Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Myotubularin-related protein 14

Gene

MTMR14

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:26190. MTMR14.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • perinuclear region of cytoplasm Source: UniProtKB
  • ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Myopathy, centronuclear, 1 (CNM1)1 Publication

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).

Disease descriptionA 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.

See also OMIM:160150
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.

Polymorphism and mutation databases

BioMutaiMTMR14.
DMDMi118568016.

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

DEPODiQ8NCE2.
PhosphoSiteiQ8NCE2.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ8NCE2.
ExpressionAtlasiQ8NCE2. baseline and differential.
GenevisibleiQ8NCE2. HS.

Organism-specific databases

HPAiHPA054063.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TP53BP2Q13625-33EBI-5658424,EBI-10175039

Protein-protein interaction databases

BioGridi122168. 7 interactions.
IntActiQ8NCE2. 5 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.
GeneTreeiENSGT00390000018852.
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. AlignAdd to basket

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

        10         20         30         40         50
MAGARAAAAA ASAGSSASSG NQPPQELGLG ELLEEFSRTQ YRAKDGSGTG
60 70 80 90 100
GSKVERIEKR CLELFGRDYC FSVIPNTNGD ICGHYPRHIV FLEYESSEKE
110 120 130 140 150
KDTFESTVQV SKLQDLIHRS KMARCRGRFV CPVILFKGKH ICRSATLAGW
160 170 180 190 200
GELYGRSGYN YFFSGGADDA WADVEDVTEE DCALRSGDTH LFDKVRGYDI
210 220 230 240 250
KLLRYLSVKY ICDLMVENKK VKFGMNVTSS EKVDKAQRYA DFTLLSIPYP
260 270 280 290 300
GCEFFKEYKD RDYMAEGLIF NWKQDYVDAP LSIPDFLTHS LNIDWSQYQC
310 320 330 340 350
WDLVQQTQNY LKLLLSLVNS DDDSGLLVHC ISGWDRTPLF ISLLRLSLWA
360 370 380 390 400
DGLIHTSLKP TEILYLTVAY DWFLFGHMLV DRLSKGEEIF FFCFNFLKHI
410 420 430 440 450
TSEEFSALKT QRRKSLPARD GGFTLEDICM LRRKDRGSTT SLGSDFSLVM
460 470 480 490 500
ESSPGATGSF TYEAVELVPA GAPTQAAWRK SHSSSPQSVL WNRPQPSEDR
510 520 530 540 550
LPSQQGLAEA RSSSSSSSNH SDNFFRMGSS PLEVPKPRSV DHPLPGSSLS
560 570 580 590 600
TDYGSWQMVT GCGSIQERAV LHTDSSLPFS FPDELPNSCL LAALSDRETR
610 620 630 640 650
LQEVRSAFLA AYSSTVGLRA VAPSPSGAIG GLLEQFARGV GLRSISSNAL
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. Curated

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 (Ref. 5) Curated
Sequence conflicti554 – 5574GSWQ → AAGM in AAS50151 (Ref. 5) Curated
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:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi122168. 7 interactions.
IntActiQ8NCE2. 5 interactions.
MINTiMINT-3042111.

PTM databases

DEPODiQ8NCE2.
PhosphoSiteiQ8NCE2.

Polymorphism and mutation databases

BioMutaiMTMR14.
DMDMi118568016.

Proteomic databases

MaxQBiQ8NCE2.
PaxDbiQ8NCE2.
PRIDEiQ8NCE2.

Protocols and materials databases

DNASUi64419.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi64419.
GeneCardsiGC03P009691.
HGNCiHGNC:26190. MTMR14.
HPAiHPA054063.
MIMi160150. phenotype.
611089. gene.
neXtProtiNX_Q8NCE2.
Orphaneti169189. Autosomal dominant centronuclear myopathy.
PharmGKBiPA162396265.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG84393.
GeneTreeiENSGT00390000018852.
HOVERGENiHBG062969.
InParanoidiQ8NCE2.
KOiK18086.
OMAiDTHLFDK.
OrthoDBiEOG73BVC8.
PhylomeDBiQ8NCE2.
TreeFamiTF324044.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiMTMR14. human.
GeneWikiiMTMR14.
GenomeRNAii64419.
NextBioi66391.
PROiQ8NCE2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NCE2.
ExpressionAtlasiQ8NCE2. baseline and differential.
GenevisibleiQ8NCE2. HS.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: June 24, 2015
This is version 103 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.