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Q9GZQ8

- MLP3B_HUMAN

UniProt

Q9GZQ8 - MLP3B_HUMAN

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Protein
Microtubule-associated proteins 1A/1B light chain 3B
Gene
MAP1LC3B, MAP1ALC3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 ATG4B By similarity

GO - Molecular functioni

  1. GABA receptor binding Source: RefGenome
  2. microtubule binding Source: RefGenome
  3. phosphatidylethanolamine binding Source: RefGenome
  4. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. CVT pathway Source: RefGenome
  2. autophagic vacuole assembly Source: RefGenome
  3. cellular response to nitrogen starvation Source: RefGenome
  4. late nucleophagy Source: RefGenome
  5. mitochondrion degradation Source: RefGenome
  6. piecemeal microautophagy of nucleus Source: RefGenome
  7. protein targeting to vacuole involved in autophagy Source: RefGenome
Complete GO annotation...

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
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.3 Publications

GO - Cellular componenti

  1. autophagic vacuole Source: UniProtKB
  2. autophagic vacuole membrane Source: RefGenome
  3. axoneme Source: UniProtKB
  4. cytoplasmic vesicle Source: UniProtKB-KW
  5. cytosol Source: RefGenome
  6. endomembrane system Source: UniProtKB-SubCell
  7. intracellular Source: LIFEdb
  8. microtubule Source: UniProtKB-KW
  9. organelle membrane Source: UniProtKB
  10. pre-autophagosomal structure Source: RefGenome
Complete GO annotation...

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 – 11Removed By similarity
Chaini2 – 120119Microtubule-associated proteins 1A/1B light chain 3B
PRO_0000017198Add
BLAST
Propeptidei121 – 1255Removed in mature form
PRO_0000017199

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphothreonine; by PKA By similarity
Lipidationi120 – 1201Phosphatidylethanolamine amidated glycine Inferred

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 (1 Publication).4 Publications
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.

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 TECPR2.9 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

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.

Miscellaneous databases

EvolutionaryTraceiQ9GZQ8.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATG8 family.

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

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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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611S → G in AAH67797. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 139 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

1 Publication has shown that the protein is cleaved at Lys-122 but 1 Publication has shown that the cleavage site is at Gly-120 as in other mammalian orthologs.

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

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