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Q9Y215

- COLQ_HUMAN

UniProt

Q9Y215 - COLQ_HUMAN

Protein

Acetylcholinesterase collagenic tail peptide

Gene

COLQ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina.

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. acetylcholine catabolic process in synaptic cleft Source: ProtInc
    2. asymmetric protein localization Source: ProtInc

    Keywords - Biological processi

    Neurotransmitter degradation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetylcholinesterase collagenic tail peptide
    Alternative name(s):
    AChE Q subunit
    Acetylcholinesterase-associated collagen
    Gene namesi
    Name:COLQ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:2226. COLQ.

    Subcellular locationi

    GO - Cellular componenti

    1. basal lamina Source: ProtInc
    2. cell junction Source: UniProtKB-KW
    3. collagen trimer Source: UniProtKB-KW
    4. extracellular space Source: ProtInc
    5. synapse Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Synapse

    Pathology & Biotechi

    Involvement in diseasei

    Myasthenic syndrome, congenital, Engel type (CMSE) [MIM:603034]: A rare autosomal recessive congenital myasthenic syndrome characterized by onset during childhood, generalized weakness, abnormal fatigability on exertion, refrectoriness to acetylcholinesterase drugs, decremental electromyographic response and morphological abnormalities of the neuromuscular junctions.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti59 – 591P → Q in CMSE; abrogates binding to T subunit. 1 Publication
    VAR_010133
    Natural varianti342 – 3421D → E in CMSE; impairs anchoring to the basal lamina. 1 Publication
    VAR_010134
    Natural varianti410 – 4101R → Q in CMSE. 1 Publication
    VAR_010135
    Natural varianti430 – 4301Y → S in CMSE. 1 Publication
    VAR_010136
    Natural varianti444 – 4441C → Y in CMSE. 1 Publication
    VAR_010137

    Keywords - Diseasei

    Congenital myasthenic syndrome, Disease mutation

    Organism-specific databases

    MIMi603034. phenotype.
    Orphaneti98915. Synaptic congenital myasthenic syndromes.
    PharmGKBiPA26743.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 455433Acetylcholinesterase collagenic tail peptidePRO_0000005854Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi51 – 51Interchain (with T subunit)Sequence Analysis
    Disulfide bondi52 – 52Interchain (with T subunit)Sequence Analysis
    Disulfide bondi93 – 93InterchainSequence Analysis
    Disulfide bondi291 – 291InterchainSequence Analysis
    Disulfide bondi293 – 293InterchainSequence Analysis

    Post-translational modificationi

    The triple-helical tail is stabilized by disulfide bonds at each end.

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiQ9Y215.
    PRIDEiQ9Y215.

    PTM databases

    PhosphoSiteiQ9Y215.

    Expressioni

    Tissue specificityi

    Found at the end plate of skeletal muscle.

    Gene expression databases

    ArrayExpressiQ9Y215.
    BgeeiQ9Y215.
    GenevestigatoriQ9Y215.

    Interactioni

    Subunit structurei

    Homotrimer. Component of the asymmetric form of AChE, a disulfide-bonded oligomer composed of the collagenic subunits (Q) and a variable number of asymmetric catalytic subunits (T). The N-terminal of a collagenic subunit (Q) associates with the C-terminal of a catalytic subunit (T).1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACHEP223032EBI-1637847,EBI-1637793

    Protein-protein interaction databases

    BioGridi113897. 2 interactions.
    IntActiQ9Y215. 1 interaction.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VZJX-ray2.35I/J53-67[»]
    ProteinModelPortaliQ9Y215.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y215.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini96 – 269174Collagen-like 1Add
    BLAST
    Domaini277 – 29115Collagen-like 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni51 – 6717PRADAdd
    BLAST
    Regioni130 – 1334Heparan sulfate proteoglycan bindingSequence Analysis
    Regioni235 – 2384Heparan sulfate proteoglycan bindingSequence Analysis

    Domaini

    The proline-rich attachment domain (PRAD) binds the AChE catalytic subunits.

    Sequence similaritiesi

    Belongs to the COLQ family.Curated
    Contains 2 collagen-like domains.Curated

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG329823.
    HOVERGENiHBG102052.
    InParanoidiQ9Y215.
    PhylomeDBiQ9Y215.
    TreeFamiTF331890.

    Family and domain databases

    InterProiIPR008160. Collagen.
    IPR011936. Myxo_disulph_rpt.
    [Graphical view]
    PfamiPF01391. Collagen. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02232. myxo_disulf_rpt. 1 hit.

    Sequences (8)i

    Sequence statusi: Complete.

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

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Isoform I (identifier: Q9Y215-1) [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

    MVVLNPMTLG IYLQLFFLSI VSQPTFINSV LPISAALPSL DQKKRGGHKA    50
    CCLLTPPPPP LFPPPFFRGG RSPLLSPDMK NLMLELETSQ SPCMQGSLGS 100
    PGPPGPQGPP GLPGKTGPKG EKGELGRPGR KGRPGPPGVP GMPGPIGWPG 150
    PEGPRGEKGD LGMMGLPGSR GPMGSKGYPG SRGEKGSRGE KGDLGPKGEK 200
    GFPGFPGMLG QKGEMGPKGE PGIAGHRGPT GRPGKRGKQG QKGDSGVMGP 250
    PGKPGPSGQP GRPGPPGPPP AGQLIMGPKG ERGFPGPPGR CLCGPTMNVN 300
    NPSYGESVYG PSSPRVPVIF VVNNQEELER LNTQNAIAFR RDQRSLYFKD 350
    SLGWLPIQLT PFYPVDYTAD QHGTCGDGLL QPGEECDDGN SDVGDDCIRC 400
    HRAYCGDGHR HEGVEDCDGS DFGYLTCETY LPGSYGDLQC TQYCYIDSTP 450
    CRYFT 455
    Length:455
    Mass (Da):47,766
    Last modified:October 17, 2006 - v2
    Checksum:iA95D3E5D5ECDBE55
    GO
    Isoform II (identifier: Q9Y215-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-35: MVVLNPMTLGIYLQLFFLSIVSQPTFINSVLPISA → MTGSSFSLAHLLIISGLLCYSAGCL

    Show »
    Length:445
    Mass (Da):46,457
    Checksum:i8677E75D64046DE7
    GO
    Isoform III (identifier: Q9Y215-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         74-107: Missing.

    Show »
    Length:421
    Mass (Da):44,243
    Checksum:i490EE07243B21B03
    GO
    Isoform IV (identifier: Q9Y215-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         73-76: Missing.

    Show »
    Length:451
    Mass (Da):47,356
    Checksum:i82557E51EC65241E
    GO
    Isoform V (identifier: Q9Y215-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         124-132: Missing.

    Show »
    Length:446
    Mass (Da):46,815
    Checksum:iC3D9F2E1C1FFA6F4
    GO
    Isoform VI (identifier: Q9Y215-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         240-291: GQKGDSGVMG...RGFPGPPGRC → SSRTPCTLPR...DYISSGTERG
         292-455: Missing.

    Show »
    Length:291
    Mass (Da):30,024
    Checksum:i7DFC921C5B98D84B
    GO
    Isoform VII (identifier: Q9Y215-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         272-281: GQLIMGPKGE → DFCGQQPGGA
         282-455: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:281
    Mass (Da):28,354
    Checksum:iFE0A55A8FAE0E135
    GO
    Isoform VIII (identifier: Q9Y215-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         273-329: QLIMGPKGER...FVVNNQEELE → HMETCNAPST...VLAPSPPTFV
         330-455: Missing.

    Show »
    Length:329
    Mass (Da):33,538
    Checksum:iA3ECE29DEDE5766F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti370 – 3701D → N in AAO06818. 1 PublicationCurated
    Sequence conflicti399 – 3991R → RD in CAA12648. (PubMed:9758617)Curated
    Sequence conflicti399 – 3991R → RD in AAO06814. 1 PublicationCurated
    Sequence conflicti399 – 3991R → RD in AAO06816. 1 PublicationCurated
    Sequence conflicti399 – 3991R → RD in AAO06817. 1 PublicationCurated
    Sequence conflicti399 – 3991R → RD in AAO06818. 1 PublicationCurated
    Sequence conflicti399 – 3991R → RD in AAO06819. 1 PublicationCurated
    Sequence conflicti400 – 4001C → Y in AAO06816. 1 PublicationCurated
    Sequence conflicti404 – 4041Y → D in AAO06817. 1 PublicationCurated
    Sequence conflicti423 – 4231G → V in AAO06819. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti59 – 591P → Q in CMSE; abrogates binding to T subunit. 1 Publication
    VAR_010133
    Natural varianti312 – 3121S → G.
    Corresponds to variant rs6782980 [ dbSNP | Ensembl ].
    VAR_048809
    Natural varianti342 – 3421D → E in CMSE; impairs anchoring to the basal lamina. 1 Publication
    VAR_010134
    Natural varianti410 – 4101R → Q in CMSE. 1 Publication
    VAR_010135
    Natural varianti430 – 4301Y → S in CMSE. 1 Publication
    VAR_010136
    Natural varianti444 – 4441C → Y in CMSE. 1 Publication
    VAR_010137

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3535MVVLN…LPISA → MTGSSFSLAHLLIISGLLCY SAGCL in isoform II. 1 PublicationVSP_001175Add
    BLAST
    Alternative sequencei73 – 764Missing in isoform IV. CuratedVSP_001176
    Alternative sequencei74 – 10734Missing in isoform III. CuratedVSP_001177Add
    BLAST
    Alternative sequencei124 – 1329Missing in isoform V. CuratedVSP_001178
    Alternative sequencei240 – 29152GQKGD…PPGRC → SSRTPCTLPRRPPVPCGQGS RSPVTVVAGNESQACLLPRF EEDYISSGTERG in isoform VI. CuratedVSP_001179Add
    BLAST
    Alternative sequencei272 – 28110GQLIMGPKGE → DFCGQQPGGA in isoform VII. CuratedVSP_001180
    Alternative sequencei273 – 32957QLIMG…QEELE → HMETCNAPSTATSTPRPAAT SPEGREEKVGCAPQNWQQLL HCHQTGHVLAPSPPTFV in isoform VIII. CuratedVSP_001181Add
    BLAST
    Alternative sequencei282 – 455174Missing in isoform VII. CuratedVSP_001182Add
    BLAST
    Alternative sequencei292 – 455164Missing in isoform VI. CuratedVSP_001183Add
    BLAST
    Alternative sequencei330 – 455126Missing in isoform VIII. CuratedVSP_001184Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ225895 mRNA. Translation: CAA12648.1.
    AF057036 mRNA. Translation: AAC39927.1.
    AF229126
    , AF229117, AF229118, AF229119, AF229120, AF229121, AF229122, AF229123, AF229124, AF229125 Genomic DNA. Translation: AAF43195.1.
    AF229126
    , AF229118, AF229119, AF229120, AF229121, AF229122, AF229123, AF229124, AF229125 Genomic DNA. Translation: AAF43196.1.
    AF229126
    , AF229117, AF229118, AF229119, AF229120, AF229121, AF229122, AF229123, AF229124, AF229125 Genomic DNA. Translation: AAF43197.1.
    AF229126
    , AF229117, AF229118, AF229119, AF229120, AF229121, AF229122, AF229123, AF229124, AF229125 Genomic DNA. Translation: AAF43198.1.
    AF229126
    , AF229117, AF229118, AF229119, AF229120, AF229121, AF229122, AF229123, AF229124, AF229125 Genomic DNA. Translation: AAF43199.1.
    AF229122
    , AF229117, AF229118, AF229119, AF229120, AF229121 Genomic DNA. Translation: AAF43200.1.
    AF229124
    , AF229117, AF229118, AF229119, AF229120, AF229121, AF229122 Genomic DNA. Translation: AAF43201.1.
    AF229126
    , AF229117, AF229118, AF229119, AF229120, AF229121, AF229122 Genomic DNA. Translation: AAF43202.1.
    AY150334 mRNA. Translation: AAO06814.1.
    AY150336 mRNA. Translation: AAO06816.1.
    AY150337 mRNA. Translation: AAO06817.1.
    AY150338 mRNA. Translation: AAO06818.1.
    AY150339 mRNA. Translation: AAO06819.1.
    AK128401 mRNA. Translation: BAG54671.1.
    CH471055 Genomic DNA. Translation: EAW64250.1.
    BC074828 mRNA. Translation: AAH74828.1.
    BC074829 mRNA. Translation: AAH74829.1.
    CCDSiCCDS33709.1. [Q9Y215-1]
    CCDS43057.1. [Q9Y215-3]
    CCDS46768.1. [Q9Y215-2]
    RefSeqiNP_005668.2. NM_005677.3. [Q9Y215-1]
    NP_536799.1. NM_080538.2. [Q9Y215-2]
    NP_536800.2. NM_080539.3. [Q9Y215-3]
    UniGeneiHs.146735.

    Genome annotation databases

    EnsembliENST00000383781; ENSP00000373291; ENSG00000206561. [Q9Y215-2]
    ENST00000383786; ENSP00000373296; ENSG00000206561. [Q9Y215-3]
    ENST00000383788; ENSP00000373298; ENSG00000206561. [Q9Y215-1]
    ENST00000603808; ENSP00000474271; ENSG00000206561.
    GeneIDi8292.
    KEGGihsa:8292.
    UCSCiuc003bzv.3. human. [Q9Y215-2]
    uc003bzx.3. human. [Q9Y215-1]
    uc010heo.3. human. [Q9Y215-3]

    Polymorphism databases

    DMDMi116241309.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ225895 mRNA. Translation: CAA12648.1 .
    AF057036 mRNA. Translation: AAC39927.1 .
    AF229126
    , AF229117 , AF229118 , AF229119 , AF229120 , AF229121 , AF229122 , AF229123 , AF229124 , AF229125 Genomic DNA. Translation: AAF43195.1 .
    AF229126
    , AF229118 , AF229119 , AF229120 , AF229121 , AF229122 , AF229123 , AF229124 , AF229125 Genomic DNA. Translation: AAF43196.1 .
    AF229126
    , AF229117 , AF229118 , AF229119 , AF229120 , AF229121 , AF229122 , AF229123 , AF229124 , AF229125 Genomic DNA. Translation: AAF43197.1 .
    AF229126
    , AF229117 , AF229118 , AF229119 , AF229120 , AF229121 , AF229122 , AF229123 , AF229124 , AF229125 Genomic DNA. Translation: AAF43198.1 .
    AF229126
    , AF229117 , AF229118 , AF229119 , AF229120 , AF229121 , AF229122 , AF229123 , AF229124 , AF229125 Genomic DNA. Translation: AAF43199.1 .
    AF229122
    , AF229117 , AF229118 , AF229119 , AF229120 , AF229121 Genomic DNA. Translation: AAF43200.1 .
    AF229124
    , AF229117 , AF229118 , AF229119 , AF229120 , AF229121 , AF229122 Genomic DNA. Translation: AAF43201.1 .
    AF229126
    , AF229117 , AF229118 , AF229119 , AF229120 , AF229121 , AF229122 Genomic DNA. Translation: AAF43202.1 .
    AY150334 mRNA. Translation: AAO06814.1 .
    AY150336 mRNA. Translation: AAO06816.1 .
    AY150337 mRNA. Translation: AAO06817.1 .
    AY150338 mRNA. Translation: AAO06818.1 .
    AY150339 mRNA. Translation: AAO06819.1 .
    AK128401 mRNA. Translation: BAG54671.1 .
    CH471055 Genomic DNA. Translation: EAW64250.1 .
    BC074828 mRNA. Translation: AAH74828.1 .
    BC074829 mRNA. Translation: AAH74829.1 .
    CCDSi CCDS33709.1. [Q9Y215-1 ]
    CCDS43057.1. [Q9Y215-3 ]
    CCDS46768.1. [Q9Y215-2 ]
    RefSeqi NP_005668.2. NM_005677.3. [Q9Y215-1 ]
    NP_536799.1. NM_080538.2. [Q9Y215-2 ]
    NP_536800.2. NM_080539.3. [Q9Y215-3 ]
    UniGenei Hs.146735.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VZJ X-ray 2.35 I/J 53-67 [» ]
    ProteinModelPortali Q9Y215.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113897. 2 interactions.
    IntActi Q9Y215. 1 interaction.

    PTM databases

    PhosphoSitei Q9Y215.

    Polymorphism databases

    DMDMi 116241309.

    Proteomic databases

    PaxDbi Q9Y215.
    PRIDEi Q9Y215.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000383781 ; ENSP00000373291 ; ENSG00000206561 . [Q9Y215-2 ]
    ENST00000383786 ; ENSP00000373296 ; ENSG00000206561 . [Q9Y215-3 ]
    ENST00000383788 ; ENSP00000373298 ; ENSG00000206561 . [Q9Y215-1 ]
    ENST00000603808 ; ENSP00000474271 ; ENSG00000206561 .
    GeneIDi 8292.
    KEGGi hsa:8292.
    UCSCi uc003bzv.3. human. [Q9Y215-2 ]
    uc003bzx.3. human. [Q9Y215-1 ]
    uc010heo.3. human. [Q9Y215-3 ]

    Organism-specific databases

    CTDi 8292.
    GeneCardsi GC03M015491.
    GeneReviewsi COLQ.
    HGNCi HGNC:2226. COLQ.
    MIMi 603033. gene.
    603034. phenotype.
    neXtProti NX_Q9Y215.
    Orphaneti 98915. Synaptic congenital myasthenic syndromes.
    PharmGKBi PA26743.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG329823.
    HOVERGENi HBG102052.
    InParanoidi Q9Y215.
    PhylomeDBi Q9Y215.
    TreeFami TF331890.

    Miscellaneous databases

    EvolutionaryTracei Q9Y215.
    GeneWikii COLQ.
    GenomeRNAii 8292.
    NextBioi 31075.
    PROi Q9Y215.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y215.
    Bgeei Q9Y215.
    Genevestigatori Q9Y215.

    Family and domain databases

    InterProi IPR008160. Collagen.
    IPR011936. Myxo_disulph_rpt.
    [Graphical view ]
    Pfami PF01391. Collagen. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02232. myxo_disulf_rpt. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Mutation in the human acetylcholinesterase-associated collagen gene, COLQ, is responsible for congenital myasthenic syndrome with end-plate acetylcholinesterase deficiency (Type Ic)."
      Donger C., Krejci E., Serradell A.P., Eymard B., Bon S., Nicole S., Chateau D., Gary F., Fardeau M., Massoulie J., Guicheney P.
      Am. J. Hum. Genet. 63:967-975(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CMSE SER-430.
      Tissue: Blood and Skeletal muscle.
    2. "Human endplate acetylcholinesterase deficiency caused by mutations in the collagen-like tail subunit (ColQ) of the asymmetric enzyme."
      Ohno K., Brengman J., Tsujino A., Engel A.G.
      Proc. Natl. Acad. Sci. U.S.A. 95:9654-9659(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING.
      Tissue: Skeletal muscle.
    3. Arredondo J., DeLeon M.
      Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "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] (ISOFORM II).
      Tissue: Thymus.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Lung.
    7. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    8. "The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix."
      Dvir H., Harel M., Bon S., Liu W.-Q., Vidal M., Garbay C., Sussman J.L., Massoulie J., Silman I.
      EMBO J. 23:4394-4405(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 53-67 IN COMPLEX WITH ACHE.
    9. Cited for: VARIANTS CMSE GLN-59; GLU-342; GLN-410 AND TYR-444.
      Tissue: Blood and Muscle.

    Entry informationi

    Entry nameiCOLQ_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y215
    Secondary accession number(s): B3KY09
    , Q6DK18, Q6YH18, Q6YH19, Q6YH20, Q6YH21, Q9NP18, Q9NP19, Q9NP20, Q9NP21, Q9NP22, Q9NP23, Q9NP24, Q9UP88
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 134 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 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3