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Q8NCE2

- MTMRE_HUMAN

UniProt

Q8NCE2 - MTMRE_HUMAN

Protein

Myotubularin-related protein 14

Gene

MTMR14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 2 (28 Nov 2006)
      Previous versions | rss
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    Functioni

    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)P3.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei330 – 3301Phosphocysteine intermediateBy similarity

    GO - Molecular functioni

    1. phosphatidylinositol-3-phosphatase activity Source: UniProtKB
    2. protein tyrosine phosphatase activity Source: InterPro

    GO - Biological processi

    1. phosphatidylinositol biosynthetic process Source: Reactome
    2. phospholipid metabolic process Source: Reactome
    3. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08920-MONOMER.
    BRENDAi3.1.3.64. 2681.
    ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:MTMR14
    Synonyms:C3orf29
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:26190. MTMR14.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Found in reticular structures and plasma membrane ruffles. Concentrated near the nucleus.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. perinuclear region of cytoplasm Source: UniProtKB
    3. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    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 (PubMed:17008356). This raises the possibility of MTMR14 being a modifier of the phenotype in some cases of centronuclear myopathy (PubMed:17008356).1 Publication
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti336 – 3361R → Q in CNM1; may act as a phenotype modifier; drastically reduced enzymatic activity. 1 Publication
    Corresponds to variant rs121434509 [ dbSNP | Ensembl ].
    VAR_033370
    Natural varianti462 – 4621Y → C in CNM1; may act as a disease modifier; mutation found in a patient also carrying mutation Lys-368 in DNM2; reduced enzymatic activity. 1 Publication
    Corresponds to variant rs121434510 [ dbSNP | Ensembl ].
    VAR_033371

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi330 – 3301C → S: Drastically reduced enzymatic activity. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi160150. phenotype.
    Orphaneti169189. Autosomal dominant centronuclear myopathy.
    PharmGKBiPA162396265.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 650650Myotubularin-related protein 14PRO_0000260214Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei194 – 1941N6-acetyllysine1 Publication
    Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi519 – 5191N-linked (GlcNAc...)Sequence Analysis
    Modified residuei580 – 5801Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ8NCE2.
    PaxDbiQ8NCE2.
    PRIDEiQ8NCE2.

    PTM databases

    PhosphoSiteiQ8NCE2.

    Expressioni

    Tissue specificityi

    Expressed in various tissues, including heart, skeletal muscle, placenta, liver, lung, kidney and pancreas.1 Publication

    Gene expression databases

    ArrayExpressiQ8NCE2.
    BgeeiQ8NCE2.
    GenevestigatoriQ8NCE2.

    Organism-specific databases

    HPAiHPA054063.

    Interactioni

    Protein-protein interaction databases

    BioGridi122168. 2 interactions.
    IntActiQ8NCE2. 4 interactions.
    MINTiMINT-3042111.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8NCE2.
    SMRiQ8NCE2. Positions 303-386.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi512 – 5187Poly-Ser

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG84393.
    HOVERGENiHBG062969.
    InParanoidiQ8NCE2.
    KOiK18086.
    OMAiDTHLFDK.
    OrthoDBiEOG73BVC8.
    PhylomeDBiQ8NCE2.
    TreeFamiTF324044.

    Family and domain databases

    Gene3Di3.90.190.10. 2 hits.
    InterProiIPR029021. Prot-tyrosine_phosphatase-like.
    IPR016130. Tyr_Pase_AS.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 2 hits.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8NCE2-1) [UniParc]FASTAAdd to Basket

    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

    MAGARAAAAA ASAGSSASSG NQPPQELGLG ELLEEFSRTQ YRAKDGSGTG    50
    GSKVERIEKR CLELFGRDYC FSVIPNTNGD ICGHYPRHIV FLEYESSEKE 100
    KDTFESTVQV SKLQDLIHRS KMARCRGRFV CPVILFKGKH ICRSATLAGW 150
    GELYGRSGYN YFFSGGADDA WADVEDVTEE DCALRSGDTH LFDKVRGYDI 200
    KLLRYLSVKY ICDLMVENKK VKFGMNVTSS EKVDKAQRYA DFTLLSIPYP 250
    GCEFFKEYKD RDYMAEGLIF NWKQDYVDAP LSIPDFLTHS LNIDWSQYQC 300
    WDLVQQTQNY LKLLLSLVNS DDDSGLLVHC ISGWDRTPLF ISLLRLSLWA 350
    DGLIHTSLKP TEILYLTVAY DWFLFGHMLV DRLSKGEEIF FFCFNFLKHI 400
    TSEEFSALKT QRRKSLPARD GGFTLEDICM LRRKDRGSTT SLGSDFSLVM 450
    ESSPGATGSF TYEAVELVPA GAPTQAAWRK SHSSSPQSVL WNRPQPSEDR 500
    LPSQQGLAEA RSSSSSSSNH SDNFFRMGSS PLEVPKPRSV DHPLPGSSLS 550
    TDYGSWQMVT GCGSIQERAV LHTDSSLPFS FPDELPNSCL LAALSDRETR 600
    LQEVRSAFLA AYSSTVGLRA VAPSPSGAIG GLLEQFARGV GLRSISSNAL 650
    Length:650
    Mass (Da):72,203
    Last modified:November 28, 2006 - v2
    Checksum:iC1B70E5140EF0716
    GO
    Isoform 2 (identifier: Q8NCE2-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:598
    Mass (Da):66,654
    Checksum:iFC7244F7B81672CC
    GO
    Isoform 3 (identifier: Q8NCE2-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:538
    Mass (Da):60,035
    Checksum:i6EA5D5AC9EE34FB0
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281G → R in CAL38187. (PubMed:17974005)Curated
    Sequence conflicti55 – 551E → G in CAL37928. (PubMed:17974005)Curated
    Sequence conflicti126 – 1261R → G in CAL38187. (PubMed:17974005)Curated
    Sequence conflicti390 – 3901F → S in BAC11211. (PubMed:14702039)Curated
    Sequence conflicti403 – 4064EEFS → ALFA in AAS50151. 1 PublicationCurated
    Sequence conflicti554 – 5574GSWQ → AAGM in AAS50151. 1 PublicationCurated
    Sequence conflicti646 – 6461S → N in CAL37928. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti336 – 3361R → Q in CNM1; may act as a phenotype modifier; drastically reduced enzymatic activity. 1 Publication
    Corresponds to variant rs121434509 [ dbSNP | Ensembl ].
    VAR_033370
    Natural varianti462 – 4621Y → C in CNM1; may act as a disease modifier; mutation found in a patient also carrying mutation Lys-368 in DNM2; reduced enzymatic activity. 1 Publication
    Corresponds to variant rs121434510 [ dbSNP | Ensembl ].
    VAR_033371

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei479 – 53860Missing in isoform 3. 3 PublicationsVSP_021585Add
    BLAST
    Alternative sequencei539 – 59052Missing in isoform 2 and isoform 3. 4 PublicationsVSP_021586Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS43043.1. [Q8NCE2-1]
    CCDS43044.1. [Q8NCE2-2]
    CCDS43045.1. [Q8NCE2-3]
    RefSeqiNP_001070993.1. NM_001077525.2. [Q8NCE2-1]
    NP_001070994.1. NM_001077526.2. [Q8NCE2-2]
    NP_071930.2. NM_022485.4. [Q8NCE2-3]
    UniGeneiHs.475382.

    Genome annotation databases

    EnsembliENST00000296003; ENSP00000296003; ENSG00000163719. [Q8NCE2-1]
    ENST00000351233; ENSP00000334070; ENSG00000163719. [Q8NCE2-3]
    ENST00000353332; ENSP00000323462; ENSG00000163719. [Q8NCE2-2]
    GeneIDi64419.
    KEGGihsa:64419.
    UCSCiuc003brz.3. human. [Q8NCE2-1]
    uc003bsa.3. human. [Q8NCE2-2]
    uc003bsb.3. human. [Q8NCE2-3]

    Polymorphism databases

    DMDMi118568016.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS43043.1. [Q8NCE2-1 ]
    CCDS43044.1. [Q8NCE2-2 ]
    CCDS43045.1. [Q8NCE2-3 ]
    RefSeqi NP_001070993.1. NM_001077525.2. [Q8NCE2-1 ]
    NP_001070994.1. NM_001077526.2. [Q8NCE2-2 ]
    NP_071930.2. NM_022485.4. [Q8NCE2-3 ]
    UniGenei Hs.475382.

    3D structure databases

    ProteinModelPortali Q8NCE2.
    SMRi Q8NCE2. Positions 303-386.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122168. 2 interactions.
    IntActi Q8NCE2. 4 interactions.
    MINTi MINT-3042111.

    PTM databases

    PhosphoSitei Q8NCE2.

    Polymorphism databases

    DMDMi 118568016.

    Proteomic databases

    MaxQBi Q8NCE2.
    PaxDbi Q8NCE2.
    PRIDEi Q8NCE2.

    Protocols and materials databases

    DNASUi 64419.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296003 ; ENSP00000296003 ; ENSG00000163719 . [Q8NCE2-1 ]
    ENST00000351233 ; ENSP00000334070 ; ENSG00000163719 . [Q8NCE2-3 ]
    ENST00000353332 ; ENSP00000323462 ; ENSG00000163719 . [Q8NCE2-2 ]
    GeneIDi 64419.
    KEGGi hsa:64419.
    UCSCi uc003brz.3. human. [Q8NCE2-1 ]
    uc003bsa.3. human. [Q8NCE2-2 ]
    uc003bsb.3. human. [Q8NCE2-3 ]

    Organism-specific databases

    CTDi 64419.
    GeneCardsi GC03P009691.
    HGNCi HGNC:26190. MTMR14.
    HPAi HPA054063.
    MIMi 160150. phenotype.
    611089. gene.
    neXtProti NX_Q8NCE2.
    Orphaneti 169189. Autosomal dominant centronuclear myopathy.
    PharmGKBi PA162396265.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG84393.
    HOVERGENi HBG062969.
    InParanoidi Q8NCE2.
    KOi K18086.
    OMAi DTHLFDK.
    OrthoDBi EOG73BVC8.
    PhylomeDBi Q8NCE2.
    TreeFami TF324044.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS08920-MONOMER.
    BRENDAi 3.1.3.64. 2681.
    Reactomei REACT_121025. Synthesis of PIPs at the plasma membrane.

    Miscellaneous databases

    GeneWikii MTMR14.
    GenomeRNAii 64419.
    NextBioi 66391.
    PROi Q8NCE2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8NCE2.
    Bgeei Q8NCE2.
    Genevestigatori Q8NCE2.

    Family and domain databases

    Gene3Di 3.90.190.10. 2 hits.
    InterProi IPR029021. Prot-tyrosine_phosphatase-like.
    IPR016130. Tyr_Pase_AS.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 2 hits.
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiMTMRE_HUMAN
    AccessioniPrimary (citable) accession number: Q8NCE2
    Secondary accession number(s): Q0JTH5
    , Q0JU83, Q6PIZ4, Q6QE21, Q86VK9, Q8IYK1, Q8TCM7, Q9H6C0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 96 of the entry and version 2 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 3
      Human chromosome 3: 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