Q9Y215 (COLQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetylcholinesterase collagenic tail peptide

Alternative name(s):
AChE Q subunit
Acetylcholinesterase-associated collagen

Gene names

Name:

COLQ

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	455 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina.
Subunit structure	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).
Subcellular location	Cell junction › synapse.
Tissue specificity	Found at the end plate of skeletal muscle.
Domain	The proline-rich attachment domain (PRAD) binds the AChE catalytic subunits.
Post-translational modification	The triple-helical tail is stabilized by disulfide bonds at each end.
Involvement in disease	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. Ref.1 Ref.9
Sequence similarities	Belongs to the COLQ family. Contains 2 collagen-like domains.

Ontologies

Keywords
Biological process	Neurotransmitter degradation
Cellular component	Cell junction Synapse
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Congenital myasthenic syndrome Disease mutation
Domain	Collagen Repeat Signal
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acetylcholine catabolic process in synaptic cleft Traceable author statement Ref.2. Source: ProtInc asymmetric protein localization Traceable author statement Ref.2. Source: ProtInc
Cellular_component	basal lamina Traceable author statement Ref.2. Source: ProtInc cell junction Inferred from electronic annotation. Source: UniProtKB-KW collagen Inferred from electronic annotation. Source: UniProtKB-KW extracellular space Traceable author statement Ref.2. Source: ProtInc synapse Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACHE	P22303	2	EBI-1637847,EBI-1637793

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Isoform I (identifier: Q9Y215-1)

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.

Isoform II (identifier: Q9Y215-2)

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

Isoform III (identifier: Q9Y215-3)

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

Isoform IV (identifier: Q9Y215-4)

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

Isoform V (identifier: Q9Y215-5)

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

Isoform VI (identifier: Q9Y215-6)

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

Isoform VII (identifier: Q9Y215-7)

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.

Isoform VIII (identifier: Q9Y215-8)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 455	433	Acetylcholinesterase collagenic tail peptide		PRO_0000005854
Regions
	Domain	96 – 269	174	Collagen-like 1
	Domain	277 – 291	15	Collagen-like 2
	Region	51 – 67	17	PRAD
	Region	130 – 133	4	Heparan sulfate proteoglycan binding Potential
	Region	235 – 238	4	Heparan sulfate proteoglycan binding Potential
Amino acid modifications
	Disulfide bond	51		Interchain (with T subunit) Potential
	Disulfide bond	52		Interchain (with T subunit) Potential
	Disulfide bond	93		Interchain Potential
	Disulfide bond	291		Interchain Potential
	Disulfide bond	293		Interchain Potential
Natural variations
	Alternative sequence	1 – 35	35	MVVLN…LPISA → MTGSSFSLAHLLIISGLLCY SAGCL in isoform II.		VSP_001175
	Alternative sequence	73 – 76	4	Missing in isoform IV.		VSP_001176
	Alternative sequence	74 – 107	34	Missing in isoform III.		VSP_001177
	Alternative sequence	124 – 132	9	Missing in isoform V.		VSP_001178
	Alternative sequence	240 – 291	52	GQKGD…PPGRC → SSRTPCTLPRRPPVPCGQGS RSPVTVVAGNESQACLLPRF EEDYISSGTERG in isoform VI.		VSP_001179
	Alternative sequence	272 – 281	10	GQLIMGPKGE → DFCGQQPGGA in isoform VII.		VSP_001180
	Alternative sequence	273 – 329	57	QLIMG…QEELE → HMETCNAPSTATSTPRPAAT SPEGREEKVGCAPQNWQQLL HCHQTGHVLAPSPPTFV in isoform VIII.		VSP_001181
	Alternative sequence	282 – 455	174	Missing in isoform VII.		VSP_001182
	Alternative sequence	292 – 455	164	Missing in isoform VI.		VSP_001183
	Alternative sequence	330 – 455	126	Missing in isoform VIII.		VSP_001184
	Natural variant	59	1	P → Q in CMSE; abrogates binding to T subunit. Ref.9		VAR_010133
	Natural variant	312	1	S → G. Corresponds to variant rs6782980 [ dbSNP | Ensembl ].		VAR_048809
	Natural variant	342	1	D → E in CMSE; impairs anchoring to the basal lamina. Ref.9		VAR_010134
	Natural variant	410	1	R → Q in CMSE. Ref.9		VAR_010135
	Natural variant	430	1	Y → S in CMSE. Ref.1		VAR_010136
	Natural variant	444	1	C → Y in CMSE. Ref.9		VAR_010137
Experimental info
	Sequence conflict	370	1	D → N in AAO06818. Ref.3
	Sequence conflict	399	1	R → RD in CAA12648. Ref.1
	Sequence conflict	399	1	R → RD in AAO06814. Ref.3
	Sequence conflict	399	1	R → RD in AAO06816. Ref.3
	Sequence conflict	399	1	R → RD in AAO06817. Ref.3
	Sequence conflict	399	1	R → RD in AAO06818. Ref.3
	Sequence conflict	399	1	R → RD in AAO06819. Ref.3
	Sequence conflict	400	1	C → Y in AAO06816. Ref.3
	Sequence conflict	404	1	Y → D in AAO06817. Ref.3
	Sequence conflict	423	1	G → V in AAO06819. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform I [UniParc]. Last modified October 17, 2006. Version 2. Checksum: A95D3E5D5ECDBE55	FASTA	455	47,766
	10 20 30 40 50 60 MVVLNPMTLG IYLQLFFLSI VSQPTFINSV LPISAALPSL DQKKRGGHKA CCLLTPPPPP 70 80 90 100 110 120 LFPPPFFRGG RSPLLSPDMK NLMLELETSQ SPCMQGSLGS PGPPGPQGPP GLPGKTGPKG 130 140 150 160 170 180 EKGELGRPGR KGRPGPPGVP GMPGPIGWPG PEGPRGEKGD LGMMGLPGSR GPMGSKGYPG 190 200 210 220 230 240 SRGEKGSRGE KGDLGPKGEK GFPGFPGMLG QKGEMGPKGE PGIAGHRGPT GRPGKRGKQG 250 260 270 280 290 300 QKGDSGVMGP PGKPGPSGQP GRPGPPGPPP AGQLIMGPKG ERGFPGPPGR CLCGPTMNVN 310 320 330 340 350 360 NPSYGESVYG PSSPRVPVIF VVNNQEELER LNTQNAIAFR RDQRSLYFKD SLGWLPIQLT 370 380 390 400 410 420 PFYPVDYTAD QHGTCGDGLL QPGEECDDGN SDVGDDCIRC HRAYCGDGHR HEGVEDCDGS 430 440 450 DFGYLTCETY LPGSYGDLQC TQYCYIDSTP CRYFT
	Isoform II [UniParc]. Checksum: 8677E75D64046DE7	FASTA	445	46,457
	10 20 30 40 50 60 MTGSSFSLAH LLIISGLLCY SAGCLALPSL DQKKRGGHKA CCLLTPPPPP LFPPPFFRGG 70 80 90 100 110 120 RSPLLSPDMK NLMLELETSQ SPCMQGSLGS PGPPGPQGPP GLPGKTGPKG EKGELGRPGR 130 140 150 160 170 180 KGRPGPPGVP GMPGPIGWPG PEGPRGEKGD LGMMGLPGSR GPMGSKGYPG SRGEKGSRGE 190 200 210 220 230 240 KGDLGPKGEK GFPGFPGMLG QKGEMGPKGE PGIAGHRGPT GRPGKRGKQG QKGDSGVMGP 250 260 270 280 290 300 PGKPGPSGQP GRPGPPGPPP AGQLIMGPKG ERGFPGPPGR CLCGPTMNVN NPSYGESVYG 310 320 330 340 350 360 PSSPRVPVIF VVNNQEELER LNTQNAIAFR RDQRSLYFKD SLGWLPIQLT PFYPVDYTAD 370 380 390 400 410 420 QHGTCGDGLL QPGEECDDGN SDVGDDCIRC HRAYCGDGHR HEGVEDCDGS DFGYLTCETY 430 440 LPGSYGDLQC TQYCYIDSTP CRYFT
	Isoform III [UniParc]. Checksum: 490EE07243B21B03	FASTA	421	44,243
	10 20 30 40 50 60 MVVLNPMTLG IYLQLFFLSI VSQPTFINSV LPISAALPSL DQKKRGGHKA CCLLTPPPPP 70 80 90 100 110 120 LFPPPFFRGG RSPGPPGLPG KTGPKGEKGE LGRPGRKGRP GPPGVPGMPG PIGWPGPEGP 130 140 150 160 170 180 RGEKGDLGMM GLPGSRGPMG SKGYPGSRGE KGSRGEKGDL GPKGEKGFPG FPGMLGQKGE 190 200 210 220 230 240 MGPKGEPGIA GHRGPTGRPG KRGKQGQKGD SGVMGPPGKP GPSGQPGRPG PPGPPPAGQL 250 260 270 280 290 300 IMGPKGERGF PGPPGRCLCG PTMNVNNPSY GESVYGPSSP RVPVIFVVNN QEELERLNTQ 310 320 330 340 350 360 NAIAFRRDQR SLYFKDSLGW LPIQLTPFYP VDYTADQHGT CGDGLLQPGE ECDDGNSDVG 370 380 390 400 410 420 DDCIRCHRAY CGDGHRHEGV EDCDGSDFGY LTCETYLPGS YGDLQCTQYC YIDSTPCRYF T
	Isoform IV [UniParc]. Checksum: 82557E51EC65241E	FASTA	451	47,356
	10 20 30 40 50 60 MVVLNPMTLG IYLQLFFLSI VSQPTFINSV LPISAALPSL DQKKRGGHKA CCLLTPPPPP 70 80 90 100 110 120 LFPPPFFRGG RSPDMKNLML ELETSQSPCM QGSLGSPGPP GPQGPPGLPG KTGPKGEKGE 130 140 150 160 170 180 LGRPGRKGRP GPPGVPGMPG PIGWPGPEGP RGEKGDLGMM GLPGSRGPMG SKGYPGSRGE 190 200 210 220 230 240 KGSRGEKGDL GPKGEKGFPG FPGMLGQKGE MGPKGEPGIA GHRGPTGRPG KRGKQGQKGD 250 260 270 280 290 300 SGVMGPPGKP GPSGQPGRPG PPGPPPAGQL IMGPKGERGF PGPPGRCLCG PTMNVNNPSY 310 320 330 340 350 360 GESVYGPSSP RVPVIFVVNN QEELERLNTQ NAIAFRRDQR SLYFKDSLGW LPIQLTPFYP 370 380 390 400 410 420 VDYTADQHGT CGDGLLQPGE ECDDGNSDVG DDCIRCHRAY CGDGHRHEGV EDCDGSDFGY 430 440 450 LTCETYLPGS YGDLQCTQYC YIDSTPCRYF T
	Isoform V [UniParc]. Checksum: C3D9F2E1C1FFA6F4	FASTA	446	46,815
	10 20 30 40 50 60 MVVLNPMTLG IYLQLFFLSI VSQPTFINSV LPISAALPSL DQKKRGGHKA CCLLTPPPPP 70 80 90 100 110 120 LFPPPFFRGG RSPLLSPDMK NLMLELETSQ SPCMQGSLGS PGPPGPQGPP GLPGKTGPKG 130 140 150 160 170 180 EKGRPGPPGV PGMPGPIGWP GPEGPRGEKG DLGMMGLPGS RGPMGSKGYP GSRGEKGSRG 190 200 210 220 230 240 EKGDLGPKGE KGFPGFPGML GQKGEMGPKG EPGIAGHRGP TGRPGKRGKQ GQKGDSGVMG 250 260 270 280 290 300 PPGKPGPSGQ PGRPGPPGPP PAGQLIMGPK GERGFPGPPG RCLCGPTMNV NNPSYGESVY 310 320 330 340 350 360 GPSSPRVPVI FVVNNQEELE RLNTQNAIAF RRDQRSLYFK DSLGWLPIQL TPFYPVDYTA 370 380 390 400 410 420 DQHGTCGDGL LQPGEECDDG NSDVGDDCIR CHRAYCGDGH RHEGVEDCDG SDFGYLTCET 430 440 YLPGSYGDLQ CTQYCYIDST PCRYFT
	Isoform VI [UniParc]. Checksum: 7DFC921C5B98D84B	FASTA	291	30,024
	10 20 30 40 50 60 MVVLNPMTLG IYLQLFFLSI VSQPTFINSV LPISAALPSL DQKKRGGHKA CCLLTPPPPP 70 80 90 100 110 120 LFPPPFFRGG RSPLLSPDMK NLMLELETSQ SPCMQGSLGS PGPPGPQGPP GLPGKTGPKG 130 140 150 160 170 180 EKGELGRPGR KGRPGPPGVP GMPGPIGWPG PEGPRGEKGD LGMMGLPGSR GPMGSKGYPG 190 200 210 220 230 240 SRGEKGSRGE KGDLGPKGEK GFPGFPGMLG QKGEMGPKGE PGIAGHRGPT GRPGKRGKQS 250 260 270 280 290 SRTPCTLPRR PPVPCGQGSR SPVTVVAGNE SQACLLPRFE EDYISSGTER G
	Isoform VII [UniParc]. Checksum: FE0A55A8FAE0E135	FASTA	281	28,354
	10 20 30 40 50 60 MVVLNPMTLG IYLQLFFLSI VSQPTFINSV LPISAALPSL DQKKRGGHKA CCLLTPPPPP 70 80 90 100 110 120 LFPPPFFRGG RSPLLSPDMK NLMLELETSQ SPCMQGSLGS PGPPGPQGPP GLPGKTGPKG 130 140 150 160 170 180 EKGELGRPGR KGRPGPPGVP GMPGPIGWPG PEGPRGEKGD LGMMGLPGSR GPMGSKGYPG 190 200 210 220 230 240 SRGEKGSRGE KGDLGPKGEK GFPGFPGMLG QKGEMGPKGE PGIAGHRGPT GRPGKRGKQG 250 260 270 280 QKGDSGVMGP PGKPGPSGQP GRPGPPGPPP ADFCGQQPGG A
	Isoform VIII [UniParc]. Checksum: A3ECE29DEDE5766F	FASTA	329	33,538
	10 20 30 40 50 60 MVVLNPMTLG IYLQLFFLSI VSQPTFINSV LPISAALPSL DQKKRGGHKA CCLLTPPPPP 70 80 90 100 110 120 LFPPPFFRGG RSPLLSPDMK NLMLELETSQ SPCMQGSLGS PGPPGPQGPP GLPGKTGPKG 130 140 150 160 170 180 EKGELGRPGR KGRPGPPGVP GMPGPIGWPG PEGPRGEKGD LGMMGLPGSR GPMGSKGYPG 190 200 210 220 230 240 SRGEKGSRGE KGDLGPKGEK GFPGFPGMLG QKGEMGPKGE PGIAGHRGPT GRPGKRGKQG 250 260 270 280 290 300 QKGDSGVMGP PGKPGPSGQP GRPGPPGPPP AGHMETCNAP STATSTPRPA ATSPEGREEK 310 320 VGCAPQNWQQ LLHCHQTGHV LAPSPPTFV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract] 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]	"The spectrum of mutations causing end-plate acetylcholinesterase deficiency." Ohno K., Engel A.G., Brengman J.M., Shen X.-M., Heidenreich F., Vincent A., Milone M., Tan E., Demirci M., Walsh P., Nakano S., Akiguchi I. Ann. Neurol. 47:162-170(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CMSE GLN-59; GLU-342; GLN-410 AND TYR-444. Tissue: Blood and Muscle.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00031687.
IPI00220970.
IPI00220971.
IPI00220972.
IPI00220973.
IPI00220974.
IPI00220976.
IPI00334651.

RefSeq

NP_005668.2. NM_005677.3.
NP_536799.1. NM_080538.2.
NP_536800.2. NM_080539.3.

UniGene

Hs.146735.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VZJ	X-ray	2.35	I/J	53-67	[»]

ProteinModelPortal

Q9Y215.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y215. 1 interaction.

PTM databases

PhosphoSite

Q9Y215.

Polymorphism databases

DMDM

116241309.

Proteomic databases

PaxDb

Q9Y215.

PRIDE

Q9Y215.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000383781; ENSP00000373291; ENSG00000206561.
ENST00000383786; ENSP00000373296; ENSG00000206561.
ENST00000383787; ENSP00000373297; ENSG00000206561.
ENST00000383788; ENSP00000373298; ENSG00000206561.
ENST00000420589; ENSP00000394433; ENSG00000206561.
ENST00000454772; ENSP00000410554; ENSG00000206561.

GeneID

8292.

KEGG

hsa:8292.

UCSC

uc003bzv.3. human.
uc003bzx.3. human.
uc010heo.3. human.

Organism-specific databases

CTD

8292.

GeneCards

GC03M015491.

HGNC

HGNC:2226. COLQ.

MIM

603033. gene.
603034. phenotype.

neXtProt

NX_Q9Y215.

Orphanet

98915. Synaptic congenital myasthenic syndromes.

PharmGKB

PA26743.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG329823.

HOVERGEN

HBG102052.

InParanoid

Q9Y215.

OrthoDB

EOG4Z36F5.

Gene expression databases

ArrayExpress

Q9Y215.

Bgee

Q9Y215.

Genevestigator

Q9Y215.

GermOnline

ENSG00000206561. Homo sapiens.

Family and domain databases

InterPro

IPR008160. Collagen.
IPR011936. Myxo_disulph_rpt.
[Graphical view]

Pfam

PF01391. Collagen. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02232. myxo_disulf_rpt. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q9Y215.

GenomeRNAi

8292.

NextBio

31075.

SOURCE

Search...

Entry information

Entry name

COLQ_HUMAN

Accession

Primary (citable) accession number: Q9Y215
Secondary accession number(s): B3KY09 , Q6DK18, Q6YH18, Q6YH19, Q6YH20, Q6YH21, Q9NP18, Q9NP19, Q9NP20, Q9NP21, Q9NP22, Q9NP23, Q9NP24, Q9UP88

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.