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Q9GZQ8

- MLP3B_HUMAN

UniProt

Q9GZQ8 - MLP3B_HUMAN

Protein

Microtubule-associated proteins 1A/1B light chain 3B

Gene

MAP1LC3B

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

    Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei120 – 1212Cleavage; by ATG4BBy similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. autophagy Source: UniProtKB-KW

    Keywords - Biological processi

    Autophagy, Ubl conjugation pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Microtubule-associated proteins 1A/1B light chain 3B
    Alternative name(s):
    Autophagy-related protein LC3 B
    Autophagy-related ubiquitin-like modifier LC3 B
    MAP1 light chain 3-like protein 2
    MAP1A/MAP1B light chain 3 B
    Short name:
    MAP1A/MAP1B LC3 B
    Microtubule-associated protein 1 light chain 3 beta
    Gene namesi
    Name:MAP1LC3B
    Synonyms:MAP1ALC3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:13352. MAP1LC3B.

    Subcellular locationi

    Cytoplasmcytoskeleton. Endomembrane system; Lipid-anchor. Cytoplasmic vesicleautophagosome membrane; Lipid-anchor
    Note: LC3-II binds to the autophagic membranes. Localizes also to discrete punctae along the ciliary axoneme By similarity.By similarity

    GO - Cellular componenti

    1. autophagic vacuole Source: UniProtKB
    2. autophagic vacuole membrane Source: UniProtKB-SubCell
    3. axoneme Source: UniProtKB
    4. cytoplasmic vesicle Source: UniProtKB-KW
    5. endomembrane system Source: UniProtKB-SubCell
    6. intracellular Source: LIFEdb
    7. microtubule Source: UniProtKB-KW
    8. organelle membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Microtubule

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi52 – 532FL → AA: No effect on interaction with TECPR2.
    Mutagenesisi68 – 681R → A: Impairs cleavage by ATG4B. 1 Publication
    Mutagenesisi70 – 701R → A: Abolishes interaction with TECPR2. 1 Publication
    Mutagenesisi120 – 1201G → A: No processing of precursor. 1 Publication
    Mutagenesisi122 – 1221K → A: No effect on processing of precursor. 1 Publication

    Organism-specific databases

    PharmGKBiPA134923100.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 120119Microtubule-associated proteins 1A/1B light chain 3BPRO_0000017198Add
    BLAST
    Propeptidei121 – 1255Removed in mature formPRO_0000017199

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei12 – 121Phosphothreonine; by PKABy similarity
    Lipidationi120 – 1201Phosphatidylethanolamine amidated glycine1 Publication

    Post-translational modificationi

    The precursor molecule is cleaved by ATG4B to form the cytosolic form, LC3-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, LC3-II (PubMed:15187094).1 Publication
    The Legionella effector RavZ is a deconjugating enzyme that produces an ATG8 product that would be resistant to reconjugation by the host machinery due to the cleavage of the reactive C-terminal glycine.
    Phosphorylation at Thr-12 by PKA inhibits conjugation to phosphatidylethanolamine (PE) By similarity. Interaction with MAPK15 reduces the inhibitory phosphorylation and increases autophagy activity.By similarity2 Publications

    Keywords - PTMi

    Lipoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ9GZQ8.
    PaxDbiQ9GZQ8.
    PRIDEiQ9GZQ8.

    PTM databases

    PhosphoSiteiQ9GZQ8.

    Miscellaneous databases

    PMAP-CutDBQ9GZQ8.

    Expressioni

    Tissue specificityi

    Most abundant in heart, brain, skeletal muscle and testis. Little expression observed in liver.1 Publication

    Gene expression databases

    ArrayExpressiQ9GZQ8.
    BgeeiQ9GZQ8.
    CleanExiHS_MAP1LC3B.
    GenevestigatoriQ9GZQ8.

    Organism-specific databases

    HPAiCAB037216.

    Interactioni

    Subunit structurei

    3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins By similarity. Interacts at microtubules with CABP1 (via EF-hands 1 and 2) but not with calmodulin. Interacts with FYCO1 (via C-terminus). Interacts with TP53INP1 and TP53INP2. Interacts with TBC1D25. Directly interacts with SQSTM1; this interaction leads to MAP1LC3B recruitment to inclusion bodies containing polyubiquitinated protein aggregates and to inclusion body degradation by autophagy. Interacts with ATG4B, MAPK15 and BNIP3. Interacts with MAPB1, KEAP1, PCM1, OFD1, CEP131, and TECPR2.By similarity10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATG13O751432EBI-373144,EBI-2798775
    ATG16L1Q676U52EBI-373144,EBI-535909
    ATG2AQ2TAZ02EBI-373144,EBI-2514077
    ATG3Q9NT627EBI-373144,EBI-988094
    ATG4BQ9Y4P111EBI-373144,EBI-712014
    ATG5Q9H1Y02EBI-373144,EBI-1047414
    ATG7O953527EBI-373144,EBI-987834
    Bnip3lQ9Z2F75EBI-373144,EBI-1774669From a different organism.
    CLINT1Q146772EBI-373144,EBI-1171113
    CTNNB1P352225EBI-373144,EBI-491549
    FYCO1Q9BQS87EBI-373144,EBI-2869338
    GBASO753234EBI-373144,EBI-307133
    HADHAP409394EBI-373144,EBI-356720
    IPO5O004102EBI-373144,EBI-356424
    KBTBD6Q86V972EBI-373144,EBI-2514778
    KBTBD7Q8WVZ94EBI-373144,EBI-473695
    LUC7L2Q9Y3833EBI-373144,EBI-352851
    NBR1Q145968EBI-373144,EBI-742698
    Nbr1P974322EBI-373144,EBI-642554From a different organism.
    NEK9Q8TD192EBI-373144,EBI-1044009
    PINK1Q9BXM73EBI-373144,EBI-2846068
    RASSF1Q9NS232EBI-373144,EBI-367363
    RASSF5Q8WWW05EBI-373144,EBI-367390
    SAFBQ154243EBI-373144,EBI-348298
    SAFB2Q141513EBI-373144,EBI-352869
    SQSTM1Q1350115EBI-373144,EBI-307104
    Sqstm1Q643376EBI-373144,EBI-645025From a different organism.
    STBD1O952102EBI-373144,EBI-2947137
    STK3Q131885EBI-373144,EBI-992580
    STK4Q130437EBI-373144,EBI-367376
    TBC1D15Q8TC072EBI-373144,EBI-1048247
    TBC1D2BQ9UPU73EBI-373144,EBI-2947180
    UBA5Q9GZZ92EBI-373144,EBI-747805
    ULK1O753852EBI-373144,EBI-908831

    Protein-protein interaction databases

    BioGridi123565. 78 interactions.
    DIPiDIP-29760N.
    IntActiQ9GZQ8. 358 interactions.
    MINTiMINT-1369587.
    STRINGi9606.ENSP00000268607.

    Structurei

    Secondary structure

    1
    125
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 104
    Helixi13 – 2614
    Beta strandi30 – 378
    Beta strandi42 – 443
    Beta strandi51 – 555
    Helixi60 – 7112
    Turni75 – 773
    Beta strandi79 – 835
    Turni84 – 863
    Turni89 – 913
    Helixi95 – 1028
    Beta strandi109 – 1157
    Helixi116 – 1216

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1V49NMR-A1-120[»]
    2LUENMR-A5-119[»]
    2ZJDX-ray1.56A/C1-125[»]
    3VTUX-ray1.60A2-119[»]
    3VTVX-ray1.70A2-119[»]
    3VTWX-ray2.52A/B/C2-119[»]
    3WAOX-ray2.60A/B/C/D2-119[»]
    ProteinModelPortaliQ9GZQ8.
    SMRiQ9GZQ8. Positions 1-122.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9GZQ8.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATG8 family.Curated

    Phylogenomic databases

    eggNOGiNOG283348.
    HOGENOMiHOG000232034.
    HOVERGENiHBG051706.
    InParanoidiQ9GZQ8.
    KOiK10435.
    OMAiIRDQHPT.
    OrthoDBiEOG7XH6RV.
    PhylomeDBiQ9GZQ8.
    TreeFamiTF312964.

    Family and domain databases

    InterProiIPR004241. Atg8_like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PANTHERiPTHR10969. PTHR10969. 1 hit.
    PfamiPF02991. Atg8. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9GZQ8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPSEKTFKQR RTFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT    50
    KFLVPDHVNM SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE 100
    SEKDEDGFLY MVYASQETFG MKLSV 125
    Length:125
    Mass (Da):14,688
    Last modified:January 23, 2007 - v3
    Checksum:iBB141DEC7653E83F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 611S → G in AAH67797. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF303888 mRNA. Translation: AAG23182.1.
    AF183417 mRNA. Translation: AAG09686.1.
    AF087871 mRNA. Translation: AAM10499.1.
    AK025556 mRNA. Translation: BAB15169.1.
    BC018634 mRNA. Translation: AAH18634.1.
    BC041874 mRNA. Translation: AAH41874.1.
    BC067797 mRNA. Translation: AAH67797.1.
    CCDSiCCDS10960.1.
    RefSeqiNP_073729.1. NM_022818.4.
    XP_005256241.1. XM_005256184.1.
    UniGeneiHs.356061.

    Genome annotation databases

    EnsembliENST00000268607; ENSP00000268607; ENSG00000140941.
    GeneIDi81631.
    KEGGihsa:81631.
    UCSCiuc002fjx.3. human.

    Polymorphism databases

    DMDMi17433141.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF303888 mRNA. Translation: AAG23182.1 .
    AF183417 mRNA. Translation: AAG09686.1 .
    AF087871 mRNA. Translation: AAM10499.1 .
    AK025556 mRNA. Translation: BAB15169.1 .
    BC018634 mRNA. Translation: AAH18634.1 .
    BC041874 mRNA. Translation: AAH41874.1 .
    BC067797 mRNA. Translation: AAH67797.1 .
    CCDSi CCDS10960.1.
    RefSeqi NP_073729.1. NM_022818.4.
    XP_005256241.1. XM_005256184.1.
    UniGenei Hs.356061.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1V49 NMR - A 1-120 [» ]
    2LUE NMR - A 5-119 [» ]
    2ZJD X-ray 1.56 A/C 1-125 [» ]
    3VTU X-ray 1.60 A 2-119 [» ]
    3VTV X-ray 1.70 A 2-119 [» ]
    3VTW X-ray 2.52 A/B/C 2-119 [» ]
    3WAO X-ray 2.60 A/B/C/D 2-119 [» ]
    ProteinModelPortali Q9GZQ8.
    SMRi Q9GZQ8. Positions 1-122.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123565. 78 interactions.
    DIPi DIP-29760N.
    IntActi Q9GZQ8. 358 interactions.
    MINTi MINT-1369587.
    STRINGi 9606.ENSP00000268607.

    PTM databases

    PhosphoSitei Q9GZQ8.

    Polymorphism databases

    DMDMi 17433141.

    Proteomic databases

    MaxQBi Q9GZQ8.
    PaxDbi Q9GZQ8.
    PRIDEi Q9GZQ8.

    Protocols and materials databases

    DNASUi 81631.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000268607 ; ENSP00000268607 ; ENSG00000140941 .
    GeneIDi 81631.
    KEGGi hsa:81631.
    UCSCi uc002fjx.3. human.

    Organism-specific databases

    CTDi 81631.
    GeneCardsi GC16P087425.
    HGNCi HGNC:13352. MAP1LC3B.
    HPAi CAB037216.
    MIMi 609604. gene.
    neXtProti NX_Q9GZQ8.
    PharmGKBi PA134923100.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG283348.
    HOGENOMi HOG000232034.
    HOVERGENi HBG051706.
    InParanoidi Q9GZQ8.
    KOi K10435.
    OMAi IRDQHPT.
    OrthoDBi EOG7XH6RV.
    PhylomeDBi Q9GZQ8.
    TreeFami TF312964.

    Miscellaneous databases

    ChiTaRSi MAP1LC3B. human.
    EvolutionaryTracei Q9GZQ8.
    GeneWikii MAP1LC3B.
    GenomeRNAii 81631.
    NextBioi 72018.
    PMAP-CutDB Q9GZQ8.
    PROi Q9GZQ8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9GZQ8.
    Bgeei Q9GZQ8.
    CleanExi HS_MAP1LC3B.
    Genevestigatori Q9GZQ8.

    Family and domain databases

    InterProi IPR004241. Atg8_like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    PANTHERi PTHR10969. PTHR10969. 1 hit.
    Pfami PF02991. Atg8. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung carcinoma.
    2. "The gene expression profiling of sporadic pheochromocytoma and novel full-length cDNAs cloning."
      Yang Y.-S., Song H.-D., Peng Y.-D., Huang Q.-H., Li R.-Y., Zhu Z.-D., Hu R.-M., Han Z.-G., Chen J.-L.
      Endocr. Relat. Cancer 10:621-627(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Pheochromocytoma.
    3. "Post-translational modifications of three members of the human MAP1LC3 family and detection of a novel type of modification for MAP1LC3B."
      He H., Dang Y., Dai F., Guo Z., Wu J., She X., Pei Y., Chen Y., Ling W., Wu C., Zhao S., Liu J.O., Yu L.
      J. Biol. Chem. 278:29278-29287(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, CLEAVAGE, TISSUE SPECIFICITY.
    4. "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].
      Tissue: Hepatoma.
    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].
      Tissue: Brain, Pancreas and Testis.
    6. "HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three human Atg8 homologues and delipidates microtubule-associated protein light chain 3- and GABAA receptor-associated protein-phospholipid conjugates."
      Tanida I., Sou Y.-S., Ezaki J., Minematsu-Ikeguchi N., Ueno T., Kominami E.
      J. Biol. Chem. 279:36268-36276(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: LIPIDATION AT GLY-120, CLEAVAGE BY ATG4B.
    7. "Human light chain 3/MAP1LC3B is cleaved at its carboxyl-terminal Met121 to expose Gly120 for lipidation and targeting to autophagosomal membranes."
      Tanida I., Ueno T., Kominami E.
      J. Biol. Chem. 279:47704-47710(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE, MUTAGENESIS OF GLY-120 AND LYS-122.
    8. Cited for: REVIEW.
    9. "Caldendrin but not calmodulin binds to light chain 3 of MAP1A/B: an association with the microtubule cytoskeleton highlighting exclusive binding partners for neuronal Ca(2+)-sensor proteins."
      Seidenbecher C.I., Landwehr M., Smalla K.H., Kreutz M., Dieterich D.C., Zuschratter W., Reissner C., Hammarback J.A., Bockers T.M., Gundelfinger E.D., Kreutz M.R.
      J. Mol. Biol. 336:957-970(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CABP1.
    10. "p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy."
      Pankiv S., Clausen T.H., Lamark T., Brech A., Bruun J.A., Outzen H., Overvatn A., Bjorkoy G., Johansen T.
      J. Biol. Chem. 282:24131-24145(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION.
    11. "LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis."
      Weidberg H., Shvets E., Shpilka T., Shimron F., Shinder V., Elazar Z.
      EMBO J. 29:1792-1802(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport."
      Pankiv S., Alemu E.A., Brech A., Bruun J.A., Lamark T., Overvatn A., Bjorkoy G., Johansen T.
      J. Cell Biol. 188:253-269(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FYCO1.
    13. "Network organization of the human autophagy system."
      Behrends C., Sowa M.E., Gygi S.P., Harper J.W.
      Nature 466:68-76(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TECPR2, MUTAGENESIS OF 52-PHE-LYS-53 AND ARG-70.
    14. "OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation."
      Itoh T., Kanno E., Uemura T., Waguri S., Fukuda M.
      J. Cell Biol. 192:839-853(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TBC1D25.
    15. Cited for: INTERACTION WITH MAPK15, PHOSPHORYLATION.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    17. "DOR/Tp53inp2 and Tp53inp1 constitute a metazoan gene family encoding dual regulators of autophagy and transcription."
      Sancho A., Duran J., Garcia-Espana A., Mauvezin C., Alemu E.A., Lamark T., Macias M.J., Desalle R., Royo M., Sala D., Chicote J.U., Palacin M., Johansen T., Zorzano A.
      PLoS ONE 7:E34034-E34034(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TP53INP1 AND TP53INP2.
    18. "The Legionella effector RavZ inhibits host autophagy through irreversible Atg8 deconjugation."
      Choy A., Dancourt J., Mugo B., O'Connor T.J., Isberg R.R., Melia T.J., Roy C.R.
      Science 338:1072-1076(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DECONJUGATION BY LEGIONELLA RAVZ.
    19. "Arginine68 is an essential residue for the C-terminal cleavage of human Atg8 family proteins."
      Liu C., Ma H., Wu J., Huang Q., Liu J.O., Yu L.
      BMC Cell Biol. 14:27-27(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-68, CLEAVAGE BY ATG4B.
    20. "Modulation of serines 17 and 24 in the LC3-interacting region of Bnip3 determines pro-survival mitophagy versus apoptosis."
      Zhu Y., Massen S., Terenzio M., Lang V., Chen-Lindner S., Eils R., Novak I., Dikic I., Hamacher-Brady A., Brady N.R.
      J. Biol. Chem. 288:1099-1113(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BNIP3, FUNCTION.
    21. "Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites."
      Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B., Zhong Q.
      Nature 502:254-257(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAPB1; FYCO1; SQSTM1; KEAP1; PCM1; OFD1 AND CEP131, FUNCTION.
    22. "Solution structure of microtubule-associated protein light chain 3 and identification of its functional subdomains."
      Kouno T., Mizuguchi M., Tanida I., Ueno T., Kanematsu T., Mori Y., Shinoda H., Hirata M., Kominami E., Kawano K.
      J. Biol. Chem. 280:24610-24617(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-120.
    23. Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) IN COMPLEX WITH AN LC3 RECOGNITION SEQUENCE (LRS).

    Entry informationi

    Entry nameiMLP3B_HUMAN
    AccessioniPrimary (citable) accession number: Q9GZQ8
    Secondary accession number(s): Q6NW02
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 5, 2001
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 140 of the entry and version 3 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

    Caution

    PubMed:12740394 has shown that the protein is cleaved at Lys-122 but PubMed:15355958 has shown that the cleavage site is at Gly-120 as in other mammalian orthologs.Curated

    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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3