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Q13615

- MTMR3_HUMAN

UniProt

Q13615 - MTMR3_HUMAN

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Protein
Myotubularin-related protein 3
Gene
MTMR3, KIAA0371, ZFYVE10
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. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate. May also dephosphorylate proteins phosphorylated on Ser, Thr, and Tyr residues.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei413 – 4131Phosphocysteine intermediate By similarity
Binding sitei459 – 4591Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1119 – 117961FYVE-type
Add
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphatidylinositol-3-phosphatase activity Source: UniProtKB
  3. protein serine/threonine phosphatase activity Source: UniProtKB
  4. 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 - 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:3.1.3.48)
Alternative name(s):
FYVE domain-containing dual specificity protein phosphatase 1
Short name:
FYVE-DSP1
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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. membrane Source: UniProtKB
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

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

Organism-specific databases

PharmGKBiPA31254.

PTM / Processingi

Molecule processing

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

PhosphoSiteiQ13615.

Expressioni

Gene expression databases

ArrayExpressiQ13615.
BgeeiQ13615.
CleanExiHS_MTMR3.
GenevestigatoriQ13615.

Organism-specific databases

HPAiHPA034515.
HPA034516.

Interactioni

Protein-protein interaction databases

BioGridi114414. 3 interactions.
IntActiQ13615. 6 interactions.
STRINGi9606.ENSP00000384651.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini155 – 576422Myotubularin phosphatase
Add
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1029 – 106234 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG322789.
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

MDEETRHSLE CIQANQIFPR KQLIREDENL QVPFLELHGE STEFVGRAED     50
AIIALSNYRL HIKFKESLVN VPLQLIESVE CRDIFQLHLT CKDCKVIRCQ 100
FSTFEQCQEW LKRLNNAIRP PAKIEDLFSF AYHAWCMEVY ASEKEQHGDL 150
CRPGEHVTSR FKNEVERMGF DMNNAWRISN INEKYKLCGS YPQELIVPAW 200
ITDKELESVS SFRSWKRIPA VIYRHQSNGA VIARCGQPEV SWWGWRNADD 250
EHLVQSVAKA CASDSRSSGS KLSTRNTSRD FPNGGDLSDV EFDSSLSNAS 300
GAESLAIQPQ KLLILDARSY AAAVANRAKG GGCECPEYYP NCEVVFMGMA 350
NIHSIRRSFQ SLRLLCTQMP DPGNWLSALE STKWLHHLSV LLKSALLVVH 400
AVDQDQRPVL VHCSDGWDRT PQIVALAKLL LDPYYRTIEG FQVLVEMEWL 450
DFGHKFADRC GHGENSDDLN ERCPVFLQWL DCVHQLQRQF PCSFEFNEAF 500
LVKLVQHTYS CLFGTFLCNN AKERGEKHTQ ERTCSVWSLL RAGNKAFKNL 550
LYSSQSEAVL YPVCHVRNLM LWSAVYLPCP SPTTPVDDSC APYPAPGTSP 600
DDPPLSRLPK TRSYDNLTTA CDNTVPLASR RCSDPSLNEK WQEHRRSLEL 650
SSLAGPGEDP LSADSLGKPT RVPGGAELSV AAGVAEGQME NILQEATKEE 700
SGVEEPAHRA GIEIQEGKED PLLEKESRRK TPEASAIGLH QDPELGDAAL 750
RSHLDMSWPL FSQGISEQQS GLSVLLSSLQ VPPRGEDSLE VPVEQFRIEE 800
IAEGREEAVL PIPVDAKVGY GTSQSCSLLP SQVPFETRGP NVDSSTDMLV 850
EDKVKSVSGP QGHHRSCLVN SGKDRLPQTM EPSPSETSLV ERPQVGSVVH 900
RTSLGSTLSL TRSPCALPLA ECKEGLVCNG APETENRASE QPPGLSTLQM 950
YPTPNGHCAN GEAGRSKDSL SRQLSAMSCS SAHLHSRNLH HKWLHSHSGR 1000
PSATSSPDQP SRSHLDDDGM SVYTDTIQQR LRQIESGHQQ EVETLKKQVQ 1050
ELKSRLESQY LTSSLHFNGD FGDEVTSIPD SESNLDQNCL SRCSTEIFSE 1100
ASWEQVDKQD TEMTRWLPDH LAAHCYACDS AFWLASRKHH CRNCGNVFCS 1150
SCCNQKVPVP SQQLFEPSRV CKSCYSSLHP TSSSIDLELD KPIAATSN 1198
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.

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.
VSP_007781Add
BLAST
Alternative sequencei1142 – 11421R → RDTDRVDQTW in isoform A.
VSP_007782

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti560 – 57819LYPVC…AVYLP → CILQPFHCGQQKEFGVGYI1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS13870.1. [Q13615-1 ]
CCDS13871.1. [Q13615-2 ]
CCDS46682.1. [Q13615-3 ]
RefSeqi NP_066576.1. NM_021090.3. [Q13615-1 ]
NP_694690.1. NM_153050.2. [Q13615-2 ]
NP_694691.1. NM_153051.2. [Q13615-3 ]
UniGenei Hs.474536.

3D structure databases

ProteinModelPortali Q13615.
SMRi Q13615. Positions 53-577, 1125-1175.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114414. 3 interactions.
IntActi Q13615. 6 interactions.
STRINGi 9606.ENSP00000384651.

PTM databases

PhosphoSitei Q13615.

Polymorphism databases

DMDMi 33112668.

Proteomic databases

MaxQBi Q13615.
PaxDbi Q13615.
PRIDEi Q13615.

Protocols and materials databases

DNASUi 8897.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000333027 ; ENSP00000331649 ; ENSG00000100330 . [Q13615-2 ]
ENST00000351488 ; ENSP00000307271 ; ENSG00000100330 . [Q13615-3 ]
ENST00000401950 ; ENSP00000384651 ; ENSG00000100330 . [Q13615-1 ]
ENST00000406629 ; ENSP00000384077 ; ENSG00000100330 . [Q13615-2 ]
GeneIDi 8897.
KEGGi hsa:8897.
UCSCi uc003agu.4. human. [Q13615-2 ]
uc003agv.4. human. [Q13615-1 ]
uc003agw.4. human. [Q13615-3 ]

Organism-specific databases

CTDi 8897.
GeneCardsi GC22P030279.
HGNCi HGNC:7451. MTMR3.
HPAi HPA034515.
HPA034516.
MIMi 603558. gene.
neXtProti NX_Q13615.
PharmGKBi PA31254.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG322789.
HOVERGENi HBG052526.
InParanoidi Q13615.
KOi K18082.
OMAi TDTIQQR.
OrthoDBi EOG7PVWNJ.
PhylomeDBi Q13615.
TreeFami TF315197.

Enzyme and pathway databases

BioCyci MetaCyc:HS02045-MONOMER.
Reactomei REACT_121025. Synthesis of PIPs at the plasma membrane.

Miscellaneous databases

ChiTaRSi MTMR3. human.
GeneWikii MTMR3.
GenomeRNAii 8897.
NextBioi 33415.
PROi Q13615.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13615.
Bgeei Q13615.
CleanExi HS_MTMR3.
Genevestigatori Q13615.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR010569. 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 ]
Pfami PF01363. FYVE. 1 hit.
PF06602. Myotub-related. 1 hit.
[Graphical view ]
SMARTi SM00064. FYVE. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 2 hits.
SSF57903. SSF57903. 1 hit.
PROSITEi PS51339. PPASE_MYOTUBULARIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.
  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.
  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: September 3, 2014
This is version 137 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