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Unreviewed, UniProtKB/TrEMBL Q9CU20 (Q9CU20_MOUSE)

Last modified January 19, 2010. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

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Names and origin

Protein namesSubmitted name:
    Putative uncharacterized protein EMBL BAB31387.1
Gene names
Name: Cpt2 MGI 109176
OrganismMus musculus (Mouse) EMBL BAB31387.1
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length122 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Sequence similarities

Belongs to the carnitine/choline acetyltransferase family.

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Ontologies

Keywords
   Molecular functionAcyltransferase RuleBase RU003801V0
Transferase
Gene Ontology (GO)
   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

   Molecular functionacyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Experimental info

Non-terminal residue1221 EMBL BAB31387.1

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Sequences

Sequence LengthMass (Da)Tools
Q9CU20-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: A53047619711C377

FASTA12214,016
        10         20         30         40         50         60 
MMPRLLLRDW PRCPSLVLGA PSRPLSAVSG PAEYLQHSIV PTMHYQDSLP RLPIPKLEDT 

        70         80         90        100        110        120 
MKRYLSAQKP LLNDSQFRKT EVLCKDFENG IGKELHAHLL AQDKQNKHTS YISGPWFDMY 


LT

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References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J EMBL BAB31387.1.
Tissue: Kidney EMBL BAB31387.1.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK018752 mRNA. Translation: BAB31387.1.
IPIIPI00881401.
UniGeneMm.307620

3D structure databases

HSSPHSSP built from PDB template 1NDF based on UniProtKB P47934.
SMRQ9CU20. Positions 33-122.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9CU20.

Genome annotation databases

EnsemblENSMUST00000030345; ENSMUSP00000030345; ENSMUSG00000028607; Mus musculus. [Genome view]

Organism-specific databases

MGIMGI:109176. Cpt2.

Phylogenomic databases

HOVERGENQ9CU20.
InParanoidQ9CU20.

Gene expression databases

ArrayExpressQ9CU20.
BgeeQ9CU20.
GenevestigatorQ9CU20.

Family and domain databases

InterProIPR000542. Carn_acyl_trans.
[Graphical view]
PANTHERPTHR22589. Carn_acyl_trans. 1 hit.
PfamPF00755. Carn_acyltransf. 1 hit.
[Graphical view]
PROSITEPS00439. ACYLTRANSF_C_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

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Entry information

Entry nameQ9CU20_MOUSE
AccessionPrimary (citable) accession number: Q9CU20
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2001
Last sequence update: June 1, 2001
Last modified: January 19, 2010
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information