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Protein

Myotubularin-related protein 3

Gene

MTMR3

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. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate. May also dephosphorylate proteins phosphorylated on Ser, Thr, and Tyr residues (PubMed:10733931).2 Publications

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O = 1-phosphatidyl-1D-myo-inositol + phosphate.1 Publication
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate.1 Publication
Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 PublicationPROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei413 – 4131Phosphocysteine intermediateCuratedPROSITE-ProRule annotation
Binding sitei459 – 4591SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1119 – 117961FYVE-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity Source: UniProtKB
  3. phosphatidylinositol-3-phosphatase activity Source: UniProtKB
  4. protein serine/threonine phosphatase activity Source: UniProtKB
  5. protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Lipid metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS02045-MONOMER.
ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Myotubularin-related protein 3 (EC:3.1.3.481 Publication)
Alternative name(s):
FYVE domain-containing dual specificity protein phosphatase 1
Short name:
FYVE-DSP1
Phosphatidylinositol-3,5-bisphosphate 3-phosphatase (EC:3.1.3.951 Publication)
Phosphatidylinositol-3-phosphate phosphatase (EC:3.1.3.641 Publication)
Zinc finger FYVE domain-containing protein 10
Gene namesi
Name:MTMR3
Synonyms:KIAA0371, ZFYVE10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:7451. MTMR3.

Subcellular locationi

Cytoplasm 1 Publication. Membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extrinsic component of membrane Source: UniProtKB
  4. membrane Source: UniProtKB
  5. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi413 – 4131C → S: Loss of lipid phosphatase activity. 1 Publication

Organism-specific databases

PharmGKBiPA31254.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11981198Myotubularin-related protein 3PRO_0000094936Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei633 – 6331Phosphoserine1 Publication
Modified residuei647 – 6471Phosphoserine2 Publications
Modified residuei731 – 7311Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13615.
PaxDbiQ13615.
PRIDEiQ13615.

PTM databases

DEPODiQ13615.
PhosphoSiteiQ13615.

Expressioni

Gene expression databases

BgeeiQ13615.
CleanExiHS_MTMR3.
ExpressionAtlasiQ13615. baseline and differential.
GenevestigatoriQ13615.

Organism-specific databases

HPAiHPA034515.
HPA034516.

Interactioni

Protein-protein interaction databases

BioGridi114414. 6 interactions.
IntActiQ13615. 6 interactions.
STRINGi9606.ENSP00000384651.

Structurei

3D structure databases

ProteinModelPortaliQ13615.
SMRiQ13615. Positions 53-577, 1125-1175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini155 – 576422Myotubularin phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni326 – 3294Substrate bindingBy similarity
Regioni351 – 3522Substrate bindingBy similarity
Regioni413 – 4197Substrate bindingBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1029 – 106234Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation
Contains 1 myotubularin phosphatase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1119 – 117961FYVE-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG322789.
GeneTreeiENSGT00760000118832.
HOVERGENiHBG052526.
InParanoidiQ13615.
KOiK18082.
OMAiTDTIQQR.
OrthoDBiEOG7PVWNJ.
PhylomeDBiQ13615.
TreeFamiTF315197.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR010569. Myotubularin-like_Pase_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF06602. Myotub-related. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 2 hits.
SSF57903. SSF57903. 1 hit.
PROSITEiPS51339. PPASE_MYOTUBULARIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform B (identifier: Q13615-1) [UniParc]FASTAAdd to Basket

Also known as: FYVE-DSP1b

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
MDEETRHSLE CIQANQIFPR KQLIREDENL QVPFLELHGE STEFVGRAED
60 70 80 90 100
AIIALSNYRL HIKFKESLVN VPLQLIESVE CRDIFQLHLT CKDCKVIRCQ
110 120 130 140 150
FSTFEQCQEW LKRLNNAIRP PAKIEDLFSF AYHAWCMEVY ASEKEQHGDL
160 170 180 190 200
CRPGEHVTSR FKNEVERMGF DMNNAWRISN INEKYKLCGS YPQELIVPAW
210 220 230 240 250
ITDKELESVS SFRSWKRIPA VIYRHQSNGA VIARCGQPEV SWWGWRNADD
260 270 280 290 300
EHLVQSVAKA CASDSRSSGS KLSTRNTSRD FPNGGDLSDV EFDSSLSNAS
310 320 330 340 350
GAESLAIQPQ KLLILDARSY AAAVANRAKG GGCECPEYYP NCEVVFMGMA
360 370 380 390 400
NIHSIRRSFQ SLRLLCTQMP DPGNWLSALE STKWLHHLSV LLKSALLVVH
410 420 430 440 450
AVDQDQRPVL VHCSDGWDRT PQIVALAKLL LDPYYRTIEG FQVLVEMEWL
460 470 480 490 500
DFGHKFADRC GHGENSDDLN ERCPVFLQWL DCVHQLQRQF PCSFEFNEAF
510 520 530 540 550
LVKLVQHTYS CLFGTFLCNN AKERGEKHTQ ERTCSVWSLL RAGNKAFKNL
560 570 580 590 600
LYSSQSEAVL YPVCHVRNLM LWSAVYLPCP SPTTPVDDSC APYPAPGTSP
610 620 630 640 650
DDPPLSRLPK TRSYDNLTTA CDNTVPLASR RCSDPSLNEK WQEHRRSLEL
660 670 680 690 700
SSLAGPGEDP LSADSLGKPT RVPGGAELSV AAGVAEGQME NILQEATKEE
710 720 730 740 750
SGVEEPAHRA GIEIQEGKED PLLEKESRRK TPEASAIGLH QDPELGDAAL
760 770 780 790 800
RSHLDMSWPL FSQGISEQQS GLSVLLSSLQ VPPRGEDSLE VPVEQFRIEE
810 820 830 840 850
IAEGREEAVL PIPVDAKVGY GTSQSCSLLP SQVPFETRGP NVDSSTDMLV
860 870 880 890 900
EDKVKSVSGP QGHHRSCLVN SGKDRLPQTM EPSPSETSLV ERPQVGSVVH
910 920 930 940 950
RTSLGSTLSL TRSPCALPLA ECKEGLVCNG APETENRASE QPPGLSTLQM
960 970 980 990 1000
YPTPNGHCAN GEAGRSKDSL SRQLSAMSCS SAHLHSRNLH HKWLHSHSGR
1010 1020 1030 1040 1050
PSATSSPDQP SRSHLDDDGM SVYTDTIQQR LRQIESGHQQ EVETLKKQVQ
1060 1070 1080 1090 1100
ELKSRLESQY LTSSLHFNGD FGDEVTSIPD SESNLDQNCL SRCSTEIFSE
1110 1120 1130 1140 1150
ASWEQVDKQD TEMTRWLPDH LAAHCYACDS AFWLASRKHH CRNCGNVFCS
1160 1170 1180 1190
SCCNQKVPVP SQQLFEPSRV CKSCYSSLHP TSSSIDLELD KPIAATSN
Length:1,198
Mass (Da):133,619
Last modified:July 19, 2003 - v3
Checksum:iFE6F4B165074D5F8
GO
Isoform A (identifier: Q13615-2) [UniParc]FASTAAdd to Basket

Also known as: FYVE-DSP1a

The sequence of this isoform differs from the canonical sequence as follows:
     1076-1112: Missing.
     1142-1142: R → RDTDRVDQTW

Show »
Length:1,170
Mass (Da):130,561
Checksum:iB51B10E3E7245433
GO
Isoform C (identifier: Q13615-3) [UniParc]FASTAAdd to Basket

Also known as: FYVE-DSP1c

The sequence of this isoform differs from the canonical sequence as follows:
     1076-1112: Missing.

Show »
Length:1,161
Mass (Da):129,444
Checksum:i18C795D42EFB1177
GO

Sequence cautioni

The sequence BAA20826.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti560 – 57819LYPVC…AVYLP → CILQPFHCGQQKEFGVGYI(PubMed:9736772)CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti221 – 2211V → L in a breast cancer sample; somatic mutation. 1 Publication
VAR_035656

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1076 – 111237Missing in isoform A and isoform C. 1 PublicationVSP_007781Add
BLAST
Alternative sequencei1142 – 11421R → RDTDRVDQTW in isoform A. CuratedVSP_007782

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF233436 mRNA. Translation: AAF40203.2.
AF233437 mRNA. Translation: AAF40204.1.
AF233438 mRNA. Translation: AAF40205.1.
AB002369 mRNA. Translation: BAA20826.2. Different initiation.
CR456525 mRNA. Translation: CAG30411.1.
CH471095 Genomic DNA. Translation: EAW59852.1.
CH471095 Genomic DNA. Translation: EAW59855.1.
BC142713 mRNA. Translation: AAI42714.1.
BC148216 mRNA. Translation: AAI48217.1.
BC152455 mRNA. Translation: AAI52456.1.
AC003071 Genomic DNA. Translation: AAB83949.1.
U58034 Genomic DNA. Translation: AAC79119.1.
CCDSiCCDS13870.1. [Q13615-1]
CCDS13871.1. [Q13615-2]
CCDS46682.1. [Q13615-3]
RefSeqiNP_066576.1. NM_021090.3. [Q13615-1]
NP_694690.1. NM_153050.2. [Q13615-2]
NP_694691.1. NM_153051.2. [Q13615-3]
UniGeneiHs.474536.

Genome annotation databases

EnsembliENST00000333027; ENSP00000331649; ENSG00000100330. [Q13615-2]
ENST00000351488; ENSP00000307271; ENSG00000100330. [Q13615-3]
ENST00000401950; ENSP00000384651; ENSG00000100330. [Q13615-1]
ENST00000406629; ENSP00000384077; ENSG00000100330. [Q13615-2]
GeneIDi8897.
KEGGihsa:8897.
UCSCiuc003agu.4. human. [Q13615-2]
uc003agv.4. human. [Q13615-1]
uc003agw.4. human. [Q13615-3]

Polymorphism databases

DMDMi33112668.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF233436 mRNA. Translation: AAF40203.2.
AF233437 mRNA. Translation: AAF40204.1.
AF233438 mRNA. Translation: AAF40205.1.
AB002369 mRNA. Translation: BAA20826.2. Different initiation.
CR456525 mRNA. Translation: CAG30411.1.
CH471095 Genomic DNA. Translation: EAW59852.1.
CH471095 Genomic DNA. Translation: EAW59855.1.
BC142713 mRNA. Translation: AAI42714.1.
BC148216 mRNA. Translation: AAI48217.1.
BC152455 mRNA. Translation: AAI52456.1.
AC003071 Genomic DNA. Translation: AAB83949.1.
U58034 Genomic DNA. Translation: AAC79119.1.
CCDSiCCDS13870.1. [Q13615-1]
CCDS13871.1. [Q13615-2]
CCDS46682.1. [Q13615-3]
RefSeqiNP_066576.1. NM_021090.3. [Q13615-1]
NP_694690.1. NM_153050.2. [Q13615-2]
NP_694691.1. NM_153051.2. [Q13615-3]
UniGeneiHs.474536.

3D structure databases

ProteinModelPortaliQ13615.
SMRiQ13615. Positions 53-577, 1125-1175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114414. 6 interactions.
IntActiQ13615. 6 interactions.
STRINGi9606.ENSP00000384651.

PTM databases

DEPODiQ13615.
PhosphoSiteiQ13615.

Polymorphism databases

DMDMi33112668.

Proteomic databases

MaxQBiQ13615.
PaxDbiQ13615.
PRIDEiQ13615.

Protocols and materials databases

DNASUi8897.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333027; ENSP00000331649; ENSG00000100330. [Q13615-2]
ENST00000351488; ENSP00000307271; ENSG00000100330. [Q13615-3]
ENST00000401950; ENSP00000384651; ENSG00000100330. [Q13615-1]
ENST00000406629; ENSP00000384077; ENSG00000100330. [Q13615-2]
GeneIDi8897.
KEGGihsa:8897.
UCSCiuc003agu.4. human. [Q13615-2]
uc003agv.4. human. [Q13615-1]
uc003agw.4. human. [Q13615-3]

Organism-specific databases

CTDi8897.
GeneCardsiGC22P030279.
HGNCiHGNC:7451. MTMR3.
HPAiHPA034515.
HPA034516.
MIMi603558. gene.
neXtProtiNX_Q13615.
PharmGKBiPA31254.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG322789.
GeneTreeiENSGT00760000118832.
HOVERGENiHBG052526.
InParanoidiQ13615.
KOiK18082.
OMAiTDTIQQR.
OrthoDBiEOG7PVWNJ.
PhylomeDBiQ13615.
TreeFamiTF315197.

Enzyme and pathway databases

BioCyciMetaCyc:HS02045-MONOMER.
ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.

Miscellaneous databases

ChiTaRSiMTMR3. human.
GeneWikiiMTMR3.
GenomeRNAii8897.
NextBioi33415.
PROiQ13615.
SOURCEiSearch...

Gene expression databases

BgeeiQ13615.
CleanExiHS_MTMR3.
ExpressionAtlasiQ13615. baseline and differential.
GenevestigatoriQ13615.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR010569. Myotubularin-like_Pase_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF06602. Myotub-related. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 2 hits.
SSF57903. SSF57903. 1 hit.
PROSITEiPS51339. PPASE_MYOTUBULARIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "FYVE-DSP1, a dual-specificity protein phosphatase containing an FYVE domain."
    Zhao R., Qi Y., Zhao Z.J.
    Biochem. Biophys. Res. Commun. 270:222-229(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS A; B AND C), CHARACTERIZATION, CATALYTIC ACTIVITY, FUNCTION.
  2. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
  4. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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] (ISOFORMS B AND C).
  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 OF 374-578.
  8. "A gene mutated in X-linked myotubular myopathy defines a new putative tyrosine phosphatase family conserved in yeast."
    Laporte J., Hu L.-J., Kretz C., Mandel J.-L., Kioschis P., Coy J., Klauck S.M., Poutska A., Dahl N.
    Nat. Genet. 13:175-182(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 381-463.
  9. "Characterization of MTMR3. an inositol lipid 3-phosphatase with novel substrate specificity."
    Walker D.M., Urbe S., Dove S.K., Tenza D., Raposo G., Clague M.J.
    Curr. Biol. 11:1600-1605(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-413, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-647, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-633; SER-647 AND THR-731, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-221.

Entry informationi

Entry nameiMTMR3_HUMAN
AccessioniPrimary (citable) accession number: Q13615
Secondary accession number(s): A5PL26
, A7MD32, Q9NYN5, Q9NYN6, Q9UDX6, Q9UEG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 19, 2003
Last modified: February 4, 2015
This is version 141 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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.