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Q8NCE2 (MTMRE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. 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 14

EC=3.1.3.-
Alternative name(s):
HCV NS5A-transactivated protein 4 splice variant A-binding protein 1
Short name=NS5ATP4ABP1
hJumpy
Gene names
Name:MTMR14
Synonyms:C3orf29
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length650 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Lipid phosphatase which efficiently dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P) and PtdIns(3,5)P2; inactive toward PtdIns4P, PtdIns(3,4)P2, PtdIns(4,5)P2 and PtdIns(3,4,5)P3. Ref.6

Subcellular location

Cytoplasm. Note: Found in reticular structures and plasma membrane ruffles. Concentrated near the nucleus. Ref.6

Tissue specificity

Expressed in various tissues, including heart, skeletal muscle, placenta, liver, lung, kidney and pancreas. Ref.6

Involvement in disease

Myopathy, centronuclear, 1 (CNM1) [MIM:160150]: A congenital muscle disorder characterized by progressive muscular weakness and wasting involving mainly limb girdle, trunk, and neck muscles. It may also affect distal muscles. Weakness may be present during childhood or adolescence or may not become evident until the third decade of life. Ptosis is a frequent clinical feature. The most prominent histopathologic features include high frequency of centrally located nuclei in muscle fibers not secondary to regeneration, radial arrangement of sarcoplasmic strands around the central nuclei, and predominance and hypotrophy of type 1 fibers.
Note: The gene represented in this entry may act as a disease modifier. MTMR14 mutations affecting enzymatic function have been found in sporadic cases of centronuclear myopathy, one of them carrying a disease-associated mutation in DNM2 (Ref.6). This raises the possibility of MTMR14 being a modifier of the phenotype in some cases of centronuclear myopathy (Ref.6). Ref.6

Sequence similarities

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

Sequence caution

The sequence BAB15340.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NCE2-1)

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 2 (identifier: Q8NCE2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     539-590: Missing.
Isoform 3 (identifier: Q8NCE2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     479-538: Missing.
     539-590: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 650650Myotubularin-related protein 14
PRO_0000260214

Regions

Compositional bias512 – 5187Poly-Ser

Sites

Active site3301Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue1941N6-acetyllysine Ref.9
Modified residue5801Phosphoserine Ref.7
Glycosylation2261N-linked (GlcNAc...) Potential
Glycosylation5191N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence479 – 53860Missing in isoform 3.
VSP_021585
Alternative sequence539 – 59052Missing in isoform 2 and isoform 3.
VSP_021586
Natural variant3361R → Q in CNM1; may act as a phenotype modifier; drastically reduced enzymatic activity. Ref.6
Corresponds to variant rs121434509 [ dbSNP | Ensembl ].
VAR_033370
Natural variant4621Y → C in CNM1; may act as a disease modifier; mutation found in a patient also carrying mutation Lys-368 in DNM2; reduced enzymatic activity. Ref.6
Corresponds to variant rs121434510 [ dbSNP | Ensembl ].
VAR_033371

Experimental info

Mutagenesis3301C → S: Drastically reduced enzymatic activity. Ref.6
Sequence conflict281G → R in CAL38187. Ref.3
Sequence conflict551E → G in CAL37928. Ref.3
Sequence conflict1261R → G in CAL38187. Ref.3
Sequence conflict3901F → S in BAC11211. Ref.2
Sequence conflict403 – 4064EEFS → ALFA in AAS50151. Ref.5
Sequence conflict554 – 5574GSWQ → AAGM in AAS50151. Ref.5
Sequence conflict6461S → N in CAL37928. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 28, 2006. Version 2.
Checksum: C1B70E5140EF0716

FASTA65072,203
        10         20         30         40         50         60 
MAGARAAAAA ASAGSSASSG NQPPQELGLG ELLEEFSRTQ YRAKDGSGTG GSKVERIEKR 

        70         80         90        100        110        120 
CLELFGRDYC FSVIPNTNGD ICGHYPRHIV FLEYESSEKE KDTFESTVQV SKLQDLIHRS 

       130        140        150        160        170        180 
KMARCRGRFV CPVILFKGKH ICRSATLAGW GELYGRSGYN YFFSGGADDA WADVEDVTEE 

       190        200        210        220        230        240 
DCALRSGDTH LFDKVRGYDI KLLRYLSVKY ICDLMVENKK VKFGMNVTSS EKVDKAQRYA 

       250        260        270        280        290        300 
DFTLLSIPYP GCEFFKEYKD RDYMAEGLIF NWKQDYVDAP LSIPDFLTHS LNIDWSQYQC 

       310        320        330        340        350        360 
WDLVQQTQNY LKLLLSLVNS DDDSGLLVHC ISGWDRTPLF ISLLRLSLWA DGLIHTSLKP 

       370        380        390        400        410        420 
TEILYLTVAY DWFLFGHMLV DRLSKGEEIF FFCFNFLKHI TSEEFSALKT QRRKSLPARD 

       430        440        450        460        470        480 
GGFTLEDICM LRRKDRGSTT SLGSDFSLVM ESSPGATGSF TYEAVELVPA GAPTQAAWRK 

       490        500        510        520        530        540 
SHSSSPQSVL WNRPQPSEDR LPSQQGLAEA RSSSSSSSNH SDNFFRMGSS PLEVPKPRSV 

       550        560        570        580        590        600 
DHPLPGSSLS TDYGSWQMVT GCGSIQERAV LHTDSSLPFS FPDELPNSCL LAALSDRETR 

       610        620        630        640        650 
LQEVRSAFLA AYSSTVGLRA VAPSPSGAIG GLLEQFARGV GLRSISSNAL 

« Hide

Isoform 2 [UniParc].

Checksum: FC7244F7B81672CC
Show »

FASTA59866,654
Isoform 3 [UniParc].

Checksum: 6EA5D5AC9EE34FB0
Show »

FASTA53860,035

References

« Hide 'large scale' references
[1]"Screening and cloning of interaction protein 1 of HCV NS5A-transactivated protein 4 splice variant A."
Chen L.D., Cheng J., Wang Q., Hong Y., Zhang L.F., Han L., Yuan J.
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"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. expand/collapse author list , 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 3).
Tissue: Kidney epithelium and Teratocarcinoma.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[4]"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 1; 2 AND 3).
Tissue: Duodenal adenocarcinoma, Leukocyte, Retinal pigment epithelium and Rhabdomyosarcoma.
[5]Sales M.M., Ferrasi A.C., Pereira A.A., Pardini M.I.M.C., Sogayar M.C., Camargo A.A.
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 403-557 (ISOFORM 1).
Tissue: Melanoma.
[6]"A novel PtdIns3P and PtdIns(3,5)P2 phosphatase with an inactivating variant in centronuclear myopathy."
Tosch V., Rohde H.M., Tronchere H., Zanoteli E., Monroy N., Kretz C., Dondaine N., Payrastre B., Mandel J.-L., Laporte J.
Hum. Mol. Genet. 15:3098-3106(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INVOLVEMENT IN CNM1 AS MODIFIER OF PHENOTYPE, VARIANTS CNM1 GLN-336 AND CYS-462, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-330.
[7]"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-580, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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.
[9]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ630520 mRNA. Translation: ABG02221.1.
AK026058 mRNA. Translation: BAB15340.1. Different initiation.
AK074792 mRNA. Translation: BAC11211.1.
AL713695 mRNA. Translation: CAD28494.1.
AM393309 mRNA. Translation: CAL38187.1.
AM393050 mRNA. Translation: CAL37928.1.
BC001674 mRNA. Translation: AAH01674.2.
BC025952 mRNA. Translation: AAH25952.2.
BC035690 mRNA. Translation: AAH35690.1.
BC050626 mRNA. Translation: AAH50626.1.
AY545552 mRNA. Translation: AAS50151.1.
CCDSCCDS43043.1. [Q8NCE2-1]
CCDS43044.1. [Q8NCE2-2]
CCDS43045.1. [Q8NCE2-3]
RefSeqNP_001070993.1. NM_001077525.2. [Q8NCE2-1]
NP_001070994.1. NM_001077526.2. [Q8NCE2-2]
NP_071930.2. NM_022485.4. [Q8NCE2-3]
UniGeneHs.475382.

3D structure databases

ProteinModelPortalQ8NCE2.
SMRQ8NCE2. Positions 303-386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122168. 2 interactions.
IntActQ8NCE2. 4 interactions.
MINTMINT-3042111.

PTM databases

PhosphoSiteQ8NCE2.

Polymorphism databases

DMDM118568016.

Proteomic databases

MaxQBQ8NCE2.
PaxDbQ8NCE2.
PRIDEQ8NCE2.

Protocols and materials databases

DNASU64419.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296003; ENSP00000296003; ENSG00000163719. [Q8NCE2-1]
ENST00000351233; ENSP00000334070; ENSG00000163719. [Q8NCE2-3]
ENST00000353332; ENSP00000323462; ENSG00000163719. [Q8NCE2-2]
GeneID64419.
KEGGhsa:64419.
UCSCuc003brz.3. human. [Q8NCE2-1]
uc003bsa.3. human. [Q8NCE2-2]
uc003bsb.3. human. [Q8NCE2-3]

Organism-specific databases

CTD64419.
GeneCardsGC03P009691.
HGNCHGNC:26190. MTMR14.
HPAHPA054063.
MIM160150. phenotype.
611089. gene.
neXtProtNX_Q8NCE2.
Orphanet169189. Autosomal dominant centronuclear myopathy.
PharmGKBPA162396265.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG84393.
HOVERGENHBG062969.
InParanoidQ8NCE2.
KOK18086.
OMADTHLFDK.
OrthoDBEOG73BVC8.
PhylomeDBQ8NCE2.
TreeFamTF324044.

Enzyme and pathway databases

BioCycMetaCyc:HS08920-MONOMER.
BRENDA3.1.3.64. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ8NCE2.
BgeeQ8NCE2.
GenevestigatorQ8NCE2.

Family and domain databases

Gene3D3.90.190.10. 2 hits.
InterProIPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
[Graphical view]
SUPFAMSSF52799. SSF52799. 2 hits.
ProtoNetSearch...

Other

GeneWikiMTMR14.
GenomeRNAi64419.
NextBio66391.
PROQ8NCE2.
SOURCESearch...

Entry information

Entry nameMTMRE_HUMAN
AccessionPrimary (citable) accession number: Q8NCE2
Secondary accession number(s): Q0JTH5 expand/collapse secondary AC list , Q0JU83, Q6PIZ4, Q6QE21, Q86VK9, Q8IYK1, Q8TCM7, Q9H6C0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: July 9, 2014
This is version 94 of the entry and version 2 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 3

Human chromosome 3: entries, gene names and cross-references to MIM