{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q80X71","secondaryAccessions":["Q9D737"],"uniProtkbId":"T106B_MOUSE","entryAudit":{"firstPublicDate":"2006-06-27","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2003-06-01","entryVersion":141,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Mus musculus","commonName":"Mouse","taxonId":10090,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Transmembrane protein 106B"}}},"genes":[{"geneName":{"value":"Tmem106b"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6AYA5"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25066864"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28728022"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32160553"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"32160553"}],"value":"In neurons, involved in the transport of late endosomes/lysosomes (PubMed:25066864, PubMed:32160553). May be involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking (PubMed:25066864). May act as a molecular brake for retrograde transport of late endosomes/lysosomes, possibly via its interaction with MAP6 (By similarity). In motoneurons, may mediate the axonal transport of lysosomes and axonal sorting at the initial segment (PubMed:32160553). It remains unclear whether TMEM106B affects the transport of moving lysosomes in the anterograde or retrograde direction in neurites and whether it is particularly important in the sorting of lysosomes in axons or in dendrites (Probable). In neurons, may also play a role in the regulation of lysosomal size and responsiveness to stress (PubMed:25066864). Required for proper lysosomal acidification (PubMed:28728022)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9NUM4"}],"value":"Can form homomers (By similarity). Interacts (via N-terminus) with MAP6 (via C-terminus) (By similarity). Interacts (via C-terminus) with the vacuolar-type ATPase subunit ATP6AP1 (By similarity). Interacts (via N-terminus) with AP2M1 and CLTC (By similarity). Interacts with TMEM106C (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9NUM4"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23136129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25066864"}],"value":"Colocalizes with LAMP1. A small fraction resides on the cell surface (By similarity)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23136129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25066864"}],"value":"Late endosome membrane","id":"SL-0151"},"topology":{"value":"Single-pass type II membrane protein","id":"SL-9906"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23136129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25066864"}],"value":"Lysosome membrane","id":"SL-0157"},"topology":{"value":"Single-pass type II membrane protein","id":"SL-9906"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9NUM4"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Single-pass type II membrane protein","id":"SL-9906"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25066864"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28728022"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29855382"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32160553"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32761777"}],"value":"Expressed in the brain, in neurons (at protein level) (PubMed:25066864, PubMed:28728022, PubMed:29855382, PubMed:32160553, PubMed:32761777). Expressed in the spinal cord (at protein level) (PubMed:32160553)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28728022"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29855382"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32160553"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32761777"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32852886"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32929860"}],"value":"Knockout mice are born at the expected Mendelian ratio and young animals appear phenotypically normal (PubMed:28728022, PubMed:29855382, PubMed:32160553, PubMed:32852886). At 10 weeks of age, knockout mice develop proximal axonal swellings caused by drastically enlarged LAMP1-positive vacuoles (lysosomes/endosomes), increased retrograde axonal transport of lysosomes, and accumulation of lipofuscin and autophagosomes. Giant vacuoles specifically accumulate at the distal end and within the axon initial segment, but not in peripheral nerves or at axon terminals, resulting in an impaired facial-nerve-dependent motor performance (PubMed:32160553, PubMed:32852886). Using a different experimental approach to create the knockout, a more subtle, exclusively lysosomal phenotype is observed. At 2 months of age, numerous lysosomal proteins, including cathepsin B/CTSB, cathepsin L/CTSL, dipeptidyl peptidase 2/DPP7, LAMP1 and vacuolar-type ATPase subunits, are down-regulated and lysosomal acidification is impaired (PubMed:28728022). It has been suggested that these phenotypic differences might be due to incomplete knockout in animals with milder phenotypes (PubMed:32160553). Mice deficient in both PGRN and TMEM106B are born at normal Mendelian frequency and do not show any obvious growth defects or body weight changes. At around 3.5 months of age, the animals develop severe ataxia, hindlimb weakness, reduced motor activity, altered clasping behavior and eventually premature death. Neuronal loss and severe microglia and astrocyte activation are observed in the spinal cord, retina, and brain (PubMed:32761777, PubMed:32852886, PubMed:32929860). Myelin degeneration occurs in the spinal cord (PubMed:32761777). Drastic autophagy and lysosomal abnormalities, as well as other pathological changes related to frontotemporal lobar degeneration (FTLD)/amyotrophic lateral sclerosis are observed (PubMed:32761777, PubMed:32852886, PubMed:32929860). Most studies consistently show that loss of TMEM106B exacerbates lysosome abnormalities found in GRN-single knockout animals, likely contributing to neuronal dysfunction and neuronal death (PubMed:32761777, PubMed:32852886, PubMed:32929860). However, one study reports that the expression levels of most lysosomal proteins are normalized in double knockout mice and comparable to those of wild-type animals and some behavioral phenotypes observed in GRN-single knockout mice, such as locomotor hyperactivity and disinhibition, are rescued in double knockout (PubMed:28728022). TMEM106B knockout does not rescue FTLD-like phenotypes in a mouse model mimicking the toxic gain-of-functions associated with overexpression of hexanucleotide repeat (GGGGCC) expansions in C9ORF72 (PubMed:29855382)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the TMEM106 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9NUM4"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"Transmembrane protein 106B","featureId":"PRO_0000242651"},{"type":"Topological domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9NUM4"}]},{"type":"Transmembrane","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Topological domain","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9NUM4"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Modified residue","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9NUM4"}]},{"type":"Lipidation","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"N-myristoyl glycine","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9NUM4"}]},{"type":"Glycosylation","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Disulfide bond","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9NUM4"}]},{"type":"Sequence conflict","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"in Ref. 1; BAB26411","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["Y"]}}],"keywords":[{"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0967","category":"Cellular component","name":"Endosome"},{"id":"KW-0325","category":"PTM","name":"Glycoprotein"},{"id":"KW-0449","category":"PTM","name":"Lipoprotein"},{"id":"KW-0458","category":"Cellular component","name":"Lysosome"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0519","category":"PTM","name":"Myristate"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0735","category":"Domain","name":"Signal-anchor"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"16141072","citationType":"journal article","authors":["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."],"citationCrossReferences":[{"database":"PubMed","id":"16141072"},{"database":"DOI","id":"10.1126/science.1112014"}],"title":"The transcriptional landscape of the mammalian genome.","publicationDate":"2005","journal":"Science","firstPage":"1559","lastPage":"1563","volume":"309"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]"],"referenceComments":[{"value":"C57BL/6J","type":"STRAIN"},{"value":"Tongue","type":"TISSUE"}]},{"referenceNumber":2,"citation":{"id":"15489334","citationType":"journal article","authoringGroup":["The MGC Project Team"],"citationCrossReferences":[{"database":"PubMed","id":"15489334"},{"database":"DOI","id":"10.1101/gr.2596504"}],"title":"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).","publicationDate":"2004","journal":"Genome Res.","firstPage":"2121","lastPage":"2127","volume":"14"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]"],"referenceComments":[{"value":"Olfactory epithelium","type":"TISSUE"}]},{"referenceNumber":3,"citation":{"id":"19144319","citationType":"journal article","authors":["Trost M.","English L.","Lemieux S.","Courcelles M.","Desjardins M.","Thibault P."],"citationCrossReferences":[{"database":"PubMed","id":"19144319"},{"database":"DOI","id":"10.1016/j.immuni.2008.11.006"}],"title":"The phagosomal proteome in interferon-gamma-activated macrophages.","publicationDate":"2009","journal":"Immunity","firstPage":"143","lastPage":"154","volume":"30"},"referencePositions":["IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]"]},{"referenceNumber":4,"citation":{"id":"23136129","citationType":"journal article","authors":["Brady O.A.","Zheng Y.","Murphy K.","Huang M.","Hu F."],"citationCrossReferences":[{"database":"PubMed","id":"23136129"},{"database":"DOI","id":"10.1093/hmg/dds475"}],"title":"The frontotemporal lobar degeneration risk factor, TMEM106B, regulates lysosomal morphology and function.","publicationDate":"2013","journal":"Hum. Mol. Genet.","firstPage":"685","lastPage":"695","volume":"22"},"referencePositions":["SUBCELLULAR LOCATION"]},{"referenceNumber":5,"citation":{"id":"25066864","citationType":"journal article","authors":["Stagi M.","Klein Z.A.","Gould T.J.","Bewersdorf J.","Strittmatter S.M."],"citationCrossReferences":[{"database":"PubMed","id":"25066864"},{"database":"DOI","id":"10.1016/j.mcn.2014.07.006"}],"title":"Lysosome size, motility and stress response regulated by fronto-temporal dementia modifier TMEM106B.","publicationDate":"2014","journal":"Mol. Cell. Neurosci.","firstPage":"226","lastPage":"240","volume":"61"},"referencePositions":["FUNCTION","SUBCELLULAR LOCATION","TISSUE SPECIFICITY"]},{"referenceNumber":6,"citation":{"id":"28728022","citationType":"journal article","authors":["Klein Z.A.","Takahashi H.","Ma M.","Stagi M.","Zhou M.","Lam T.T.","Strittmatter S.M."],"citationCrossReferences":[{"database":"PubMed","id":"28728022"},{"database":"DOI","id":"10.1016/j.neuron.2017.06.026"}],"title":"Loss of TMEM106B ameliorates lysosomal and frontotemporal dementia-related phenotypes in progranulin-deficient mice.","publicationDate":"2017","journal":"Neuron","firstPage":"281","lastPage":"296","volume":"95"},"referencePositions":["DISRUPTION PHENOTYPE","FUNCTION","TISSUE SPECIFICITY"]},{"referenceNumber":7,"citation":{"id":"29855382","citationType":"journal article","authors":["Nicholson A.M.","Zhou X.","Perkerson R.B.","Parsons T.M.","Chew J.","Brooks M.","DeJesus-Hernandez M.","Finch N.A.","Matchett B.J.","Kurti A.","Jansen-West K.R.","Perkerson E.","Daughrity L.","Castanedes-Casey M.","Rousseau L.","Phillips V.","Hu F.","Gendron T.F.","Murray M.E.","Dickson D.W.","Fryer J.D.","Petrucelli L.","Rademakers R."],"citationCrossReferences":[{"database":"PubMed","id":"29855382"},{"database":"DOI","id":"10.1186/s40478-018-0545-x"}],"title":"Loss of Tmem106b is unable to ameliorate frontotemporal dementia-like phenotypes in an AAV mouse model of C9ORF72-repeat induced toxicity.","publicationDate":"2018","journal":"Acta Neuropathol. Commun.","firstPage":"42","lastPage":"42","volume":"6"},"referencePositions":["DISRUPTION PHENOTYPE","TISSUE SPECIFICITY"]},{"referenceNumber":8,"citation":{"id":"32160553","citationType":"journal article","authors":["Lueningschroer P.","Werner G.","Stroobants S.","Kakuta S.","Dombert B.","Sinske D.","Wanner R.","Luellmann-Rauch R.","Wefers B.","Wurst W.","D'Hooge R.","Uchiyama Y.","Sendtner M.","Haass C.","Saftig P.","Knoell B.","Capell A.","Damme M."],"citationCrossReferences":[{"database":"PubMed","id":"32160553"},{"database":"DOI","id":"10.1016/j.celrep.2020.02.060"}],"title":"The FTLD risk factor TMEM106B regulates the transport of lysosomes at the axon initial segment of motoneurons.","publicationDate":"2020","journal":"Cell Rep.","firstPage":"3506","lastPage":"3519","volume":"30"},"referencePositions":["DISRUPTION PHENOTYPE","TISSUE SPECIFICITY"]},{"referenceNumber":9,"citation":{"id":"32761777","citationType":"journal article","authors":["Zhou X.","Brooks M.","Jiang P.","Koga S.","Zuberi A.R.","Baker M.C.","Parsons T.M.","Castanedes-Casey M.","Phillips V.","Librero A.L.","Kurti A.","Fryer J.D.","Bu G.","Lutz C.","Dickson D.W.","Rademakers R."],"citationCrossReferences":[{"database":"PubMed","id":"32761777"},{"database":"DOI","id":"10.15252/embr.202050197"}],"title":"Loss of Tmem106b exacerbates FTLD pathologies and causes motor deficits in progranulin-deficient mice.","publicationDate":"2020","journal":"EMBO Rep.","firstPage":"e50197","lastPage":"e50197","volume":"21"},"referencePositions":["TISSUE SPECIFICITY","DISRUPTION PHENOTYPE"]},{"referenceNumber":10,"citation":{"id":"32852886","citationType":"journal article","authors":["Feng T.","Mai S.","Roscoe J.M.","Sheng R.R.","Ullah M.","Zhang J.","Katz I.I.","Yu H.","Xiong W.","Hu F."],"citationCrossReferences":[{"database":"PubMed","id":"32852886"},{"database":"DOI","id":"10.15252/embr.202050219"}],"title":"Loss of TMEM106B and PGRN leads to severe lysosomal abnormalities and neurodegeneration in mice.","publicationDate":"2020","journal":"EMBO Rep.","firstPage":"e50219","lastPage":"e50219","volume":"21"},"referencePositions":["DISRUPTION PHENOTYPE"]},{"referenceNumber":11,"citation":{"id":"32929860","citationType":"journal article","authors":["Werner G.","Damme M.","Schludi M.","Gnoerich J.","Wind K.","Fellerer K.","Wefers B.","Wurst W.","Edbauer D.","Brendel M.","Haass C.","Capell A."],"citationCrossReferences":[{"database":"PubMed","id":"32929860"},{"database":"DOI","id":"10.15252/embr.202050241"}],"title":"Loss of TMEM106B potentiates lysosomal and FTLD-like pathology in progranulin-deficient mice.","publicationDate":"2020","journal":"EMBO Rep.","firstPage":"e50241","lastPage":"e50241","volume":"21"},"referencePositions":["DISRUPTION PHENOTYPE"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AK009646","properties":[{"key":"ProteinId","value":"BAB26411.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"EMBL","id":"BC050246","properties":[{"key":"ProteinId","value":"AAH50246.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"CCDS","id":"CCDS19914.1","properties":[{"key":"Description","value":"-"}]},{"database":"RefSeq","id":"NP_082268.2","properties":[{"key":"NucleotideSequenceId","value":"NM_027992.3"}]},{"database":"RefSeq","id":"XP_006505232.1","properties":[{"key":"NucleotideSequenceId","value":"XM_006505169.5"}]},{"database":"AlphaFoldDB","id":"Q80X71","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID","id":"215015","properties":[{"key":"Interactions","value":"2"}]},{"database":"FunCoup","id":"Q80X71","properties":[{"key":"Number of interactors","value":"1244"}]},{"database":"STRING","id":"10090.ENSMUSP00000031556","properties":[{"key":"Description","value":"-"}]},{"database":"GlyConnect","id":"Q80X71","properties":[{"key":"glycosylation","value":"6 N-Linked glycans (1 site)"}]},{"database":"GlyCosmos","id":"Q80X71","properties":[{"key":"glycosylation","value":"5 sites, 6 glycans"}]},{"database":"GlyGen","id":"Q80X71","properties":[{"key":"glycosylation","value":"6 sites, 9 N-linked glycans (3 sites), 1 O-linked glycan (1 site)"}]},{"database":"iPTMnet","id":"Q80X71","properties":[{"key":"Description","value":"-"}]},{"database":"PhosphoSitePlus","id":"Q80X71","properties":[{"key":"Description","value":"-"}]},{"database":"SwissPalm","id":"Q80X71","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"10090-ENSMUSP00000031556","properties":[{"key":"Description","value":"-"}]},{"database":"PeptideAtlas","id":"Q80X71","properties":[{"key":"Description","value":"-"}]},{"database":"ProteomicsDB","id":"253454","properties":[{"key":"Description","value":"-"}]},{"database":"Pumba","id":"Q80X71","properties":[{"key":"Description","value":"-"}]},{"database":"Antibodypedia","id":"43908","properties":[{"key":"antibodies","value":"128 antibodies from 31 providers"}]},{"database":"DNASU","id":"71900","properties":[{"key":"Description","value":"-"}]},{"database":"Ensembl","id":"ENSMUST00000031556.14","properties":[{"key":"ProteinId","value":"ENSMUSP00000031556.8"},{"key":"GeneId","value":"ENSMUSG00000029571.15"}]},{"database":"GeneID","id":"71900","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"mmu:71900","properties":[{"key":"Description","value":"-"}]},{"database":"UCSC","id":"uc009ayk.2","properties":[{"key":"OrganismName","value":"mouse"}]},{"database":"AGR","id":"MGI:1919150","properties":[{"key":"Description","value":"-"}]},{"database":"CTD","id":"54664","properties":[{"key":"Description","value":"-"}]},{"database":"MGI","id":"MGI:1919150","properties":[{"key":"GeneName","value":"Tmem106b"}]},{"database":"VEuPathDB","id":"HostDB:ENSMUSG00000029571","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"ENOG502QQRZ","properties":[{"key":"ToxonomicScope","value":"Eukaryota"}]},{"database":"GeneTree","id":"ENSGT00940000158360","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"Q80X71","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"FGHSEQT","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"OrthoDB","id":"508875at2759","properties":[{"key":"Description","value":"-"}]},{"database":"PhylomeDB","id":"Q80X71","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID-ORCS","id":"71900","properties":[{"key":"hits","value":"1 hit in 77 CRISPR screens"}]},{"database":"PRO","id":"PR:Q80X71","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000000589","properties":[{"key":"Component","value":"Chromosome 6"}]},{"database":"RNAct","id":"Q80X71","properties":[{"key":"moleculeType","value":"protein"}]},{"database":"Bgee","id":"ENSMUSG00000029571","properties":[{"key":"ExpressionPatterns","value":"Expressed in vestibular membrane of cochlear duct and 236 other cell types or tissues"}]},{"database":"ExpressionAtlas","id":"Q80X71","properties":[{"key":"ExpressionPatterns","value":"baseline and differential"}]},{"database":"GO","id":"GO:0005768","properties":[{"key":"GoTerm","value":"C:endosome"},{"key":"GoEvidenceType","value":"ISO:GO_Central"}]},{"database":"GO","id":"GO:0031902","properties":[{"key":"GoTerm","value":"C:late endosome membrane"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23136129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25066864"}]},{"database":"GO","id":"GO:0005765","properties":[{"key":"GoTerm","value":"C:lysosomal membrane"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23136129"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25066864"}]},{"database":"GO","id":"GO:0005764","properties":[{"key":"GoTerm","value":"C:lysosome"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"26370502"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0051117","properties":[{"key":"GoTerm","value":"F:ATPase binding"},{"key":"GoEvidenceType","value":"IPI:MGI"}],"evidences":[{"evidenceCode":"ECO:0000353","source":"PubMed","id":"28728022"}]},{"database":"GO","id":"GO:0048813","properties":[{"key":"GoTerm","value":"P:dendrite morphogenesis"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0007042","properties":[{"key":"GoTerm","value":"P:lysosomal lumen acidification"},{"key":"GoEvidenceType","value":"IMP:MGI"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"28728022"}]},{"database":"GO","id":"GO:1905146","properties":[{"key":"GoTerm","value":"P:lysosomal protein catabolic process"},{"key":"GoEvidenceType","value":"IMP:MGI"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"28728022"}]},{"database":"GO","id":"GO:0007041","properties":[{"key":"GoTerm","value":"P:lysosomal transport"},{"key":"GoEvidenceType","value":"IMP:MGI"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"25066864"}]},{"database":"GO","id":"GO:0032418","properties":[{"key":"GoTerm","value":"P:lysosome localization"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0007040","properties":[{"key":"GoTerm","value":"P:lysosome organization"},{"key":"GoEvidenceType","value":"IMP:MGI"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"25066864"}]},{"database":"GO","id":"GO:1900006","properties":[{"key":"GoTerm","value":"P:positive regulation of dendrite development"},{"key":"GoEvidenceType","value":"IMP:MGI"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"25066864"}]},{"database":"GO","id":"GO:0051345","properties":[{"key":"GoTerm","value":"P:positive regulation of hydrolase activity"},{"key":"GoEvidenceType","value":"IMP:MGI"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"28728022"}]},{"database":"GO","id":"GO:1905671","properties":[{"key":"GoTerm","value":"P:regulation of lysosome organization"},{"key":"GoEvidenceType","value":"IMP:MGI"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"28728022"}]},{"database":"InterPro","id":"IPR009790","properties":[{"key":"EntryName","value":"TMEM106"}]},{"database":"InterPro","id":"IPR048509","properties":[{"key":"EntryName","value":"TMEM106_C"}]},{"database":"InterPro","id":"IPR048511","properties":[{"key":"EntryName","value":"TMEM106_N"}]},{"database":"PANTHER","id":"PTHR28556","properties":[{"key":"EntryName","value":"TRANSMEMBRANE PROTEIN 106B"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR28556:SF1","properties":[{"key":"EntryName","value":"TRANSMEMBRANE PROTEIN 106B"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07092","properties":[{"key":"EntryName","value":"TMEM106"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21002","properties":[{"key":"EntryName","value":"TMEM106_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF117070","properties":[{"key":"EntryName","value":"LEA14-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGKSLSHLPLHSNKEDGYDGVTSTDNMRNGLVSSEVHNEDGRNGDVSQFPYVEFTGRDSVTCPTCQGTGRIPRGQENQLVALIPYSDQRLRPRRTKLYVMASVFVCLLLSGLAVFFLFPRSIEVKYIGVKSAYVSYDAEKRTIYLNITNTLNITNNNYYSVEVENITAQVQFSKTVIGKARLNNITNIGPLDMKQIDYTVPTVIAEEMSYMYDFCTLLSIKVHNIVLMMQVTVTTAYFGHSEQISQERYQYVDCGRNTTYQLAQSEYLNVLQPQQ","length":275,"molWeight":31172,"crc64":"4075221F1280EC4A","md5":"C99F26637C54A35D5ADF6DADB210D45D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"TISSUE SPECIFICITY":1,"DISRUPTION PHENOTYPE":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Topological domain":2,"Transmembrane":1,"Region":1,"Modified residue":1,"Lipidation":1,"Glycosylation":5,"Disulfide bond":1,"Sequence conflict":1},"uniParcId":"UPI000002323E"}}