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Protein

Myotubularin-related protein 6

Gene

MTMR6

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

Functioni

Phosphatase that acts on lipids with a phosphoinositol headgroup. Acts as a negative regulator of KCNN4/KCa3.1 channel activity in CD4+ T-cells possibly by decreasing intracellular levels of phosphatidylinositol 3 phosphatase. Negatively regulates proliferation of reactivated CD4+ T-cells.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei336 – 3361Phosphocysteine intermediatePROSITE-ProRule annotation
Binding sitei382 – 3821SubstrateBy similarity

GO - Molecular functioni

  • calcium-activated potassium channel activity Source: UniProtKB
  • phosphatidylinositol phosphate phosphatase activity Source: InterPro
  • protein serine/threonine phosphatase activity Source: UniProtKB
  • protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  • peptidyl-tyrosine dephosphorylation Source: GOC
  • phosphatidylinositol biosynthetic process Source: Reactome
  • phosphatidylinositol dephosphorylation Source: InterPro
  • phospholipid metabolic process Source: Reactome
  • potassium ion transmembrane transport Source: GOC
  • protein dephosphorylation Source: UniProtKB
  • small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.1.3.95. 2681.
ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Myotubularin-related protein 6 (EC:3.1.3.-)
Gene namesi
Name:MTMR6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:7453. MTMR6.

Subcellular locationi

  • Nucleus envelope 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31256.

Polymorphism and mutation databases

BioMutaiMTMR6.
DMDMi317373414.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 621621Myotubularin-related protein 6PRO_0000094939Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei108 – 1081PhosphotyrosineBy similarity
Modified residuei556 – 5561Phosphoserine1 Publication
Modified residuei561 – 5611Phosphoserine2 Publications
Modified residuei589 – 5891Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y217.
PaxDbiQ9Y217.
PRIDEiQ9Y217.

PTM databases

DEPODiQ9Y217.
PhosphoSiteiQ9Y217.

Expressioni

Tissue specificityi

Expressed in CD4+ T-cells.1 Publication

Gene expression databases

BgeeiQ9Y217.
CleanExiHS_MTMR6.
GenevisibleiQ9Y217. HS.

Organism-specific databases

HPAiHPA034778.

Interactioni

Subunit structurei

Interacts with ALKBH4, KCNN4, MTMR7, MTMR8 and MTMR9.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AMOTL2Q9Y2J4-43EBI-766064,EBI-10187270
MTMR9Q96QG76EBI-766064,EBI-744593
MTUS2Q5JR593EBI-766064,EBI-742948
NMIQ132873EBI-766064,EBI-372942
NMIQ8WTW23EBI-766064,EBI-10174268
TRIM27P143733EBI-766064,EBI-719493

Protein-protein interaction databases

BioGridi114558. 11 interactions.
IntActiQ9Y217. 8 interactions.
MINTiMINT-2822863.
STRINGi9606.ENSP00000371221.

Structurei

Secondary structure

1
621
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 117Combined sources
Beta strandi26 – 316Combined sources
Beta strandi33 – 4311Combined sources
Beta strandi45 – 495Combined sources
Helixi50 – 523Combined sources
Beta strandi53 – 586Combined sources
Beta strandi65 – 728Combined sources
Beta strandi77 – 837Combined sources
Helixi85 – 9814Combined sources
Helixi108 – 1103Combined sources
Helixi119 – 1257Combined sources
Helixi130 – 1367Combined sources
Beta strandi140 – 1478Combined sources
Helixi148 – 1503Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi161 – 1699Combined sources
Helixi171 – 18010Combined sources
Helixi182 – 1843Combined sources
Beta strandi188 – 1925Combined sources
Turni194 – 1963Combined sources
Beta strandi199 – 2024Combined sources
Helixi215 – 22713Combined sources
Beta strandi234 – 2385Combined sources
Turni258 – 2603Combined sources
Beta strandi264 – 2685Combined sources
Helixi274 – 28815Combined sources
Helixi295 – 30410Combined sources
Helixi307 – 32620Combined sources
Beta strandi332 – 3343Combined sources
Turni336 – 3383Combined sources
Beta strandi339 – 3413Combined sources
Helixi342 – 35413Combined sources
Helixi357 – 3593Combined sources
Helixi361 – 37111Combined sources
Turni372 – 3765Combined sources
Helixi379 – 3835Combined sources
Beta strandi385 – 3873Combined sources
Helixi390 – 3923Combined sources
Helixi396 – 41015Combined sources
Turni412 – 4143Combined sources
Helixi419 – 42911Combined sources
Turni430 – 4323Combined sources
Beta strandi439 – 4413Combined sources
Helixi442 – 4476Combined sources
Helixi450 – 4534Combined sources
Helixi458 – 4614Combined sources
Helixi465 – 4684Combined sources
Beta strandi488 – 4914Combined sources
Helixi496 – 5027Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YF0X-ray2.65A1-505[»]
ProteinModelPortaliQ9Y217.
SMRiQ9Y217. Positions 4-505.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini124 – 499376Myotubularin phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni248 – 2514Substrate bindingBy similarity
Regioni273 – 2742Substrate bindingBy similarity
Regioni336 – 3427Substrate bindingBy similarity

Sequence similaritiesi

Contains 1 myotubularin phosphatase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG322789.
GeneTreeiENSGT00760000118832.
HOVERGENiHBG000220.
InParanoidiQ9Y217.
KOiK18083.
OMAiLAPQCIK.
OrthoDBiEOG71RXJC.
PhylomeDBiQ9Y217.
TreeFamiTF315197.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR030581. MTMR6.
IPR010569. Myotubularin-like_Pase_dom.
IPR030564. Myotubularin_fam.
IPR011993. PH-like_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10807. PTHR10807. 1 hit.
PTHR10807:SF34. PTHR10807:SF34. 1 hit.
PfamiPF06602. Myotub-related. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS51339. PPASE_MYOTUBULARIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y217-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEHIRTTKVE QVKLLDRFST SNKSLTGTLY LTATHLLFID SHQKETWILH
60 70 80 90 100
HHIASVEKLA LTTSGCPLVI QCKNFRTVHF IVPRERDCHD IYNSLLQLSK
110 120 130 140 150
QAKYEDLYAF SYNPKQNDSE RLQGWQLIDL AEEYKRMGVP NSHWQLSDAN
160 170 180 190 200
RDYKICETYP RELYVPRIAS KPIIVGSSKF RSKGRFPVLS YYHQDKEAAI
210 220 230 240 250
CRCSQPLSGF SARCLEDEHL LQAISKANPV NRYMYVMDTR PKLNAMANRA
260 270 280 290 300
AGKGYENEDN YSNIRFQFVG IENIHVMRSS LQKLLEVNGT KGLSVNDFYS
310 320 330 340 350
GLESSGWLRH IKAVMDAAIF LAKAITVENA SVLVHCSDGW DRTSQVCSLG
360 370 380 390 400
SLLLDSYYRT IKGFMVLIEK DWISFGHKFS ERCGQLDGDP KEVSPVFTQF
410 420 430 440 450
LECVWHLTEQ FPQAFEFSEA FLLQIHEHIH SCQFGNFLGN CQKEREELKL
460 470 480 490 500
KEKTYSLWPF LLEDQKKYLN PLYSSESHRF TVLEPNTVSF NFKFWRNMYH
510 520 530 540 550
QFDRTLHPRQ SVFNIIMNMN EQNKQLEKDI KDLESKIKQR KNKQTDGILT
560 570 580 590 600
KELLHSVHPE SPNLKTSLCF KEQTLLPVND ALRTIEGSSP ADNRYSEYAE
610 620
EFSKSEPAVV SLEYGVARMT C
Length:621
Mass (Da):71,968
Last modified:January 11, 2011 - v3
Checksum:i1F34608F99DCEA39
GO
Isoform 2 (identifier: Q9Y217-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     536-548: KIKQRKNKQTDGI → LTSYSSFKIIVGQ
     549-621: Missing.

Note: No experimental confirmation available.
Show »
Length:548
Mass (Da):63,743
Checksum:i161703C7D46CBD88
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891H → R in CAD89918 (PubMed:17974005).Curated
Sequence conflicti114 – 1141P → S in BAG37162 (PubMed:14702039).Curated
Sequence conflicti125 – 1251W → R in CAD89918 (PubMed:17974005).Curated
Sequence conflicti333 – 3331L → S in AAL01037 (Ref. 2) Curated
Sequence conflicti333 – 3331L → S in AAC78841 (PubMed:9736772).Curated
Sequence conflicti368 – 3681I → T in BAG37162 (PubMed:14702039).Curated
Sequence conflicti430 – 4301H → D in BAG52676 (PubMed:14702039).Curated
Sequence conflicti442 – 4421Q → P in AAL01037 (Ref. 2) Curated
Sequence conflicti442 – 4421Q → P in AAC78841 (PubMed:9736772).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti131 – 1311A → T.
Corresponds to variant rs34885345 [ dbSNP | Ensembl ].
VAR_057143
Natural varianti319 – 3191I → V.5 Publications
Corresponds to variant rs7995033 [ dbSNP | Ensembl ].
VAR_024583

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei536 – 54813KIKQR…QTDGI → LTSYSSFKIIVGQ in isoform 2. 1 PublicationVSP_036614Add
BLAST
Alternative sequencei549 – 62173Missing in isoform 2. 1 PublicationVSP_036615Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF406619 mRNA. Translation: AAL01037.1.
AK093237 mRNA. Translation: BAG52676.1.
AK314587 mRNA. Translation: BAG37162.1.
AL832017 mRNA. Translation: CAD89918.1.
AL590787 Genomic DNA. Translation: CAI39897.1.
BC040012 mRNA. Translation: AAH40012.1.
AF072928 mRNA. Translation: AAC78841.1.
CCDSiCCDS9313.1. [Q9Y217-1]
RefSeqiNP_004676.3. NM_004685.3. [Q9Y217-1]
UniGeneiHs.643702.

Genome annotation databases

EnsembliENST00000381801; ENSP00000371221; ENSG00000139505.
GeneIDi9107.
KEGGihsa:9107.
UCSCiuc001uqe.1. human. [Q9Y217-2]
uc001uqf.4. human. [Q9Y217-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF406619 mRNA. Translation: AAL01037.1.
AK093237 mRNA. Translation: BAG52676.1.
AK314587 mRNA. Translation: BAG37162.1.
AL832017 mRNA. Translation: CAD89918.1.
AL590787 Genomic DNA. Translation: CAI39897.1.
BC040012 mRNA. Translation: AAH40012.1.
AF072928 mRNA. Translation: AAC78841.1.
CCDSiCCDS9313.1. [Q9Y217-1]
RefSeqiNP_004676.3. NM_004685.3. [Q9Y217-1]
UniGeneiHs.643702.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YF0X-ray2.65A1-505[»]
ProteinModelPortaliQ9Y217.
SMRiQ9Y217. Positions 4-505.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114558. 11 interactions.
IntActiQ9Y217. 8 interactions.
MINTiMINT-2822863.
STRINGi9606.ENSP00000371221.

PTM databases

DEPODiQ9Y217.
PhosphoSiteiQ9Y217.

Polymorphism and mutation databases

BioMutaiMTMR6.
DMDMi317373414.

Proteomic databases

MaxQBiQ9Y217.
PaxDbiQ9Y217.
PRIDEiQ9Y217.

Protocols and materials databases

DNASUi9107.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381801; ENSP00000371221; ENSG00000139505.
GeneIDi9107.
KEGGihsa:9107.
UCSCiuc001uqe.1. human. [Q9Y217-2]
uc001uqf.4. human. [Q9Y217-1]

Organism-specific databases

CTDi9107.
GeneCardsiGC13M025820.
H-InvDBHIX0011183.
HIX0171878.
HGNCiHGNC:7453. MTMR6.
HPAiHPA034778.
MIMi603561. gene.
neXtProtiNX_Q9Y217.
PharmGKBiPA31256.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG322789.
GeneTreeiENSGT00760000118832.
HOVERGENiHBG000220.
InParanoidiQ9Y217.
KOiK18083.
OMAiLAPQCIK.
OrthoDBiEOG71RXJC.
PhylomeDBiQ9Y217.
TreeFamiTF315197.

Enzyme and pathway databases

BRENDAi3.1.3.95. 2681.
ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.

Miscellaneous databases

ChiTaRSiMTMR6. human.
GeneWikiiMTMR6.
GenomeRNAii9107.
NextBioi34137.
PROiQ9Y217.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y217.
CleanExiHS_MTMR6.
GenevisibleiQ9Y217. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR030581. MTMR6.
IPR010569. Myotubularin-like_Pase_dom.
IPR030564. Myotubularin_fam.
IPR011993. PH-like_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10807. PTHR10807. 1 hit.
PTHR10807:SF34. PTHR10807:SF34. 1 hit.
PfamiPF06602. Myotub-related. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS51339. PPASE_MYOTUBULARIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of myotubularin-related protein 7 and its binding partner, myotubularin-related protein 9."
    Mochizuki Y., Majerus P.W.
    Proc. Natl. Acad. Sci. U.S.A. 100:9768-9773(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH MTMR9.
  2. Hong W.
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-319.
  3. "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] (ISOFORMS 1 AND 2), VARIANT VAL-319.
    Tissue: Testis and Trachea.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-319.
    Tissue: Skeletal muscle.
  5. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [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] (ISOFORM 1), VARIANT VAL-319.
    Tissue: Eye.
  7. "Characterization of the myotubularin dual specificity phosphatase gene family from yeast to human."
    Laporte J., Blondeau F., Buj-Bello A., Tentler D., Kretz C., Dahl N., Mandel J.-L.
    Hum. Mol. Genet. 7:1703-1712(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 157-621 (ISOFORM 1), VARIANT VAL-319.
  8. "The phosphatidylinositol 3-phosphate phosphatase myotubularin-related protein 6 (MTMR6) is a negative regulator of the Ca2+-activated K+ channel KCa3.1."
    Srivastava S., Li Z., Lin L., Liu G., Ko K., Coetzee W.A., Skolnik E.Y.
    Mol. Cell. Biol. 25:3630-3638(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KCNN4.
  9. "Systematic analysis of myotubularins: heteromeric interactions, subcellular localisation and endosome related functions."
    Lorenzo O., Urbe S., Clague M.J.
    J. Cell Sci. 119:2953-2959(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MTMR7; MTMR8 AND MTMR9.
  10. "Phosphatidylinositol-3 phosphatase myotubularin-related protein 6 negatively regulates CD4 T cells."
    Srivastava S., Ko K., Choudhury P., Li Z., Johnson A.K., Nadkarni V., Unutmaz D., Coetzee W.A., Skolnik E.Y.
    Mol. Cell. Biol. 26:5595-5602(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561 AND SER-589, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Human ALKBH4 interacts with proteins associated with transcription."
    Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A., Falnes P.O.
    PLoS ONE 7:E49045-E49045(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ALKBH4.
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-556 AND SER-561, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMTMR6_HUMAN
AccessioniPrimary (citable) accession number: Q9Y217
Secondary accession number(s): B2RBB5
, B3KSB4, Q5JRG6, Q86TB7, Q86YH4, Q96P80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 11, 2011
Last modified: July 22, 2015
This is version 143 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.