Q8NCE2 (MTMRE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	650 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
Molecular function	Hydrolase
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC phosphatidylinositol biosynthetic process Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome perinuclear region of cytoplasm Inferred from direct assay Ref.6. Source: UniProtKB ruffle Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	phosphatidylinositol-3-phosphatase activity Inferred from direct assay Ref.6. Source: UniProtKB protein tyrosine phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 650	650	Myotubularin-related protein 14		PRO_0000260214
Regions
	Compositional bias	512 – 518	7	Poly-Ser
Amino acid modifications
	Modified residue	194	1	N6-acetyllysine Ref.9
	Modified residue	580	1	Phosphoserine Ref.7
	Glycosylation	226	1	N-linked (GlcNAc...) Potential
	Glycosylation	519	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	479 – 538	60	Missing in isoform 3.		VSP_021585
	Alternative sequence	539 – 590	52	Missing in isoform 2 and isoform 3.		VSP_021586
	Natural variant	336	1	R → Q in CNM1; may act as a phenotype modifier; drastically reduced enzymatic activity. Ref.6 Corresponds to variant rs121434509 [ dbSNP | Ensembl ].		VAR_033370
	Natural variant	462	1	Y → 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
	Mutagenesis	330	1	C → S: Drastically reduced enzymatic activity. Ref.6
	Sequence conflict	28	1	G → R in CAL38187. Ref.3
	Sequence conflict	55	1	E → G in CAL37928. Ref.3
	Sequence conflict	126	1	R → G in CAL38187. Ref.3
	Sequence conflict	390	1	F → S in BAC11211. Ref.2
	Sequence conflict	403 – 406	4	EEFS → ALFA in AAS50151. Ref.5
	Sequence conflict	554 – 557	4	GSWQ → AAGM in AAS50151. Ref.5
	Sequence conflict	646	1	S → N in CAL37928. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 28, 2006. Version 2. Checksum: C1B70E5140EF0716	FASTA	650	72,203
	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
	Isoform 2 [UniParc]. Checksum: FC7244F7B81672CC	FASTA	598	66,654
	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 PLEVPKPRLA 550 560 570 580 590 ALSDRETRLQ EVRSAFLAAY SSTVGLRAVA PSPSGAIGGL LEQFARGVGL RSISSNAL
	Isoform 3 [UniParc]. Checksum: 6EA5D5AC9EE34FB0	FASTA	538	60,035
	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 GAPTQAAWLA 490 500 510 520 530 ALSDRETRLQ EVRSAFLAAY SSTVGLRAVA PSPSGAIGGL LEQFARGVGL RSISSNAL

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.
IPI	IPI00152391. IPI00168378. IPI00384329.
RefSeq	NP_001070993.1. NM_001077525.2. NP_001070994.1. NM_001077526.2. NP_071930.2. NM_022485.4.
UniGene	Hs.475382.
3D structure databases
ProteinModelPortal	Q8NCE2.
SMR	Q8NCE2. Positions 302-386.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8NCE2. 1 interaction.
PTM databases
PhosphoSite	Q8NCE2.
Polymorphism databases
DMDM	118568016.
Proteomic databases
PaxDb	Q8NCE2.
PRIDE	Q8NCE2.
Protocols and materials databases
DNASU	64419.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000296003; ENSP00000296003; ENSG00000163719. ENST00000351233; ENSP00000334070; ENSG00000163719. ENST00000353332; ENSP00000323462; ENSG00000163719.
GeneID	64419.
KEGG	hsa:64419.
UCSC	uc003brz.3. human. uc003bsa.3. human. uc003bsb.3. human.
Organism-specific databases
CTD	64419.
GeneCards	GC03P009691.
HGNC	HGNC:26190. MTMR14.
MIM	160150. phenotype. 611089. gene.
neXtProt	NX_Q8NCE2.
Orphanet	169189. Autosomal dominant centronuclear myopathy.
PharmGKB	PA162396265.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG84393.
HOVERGEN	HBG062969.
InParanoid	Q8NCE2.
OMA	GRTGYNY.
PhylomeDB	Q8NCE2.
Enzyme and pathway databases
BioCyc	MetaCyc:HS08920-MONOMER.
BRENDA	3.1.3.64. 2681.
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q8NCE2.
Bgee	Q8NCE2.
Genevestigator	Q8NCE2.
GermOnline	ENSG00000163719. Homo sapiens.
Family and domain databases
InterPro	IPR016130. Tyr_Pase_AS. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	64419.
NextBio	66391.
SOURCE	Search...

Entry information

Entry name

MTMRE_HUMAN

Accession

Primary (citable) accession number: Q8NCE2
Secondary accession number(s): Q0JTH5 , 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:	May 1, 2013
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.