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Q9Y215

- COLQ_HUMAN

UniProt

Q9Y215 - COLQ_HUMAN

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Protein
Acetylcholinesterase collagenic tail peptide
Gene
COLQ
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

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

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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 – 2222 Reviewed prediction
Add
BLAST
Chaini23 – 455433Acetylcholinesterase collagenic tail peptide
PRO_0000005854Add
BLAST

Amino acid modifications

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

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).

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.

Miscellaneous databases

EvolutionaryTraceiQ9Y215.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 6717PRAD
Add
BLAST
Regioni130 – 1334Heparan sulfate proteoglycan binding Reviewed prediction
Regioni235 – 2384Heparan sulfate proteoglycan binding Reviewed prediction

Domaini

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

Sequence similaritiesi

Belongs to the COLQ family.

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

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.
VSP_001175Add
BLAST
Alternative sequencei73 – 764Missing in isoform IV.
VSP_001176
Alternative sequencei74 – 10734Missing in isoform III.
VSP_001177Add
BLAST
Alternative sequencei124 – 1329Missing in isoform V.
VSP_001178
Alternative sequencei240 – 29152GQKGD…PPGRC → SSRTPCTLPRRPPVPCGQGS RSPVTVVAGNESQACLLPRF EEDYISSGTERG in isoform VI.
VSP_001179Add
BLAST
Alternative sequencei272 – 28110GQLIMGPKGE → DFCGQQPGGA in isoform VII.
VSP_001180
Alternative sequencei273 – 32957QLIMG…QEELE → HMETCNAPSTATSTPRPAAT SPEGREEKVGCAPQNWQQLL HCHQTGHVLAPSPPTFV in isoform VIII.
VSP_001181Add
BLAST
Alternative sequencei282 – 455174Missing in isoform VII.
VSP_001182Add
BLAST
Alternative sequencei292 – 455164Missing in isoform VI.
VSP_001183Add
BLAST
Alternative sequencei330 – 455126Missing in isoform VIII.
VSP_001184Add
BLAST

Sequence conflict

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

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]
ENST00000383787; ENSP00000373297; ENSG00000206561. [Q9Y215-5]
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...

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 ]
ENST00000383787 ; ENSP00000373297 ; ENSG00000206561 . [Q9Y215-5 ]
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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 133 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

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