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Q04844

- ACHE_HUMAN

UniProt

Q04844 - ACHE_HUMAN

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Protein

Acetylcholine receptor subunit epsilon

Gene

CHRNE

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

Functioni

After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.

GO - Molecular functioni

  1. acetylcholine-activated cation-selective channel activity Source: ProtInc
  2. acetylcholine receptor activity Source: ProtInc
  3. cation transmembrane transporter activity Source: ProtInc

GO - Biological processi

  1. cation transmembrane transport Source: GOC
  2. cation transport Source: GOC
  3. muscle contraction Source: ProtInc
  4. regulation of membrane potential Source: Ensembl
  5. signal transduction Source: ProtInc
  6. synaptic transmission Source: Reactome
  7. synaptic transmission, cholinergic Source: ProtInc
  8. transport Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_22223. Highly sodium permeable acetylcholine nicotinic receptors.

Protein family/group databases

TCDBi1.A.9.1.1. the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylcholine receptor subunit epsilon
Gene namesi
Name:CHRNE
Synonyms:ACHRE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:1966. CHRNE.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 239219ExtracellularSequence AnalysisAdd
BLAST
Transmembranei240 – 26425HelicalSequence AnalysisAdd
BLAST
Topological domaini265 – 2728CytoplasmicSequence Analysis
Transmembranei273 – 29119HelicalSequence AnalysisAdd
BLAST
Topological domaini292 – 30615ExtracellularSequence AnalysisAdd
BLAST
Transmembranei307 – 32822HelicalSequence AnalysisAdd
BLAST
Topological domaini329 – 456128CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei457 – 48024HelicalSequence AnalysisAdd
BLAST
Topological domaini481 – 49313ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. acetylcholine-gated channel complex Source: ProtInc
  2. cell junction Source: UniProtKB-KW
  3. integral component of plasma membrane Source: ProtInc
  4. plasma membrane Source: Reactome
  5. postsynaptic membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Involvement in diseasei

The muscle AChR is the major target antigen in the autoimmune disease myasthenia gravis. Myasthenia gravis is characterized by sporadic muscular fatigability and weakness, occurring chiefly in muscles innervated by cranial nerves, and characteristically improved by cholinesterase-inhibiting drugs.
Myasthenic syndrome, congenital, slow-channel (SCCMS) [MIM:601462]: A common congenital myasthenic syndrome. Congenital myasthenic syndromes are characterized by muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. Congenital myasthenic syndrome slow-channel type is caused by kinetic abnormalities of the AChR, resulting in prolonged endplate currents and prolonged AChR channel opening episodes.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti98 – 981L → P in SCCMS; rare example of recessive inheritance. 1 Publication
Corresponds to variant rs28929768 [ dbSNP | Ensembl ].
VAR_019567
Natural varianti241 – 2411L → F in SCCMS; mild form with variable penetrance. 1 Publication
Corresponds to variant rs28999110 [ dbSNP | Ensembl ].
VAR_019568
Natural varianti284 – 2841T → P in SCCMS; markedly prolonged channel openings in presence of agonist; as well as opening in the absence of agonist. 1 Publication
VAR_000292
Natural varianti289 – 2891L → F in SCCMS; slows rate of AChR channel closure and increases apparent affinity for ACh; causes pathologic channel openings even in the absence of ACh resulting in a leaky channel. 2 Publications
VAR_000293
Myasthenic syndrome, congenital, fast-channel (FCCMS) [MIM:608930]: A congenital myasthenic syndrome characterized by kinetic abnormalities of the AChR. Due in most cases to mutations that decrease activity of the AChR by slowing the rate of opening of the receptor channel, speeding the rate of closure of the channel, or decreasing the number of openings of the channel during ACh occupancy. The result is failure to achieve threshold depolarization of the endplate and consequent failure to fire an action potential.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131G → R in FCCMS; impaired association with alpha CHRNA1 subunit of AChR. 1 Publication
VAR_021213
Natural varianti75 – 751W → R in FCCMS; strongly reduces agonist affinity and gating efficiency. 1 Publication
VAR_071629
Natural varianti141 – 1411P → L in FCCMS; marked decrease in rate of AChR channel opening; reduction in frequency of open channel state and resistance to desensitization by ACh. 1 Publication
VAR_000289
Natural varianti163 – 1631S → L in FCCMS; fails to assemble with alpha CHRNA1 subunit of AChR. 1 Publication
VAR_021214
Natural varianti431 – 4311A → P in FCCMS; causes an increase in distributions of rates for channel opening and closing increasing the range of activation kinetics. 1 Publication
VAR_021215
Myasthenic syndrome, congenital, associated with acetylcholine receptor deficiency (CMS-ACHRD) [MIM:608931]: A post-synaptic congenital myasthenic syndrome. Congenital myasthenic syndromes (CMS) are inherited disorders of neuromuscular transmission that stem from mutations in presynaptic, synaptic, or postsynaptic proteins.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti167 – 1671R → L in CMS-ACHRD; significantly reduced AChR expression. 1 Publication
VAR_000290
Natural varianti265 – 2651P → L in CMS-ACHRD; prolongs burst open duration 2-fold by slowing the rate of channel closing. 1 Publication
VAR_000291
Natural varianti331 – 3311R → W in CMS-ACHRD; shortens burst duration 2-fold by slowing the rate of channel opening and speeding the rate of ACh dissociation; has a mild fast-channel kinetic effect on the AChR by shortening the long burst and increasing the decay of the endplate current. 1 Publication
VAR_000294

Keywords - Diseasei

Congenital myasthenic syndrome, Disease mutation

Organism-specific databases

MIMi254200. phenotype.
601462. phenotype.
608930. phenotype.
608931. phenotype.
Orphaneti98913. Postsynaptic congenital myasthenic syndromes.
PharmGKBiPA26498.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 493473Acetylcholine receptor subunit epsilonPRO_0000000329Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi86 – 861N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi148 ↔ 162By similarity
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ04844.
PRIDEiQ04844.

Expressioni

Gene expression databases

BgeeiQ04844.
CleanExiHS_CHRNE.
ExpressionAtlasiQ04844. baseline.
GenevestigatoriQ04844.

Interactioni

Subunit structurei

Pentamer of two alpha chains, and one each of the beta, delta, and gamma (in immature muscle) or epsilon (in mature muscle) chains.

Protein-protein interaction databases

BioGridi107567. 1 interaction.
STRINGi9606.ENSP00000293780.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DF9model-A240-332[»]
ProteinModelPortaliQ04844.
SMRiQ04844. Positions 20-485.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG291810.
GeneTreeiENSGT00770000120477.
HOGENOMiHOG000006757.
HOVERGENiHBG003756.
InParanoidiQ04844.
KOiK04817.
OMAiAIYRSTC.
OrthoDBiEOG7H7925.
PhylomeDBiQ04844.
TreeFamiTF315605.

Family and domain databases

Gene3Di1.20.120.370. 2 hits.
2.70.170.10. 1 hit.
InterProiIPR027361. Acetylcholine_rcpt_TM.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
IPR002394. Nicotinic_acetylcholine_rcpt.
[Graphical view]
PANTHERiPTHR18945. PTHR18945. 1 hit.
PfamiPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSiPR00254. NICOTINICR.
PR00252. NRIONCHANNEL.
SUPFAMiSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q04844-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARAPLGVLL LLGLLGRGVG KNEELRLYHH LFNNYDPGSR PVREPEDTVT
60 70 80 90 100
ISLKVTLTNL ISLNEKEETL TTSVWIGIDW QDYRLNYSKD DFGGIETLRV
110 120 130 140 150
PSELVWLPEI VLENNIDGQF GVAYDANVLV YEGGSVTWLP PAIYRSVCAV
160 170 180 190 200
EVTYFPFDWQ NCSLIFRSQT YNAEEVEFTF AVDNDGKTIN KIDIDTEAYT
210 220 230 240 250
ENGEWAIDFC PGVIRRHHGG ATDGPGETDV IYSLIIRRKP LFYVINIIVP
260 270 280 290 300
CVLISGLVLL AYFLPAQAGG QKCTVSINVL LAQTVFLFLI AQKIPETSLS
310 320 330 340 350
VPLLGRFLIF VMVVATLIVM NCVIVLNVSQ RTPTTHAMSP RLRHVLLELL
360 370 380 390 400
PRLLGSPPPP EAPRAASPPR RASSVGLLLR AEELILKKPR SELVFEGQRH
410 420 430 440 450
RQGTWTAAFC QSLGAAAPEV RCCVDAVNFV AESTRDQEAT GEEVSDWVRM
460 470 480 490
GNALDNICFW AALVLFSVGS SLIFLGAYFN RVPDLPYAPC IQP
Length:493
Mass (Da):54,697
Last modified:November 1, 1995 - v2
Checksum:iA34AF273AF8B31FE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131G → R in FCCMS; impaired association with alpha CHRNA1 subunit of AChR. 1 Publication
VAR_021213
Natural varianti18 – 181G → V.
Corresponds to variant rs4790235 [ dbSNP | Ensembl ].
VAR_048170
Natural varianti75 – 751W → R in FCCMS; strongly reduces agonist affinity and gating efficiency. 1 Publication
VAR_071629
Natural varianti98 – 981L → P in SCCMS; rare example of recessive inheritance. 1 Publication
Corresponds to variant rs28929768 [ dbSNP | Ensembl ].
VAR_019567
Natural varianti141 – 1411P → L in FCCMS; marked decrease in rate of AChR channel opening; reduction in frequency of open channel state and resistance to desensitization by ACh. 1 Publication
VAR_000289
Natural varianti163 – 1631S → L in FCCMS; fails to assemble with alpha CHRNA1 subunit of AChR. 1 Publication
VAR_021214
Natural varianti167 – 1671R → L in CMS-ACHRD; significantly reduced AChR expression. 1 Publication
VAR_000290
Natural varianti241 – 2411L → F in SCCMS; mild form with variable penetrance. 1 Publication
Corresponds to variant rs28999110 [ dbSNP | Ensembl ].
VAR_019568
Natural varianti265 – 2651P → L in CMS-ACHRD; prolongs burst open duration 2-fold by slowing the rate of channel closing. 1 Publication
VAR_000291
Natural varianti284 – 2841T → P in SCCMS; markedly prolonged channel openings in presence of agonist; as well as opening in the absence of agonist. 1 Publication
VAR_000292
Natural varianti289 – 2891L → F in SCCMS; slows rate of AChR channel closure and increases apparent affinity for ACh; causes pathologic channel openings even in the absence of ACh resulting in a leaky channel. 2 Publications
VAR_000293
Natural varianti331 – 3311R → W in CMS-ACHRD; shortens burst duration 2-fold by slowing the rate of channel opening and speeding the rate of ACh dissociation; has a mild fast-channel kinetic effect on the AChR by shortening the long burst and increasing the decay of the endplate current. 1 Publication
VAR_000294
Natural varianti431 – 4311A → P in FCCMS; causes an increase in distributions of rates for channel opening and closing increasing the range of activation kinetics. 1 Publication
VAR_021215

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66403 mRNA. Translation: CAA47030.1.
AF105999 Genomic DNA. Translation: AAD24503.1.
CH471108 Genomic DNA. Translation: EAW90395.1.
CH471108 Genomic DNA. Translation: EAW90396.1.
CCDSiCCDS11058.1.
PIRiS34775.
RefSeqiNP_000071.1. NM_000080.3.
UniGeneiHs.654535.

Genome annotation databases

EnsembliENST00000293780; ENSP00000293780; ENSG00000108556.
GeneIDi1145.
KEGGihsa:1145.
UCSCiuc002fzk.1. human.

Polymorphism databases

DMDMi1168301.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66403 mRNA. Translation: CAA47030.1 .
AF105999 Genomic DNA. Translation: AAD24503.1 .
CH471108 Genomic DNA. Translation: EAW90395.1 .
CH471108 Genomic DNA. Translation: EAW90396.1 .
CCDSi CCDS11058.1.
PIRi S34775.
RefSeqi NP_000071.1. NM_000080.3.
UniGenei Hs.654535.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DF9 model - A 240-332 [» ]
ProteinModelPortali Q04844.
SMRi Q04844. Positions 20-485.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107567. 1 interaction.
STRINGi 9606.ENSP00000293780.

Chemistry

BindingDBi Q04844.
ChEMBLi CHEMBL2362997.
DrugBanki DB00674. Galantamine.
GuidetoPHARMACOLOGYi 477.

Protein family/group databases

TCDBi 1.A.9.1.1. the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.

Polymorphism databases

DMDMi 1168301.

Proteomic databases

PaxDbi Q04844.
PRIDEi Q04844.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000293780 ; ENSP00000293780 ; ENSG00000108556 .
GeneIDi 1145.
KEGGi hsa:1145.
UCSCi uc002fzk.1. human.

Organism-specific databases

CTDi 1145.
GeneCardsi GC17M004801.
GeneReviewsi CHRNE.
H-InvDB HIX0027273.
HGNCi HGNC:1966. CHRNE.
MIMi 100725. gene.
254200. phenotype.
601462. phenotype.
608930. phenotype.
608931. phenotype.
neXtProti NX_Q04844.
Orphaneti 98913. Postsynaptic congenital myasthenic syndromes.
PharmGKBi PA26498.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG291810.
GeneTreei ENSGT00770000120477.
HOGENOMi HOG000006757.
HOVERGENi HBG003756.
InParanoidi Q04844.
KOi K04817.
OMAi AIYRSTC.
OrthoDBi EOG7H7925.
PhylomeDBi Q04844.
TreeFami TF315605.

Enzyme and pathway databases

Reactomei REACT_22223. Highly sodium permeable acetylcholine nicotinic receptors.

Miscellaneous databases

GeneWikii CHRNE.
GenomeRNAii 1145.
NextBioi 4764.
PROi Q04844.
SOURCEi Search...

Gene expression databases

Bgeei Q04844.
CleanExi HS_CHRNE.
ExpressionAtlasi Q04844. baseline.
Genevestigatori Q04844.

Family and domain databases

Gene3Di 1.20.120.370. 2 hits.
2.70.170.10. 1 hit.
InterProi IPR027361. Acetylcholine_rcpt_TM.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
IPR002394. Nicotinic_acetylcholine_rcpt.
[Graphical view ]
PANTHERi PTHR18945. PTHR18945. 1 hit.
Pfami PF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view ]
PRINTSi PR00254. NICOTINICR.
PR00252. NRIONCHANNEL.
SUPFAMi SSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
PROSITEi PS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of the human muscle acetylcholine receptor. cDNA cloning of the gamma and epsilon subunits."
    Beeson D.M.W., Brydson M., Betty M., Jeremiah S., Povey S., Vincent A., Newsom-Davis J.
    Eur. J. Biochem. 215:229-238(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Muscle fibroblast.
  2. Abicht A., Stucka R., Lochmuller H.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "A leucine-to-phenylalanine substitution in the acetylcholine receptor ion channel in a family with the slow-channel syndrome."
    Gomez C.M., Gammack J.T.
    Neurology 45:982-985(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SCCMS PHE-289.
  5. "Congenital myasthenic syndrome caused by prolonged acetylcholine receptor channel openings due to a mutation in the M2 domain of the epsilon subunit."
    Ohno K., Hutchinson D.O., Milone M., Brengman J.M., Bouzat C., Sine S.M., Engel A.G.
    Proc. Natl. Acad. Sci. U.S.A. 92:758-762(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SCCMS PRO-284, CHARACTERIZATION OF VARIANT SCCMS PRO-284.
  6. "New mutations in acetylcholine receptor subunit genes reveal heterogeneity in the slow-channel congenital myasthenic syndrome."
    Engel A.G., Ohno K., Milone M., Wang H.-L., Nakano S., Bouzat C., Pruitt J.N. II, Hutchinson D.O., Brengman J.M., Bren N., Sieb J.P., Sine S.M.
    Hum. Mol. Genet. 5:1217-1227(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SCCMS PHE-289, CHARACTERIZATION OF VARIANT SCCMS PHE-289.
  7. "Congenital myasthenic syndrome caused by decreased agonist binding affinity due to a mutation in the acetylcholine receptor epsilon subunit."
    Ohno K., Wang H.-L., Milone M., Bren N., Brengman J.M., Nakano S., Quiram P., Pruitt J.N. II, Sine S.M., Engel A.G.
    Neuron 17:157-170(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS FCCMS ARG-13; LEU-141 AND LEU-163, CHARACTERIZATION OF VARIANTS FCCMS ARG-13; LEU-141 AND LEU-163.
  8. "Congenital myasthenic syndromes due to heteroallelic nonsense/missense mutations in the acetylcholine receptor epsilon subunit gene: identification and functional characterization of six new mutations."
    Ohno K., Quiram P.A., Milone M., Wang H.-L., Harper M.C., Pruitt J.N. II, Brengman J.M., Pao L., Fischbeck K.H., Crawford T.O., Sine S.M., Engel A.G.
    Hum. Mol. Genet. 6:753-766(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CMS-ACHRD LEU-167; LEU-265 AND TRP-331, CHARACTERIZATION OF VARIANTS CMS-ACHRD LEU-167; LEU-265 AND TRP-331.
  9. "Fundamental gating mechanism of nicotinic receptor channel revealed by mutation causing a congenital myasthenic syndrome."
    Wang H.-L., Ohno K., Milone M., Brengman J.M., Evoli A., Batocchi A.-P., Middleton L.T., Christodoulou K., Engel A.G., Sine S.M.
    J. Gen. Physiol. 116:449-462(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FCCMS PRO-431, CHARACTERIZATION OF VARIANT FCCMS PRO-431.
  10. "Recessive inheritance and variable penetrance of slow-channel congenital myasthenic syndromes."
    Croxen R., Hatton C., Shelley C., Brydson M., Chauplannaz G., Oosterhuis H., Vincent A., Newsom-Davis J., Colquhoun D., Beeson D.
    Neurology 59:162-168(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SCCMS PRO-98 AND PHE-241.
  11. "Highly fatal fast-channel syndrome caused by AChR epsilon subunit mutation at the agonist binding site."
    Shen X.M., Brengman J.M., Edvardson S., Sine S.M., Engel A.G.
    Neurology 79:449-454(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FCCMS ARG-75, CHARACTERIZATION OF VARIANT FCCMS ARG-75.

Entry informationi

Entry nameiACHE_HUMAN
AccessioniPrimary (citable) accession number: Q04844
Secondary accession number(s): D3DTK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 142 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3