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Protein

Calcium uptake protein 1, mitochondrial

Gene

MICU1

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

Functioni

Key regulator of mitochondrial calcium uniporter (MCU) that senses calcium level via its EF-hand domains (PubMed:20693986, PubMed:23101630, PubMed:23747253, PubMed:24313810, PubMed:24332854, PubMed:24503055, PubMed:24560927, PubMed:26341627, PubMed:26903221, PubMed:27099988). MICU1 and MICU2 form a disulfide-linked heterodimer that stimulates and inhibits MCU activity, depending on the concentration of calcium. MICU1 acts both as an activator or inhibitor of mitochondrial calcium uptake (PubMed:26903221). Acts as a gatekeeper of MCU at low concentration of calcium, preventing channel opening (PubMed:26903221). Enhances MCU opening at high calcium concentration, allowing a rapid response of mitochondria to calcium signals generated in the cytoplasm (PubMed:24560927, PubMed:26903221). Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake (PubMed:22904319). Induces T-helper 1-mediated autoreactivity, which is accompanied by the release of IFNG (PubMed:16002733).12 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi231 – 242121PROSITE-ProRule annotation1 PublicationAdd
BLAST
Calcium bindingi421 – 432122PROSITE-ProRule annotation1 PublicationAdd
BLAST

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein heterodimerization activity Source: UniProtKB

GO - Biological processi

  • calcium ion import Source: UniProtKB
  • calcium ion transmembrane import into mitochondrion Source: MGI
  • defense response Source: ProtInc
  • mitochondrial calcium ion homeostasis Source: UniProtKB
  • mitochondrial calcium ion transport Source: UniProtKB
  • positive regulation of mitochondrial calcium ion concentration Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

TCDBi8.A.44.1.1. the mitochondrial ef hand ca(2+) uniporter regulator (micu) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium uptake protein 1, mitochondrial
Alternative name(s):
Atopy-related autoantigen CALC1 Publication
Short name:
ara CALC1 Publication
Calcium-binding atopy-related autoantigen 11 Publication
Allergen: Hom s 41 Publication
Gene namesi
Name:MICU1
Synonyms:CALC1 Publication, CBARA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:1530. MICU1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei34 – 5219HelicalSequence analysisAdd
BLAST
Topological domaini53 – 476424Mitochondrial intermembrane1 PublicationAdd
BLAST

GO - Cellular componenti

  • calcium channel complex Source: UniProtKB
  • integral component of mitochondrial membrane Source: UniProtKB
  • intracellular Source: ProtInc
  • mitochondrial inner membrane Source: UniProtKB
  • mitochondrial intermembrane space Source: UniProtKB
  • mitochondrion Source: HPA
  • uniplex complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Involvement in diseasei

Myopathy with extrapyramidal signs (MPXPS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry. The complex phenotype is due to alterations in mitochondrial calcium signaling characterized by increased mitochondrial Ca(2+) load (PubMed:24336167).1 Publication
Disease descriptionAn autosomal recessive disorder characterized by early-onset proximal muscle weakness with a static course and moderately to grossly elevated serum creatine kinase levels accompanied by learning difficulties. Most patients develop subtle extrapyramidal motor signs that progress to a debilitating disorder of involuntary movement with variable features, including chorea, tremor, dystonic posturing and orofacial dyskinesia. Additional variable features include ataxia, microcephaly, ophthalmoplegia, ptosis, optic atrophy and axonal peripheral neuropathy.
See also OMIM:615673

An homozygous partial MICU1 deletion is responsible for a disorder manifesting in childhood with fatigue, lethargy and muscle weakness. The disease is caused by mutations affecting the gene represented in this entry.

Allergenic propertiesi

Causes an allergic reaction in human. Binds to IgE from atopic dermatitis (AD) patients. Identified as an IgE autoantigen in atopic dermatitis (AD) patients with severe skin manifestations.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi99 – 1024KKKK → EQEQ: Abolishes interaction with EMRE/SMDT1 while maintaining intedraction with MICU2SO. 1 Publication
Mutagenesisi221 – 2211R → A: Abolishes homooligomerization. 1 Publication
Mutagenesisi231 – 2311D → A: Abolishes mitochondrial Ca(2+) uptake; when associated with A-242; A-421 and A-432. 3 Publications
Mutagenesisi242 – 2421E → A or K: Abolishes mitochondrial Ca(2+) uptake; when associated with A-231; A-421 and A-432. 3 Publications
Mutagenesisi376 – 3761D → A: Abolishes homooligomerization. 1 Publication
Mutagenesisi383 – 3853FYH → AYA: Abolishes homooligomerization. 1 Publication
Mutagenesisi421 – 4211D → A: Abolishes mitochondrial Ca(2+) uptake; when associated with A-231; A-242 and A-432. 3 Publications
Mutagenesisi432 – 4321E → A: Abolishes mitochondrial Ca(2+) uptake; when associated with A-231; A-242 and A-421. 3 Publications
Mutagenesisi432 – 4321E → K: Loss of function; when associated with A-421. 3 Publications
Mutagenesisi463 – 4631C → A: Abolishes interchain disulfide bond and heterodimer formation with MICU2. 1 Publication

Keywords - Diseasei

Allergen

Organism-specific databases

MalaCardsiMICU1.
MIMi615673. phenotype.
Orphaneti401768. Proximal myopathy with extrapyramidal signs.
PharmGKBiPA26110.

Protein family/group databases

Allergomei3325. Hom s 4.0101.
414. Hom s 4.

Polymorphism and mutation databases

BioMutaiMICU1.
DMDMi74761192.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionSequence analysis1 PublicationAdd
BLAST
Chaini34 – 476443Calcium uptake protein 1, mitochondrialPRO_0000322990Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi463 – 463Interchain (with C-413 in MICU2)1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiQ9BPX6.
MaxQBiQ9BPX6.
PaxDbiQ9BPX6.
PeptideAtlasiQ9BPX6.
PRIDEiQ9BPX6.

PTM databases

iPTMnetiQ9BPX6.
PhosphoSiteiQ9BPX6.

Expressioni

Tissue specificityi

Expressed in epithelial cell lines. Strongly expressed in epidermal keratinocytes and dermal endothelial cells.2 Publications

Gene expression databases

BgeeiENSG00000107745.
CleanExiHS_CBARA1.
ExpressionAtlasiQ9BPX6. baseline and differential.
GenevisibleiQ9BPX6. HS.

Organism-specific databases

HPAiHPA037479.
HPA037480.

Interactioni

Subunit structurei

Homohexamer; in absence of calcium (PubMed:24514027). Forms a homohexamer in absence of calcium and rearranges into a heterodimer in presence of calcium (PubMed:26489515, PubMed:24514027). Heterodimer; disulfide-linked; heterodimerizes with MICU2 (PubMed:24560927). The heterodimer formed with MICU2 associates with MCU at low calcium concentration and dissociates from MCU at high calcium level (PubMed:26387864). Component of the uniplex complex, composed of MCU, MCUB, MICU1, MICU2 and EMRE/SMDT1 (PubMed:24231807). Interacts (via polybasic region) with EMRE/SMDT1; the interaction is direct (PubMed:27099988). Interacts (via polybasic region) with MCU (via coiled coil domains); the interaction is direct and precedes formation of the heterodimer with MICU2 (PubMed:21685886, PubMed:23101630, PubMed:23178883, PubMed:24332854, PubMed:26387864). Interacts with SLC25A23 (PubMed:24430870). Interacts with CHCHD4/MIA40; which introduces the interchain disulfide bond with MICU2 (PubMed:26387864).11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself8EBI-2371996,EBI-2371996

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi115646. 24 interactions.
DIPiDIP-53438N.
IntActiQ9BPX6. 4 interactions.
STRINGi9606.ENSP00000354415.

Structurei

Secondary structure

1
476
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni103 – 1053Combined sources
Helixi109 – 12012Combined sources
Helixi124 – 1318Combined sources
Beta strandi134 – 1385Combined sources
Beta strandi143 – 1475Combined sources
Helixi149 – 1557Combined sources
Turni164 – 1663Combined sources
Beta strandi169 – 1724Combined sources
Helixi196 – 1983Combined sources
Beta strandi199 – 2024Combined sources
Helixi206 – 21611Combined sources
Helixi220 – 23011Combined sources
Helixi240 – 25112Combined sources
Turni255 – 2573Combined sources
Helixi279 – 2835Combined sources
Turni284 – 2863Combined sources
Helixi293 – 31321Combined sources
Helixi324 – 33512Combined sources
Helixi340 – 3478Combined sources
Helixi349 – 3524Combined sources
Helixi361 – 37212Combined sources
Helixi374 – 38310Combined sources
Helixi393 – 40412Combined sources
Helixi410 – 42011Combined sources
Beta strandi425 – 4284Combined sources
Turni430 – 4334Combined sources
Helixi434 – 4396Combined sources
Helixi455 – 46410Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NSCX-ray3.20A/B/C/D/E/F97-476[»]
4NSDX-ray2.70A/B97-444[»]
ProteinModelPortaliQ9BPX6.
SMRiQ9BPX6. Positions 107-464.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini218 – 25336EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini408 – 44336EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni99 – 11012Polybasic region1 PublicationAdd
BLAST
Regioni455 – 46511C-helix region1 PublicationAdd
BLAST

Domaini

The C-helix is required for assembling the Ca2+-free homohexamer (PubMed:24514027). It also plays a key role in mitochondrial calcium uptake, probably by mediating interaction with MICU2 (PubMed:24503055, PubMed:24514027).2 Publications
The EF-hand domains have high affinity for calcium and act as sensors of calcium levels (PubMed:23101630, PubMed:24560927).2 Publications

Sequence similaritiesi

Belongs to the MICU1 family. MICU1 subfamily.Curated
Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2643. Eukaryota.
ENOG410ZSC1. LUCA.
GeneTreeiENSGT00530000063089.
HOVERGENiHBG107586.
InParanoidiQ9BPX6.
PhylomeDBiQ9BPX6.
TreeFamiTF313815.

Family and domain databases

Gene3Di1.10.238.10. 4 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13202. EF-hand_5. 1 hit.
PF13833. EF-hand_8. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 3 hits.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BPX6-1) [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
MFRLNSLSAL AELAVGSRWY HGGSQPIQIR RRLMMVAFLG ASAVTASTGL
60 70 80 90 100
LWKRAHAESP PCVDNLKSDI GDKGKNKDEG DVCNHEKKTA DLAPHPEEKK
110 120 130 140 150
KKRSGFRDRK VMEYENRIRA YSTPDKIFRY FATLKVISEP GEAEVFMTPE
160 170 180 190 200
DFVRSITPNE KQPEHLGLDQ YIIKRFDGKK ISQEREKFAD EGSIFYTLGE
210 220 230 240 250
CGLISFSDYI FLTTVLSTPQ RNFEIAFKMF DLNGDGEVDM EEFEQVQSII
260 270 280 290 300
RSQTSMGMRH RDRPTTGNTL KSGLCSALTT YFFGADLKGK LTIKNFLEFQ
310 320 330 340 350
RKLQHDVLKL EFERHDPVDG RITERQFGGM LLAYSGVQSK KLTAMQRQLK
360 370 380 390 400
KHFKEGKGLT FQEVENFFTF LKNINDVDTA LSFYHMAGAS LDKVTMQQVA
410 420 430 440 450
RTVAKVELSD HVCDVVFALF DCDGNGELSN KEFVSIMKQR LMRGLEKPKD
460 470
MGFTRLMQAM WKCAQETAWD FALPKQ
Length:476
Mass (Da):54,351
Last modified:June 1, 2001 - v1
Checksum:iD83C3A38F4B28FDF
GO
Isoform 2 (identifier: Q9BPX6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     394-403: VTMQQVARTV → GKGTIFMGRR
     404-476: Missing.

Note: No experimental confirmation available.
Show »
Length:403
Mass (Da):45,975
Checksum:i2E7EB518965C6750
GO
Isoform 3 (identifier: Q9BPX6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     179-179: K → KTE

Note: No experimental confirmation available.
Show »
Length:478
Mass (Da):54,582
Checksum:i6814001923EC4054
GO
Isoform 4 (identifier: Q9BPX6-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-198: Missing.
     199-218: GECGLISFSDYIFLTTVLST → MKRIYTYRRAKEIFKDTPKA

Note: No experimental confirmation available.
Show »
Length:278
Mass (Da):32,122
Checksum:i92C650B8F161E1C2
GO
Isoform 5 (identifier: Q9BPX6-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-198: Missing.
     199-218: GECGLISFSDYIFLTTVLST → MVSLKAKLNHLRQSMLKQKA

Note: No experimental confirmation available.
Show »
Length:278
Mass (Da):31,931
Checksum:iE2736D73550EAAED
GO

Sequence cautioni

The sequence BAB14187 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA76830 differs from that shown.Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541R → G in CAB55915 (PubMed:11230166).Curated
Sequence conflicti449 – 4491K → E in BAG60593 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 198198Missing in isoform 4 and isoform 5. 1 PublicationVSP_039890Add
BLAST
Alternative sequencei179 – 1791K → KTE in isoform 3. 1 PublicationVSP_031979
Alternative sequencei199 – 21820GECGL…TVLST → MKRIYTYRRAKEIFKDTPKA in isoform 4. 1 PublicationVSP_039891Add
BLAST
Alternative sequencei199 – 21820GECGL…TVLST → MVSLKAKLNHLRQSMLKQKA in isoform 5. 1 PublicationVSP_039892Add
BLAST
Alternative sequencei394 – 40310VTMQQVARTV → GKGTIFMGRR in isoform 2. 1 PublicationVSP_031980
Alternative sequencei404 – 47673Missing in isoform 2. 1 PublicationVSP_031981Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023318 mRNA. Translation: BAG51182.1.
AK296086 mRNA. Translation: BAG58841.1.
AK298347 mRNA. Translation: BAG60593.1.
AL117423 mRNA. Translation: CAB55915.1.
AL513185, AC091769 Genomic DNA. Translation: CAI12376.1.
AL356009 Genomic DNA. No translation available.
CH471083 Genomic DNA. Translation: EAW54459.1.
BC004190 mRNA. Translation: AAH04190.1.
BC004216 mRNA. Translation: AAH04216.1.
BC016641 mRNA. Translation: AAH16641.1.
AK022697 mRNA. Translation: BAB14187.1. Different initiation.
Y17711 mRNA. Translation: CAA76830.1. Sequence problems.
CCDSiCCDS55714.1. [Q9BPX6-4]
CCDS55715.1. [Q9BPX6-1]
PIRiT17225.
RefSeqiNP_001182447.1. NM_001195518.1. [Q9BPX6-1]
NP_001182448.1. NM_001195519.1. [Q9BPX6-4]
NP_006068.2. NM_006077.3. [Q9BPX6-3]
UniGeneiHs.524367.

Genome annotation databases

EnsembliENST00000361114; ENSP00000354415; ENSG00000107745. [Q9BPX6-1]
ENST00000398763; ENSP00000381747; ENSG00000107745. [Q9BPX6-5]
ENST00000418483; ENSP00000402470; ENSG00000107745. [Q9BPX6-4]
GeneIDi10367.
KEGGihsa:10367.
UCSCiuc001jtb.3. human. [Q9BPX6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023318 mRNA. Translation: BAG51182.1.
AK296086 mRNA. Translation: BAG58841.1.
AK298347 mRNA. Translation: BAG60593.1.
AL117423 mRNA. Translation: CAB55915.1.
AL513185, AC091769 Genomic DNA. Translation: CAI12376.1.
AL356009 Genomic DNA. No translation available.
CH471083 Genomic DNA. Translation: EAW54459.1.
BC004190 mRNA. Translation: AAH04190.1.
BC004216 mRNA. Translation: AAH04216.1.
BC016641 mRNA. Translation: AAH16641.1.
AK022697 mRNA. Translation: BAB14187.1. Different initiation.
Y17711 mRNA. Translation: CAA76830.1. Sequence problems.
CCDSiCCDS55714.1. [Q9BPX6-4]
CCDS55715.1. [Q9BPX6-1]
PIRiT17225.
RefSeqiNP_001182447.1. NM_001195518.1. [Q9BPX6-1]
NP_001182448.1. NM_001195519.1. [Q9BPX6-4]
NP_006068.2. NM_006077.3. [Q9BPX6-3]
UniGeneiHs.524367.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NSCX-ray3.20A/B/C/D/E/F97-476[»]
4NSDX-ray2.70A/B97-444[»]
ProteinModelPortaliQ9BPX6.
SMRiQ9BPX6. Positions 107-464.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115646. 24 interactions.
DIPiDIP-53438N.
IntActiQ9BPX6. 4 interactions.
STRINGi9606.ENSP00000354415.

Protein family/group databases

Allergomei3325. Hom s 4.0101.
414. Hom s 4.
TCDBi8.A.44.1.1. the mitochondrial ef hand ca(2+) uniporter regulator (micu) family.

PTM databases

iPTMnetiQ9BPX6.
PhosphoSiteiQ9BPX6.

Polymorphism and mutation databases

BioMutaiMICU1.
DMDMi74761192.

Proteomic databases

EPDiQ9BPX6.
MaxQBiQ9BPX6.
PaxDbiQ9BPX6.
PeptideAtlasiQ9BPX6.
PRIDEiQ9BPX6.

Protocols and materials databases

DNASUi10367.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361114; ENSP00000354415; ENSG00000107745. [Q9BPX6-1]
ENST00000398763; ENSP00000381747; ENSG00000107745. [Q9BPX6-5]
ENST00000418483; ENSP00000402470; ENSG00000107745. [Q9BPX6-4]
GeneIDi10367.
KEGGihsa:10367.
UCSCiuc001jtb.3. human. [Q9BPX6-1]

Organism-specific databases

CTDi10367.
GeneCardsiMICU1.
HGNCiHGNC:1530. MICU1.
HPAiHPA037479.
HPA037480.
MalaCardsiMICU1.
MIMi605084. gene.
615673. phenotype.
neXtProtiNX_Q9BPX6.
Orphaneti401768. Proximal myopathy with extrapyramidal signs.
PharmGKBiPA26110.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2643. Eukaryota.
ENOG410ZSC1. LUCA.
GeneTreeiENSGT00530000063089.
HOVERGENiHBG107586.
InParanoidiQ9BPX6.
PhylomeDBiQ9BPX6.
TreeFamiTF313815.

Miscellaneous databases

GeneWikiiCBARA1.
GenomeRNAii10367.
PROiQ9BPX6.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000107745.
CleanExiHS_CBARA1.
ExpressionAtlasiQ9BPX6. baseline and differential.
GenevisibleiQ9BPX6. HS.

Family and domain databases

Gene3Di1.10.238.10. 4 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13202. EF-hand_5. 1 hit.
PF13833. EF-hand_8. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 3 hits.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMICU1_HUMAN
AccessioniPrimary (citable) accession number: Q9BPX6
Secondary accession number(s): A8MV96
, B3KN20, B4DJH9, B4DPI1, B5MBY3, D3YTJ3, O75785, Q9H9N6, Q9UFX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: June 1, 2001
Last modified: September 7, 2016
This is version 140 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

Caution

Was initially thought to act as an inhibitor of MCU based on effects following MICU1 depletion (PubMed:20693986, PubMed:23101630). However, depletion of MICU1 also eliminates MICU2, explaining the initial conclusion. It was later shown to act as a stimulator of MCU activity instead (PubMed:24560927).3 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.