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Protein

Transmembrane protein 106B

Gene

TMEM106B

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

Functioni

Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with MAP6. May act by inhibiting retrograde transport of lysosomes along dendrites. Required for dendrite branching.2 Publications

GO - Biological processi

  1. dendrite morphogenesis Source: UniProtKB
  2. lysosome localization Source: UniProtKB
  3. transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Transmembrane protein 106B
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:22407. TMEM106B.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9696CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei97 – 11721HelicalSequence AnalysisAdd
BLAST
Topological domaini118 – 274157LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. intracellular membrane-bounded organelle Source: HPA
  4. late endosome membrane Source: UniProtKB-SubCell
  5. lysosomal membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Lysosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Ubiquitin-positive frontotemporal dementia (UP-FTD)

The gene represented in this entry acts as a disease modifier. Risk alleles confer genetic susceptibility by increasing gene expression (PubMed:20154673, PubMed:21178100). Increased expression may be the result of down-regulation of microRNA miR-132 and miR-212, that repress TMEM106B expression (PubMed:22895706). Thr-185 is a risk allele associated with lower GRN protein levels and early age at onset in GRN UP-FTD mutation carriers: it presents slower protein degradation that leads to higher steady-state TMEM106B levels, leading to alterations in the intracellular versus extracellular partitioning of GRN (PubMed:23742080).

Disease descriptionFrontotemporal dementia (FTD) is the second most common cause of dementia in people under the age of 65 years. It is an autosomal dominant neurodegenerative disease.

See also OMIM:607485
Frontotemporal dementia and/or amyotrophic lateral sclerosis 1 (FTDALS1)1 Publication2 Publications

The gene represented in this entry acts as a disease modifier.

Disease descriptionAn autosomal dominant neurodegenerative disorder characterized by adult onset of frontotemporal dementia and/or amyotrophic lateral sclerosis in an affected individual. There is high intrafamilial variation. Frontotemporal dementia is characterized by frontal and temporal lobe atrophy associated with neuronal loss, gliosis, and dementia. Patients exhibit progressive changes in social, behavioral, and/or language function. Amyotrophic lateral sclerosis is characterized by the death of motor neurons in the brain, brainstem, and spinal cord, resulting in fatal paralysis.

See also OMIM:105550

Keywords - Diseasei

Amyotrophic lateral sclerosis, Neurodegeneration

Organism-specific databases

MIMi105550. phenotype.
607485. phenotype.
PharmGKBiPA142670756.

Polymorphism and mutation databases

BioMutaiTMEM106B.
DMDMi109895058.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 274274Transmembrane protein 106BPRO_0000242650Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei33 – 331Phosphoserine2 Publications
Glycosylationi145 – 1451N-linked (GlcNAc...)1 Publication
Glycosylationi151 – 1511N-linked (GlcNAc...)1 Publication
Glycosylationi164 – 1641N-linked (GlcNAc...)1 Publication
Glycosylationi183 – 1831N-linked (GlcNAc...)3 Publications
Glycosylationi256 – 2561N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9NUM4.
PaxDbiQ9NUM4.
PeptideAtlasiQ9NUM4.
PRIDEiQ9NUM4.

PTM databases

PhosphoSiteiQ9NUM4.

Miscellaneous databases

PMAP-CutDBQ9NUM4.

Expressioni

Tissue specificityi

Expressed in frontal cortex.

Gene expression databases

BgeeiQ9NUM4.
CleanExiHS_TMEM106B.
ExpressionAtlasiQ9NUM4. baseline and differential.
GenevestigatoriQ9NUM4.

Organism-specific databases

HPAiHPA058342.

Interactioni

Subunit structurei

Interacts with MAP6.1 Publication

Protein-protein interaction databases

BioGridi120093. 2 interactions.
IntActiQ9NUM4. 1 interaction.
MINTiMINT-4658429.
STRINGi9606.ENSP00000336673.

Structurei

3D structure databases

ProteinModelPortaliQ9NUM4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TMEM106 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG44552.
GeneTreeiENSGT00390000013076.
HOVERGENiHBG055025.
InParanoidiQ9NUM4.
OMAiHSNKEDG.
OrthoDBiEOG7D85X7.
PhylomeDBiQ9NUM4.
TreeFamiTF328907.

Family and domain databases

InterProiIPR009790. DUF1356_TMEM106.
[Graphical view]
PfamiPF07092. DUF1356. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NUM4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKSLSHLPL HSSKEDAYDG VTSENMRNGL VNSEVHNEDG RNGDVSQFPY
60 70 80 90 100
VEFTGRDSVT CPTCQGTGRI PRGQENQLVA LIPYSDQRLR PRRTKLYVMA
110 120 130 140 150
SVFVCLLLSG LAVFFLFPRS IDVKYIGVKS AYVSYDVQKR TIYLNITNTL
160 170 180 190 200
NITNNNYYSV EVENITAQVQ FSKTVIGKAR LNNITIIGPL DMKQIDYTVP
210 220 230 240 250
TVIAEEMSYM YDFCTLISIK VHNIVLMMQV TVTTTYFGHS EQISQERYQY
260 270
VDCGRNTTYQ LGQSEYLNVL QPQQ
Length:274
Mass (Da):31,127
Last modified:June 27, 2006 - v2
Checksum:i906C923986DC04E6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501Y → C in BAD96983 (Ref. 2) Curated
Sequence conflicti106 – 1061L → P in BAD96983 (Ref. 2) Curated
Sequence conflicti197 – 1971Y → N in BAD96983 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti185 – 1851T → S.2 Publications
Corresponds to variant rs3173615 [ dbSNP | Ensembl ].
VAR_026849

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002135 mRNA. Translation: BAA92099.1.
AK223263 mRNA. Translation: BAD96983.1.
AC007321 Genomic DNA. Translation: AAQ96840.1.
CH236948 Genomic DNA. Translation: EAL24296.1.
CH471073 Genomic DNA. Translation: EAW93638.1.
BC033901 mRNA. Translation: AAH33901.1.
BC039741 mRNA. Translation: AAH39741.1.
CCDSiCCDS5358.1.
RefSeqiNP_001127704.1. NM_001134232.1.
NP_060844.2. NM_018374.3.
XP_005249846.1. XM_005249789.1.
UniGeneiHs.396358.

Genome annotation databases

EnsembliENST00000396667; ENSP00000379901; ENSG00000106460.
ENST00000396668; ENSP00000379902; ENSG00000106460.
GeneIDi54664.
KEGGihsa:54664.
UCSCiuc003ssh.3. human.

Polymorphism and mutation databases

BioMutaiTMEM106B.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002135 mRNA. Translation: BAA92099.1.
AK223263 mRNA. Translation: BAD96983.1.
AC007321 Genomic DNA. Translation: AAQ96840.1.
CH236948 Genomic DNA. Translation: EAL24296.1.
CH471073 Genomic DNA. Translation: EAW93638.1.
BC033901 mRNA. Translation: AAH33901.1.
BC039741 mRNA. Translation: AAH39741.1.
CCDSiCCDS5358.1.
RefSeqiNP_001127704.1. NM_001134232.1.
NP_060844.2. NM_018374.3.
XP_005249846.1. XM_005249789.1.
UniGeneiHs.396358.

3D structure databases

ProteinModelPortaliQ9NUM4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120093. 2 interactions.
IntActiQ9NUM4. 1 interaction.
MINTiMINT-4658429.
STRINGi9606.ENSP00000336673.

PTM databases

PhosphoSiteiQ9NUM4.

Polymorphism and mutation databases

BioMutaiTMEM106B.
DMDMi109895058.

Proteomic databases

MaxQBiQ9NUM4.
PaxDbiQ9NUM4.
PeptideAtlasiQ9NUM4.
PRIDEiQ9NUM4.

Protocols and materials databases

DNASUi54664.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000396667; ENSP00000379901; ENSG00000106460.
ENST00000396668; ENSP00000379902; ENSG00000106460.
GeneIDi54664.
KEGGihsa:54664.
UCSCiuc003ssh.3. human.

Organism-specific databases

CTDi54664.
GeneCardsiGC07P012217.
HGNCiHGNC:22407. TMEM106B.
HPAiHPA058342.
MIMi105550. phenotype.
607485. phenotype.
613413. gene.
neXtProtiNX_Q9NUM4.
PharmGKBiPA142670756.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG44552.
GeneTreeiENSGT00390000013076.
HOVERGENiHBG055025.
InParanoidiQ9NUM4.
OMAiHSNKEDG.
OrthoDBiEOG7D85X7.
PhylomeDBiQ9NUM4.
TreeFamiTF328907.

Miscellaneous databases

ChiTaRSiTMEM106B. human.
GeneWikiiTMEM106B.
GenomeRNAii54664.
NextBioi57212.
PMAP-CutDBQ9NUM4.
PROiQ9NUM4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NUM4.
CleanExiHS_TMEM106B.
ExpressionAtlasiQ9NUM4. baseline and differential.
GenevestigatoriQ9NUM4.

Family and domain databases

InterProiIPR009790. DUF1356_TMEM106.
[Graphical view]
PfamiPF07092. DUF1356. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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], VARIANT SER-185.
    Tissue: Placenta.
  2. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Gastric mucosa.
  3. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 and Skin.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-183.
    Tissue: Liver.
  9. "Common variants at 7p21 are associated with frontotemporal lobar degeneration with TDP-43 inclusions."
    Van Deerlin V.M., Sleiman P.M., Martinez-Lage M., Chen-Plotkin A., Wang L.S., Graff-Radford N.R., Dickson D.W., Rademakers R., Boeve B.F., Grossman M., Arnold S.E., Mann D.M., Pickering-Brown S.M., Seelaar H., Heutink P., van Swieten J.C., Murrell J.R., Ghetti B.
    , Spina S., Grafman J., Hodges J., Spillantini M.G., Gilman S., Lieberman A.P., Kaye J.A., Woltjer R.L., Bigio E.H., Mesulam M., Al-Sarraj S., Troakes C., Rosenberg R.N., White C.L. III, Ferrer I., Llado A., Neumann M., Kretzschmar H.A., Hulette C.M., Welsh-Bohmer K.A., Miller B.L., Alzualde A., de Munain A.L., McKee A.C., Gearing M., Levey A.I., Lah J.J., Hardy J., Rohrer J.D., Lashley T., Mackenzie I.R., Feldman H.H., Hamilton R.L., Dekosky S.T., van der Zee J., Kumar-Singh S., Van Broeckhoven C., Mayeux R., Vonsattel J.P., Troncoso J.C., Kril J.J., Kwok J.B., Halliday G.M., Bird T.D., Ince P.G., Shaw P.J., Cairns N.J., Morris J.C., McLean C.A., DeCarli C., Ellis W.G., Freeman S.H., Frosch M.P., Growdon J.H., Perl D.P., Sano M., Bennett D.A., Schneider J.A., Beach T.G., Reiman E.M., Woodruff B.K., Cummings J., Vinters H.V., Miller C.A., Chui H.C., Alafuzoff I., Hartikainen P., Seilhean D., Galasko D., Masliah E., Cotman C.W., Tunon M.T., Martinez M.C., Munoz D.G., Carroll S.L., Marson D., Riederer P.F., Bogdanovic N., Schellenberg G.D., Hakonarson H., Trojanowski J.Q., Lee V.M.
    Nat. Genet. 42:234-239(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN UP-FTD.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: INVOLVEMENT IN UP-FTD.
  12. "Membrane orientation and subcellular localization of transmembrane protein 106B (TMEM106B), a major risk factor for frontotemporal lobar degeneration."
    Lang C.M., Fellerer K., Schwenk B.M., Kuhn P.H., Kremmer E., Edbauer D., Capell A., Haass C.
    J. Biol. Chem. 287:19355-19365(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-145; ASN-151; ASN-164; ASN-183 AND ASN-256.
  13. "TMEM106B, the risk gene for frontotemporal dementia, is regulated by the microRNA-132/212 cluster and affects progranulin pathways."
    Chen-Plotkin A.S., Unger T.L., Gallagher M.D., Bill E., Kwong L.K., Volpicelli-Daley L., Busch J.I., Akle S., Grossman M., Van Deerlin V., Trojanowski J.Q., Lee V.M.
    J. Neurosci. 32:11213-11227(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN UP-FTD.
  14. "The frontotemporal lobar degeneration risk factor, TMEM106B, regulates lysosomal morphology and function."
    Brady O.A., Zheng Y., Murphy K., Huang M., Hu F.
    Hum. Mol. Genet. 22:685-695(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  15. Cited for: INVOLVEMENT IN UP-FTD, VARIANT SER-185, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-183.
  16. "TMEM106B: a strong FTLD disease modifier."
    Deming Y., Cruchaga C.
    Acta Neuropathol. 127:419-422(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN FTDALS1.
  17. "TMEM106B is a genetic modifier of frontotemporal lobar degeneration with C9orf72 hexanucleotide repeat expansions."
    Gallagher M.D., Suh E., Grossman M., Elman L., McCluskey L., Van Swieten J.C., Al-Sarraj S., Neumann M., Gelpi E., Ghetti B., Rohrer J.D., Halliday G., Van Broeckhoven C., Seilhean D., Shaw P.J., Frosch M.P., Alafuzoff I., Antonell A.
    , Bogdanovic N., Brooks W., Cairns N.J., Cooper-Knock J., Cotman C., Cras P., Cruts M., De Deyn P.P., Decarli C., Dobson-Stone C., Engelborghs S., Fox N., Galasko D., Gearing M., Gijselinck I., Grafman J., Hartikainen P., Hatanpaa K.J., Highley J.R., Hodges J., Hulette C., Ince P.G., Jin L.W., Kirby J., Kofler J., Kril J., Kwok J.B., Levey A., Lieberman A., Llado A., Martin J.J., Masliah E., McDermott C.J., McKee A., McLean C., Mead S., Miller C.A., Miller J., Munoz D.G., Murrell J., Paulson H., Piguet O., Rossor M., Sanchez-Valle R., Sano M., Schneider J., Silbert L.C., Spina S., van der Zee J., Van Langenhove T., Warren J., Wharton S.B., White Iii C.L., Woltjer R.L., Trojanowski J.Q., Lee V.M., Van Deerlin V., Chen-Plotkin A.S.
    Acta Neuropathol. 127:407-418(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN FTDALS1.
  18. Cited for: INVOLVEMENT IN FTDALS1.
  19. "The FTLD risk factor TMEM106B and MAP6 control dendritic trafficking of lysosomes."
    Schwenk B.M., Lang C.M., Hogl S., Tahirovic S., Orozco D., Rentzsch K., Lichtenthaler S.F., Hoogenraad C.C., Capell A., Haass C., Edbauer D.
    EMBO J. 33:450-467(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAP6.

Entry informationi

Entry nameiT106B_HUMAN
AccessioniPrimary (citable) accession number: Q9NUM4
Secondary accession number(s): A4D108, Q53FL9, Q8N4L0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 27, 2006
Last modified: April 29, 2015
This is version 95 of the entry and version 2 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.