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Protein

Calcium uniporter protein, mitochondrial

Gene

MCU

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

Functioni

Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways. Activity is regulated by MICU1 and MICU2 that stimulate and inhibit MCU activity, respectively. Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake. Involved in buffering the amplitude of systolic calcium rises in cardiomyocytes.9 Publications

GO - Molecular functioni

  1. calcium channel activity Source: UniProtKB
  2. uniporter activity Source: UniProtKB

GO - Biological processi

  1. calcium ion transmembrane import into mitochondrion Source: MGI
  2. calcium-mediated signaling Source: UniProtKB
  3. glucose homeostasis Source: UniProtKB
  4. mitochondrial calcium ion transport Source: UniProtKB
  5. positive regulation of insulin secretion Source: UniProtKB
  6. positive regulation of mitochondrial calcium ion concentration Source: UniProtKB
  7. protein complex oligomerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium uniporter protein, mitochondrial
Alternative name(s):
Coiled-coil domain-containing protein 109A
Gene namesi
Name:MCU
Synonyms:C10orf42, CCDC109A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:23526. MCU.

Subcellular locationi

  1. Mitochondrion inner membrane 3 Publications; Multi-pass membrane protein 3 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini51 – 233183Mitochondrial matrixSequence AnalysisAdd
BLAST
Transmembranei234 – 25623HelicalSequence AnalysisAdd
BLAST
Topological domaini257 – 2659Mitochondrial intermembraneSequence Analysis
Transmembranei266 – 28318HelicalSequence AnalysisAdd
BLAST
Topological domaini284 – 35168Mitochondrial matrixSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. calcium channel complex Source: UniProtKB
  2. integral component of mitochondrial inner membrane Source: UniProtKB
  3. mitochondrial inner membrane Source: UniProtKB
  4. mitochondrion Source: HPA
  5. uniplex complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi257 – 2571E → A: Inhibits calcium uptake. 1 Publication
Mutagenesisi259 – 2591S → A: Does not inhibit calcium uptake. 1 Publication
Mutagenesisi261 – 2611D → A: Inhibits calcium uptake. Inhibits calcium channel activity; when associated with Q-264. 2 Publications
Mutagenesisi264 – 2641E → A: Inhibits calcium uptake. Inhibits calcium channel activity; when associated with Q-261. 2 Publications

Organism-specific databases

PharmGKBiPA134888841.

Polymorphism and mutation databases

DMDMi74730222.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5050MitochondrionSequence AnalysisAdd
BLAST
Chaini51 – 351301Calcium uniporter protein, mitochondrialPRO_0000282976Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei332 – 3321N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8NE86.
PaxDbiQ8NE86.
PeptideAtlasiQ8NE86.
PRIDEiQ8NE86.

PTM databases

PhosphoSiteiQ8NE86.

Expressioni

Gene expression databases

BgeeiQ8NE86.
CleanExiHS_CCDC109A.
ExpressionAtlasiQ8NE86. baseline and differential.
GenevestigatoriQ8NE86.

Organism-specific databases

HPAiHPA016480.

Interactioni

Subunit structurei

Component of the uniplex complex, composed of MCU, MCUB, MICU1, MICU2 and EMRE/SMDT1. Heterotetramer with CCDC109B/MCUB; this inhibits channel activity (By similarity). Homotetramer. Interacts with MICU1; MICU1 acts as an essential regulator for MCU. Interacts with MCUR1; interaction with MICU1 and MCUR1 are mutually exclusive.By similarity5 Publications

Protein-protein interaction databases

BioGridi124733. 11 interactions.
DIPiDIP-60468N.
IntActiQ8NE86. 2 interactions.
MINTiMINT-8051705.
STRINGi9606.ENSP00000362144.

Structurei

3D structure databases

ProteinModelPortaliQ8NE86.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili192 – 22332Sequence AnalysisAdd
BLAST
Coiled coili311 – 33929Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG243091.
GeneTreeiENSGT00390000004496.
HOGENOMiHOG000008081.
HOVERGENiHBG060246.
InParanoidiQ8NE86.
OMAiKTRFDLE.
OrthoDBiEOG7HF1JN.
PhylomeDBiQ8NE86.
TreeFamiTF314435.

Family and domain databases

InterProiIPR006769. Coiled-coil-dom_prot_109_C.
[Graphical view]
PfamiPF04678. DUF607. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8NE86-1) [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
MAAAAGRSLL LLLSSRGGGG GGAGGCGALT AGCFPGLGVS RHRQQQHHRT
60 70 80 90 100
VHQRIASWQN LGAVYCSTVV PSDDVTVVYQ NGLPVISVRL PSRRERCQFT
110 120 130 140 150
LKPISDSVGV FLRQLQEEDR GIDRVAIYSP DGVRVAASTG IDLLLLDDFK
160 170 180 190 200
LVINDLTYHV RPPKRDLLSH ENAATLNDVK TLVQQLYTTL CIEQHQLNKE
210 220 230 240 250
RELIERLEDL KEQLAPLEKV RIEISRKAEK RTTLVLWGGL AYMATQFGIL
260 270 280 290 300
ARLTWWEYSW DIMEPVTYFI TYGSAMAMYA YFVMTRQEYV YPEARDRQYL
310 320 330 340 350
LFFHKGAKKS RFDLEKYNQL KDAIAQAEMD LKRLRDPLQV HLPLRQIGEK

D
Length:351
Mass (Da):39,867
Last modified:October 1, 2002 - v1
Checksum:i50205D01055D66E4
GO
Isoform 2 (identifier: Q8NE86-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     166-219: DLLSHENAAT...LKEQLAPLEK → VEMGFCHVGQNGFELLTSSYLPASASQSAEIIA

Note: No experimental confirmation available.

Show »
Length:330
Mass (Da):36,996
Checksum:i56D458541240604A
GO
Isoform 3 (identifier: Q8NE86-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: MAAAAGRSLLLLLSSRGGGGGGAGGCGALTAGCFPGLGVSRHRQQQHHRT → M

Show »
Length:302
Mass (Da):35,159
Checksum:i65C6D99CD9D2D3FC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1071S → P in BAG37900 (PubMed:14702039).Curated
Sequence conflicti142 – 1421D → Y in BAG37900 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5050MAAAA…QHHRT → M in isoform 3. 1 PublicationVSP_041687Add
BLAST
Alternative sequencei166 – 21954DLLSH…APLEK → VEMGFCHVGQNGFELLTSSY LPASASQSAEIIA in isoform 2. 1 PublicationVSP_024263Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK315519 mRNA. Translation: BAG37900.1.
AK128016 mRNA. Translation: BAG54619.1.
AC016542 Genomic DNA. No translation available.
AC069548 Genomic DNA. No translation available.
CH471083 Genomic DNA. Translation: EAW54461.1.
BC010682 mRNA. Translation: AAH10682.1.
BC034235 mRNA. Translation: AAH34235.1.
CCDSiCCDS59218.1. [Q8NE86-2]
CCDS59219.1. [Q8NE86-3]
CCDS7317.1. [Q8NE86-1]
RefSeqiNP_001257608.1. NM_001270679.1. [Q8NE86-2]
NP_001257609.1. NM_001270680.1. [Q8NE86-3]
NP_612366.1. NM_138357.2. [Q8NE86-1]
UniGeneiHs.591366.

Genome annotation databases

EnsembliENST00000357157; ENSP00000349680; ENSG00000156026. [Q8NE86-2]
ENST00000373053; ENSP00000362144; ENSG00000156026. [Q8NE86-1]
ENST00000536019; ENSP00000440913; ENSG00000156026. [Q8NE86-3]
GeneIDi90550.
KEGGihsa:90550.
UCSCiuc001jtc.3. human. [Q8NE86-1]
uc001jtd.3. human. [Q8NE86-3]
uc009xqr.3. human. [Q8NE86-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK315519 mRNA. Translation: BAG37900.1.
AK128016 mRNA. Translation: BAG54619.1.
AC016542 Genomic DNA. No translation available.
AC069548 Genomic DNA. No translation available.
CH471083 Genomic DNA. Translation: EAW54461.1.
BC010682 mRNA. Translation: AAH10682.1.
BC034235 mRNA. Translation: AAH34235.1.
CCDSiCCDS59218.1. [Q8NE86-2]
CCDS59219.1. [Q8NE86-3]
CCDS7317.1. [Q8NE86-1]
RefSeqiNP_001257608.1. NM_001270679.1. [Q8NE86-2]
NP_001257609.1. NM_001270680.1. [Q8NE86-3]
NP_612366.1. NM_138357.2. [Q8NE86-1]
UniGeneiHs.591366.

3D structure databases

ProteinModelPortaliQ8NE86.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124733. 11 interactions.
DIPiDIP-60468N.
IntActiQ8NE86. 2 interactions.
MINTiMINT-8051705.
STRINGi9606.ENSP00000362144.

PTM databases

PhosphoSiteiQ8NE86.

Polymorphism and mutation databases

DMDMi74730222.

Proteomic databases

MaxQBiQ8NE86.
PaxDbiQ8NE86.
PeptideAtlasiQ8NE86.
PRIDEiQ8NE86.

Protocols and materials databases

DNASUi90550.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357157; ENSP00000349680; ENSG00000156026. [Q8NE86-2]
ENST00000373053; ENSP00000362144; ENSG00000156026. [Q8NE86-1]
ENST00000536019; ENSP00000440913; ENSG00000156026. [Q8NE86-3]
GeneIDi90550.
KEGGihsa:90550.
UCSCiuc001jtc.3. human. [Q8NE86-1]
uc001jtd.3. human. [Q8NE86-3]
uc009xqr.3. human. [Q8NE86-2]

Organism-specific databases

CTDi90550.
GeneCardsiGC10P074452.
HGNCiHGNC:23526. MCU.
HPAiHPA016480.
MIMi614197. gene.
neXtProtiNX_Q8NE86.
PharmGKBiPA134888841.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG243091.
GeneTreeiENSGT00390000004496.
HOGENOMiHOG000008081.
HOVERGENiHBG060246.
InParanoidiQ8NE86.
OMAiKTRFDLE.
OrthoDBiEOG7HF1JN.
PhylomeDBiQ8NE86.
TreeFamiTF314435.

Miscellaneous databases

ChiTaRSiMCU. human.
GenomeRNAii90550.
NextBioi76829.
PROiQ8NE86.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NE86.
CleanExiHS_CCDC109A.
ExpressionAtlasiQ8NE86. baseline and differential.
GenevestigatoriQ8NE86.

Family and domain databases

InterProiIPR006769. Coiled-coil-dom_prot_109_C.
[Graphical view]
PfamiPF04678. DUF607. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Testis and Tongue.
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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 AND 2).
    Tissue: Eye and Testis.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter."
    De Stefani D., Raffaello A., Teardo E., Szabo I., Rizzuto R.
    Nature 476:336-340(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-261 AND GLU-264, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter."
    Baughman J.M., Perocchi F., Girgis H.S., Plovanich M., Belcher-Timme C.A., Sancak Y., Bao X.R., Strittmatter L., Goldberger O., Bogorad R.L., Koteliansky V., Mootha V.K.
    Nature 476:341-345(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, OLIGOMERIZATION, INTERACTION WITH MICU1, MUTAGENESIS OF GLU-257; SER-259; ASP-261 AND GLU-264, SUBCELLULAR LOCATION.
  8. "MICU1 is an essential gatekeeper for MCU-mediated mitochondrial Ca(2+) uptake that regulates cell survival."
    Mallilankaraman K., Doonan P., Cardenas C., Chandramoorthy H.C., Muller M., Miller R., Hoffman N.E., Gandhirajan R.K., Molgo J., Birnbaum M.J., Rothberg B.S., Mak D.O., Foskett J.K., Madesh M.
    Cell 151:630-644(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MICU1.
  9. "Mitochondrial Ca2+ uptake 1 (MICU1) and mitochondrial ca2+ uniporter (MCU) contribute to metabolism-secretion coupling in clonal pancreatic beta-cells."
    Alam M.R., Groschner L.N., Parichatikanond W., Kuo L., Bondarenko A.I., Rost R., Waldeck-Weiermair M., Malli R., Graier W.F.
    J. Biol. Chem. 287:34445-34454(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. Cited for: FUNCTION, INTERACTION WITH MCUR1 AND MICU1.
  11. "The mitochondrial Ca2+ uniporter MCU is essential for glucose-induced ATP increases in pancreatic beta-cells."
    Tarasov A.I., Semplici F., Ravier M.A., Bellomo E.A., Pullen T.J., Gilon P., Sekler I., Rizzuto R., Rutter G.A.
    PLoS ONE 7:E39722-E39722(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Mitochondrial Ca2+ uptake contributes to buffering cytoplasmic Ca2+ peaks in cardiomyocytes."
    Drago I., De Stefani D., Rizzuto R., Pozzan T.
    Proc. Natl. Acad. Sci. U.S.A. 109:12986-12991(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Evolutionary diversity of the mitochondrial calcium uniporter."
    Bick A.G., Calvo S.E., Mootha V.K.
    Science 336:886-886(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  14. Cited for: FUNCTION, INTERACTION WITH MICU1.
  15. Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE UNIPLEX COMPLEX.
  16. "MICU1 and MICU2 finely tune the mitochondrial Ca(2+) uniporter by exerting opposite effects on MCU activity."
    Patron M., Checchetto V., Raffaello A., Teardo E., Vecellio Reane D., Mantoan M., Granatiero V., Szabo I., De Stefani D., Rizzuto R.
    Mol. Cell 53:726-737(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiMCU_HUMAN
AccessioniPrimary (citable) accession number: Q8NE86
Secondary accession number(s): B2RDF3, B3KXV7, Q96FL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 1, 2002
Last modified: April 29, 2015
This is version 97 of the entry and version 1 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 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.