ DEVKAVQLAI 550
    QTLFSSSEGN PGSRSDSSAD CQWLDTLRMR QIASHTSLQR SQSNPILGSP 600
    FFPYFANQDS YAAAVRRTQT PVKYQQITPS INPSRSSSPT QYGLSRNFSS 650
    LNLSSRDSGF SSLNDSSSER GRYSDRSRNK YYRGSVSLNS SPKGRYGGKS 700
    QHSTPSRERY SGKFYRLPQS ALNTHQSPDF KRSPNDHDRR VPRTIPGMPL 750
    HPETASKAGE EESRVSEGGW TKVEYRKKTH RQLSAKTSKE RTRGNYRGRR 800
    NF 802
    Length:802
    Mass (Da):91,720
    Last modified:March 1, 2001 - v1
    Checksum:iD431DF8F312A43CC
    GO
    Isoform 21 Publication (identifier: Q9ESL4-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         332-454: PSFEIGAWTE...HLKPGTGPQD → LPLSARMSEE...DAENDVDNSE
         455-802: Missing.

    Note: Contains a phosphoserine at position 434. Contains a phosphoserine at position 453.By similarity

    Show »
    Length:454
    Mass (Da):51,366
    Checksum:i35C2FC0D729D9395
    GO
    Isoform 3Curated (identifier: Q9ESL4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         285-289: CEIEA → WVAPA
         290-802: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:289
    Mass (Da):32,842
    Checksum:i440E5651076A04A4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti171 – 1711P → Q in BAC32371. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei285 – 2895CEIEA → WVAPA in isoform 3. 1 PublicationVSP_051747
    Alternative sequencei290 – 802513Missing in isoform 3. 1 PublicationVSP_051748Add
    BLAST
    Alternative sequencei332 – 454123PSFEI…TGPQD → LPLSARMSEESYFESKTEES NSAEMSCQITAASNGEGHGM NPGLQAMMLMGFGDVFSMNK AGAVLHSGMQINMQAKQNSS KTTCKRRGKKVNMALGFSDF DLSEGDDDDHDGDDAENDVD NSE in isoform 2. 1 PublicationVSP_051745Add
    BLAST
    Alternative sequencei455 – 802348Missing in isoform 2. 1 PublicationVSP_051746Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB049731 mRNA. Translation: BAB16442.1.
    AB049732 mRNA. Translation: BAB16443.1.
    AK045444 mRNA. Translation: BAC32371.1.
    AK132186 mRNA. Translation: BAE21021.1.
    BC023718 mRNA. Translation: AAH23718.1.
    CCDSiCCDS38143.1. [Q9ESL4-1]
    CCDS50605.1. [Q9ESL4-2]
    RefSeqiNP_001158263.1. NM_001164791.1. [Q9ESL4-2]
    NP_075544.1. NM_023057.5. [Q9ESL4-1]
    NP_835185.2. NM_178084.4. [Q9ESL4-3]
    XP_006500060.1. XM_006499997.1. [Q9ESL4-1]
    UniGeneiMm.304143.
    Mm.314618.

    Genome annotation databases

    EnsembliENSMUST00000090824; ENSMUSP00000088334; ENSMUSG00000004085. [Q9ESL4-1]
    ENSMUST00000135469; ENSMUSP00000118983; ENSMUSG00000004085. [Q9ESL4-2]
    GeneIDi65964.
    KEGGimmu:65964.
    UCSCiuc008kbs.2. mouse. [Q9ESL4-3]
    uc008kbv.2. mouse. [Q9ESL4-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB049731 mRNA. Translation: BAB16442.1 .
    AB049732 mRNA. Translation: BAB16443.1 .
    AK045444 mRNA. Translation: BAC32371.1 .
    AK132186 mRNA. Translation: BAE21021.1 .
    BC023718 mRNA. Translation: AAH23718.1 .
    CCDSi CCDS38143.1. [Q9ESL4-1 ]
    CCDS50605.1. [Q9ESL4-2 ]
    RefSeqi NP_001158263.1. NM_001164791.1. [Q9ESL4-2 ]
    NP_075544.1. NM_023057.5. [Q9ESL4-1 ]
    NP_835185.2. NM_178084.4. [Q9ESL4-3 ]
    XP_006500060.1. XM_006499997.1. [Q9ESL4-1 ]
    UniGenei Mm.304143.
    Mm.314618.

    3D structure databases

    ProteinModelPortali Q9ESL4.
    SMRi Q9ESL4. Positions 9-325.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9ESL4. 1 interaction.
    MINTi MINT-4129310.
    STRINGi 10090.ENSMUSP00000088334.

    PTM databases

    PhosphoSitei Q9ESL4.

    Proteomic databases

    MaxQBi Q9ESL4.
    PaxDbi Q9ESL4.
    PRIDEi Q9ESL4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000090824 ; ENSMUSP00000088334 ; ENSMUSG00000004085 . [Q9ESL4-1 ]
    ENSMUST00000135469 ; ENSMUSP00000118983 ; ENSMUSG00000004085 . [Q9ESL4-2 ]
    GeneIDi 65964.
    KEGGi mmu:65964.
    UCSCi uc008kbs.2. mouse. [Q9ESL4-3 ]
    uc008kbv.2. mouse. [Q9ESL4-1 ]

    Organism-specific databases

    CTDi 51776.
    MGIi MGI:2443258. Zak.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117425.
    HOGENOMi HOG000231813.
    HOVERGENi HBG080445.
    InParanoidi Q9ESL4.
    KOi K04424.
    OMAi HRDSHET.
    OrthoDBi EOG7D85VN.
    PhylomeDBi Q9ESL4.
    TreeFami TF106505.

    Miscellaneous databases

    NextBioi 320398.
    PROi Q9ESL4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9ESL4.
    Bgeei Q9ESL4.
    CleanExi MM_B230120H23RIK.
    Genevestigatori Q9ESL4.

    Family and domain databases

    Gene3Di 1.10.150.50. 1 hit.
    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR021129. SAM_type1.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF07714. Pkinase_Tyr. 1 hit.
    PF00536. SAM_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00454. SAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50105. SAM_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of a novel MAP kinase kinase kinase, MLTK."
      Gotoh I., Adachi M., Nishida E.
      J. Biol. Chem. 276:4276-4286(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, HOMODIMERIZATION, MUTAGENESIS OF LYS-45.
      Tissue: Heart1 Publication.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Strain: C57BL/6J.
      Tissue: Head.
    3. "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).
      Strain: FVB/NImported.
      Tissue: Mammary glandImported.
    4. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 225-233, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    5. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMLTK_MOUSE
    AccessioniPrimary (citable) accession number: Q9ESL4
    Secondary accession number(s): Q3V1X8, Q8BR73, Q9ESL3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3