P28329 (CLAT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Choline O-acetyltransferase
Short name=CHOACTase
Short name=ChAT
Short name=Choline acetylase
EC=2.3.1.6

Gene names

Name:

CHAT

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	748 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses.
Catalytic activity	Acetyl-CoA + choline = CoA + O-acetylcholine.
Involvement in disease	Myasthenic syndrome, congenital, associated with episodic apnea (CMSEA) [MIM:254210]: An autosomal recessive congenital myasthenic syndrome. Patients have myasthenic symptoms since birth or early infancy, negative tests for anti-AChR antibodies, and abrupt episodic crises with increased weakness, bulbar paralysis, and apnea precipitated by undue exertion, fever, or excitement. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.11
Sequence similarities	Belongs to the carnitine/choline acetyltransferase family.

Ontologies

Keywords
Biological process	Neurotransmitter biosynthesis
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Congenital myasthenic syndrome Disease mutation
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	adult walking behavior Inferred from electronic annotation. Source: Compara dendrite development Inferred from electronic annotation. Source: Compara establishment of synaptic specificity at neuromuscular junction Inferred from electronic annotation. Source: Compara neuromuscular synaptic transmission Inferred from electronic annotation. Source: Compara neurotransmitter biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW neurotransmitter secretion Traceable author statement. Source: Reactome phosphatidylcholine biosynthetic process Traceable author statement. Source: Reactome rhythmic behavior Inferred from electronic annotation. Source: Compara rhythmic excitation Inferred from electronic annotation. Source: Compara
Cellular_component	axon Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome mitochondrion Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara nucleus Traceable author statement PubMed 10861222. Source: ProtInc
Molecular_function	choline O-acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform M (identifier: P28329-1)

Also known as: 83 kDa;

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 S (identifier: P28329-2)

Also known as: 74 kDa;

The sequence of this isoform differs from the canonical sequence as follows:
     1-95: MGLRTAKKRG...SAEAAEPRRA → MWPECRDEALSTV

Isoform R (identifier: P28329-3)

Also known as: 70 kDa;

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 748

748

Choline O-acetyltransferase

PRO_0000210154

Regions

Region

520 – 532

13

Coenzyme A binding

Sites

Active site

442

1

Proton acceptor

Binding site

558

1

Coenzyme A

Binding site

659

1

Coenzyme A

Natural variations

Alternative sequence

1 – 118

118

Missing in isoform R.

VSP_000791

Alternative sequence

1 – 95

95

MGLRT…EPRRA → MWPECRDEALSTV in isoform S.

VSP_000790

Natural variant

47

1

D → E.
Corresponds to variant rs3810948 [ dbSNP | Ensembl ].

VAR_046683

Natural variant

120

1

A → T. Ref.2 Ref.6
Corresponds to variant rs3810950 [ dbSNP | Ensembl ].

VAR_011675

Natural variant

210

1

L → P in CMSEA; impaired activity. Ref.2
Corresponds to variant rs28930071 [ dbSNP | Ensembl ].

VAR_011666

Natural variant

211

1

P → A in CMSEA; impaired activity. Ref.2

VAR_011667

Natural variant

222

1

R → P.
Corresponds to variant rs8178989 [ dbSNP | Ensembl ].

VAR_046684

Natural variant

243

1

L → F.
Corresponds to variant rs8178990 [ dbSNP | Ensembl ].

VAR_046685

Natural variant

299

1

P → L.
Corresponds to variant rs868749 [ dbSNP | Ensembl ].

VAR_046686

Natural variant

305

1

I → T in CMSEA; impaired activity. Ref.2
Corresponds to variant rs28929482 [ dbSNP | Ensembl ].

VAR_011668

Natural variant

336

1

I → T in CMSEA. Ref.11

VAR_038605

Natural variant

392

1

A → G. Ref.1 Ref.2

VAR_011676

Natural variant

400

1

D → N.
Corresponds to variant rs8178991 [ dbSNP | Ensembl ].

VAR_046687

Natural variant

420

1

R → C in CMSEA; impaired activity. Ref.2

VAR_011669

Natural variant

441

1

E → K in CMSEA; completely lack activity. Ref.2
Corresponds to variant rs28930070 [ dbSNP | Ensembl ].

VAR_011670

Natural variant

461

1

V → M. Ref.1 Ref.2 Ref.6
Corresponds to variant rs4838544 [ dbSNP | Ensembl ].

VAR_046688

Natural variant

482

1

R → G in CMSEA; impaired activity. Ref.2
Corresponds to variant rs28929481 [ dbSNP | Ensembl ].

VAR_011671

Natural variant

498

1

S → L in CMSEA; impaired activity. Ref.2

VAR_011672

Natural variant

506

1

V → L in CMSEA; impaired activity. Ref.2

VAR_011673

Natural variant

560

1

R → H in CMSEA; impaired activity. Ref.2

VAR_011674

Experimental info

Sequence conflict

151

1

R → Q in CAA39923. Ref.7

Sequence conflict

261 – 262

2

GQ → PE in AAA14245. Ref.1

Sequence conflict

396

1

V → L in AAB23557. Ref.6

Sequence conflict

434

1

G → A in AAA14245. Ref.1

Sequence conflict

529

1

C → S in AAB23557. Ref.6

Sequence conflict

567

1

V → L in AAB23557. Ref.6

Sequence conflict

629 – 630

2

EL → DV in AAB23557. Ref.6

Sequence conflict

664

1

T → M in AAB23557. Ref.6

Secondary structure

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748

Helix Strand Turn

Details...

Helix

139 – 150

12

Helix

151 – 153

3

Helix

156 – 169

14

Helix

175 – 189

15

Beta strand

190 – 192

3

Helix

195 – 202

8

Turn

203 – 205

3

Helix

210 – 213

4

Beta strand

217 – 219

3

Helix

228 – 250

23

Beta strand

261 – 263

3

Beta strand

265 – 267

3

Helix

271 – 275

5

Beta strand

276 – 282

7

Beta strand

285 – 287

3

Beta strand

289 – 292

4

Beta strand

300 – 308

9

Beta strand

311 – 319

9

Helix

326 – 340

15

Helix

343 – 345

3

Helix

350 – 355

6

Helix

358 – 369

12

Helix

372 – 382

11

Beta strand

387 – 390

4

Helix

400 – 409

10

Turn

413 – 418

6

Beta strand

424 – 430

7

Beta strand

436 – 440

5

Beta strand

442 – 444

3

Helix

447 – 461

15

Helix

489 – 508

20

Beta strand

509 – 516

8

Helix

521 – 525

5

Turn

526 – 528

3

Helix

531 – 547

17

Beta strand

553 – 558

6

Beta strand

567 – 569

3

Helix

575 – 585

11

Helix

587 – 589

3

Helix

593 – 615

23

Helix

621 – 634

14

Helix

640 – 643

4

Helix

645 – 650

6

Beta strand

654 – 659

6

Beta strand

663 – 665

3

Beta strand

667 – 669

3

Beta strand

678 – 684

7

Beta strand

689 – 696

8

Helix

704 – 722

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform M (83 kDa) [UniParc]. Last modified December 15, 2009. Version 4. Checksum: A902364081915391	FASTA	748	82,536
	10 20 30 40 50 60 MGLRTAKKRG LGGGGKWKRE EGGGTRGRRE VRPACFLQSG GRGDPGDVGG PAGNPGCSPH 70 80 90 100 110 120 PRAATRPPPL PAHTPAHTPE WCGAASAEAA EPRRAGPHLC IPAPGLTKTP ILEKVPRKMA 130 140 150 160 170 180 AKTPSSEESG LPKLPVPPLQ QTLATYLQCM RHLVSEEQFR KSQAIVQQFG APGGLGETLQ 190 200 210 220 230 240 QKLLERQEKT ANWVSEYWLN DMYLNNRLAL PVNSSPAVIF ARQHFPGTDD QLRFAASLIS 250 260 270 280 290 300 GVLSYKALLD SHSIPTDCAK GQLSGQPLCM KQYYGLFSSY RLPGHTQDTL VAQNSSIMPE 310 320 330 340 350 360 PEHVIVACCN QFFVLDVVIN FRRLSEGDLF TQLRKIVKMA SNEDERLPPI GLLTSDGRSE 370 380 390 400 410 420 WAEARTVLVK DSTNRDSLDM IERCICLVCL DAPGGVELSD THRALQLLHG GGYSKNGANR 430 440 450 460 470 480 WYDKSLQFVV GRDGTCGVVC EHSPFDGIVL VQCTEHLLKH VTQSSRKLIR ADSVSELPAP 490 500 510 520 530 540 RRLRWKCSPE IQGHLASSAE KLQRIVKNLD FIVYKFDNYG KTFIKKQKCS PDAFIQVALQ 550 560 570 580 590 600 LAFYRLHRRL VPTYESASIR RFQEGRVDNI RSATPEALAF VRAVTDHKAA VPASEKLLLL 610 620 630 640 650 660 KDAIRAQTAY TVMAITGMAI DNHLLALREL ARAMCKELPE MFMDETYLMS NRFVLSTSQV 670 680 690 700 710 720 PTTTEMFCCY GPVVPNGYGA CYNPQPETIL FCISSFHSCK ETSSSKFAKA VEESLIDMRD 730 740 LCSLLPPTES KPLATKEKAT RPSQGHQP
	Isoform S (74 kDa) [UniParc]. Checksum: 3A521459434FF919	FASTA	666	74,361
	10 20 30 40 50 60 MWPECRDEAL STVGPHLCIP APGLTKTPIL EKVPRKMAAK TPSSEESGLP KLPVPPLQQT 70 80 90 100 110 120 LATYLQCMRH LVSEEQFRKS QAIVQQFGAP GGLGETLQQK LLERQEKTAN WVSEYWLNDM 130 140 150 160 170 180 YLNNRLALPV NSSPAVIFAR QHFPGTDDQL RFAASLISGV LSYKALLDSH SIPTDCAKGQ 190 200 210 220 230 240 LSGQPLCMKQ YYGLFSSYRL PGHTQDTLVA QNSSIMPEPE HVIVACCNQF FVLDVVINFR 250 260 270 280 290 300 RLSEGDLFTQ LRKIVKMASN EDERLPPIGL LTSDGRSEWA EARTVLVKDS TNRDSLDMIE 310 320 330 340 350 360 RCICLVCLDA PGGVELSDTH RALQLLHGGG YSKNGANRWY DKSLQFVVGR DGTCGVVCEH 370 380 390 400 410 420 SPFDGIVLVQ CTEHLLKHVT QSSRKLIRAD SVSELPAPRR LRWKCSPEIQ GHLASSAEKL 430 440 450 460 470 480 QRIVKNLDFI VYKFDNYGKT FIKKQKCSPD AFIQVALQLA FYRLHRRLVP TYESASIRRF 490 500 510 520 530 540 QEGRVDNIRS ATPEALAFVR AVTDHKAAVP ASEKLLLLKD AIRAQTAYTV MAITGMAIDN 550 560 570 580 590 600 HLLALRELAR AMCKELPEMF MDETYLMSNR FVLSTSQVPT TTEMFCCYGP VVPNGYGACY 610 620 630 640 650 660 NPQPETILFC ISSFHSCKET SSSKFAKAVE ESLIDMRDLC SLLPPTESKP LATKEKATRP SQGHQP
	Isoform R (70 kDa) [UniParc]. Checksum: 0BF3CC8F56518326	FASTA	630	70,394
	10 20 30 40 50 60 MAAKTPSSEE SGLPKLPVPP LQQTLATYLQ CMRHLVSEEQ FRKSQAIVQQ FGAPGGLGET 70 80 90 100 110 120 LQQKLLERQE KTANWVSEYW LNDMYLNNRL ALPVNSSPAV IFARQHFPGT DDQLRFAASL 130 140 150 160 170 180 ISGVLSYKAL LDSHSIPTDC AKGQLSGQPL CMKQYYGLFS SYRLPGHTQD TLVAQNSSIM 190 200 210 220 230 240 PEPEHVIVAC CNQFFVLDVV INFRRLSEGD LFTQLRKIVK MASNEDERLP PIGLLTSDGR 250 260 270 280 290 300 SEWAEARTVL VKDSTNRDSL DMIERCICLV CLDAPGGVEL SDTHRALQLL HGGGYSKNGA 310 320 330 340 350 360 NRWYDKSLQF VVGRDGTCGV VCEHSPFDGI VLVQCTEHLL KHVTQSSRKL IRADSVSELP 370 380 390 400 410 420 APRRLRWKCS PEIQGHLASS AEKLQRIVKN LDFIVYKFDN YGKTFIKKQK CSPDAFIQVA 430 440 450 460 470 480 LQLAFYRLHR RLVPTYESAS IRRFQEGRVD NIRSATPEAL AFVRAVTDHK AAVPASEKLL 490 500 510 520 530 540 LLKDAIRAQT AYTVMAITGM AIDNHLLALR ELARAMCKEL PEMFMDETYL MSNRFVLSTS 550 560 570 580 590 600 QVPTTTEMFC CYGPVVPNGY GACYNPQPET ILFCISSFHS CKETSSSKFA KAVEESLIDM 610 620 630 RDLCSLLPPT ESKPLATKEK ATRPSQGHQP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A complementary DNA for human choline acetyltransferase induces two forms of enzyme with different molecular weights in cultured cells." Oda Y., Nakanishi I., Deguchi T. Brain Res. Mol. Brain Res. 16:287-294(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLY-392 AND MET-461. Tissue: Spinal cord.
[2]	"Choline acetyltransferase mutations cause myasthenic syndrome associated with episodic apnea in humans." Ohno K., Tsujino A., Brengman J.M., Harper C.M., Bajzer Z., Udd B., Beyring R., Robb S., Kirkham F.J., Engel A.G. Proc. Natl. Acad. Sci. U.S.A. 98:2017-2022(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING, VARIANTS CMSEA PRO-210; ALA-211; THR-305; CYS-420; LYS-441; GLY-482; LEU-498; LEU-506 AND HIS-560, VARIANTS THR-120; GLY-392 AND MET-461.
[3]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORM R).
[6]	"Two mRNAs are transcribed from the human gene for choline acetyltransferase." Lorenzi M.V., Trinidad A.C., Zhang R., Strauss W.L. DNA Cell Biol. 11:593-603(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 111-669, VARIANTS THR-120 AND MET-461.
[7]	"Human choline acetyltransferase (CHAT): partial gene sequence and potential control regions." Toussaint J.L., Geoffroy V., Schmitt M., Werner A., Garnier J.-M., Simoni P., Kempf J. Genomics 12:412-416(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 109-232.
[8]	"Conservation of amino acid sequences between human and porcine choline acetyltransferase." Hersh L.B., Takane K., Gylys K., Moomaw C., Slaughter C. J. Neurochem. 51:1843-1845(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 161-182; 271-295; 340-352; 376-382; 404-415; 550-559; 572-583; 620-632; 644-648; 650-662 AND 739-748. Tissue: Placenta.
[9]	"Isolation and sub-chromosomal localization of a DNA fragment of the human choline acetyltransferase gene." Cervini R., Rocchi M., DiDonato S., Finocchiaro G. Neurosci. Lett. 132:191-194(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 688-738. Tissue: Lymphocyte.
[10]	"Substrate binding and catalytic mechanism of human choline acetyltransferase." Kim A.-R., Rylett R.J., Shilton B.H. Biochemistry 45:14621-14631(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 120-733 IN COMPLEXES WITH CHOLINE AND ACETYL COENZYME A.
[11]	"Congenital myasthenic syndrome with episodic apnea in patients homozygous for a CHAT missense mutation." Kraner S., Laufenberg I., Strassburg H.M., Sieb J.P., Steinlein O.K. Arch. Neurol. 60:761-763(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CMSEA THR-336.
+	Additional computationally mapped references.

Web resources

GeneReviews

Wikipedia

Choline acetyltransferase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S56138 mRNA. Translation: AAA14245.1.
AF305907 mRNA. Translation: AAK08953.1.
AF305906 , AF305894, AF305895, AF305896, AF305897, AF305898, AF305899, AF305900, AF305901, AF305902, AF305903, AF305904, AF305905 Genomic DNA. Translation: AAK08950.1.
AF305908 mRNA. Translation: AAK08954.1.
AF305906 , AF305894, AF305895, AF305896, AF305897, AF305898, AF305899, AF305900, AF305901, AF305902, AF305903, AF305904, AF305905 Genomic DNA. Translation: AAK08951.1.
AF305909 mRNA. Translation: AAK08955.1.
AF305906 , AF305894, AF305895, AF305896, AF305897, AF305898, AF305899, AF305900, AF305901, AF305902, AF305903, AF305904, AF305905 Genomic DNA. Translation: AAK08952.1.
AC073366 Genomic DNA. No translation available.
CH471187 Genomic DNA. Translation: EAW93086.1.
BC130615 mRNA. Translation: AAI30616.1.
S45018 mRNA. Translation: AAB23557.2.
X56585 Genomic DNA. Translation: CAA39923.1.
X56879 Genomic DNA. Translation: CAA40201.1.

IPI

IPI00220707.
IPI00220708.
IPI00305227.

PIR

A60202. I52631.

RefSeq

NP_001136401.1. NM_001142929.1.
NP_001136405.1. NM_001142933.1.
NP_001136406.1. NM_001142934.1.
NP_065574.3. NM_020549.4.
NP_066264.3. NM_020984.3.
NP_066265.3. NM_020985.3.
NP_066266.3. NM_020986.3.

UniGene

Hs.302002.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FY2	X-ray	2.25	A	120-733	[»]
2FY3	X-ray	2.27	A	120-733	[»]
2FY4	X-ray	2.30	A	120-733	[»]
2FY5	X-ray	2.60	A	120-733	[»]

ProteinModelPortal

P28329.

SMR

P28329. Positions 126-727.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000337103.

PTM databases

PhosphoSite

P28329.

Polymorphism databases

DMDM

281185509.

Proteomic databases

PaxDb

P28329.

PRIDE

P28329.

Protocols and materials databases

DNASU

1103.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000337653; ENSP00000337103; ENSG00000070748.
ENST00000339797; ENSP00000343486; ENSG00000070748.
ENST00000351556; ENSP00000345878; ENSG00000070748.
ENST00000395559; ENSP00000378926; ENSG00000070748.
ENST00000395562; ENSP00000378929; ENSG00000070748.

GeneID

1103.

KEGG

hsa:1103.

UCSC

uc001jhz.2. human.

Organism-specific databases

CTD

1103.

GeneCards

GC10P050817.

HGNC

HGNC:1912. CHAT.

HPA

CAB002313.

MIM

118490. gene.
254210. phenotype.

neXtProt

NX_P28329.

Orphanet

98914. Presynaptic congenital myasthenic syndromes.

PharmGKB

PA26448.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG70127.

HOGENOM

HOG000233845.

HOVERGEN

HBG107717.

InParanoid

P28329.

KO

K00623.

OMA

HVIVACC.

PhylomeDB

P28329.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.
REACT_13685. Neuronal System.

SABIO-RK

P28329.

Gene expression databases

ArrayExpress

P28329.

Bgee

P28329.

CleanEx

HS_CHAT.

Genevestigator

P28329.

GermOnline

ENSG00000070748. Homo sapiens.

Family and domain databases

InterPro

IPR000542. Carn_acyl_trans.
[Graphical view]

PANTHER

PTHR22589. PTHR22589. 1 hit.

Pfam

PF00755. Carn_acyltransf. 1 hit.
[Graphical view]

PROSITE

PS00439. ACYLTRANSF_C_1. 1 hit.
PS00440. ACYLTRANSF_C_2. 1 hit.
[Graphical view]

ProtoNet

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Other

ChEMBL

CHEMBL4039.

DrugBank

DB00122. Choline.

EvolutionaryTrace

P28329.

GenomeRNAi

1103.

NextBio

4562.

SOURCE

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Entry information

Entry name

CLAT_HUMAN

Accession

Primary (citable) accession number: P28329
Secondary accession number(s): A2BDF4 , Q16488, Q9BQ23, Q9BQ35, Q9BQE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 15, 2009
Last modified:	May 1, 2013
This is version 132 of the entry and version 4 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.