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Q9Y217

- MTMR6_HUMAN

UniProt

Q9Y217 - MTMR6_HUMAN

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Protein
Myotubularin-related protein 6
Gene
MTMR6
Organism
Homo sapiens (Human)
Status
Reviewed - 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 intermediate By similarity
Binding sitei382 – 3821Substrate By similarity

GO - Molecular functioni

  1. calcium-activated potassium channel activity Source: UniProtKB
  2. protein serine/threonine phosphatase activity Source: UniProtKB
  3. protein tyrosine phosphatase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. peptidyl-tyrosine dephosphorylation Source: GOC
  2. phosphatidylinositol biosynthetic process Source: Reactome
  3. phospholipid metabolic process Source: Reactome
  4. potassium ion transmembrane transport Source: GOC
  5. protein dephosphorylation Source: UniProtKB
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

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: Chromosome 13

Organism-specific databases

HGNCiHGNC:7453. MTMR6.

Subcellular locationi

Nucleus envelope 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: LIFEdb
  2. cytosol Source: Reactome
  3. nuclear envelope Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31256.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei108 – 1081Phosphotyrosine By similarity
Modified residuei561 – 5611Phosphoserine1 Publication
Modified residuei589 – 5891Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y217.
PaxDbiQ9Y217.
PRIDEiQ9Y217.

PTM databases

PhosphoSiteiQ9Y217.

Expressioni

Tissue specificityi

Expressed in CD4+ T-cells.1 Publication

Gene expression databases

ArrayExpressiQ9Y217.
BgeeiQ9Y217.
CleanExiHS_MTMR6.
GenevestigatoriQ9Y217.

Organism-specific databases

HPAiHPA034778.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi114558. 5 interactions.
IntActiQ9Y217. 3 interactions.
MINTiMINT-2822863.
STRINGi9606.ENSP00000371221.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YF0X-ray2.65A1-505[»]
ProteinModelPortaliQ9Y217.
SMRiQ9Y217. Positions 4-505.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini124 – 499376Myotubularin phosphatase
Add
BLAST

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG322789.
HOVERGENiHBG000220.
InParanoidiQ9Y217.
KOiK18083.
OMAiVFNIIMN.
OrthoDBiEOG71RXJC.
PhylomeDBiQ9Y217.
TreeFamiTF315197.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR010569. Myotubularin-like_Pase_dom.
IPR011993. PH_like_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
[Graphical view]
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. Align

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

MEHIRTTKVE QVKLLDRFST SNKSLTGTLY LTATHLLFID SHQKETWILH    50
HHIASVEKLA LTTSGCPLVI QCKNFRTVHF IVPRERDCHD IYNSLLQLSK 100
QAKYEDLYAF SYNPKQNDSE RLQGWQLIDL AEEYKRMGVP NSHWQLSDAN 150
RDYKICETYP RELYVPRIAS KPIIVGSSKF RSKGRFPVLS YYHQDKEAAI 200
CRCSQPLSGF SARCLEDEHL LQAISKANPV NRYMYVMDTR PKLNAMANRA 250
AGKGYENEDN YSNIRFQFVG IENIHVMRSS LQKLLEVNGT KGLSVNDFYS 300
GLESSGWLRH IKAVMDAAIF LAKAITVENA SVLVHCSDGW DRTSQVCSLG 350
SLLLDSYYRT IKGFMVLIEK DWISFGHKFS ERCGQLDGDP KEVSPVFTQF 400
LECVWHLTEQ FPQAFEFSEA FLLQIHEHIH SCQFGNFLGN CQKEREELKL 450
KEKTYSLWPF LLEDQKKYLN PLYSSESHRF TVLEPNTVSF NFKFWRNMYH 500
QFDRTLHPRQ SVFNIIMNMN EQNKQLEKDI KDLESKIKQR KNKQTDGILT 550
KELLHSVHPE SPNLKTSLCF KEQTLLPVND ALRTIEGSSP ADNRYSEYAE 600
EFSKSEPAVV SLEYGVARMT C 621
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

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.
VSP_036614Add
BLAST
Alternative sequencei549 – 62173Missing in isoform 2.
VSP_036615Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891H → R in CAD89918. 1 Publication
Sequence conflicti114 – 1141P → S in BAG37162. 1 Publication
Sequence conflicti125 – 1251W → R in CAD89918. 1 Publication
Sequence conflicti333 – 3331L → S in AAL01037. 1 Publication
Sequence conflicti333 – 3331L → S in AAC78841. 1 Publication
Sequence conflicti368 – 3681I → T in BAG37162. 1 Publication
Sequence conflicti430 – 4301H → D in BAG52676. 1 Publication
Sequence conflicti442 – 4421Q → P in AAL01037. 1 Publication
Sequence conflicti442 – 4421Q → P in AAC78841. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. [Q9Y217-1]
ENST00000540661; ENSP00000443161; ENSG00000139505. [Q9Y217-2]
GeneIDi9107.
KEGGihsa:9107.
UCSCiuc001uqe.1. human. [Q9Y217-2]
uc001uqf.4. human. [Q9Y217-1]

Polymorphism databases

DMDMi317373414.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS9313.1. [Q9Y217-1 ]
RefSeqi NP_004676.3. NM_004685.3. [Q9Y217-1 ]
UniGenei Hs.643702.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YF0 X-ray 2.65 A 1-505 [» ]
ProteinModelPortali Q9Y217.
SMRi Q9Y217. Positions 4-505.
ModBasei Search...

Protein-protein interaction databases

BioGridi 114558. 5 interactions.
IntActi Q9Y217. 3 interactions.
MINTi MINT-2822863.
STRINGi 9606.ENSP00000371221.

PTM databases

PhosphoSitei Q9Y217.

Polymorphism databases

DMDMi 317373414.

Proteomic databases

MaxQBi Q9Y217.
PaxDbi Q9Y217.
PRIDEi Q9Y217.

Protocols and materials databases

DNASUi 9107.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000381801 ; ENSP00000371221 ; ENSG00000139505 . [Q9Y217-1 ]
ENST00000540661 ; ENSP00000443161 ; ENSG00000139505 . [Q9Y217-2 ]
GeneIDi 9107.
KEGGi hsa:9107.
UCSCi uc001uqe.1. human. [Q9Y217-2 ]
uc001uqf.4. human. [Q9Y217-1 ]

Organism-specific databases

CTDi 9107.
GeneCardsi GC13M025820.
H-InvDB HIX0011183.
HIX0171878.
HGNCi HGNC:7453. MTMR6.
HPAi HPA034778.
MIMi 603561. gene.
neXtProti NX_Q9Y217.
PharmGKBi PA31256.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG322789.
HOVERGENi HBG000220.
InParanoidi Q9Y217.
KOi K18083.
OMAi VFNIIMN.
OrthoDBi EOG71RXJC.
PhylomeDBi Q9Y217.
TreeFami TF315197.

Enzyme and pathway databases

Reactomei REACT_121025. Synthesis of PIPs at the plasma membrane.

Miscellaneous databases

GeneWikii MTMR6.
GenomeRNAii 9107.
NextBioi 34137.
PROi Q9Y217.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y217.
Bgeei Q9Y217.
CleanExi HS_MTMR6.
Genevestigatori Q9Y217.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR010569. Myotubularin-like_Pase_dom.
IPR011993. PH_like_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
[Graphical view ]
Pfami PF06602. Myotub-related. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS51339. PPASE_MYOTUBULARIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.

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: September 3, 2014
This is version 132 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