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Q13615 (MTMR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myotubularin-related protein 3

EC=3.1.3.48
Alternative name(s):
FYVE domain-containing dual specificity protein phosphatase 1
Short name=FYVE-DSP1
Zinc finger FYVE domain-containing protein 10
Gene names
Name:MTMR3
Synonyms:KIAA0371, ZFYVE10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1198 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class myotubularin subfamily.

Contains 1 FYVE-type zinc finger.

Contains 1 myotubularin phosphatase domain.

Sequence caution

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: Q13615-1)

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.
Isoform A (identifier: Q13615-2)

Also known as: FYVE-DSP1a;

The sequence of this isoform differs from the canonical sequence as follows:
     1076-1112: Missing.
     1142-1142: R → RDTDRVDQTW
Isoform C (identifier: Q13615-3)

Also known as: FYVE-DSP1c;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11981198Myotubularin-related protein 3
PRO_0000094936

Regions

Domain155 – 576422Myotubularin phosphatase
Zinc finger1119 – 117961FYVE-type
Region326 – 3294Substrate binding By similarity
Region351 – 3522Substrate binding By similarity
Region413 – 4197Substrate binding By similarity
Coiled coil1029 – 106234 Potential

Sites

Active site4131Phosphocysteine intermediate By similarity
Binding site4591Substrate By similarity

Amino acid modifications

Modified residue6331Phosphoserine Ref.11
Modified residue6471Phosphoserine Ref.10 Ref.11
Modified residue7311Phosphothreonine Ref.11

Natural variations

Alternative sequence1076 – 111237Missing in isoform A and isoform C.
VSP_007781
Alternative sequence11421R → RDTDRVDQTW in isoform A.
VSP_007782
Natural variant2211V → L in a breast cancer sample; somatic mutation. Ref.13
VAR_035656

Experimental info

Mutagenesis4131C → S: Loss of activity. Ref.9
Sequence conflict560 – 57819LYPVC…AVYLP → CILQPFHCGQQKEFGVGYI Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform B (FYVE-DSP1b) [UniParc].

Last modified July 19, 2003. Version 3.
Checksum: FE6F4B165074D5F8

FASTA1,198133,619
        10         20         30         40         50         60 
MDEETRHSLE CIQANQIFPR KQLIREDENL QVPFLELHGE STEFVGRAED AIIALSNYRL 

        70         80         90        100        110        120 
HIKFKESLVN VPLQLIESVE CRDIFQLHLT CKDCKVIRCQ FSTFEQCQEW LKRLNNAIRP 

       130        140        150        160        170        180 
PAKIEDLFSF AYHAWCMEVY ASEKEQHGDL CRPGEHVTSR FKNEVERMGF DMNNAWRISN 

       190        200        210        220        230        240 
INEKYKLCGS YPQELIVPAW ITDKELESVS SFRSWKRIPA VIYRHQSNGA VIARCGQPEV 

       250        260        270        280        290        300 
SWWGWRNADD EHLVQSVAKA CASDSRSSGS KLSTRNTSRD FPNGGDLSDV EFDSSLSNAS 

       310        320        330        340        350        360 
GAESLAIQPQ KLLILDARSY AAAVANRAKG GGCECPEYYP NCEVVFMGMA NIHSIRRSFQ 

       370        380        390        400        410        420 
SLRLLCTQMP DPGNWLSALE STKWLHHLSV LLKSALLVVH AVDQDQRPVL VHCSDGWDRT 

       430        440        450        460        470        480 
PQIVALAKLL LDPYYRTIEG FQVLVEMEWL DFGHKFADRC GHGENSDDLN ERCPVFLQWL 

       490        500        510        520        530        540 
DCVHQLQRQF PCSFEFNEAF LVKLVQHTYS CLFGTFLCNN AKERGEKHTQ ERTCSVWSLL 

       550        560        570        580        590        600 
RAGNKAFKNL LYSSQSEAVL YPVCHVRNLM LWSAVYLPCP SPTTPVDDSC APYPAPGTSP 

       610        620        630        640        650        660 
DDPPLSRLPK TRSYDNLTTA CDNTVPLASR RCSDPSLNEK WQEHRRSLEL SSLAGPGEDP 

       670        680        690        700        710        720 
LSADSLGKPT RVPGGAELSV AAGVAEGQME NILQEATKEE SGVEEPAHRA GIEIQEGKED 

       730        740        750        760        770        780 
PLLEKESRRK TPEASAIGLH QDPELGDAAL RSHLDMSWPL FSQGISEQQS GLSVLLSSLQ 

       790        800        810        820        830        840 
VPPRGEDSLE VPVEQFRIEE IAEGREEAVL PIPVDAKVGY GTSQSCSLLP SQVPFETRGP 

       850        860        870        880        890        900 
NVDSSTDMLV EDKVKSVSGP QGHHRSCLVN SGKDRLPQTM EPSPSETSLV ERPQVGSVVH 

       910        920        930        940        950        960 
RTSLGSTLSL TRSPCALPLA ECKEGLVCNG APETENRASE QPPGLSTLQM YPTPNGHCAN 

       970        980        990       1000       1010       1020 
GEAGRSKDSL SRQLSAMSCS SAHLHSRNLH HKWLHSHSGR PSATSSPDQP SRSHLDDDGM 

      1030       1040       1050       1060       1070       1080 
SVYTDTIQQR LRQIESGHQQ EVETLKKQVQ ELKSRLESQY LTSSLHFNGD FGDEVTSIPD 

      1090       1100       1110       1120       1130       1140 
SESNLDQNCL SRCSTEIFSE ASWEQVDKQD TEMTRWLPDH LAAHCYACDS AFWLASRKHH 

      1150       1160       1170       1180       1190 
CRNCGNVFCS SCCNQKVPVP SQQLFEPSRV CKSCYSSLHP TSSSIDLELD KPIAATSN 

« Hide

Isoform A (FYVE-DSP1a) [UniParc].

Checksum: B51B10E3E7245433
Show »

FASTA1,170130,561
Isoform C (FYVE-DSP1c) [UniParc].

Checksum: 18C795D42EFB1177
Show »

FASTA1,161129,444

References

« Hide 'large scale' references
[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.
[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]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-221.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_066576.1. NM_021090.3.
NP_694690.1. NM_153050.2.
NP_694691.1. NM_153051.2.
UniGeneHs.474536.

3D structure databases

ProteinModelPortalQ13615.
SMRQ13615. Positions 53-577, 1125-1175.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114414. 3 interactions.
IntActQ13615. 6 interactions.
STRING9606.ENSP00000384651.

PTM databases

PhosphoSiteQ13615.

Polymorphism databases

DMDM33112668.

Proteomic databases

PaxDbQ13615.
PRIDEQ13615.

Protocols and materials databases

DNASU8897.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000333027; ENSP00000331649; ENSG00000100330. [Q13615-2]
ENST00000351488; ENSP00000307271; ENSG00000100330. [Q13615-3]
ENST00000401950; ENSP00000384651; ENSG00000100330. [Q13615-1]
ENST00000406629; ENSP00000384077; ENSG00000100330. [Q13615-2]
GeneID8897.
KEGGhsa:8897.
UCSCuc003agu.4. human. [Q13615-2]
uc003agv.4. human. [Q13615-1]
uc003agw.4. human. [Q13615-3]

Organism-specific databases

CTD8897.
GeneCardsGC22P030279.
HGNCHGNC:7451. MTMR3.
HPAHPA034515.
HPA034516.
MIM603558. gene.
neXtProtNX_Q13615.
PharmGKBPA31254.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG322789.
HOVERGENHBG052526.
InParanoidQ13615.
KOK01104.
OMATDTIQQR.
OrthoDBEOG7PVWNJ.
PhylomeDBQ13615.
TreeFamTF315197.

Enzyme and pathway databases

BioCycMetaCyc:HS02045-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ13615.
BgeeQ13615.
CleanExHS_MTMR3.
GenevestigatorQ13615.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR010569. Myotubularin-like_Pase_dom.
IPR016130. Tyr_Pase_AS.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF01363. FYVE. 1 hit.
PF06602. Myotub-related. 1 hit.
[Graphical view]
SMARTSM00064. FYVE. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS51339. PPASE_MYOTUBULARIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMTMR3. human.
GeneWikiMTMR3.
GenomeRNAi8897.
NextBio33415.
PROQ13615.
SOURCESearch...

Entry information

Entry nameMTMR3_HUMAN
AccessionPrimary (citable) accession number: Q13615
Secondary accession number(s): A5PL26 expand/collapse secondary AC list , A7MD32, Q9NYN5, Q9NYN6, Q9UDX6, Q9UEG3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 19, 2003
Last modified: April 16, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM