SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9Y259

- CHKB_HUMAN

UniProt

Q9Y259 - CHKB_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Choline/ethanolamine kinase

Gene
CHKB, CHETK, CHKL
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Has a key role in phospholipid biosynthesis. Catalyzes the first step in phosphatidylethanolamine biosynthesis. Phosphorylates ethanolamine, and can also act on choline (in vitro). Has higher activity with ethanolamine. May not significantly contribute to in vivo phosphatidylcholine biosynthesis.1 Publication

Catalytic activityi

ATP + choline = ADP + phosphocholine.1 Publication
ATP + ethanolamine = ADP + O-phosphoethanolamine.1 Publication

Kineticsi

  1. KM=0.57 mM for choline1 Publication
  2. KM=2.9 mM for ethanolamine1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei104 – 1041ATP
Binding sitei244 – 2441ATP
Binding sitei264 – 2641ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi75 – 817ATP
Nucleotide bindingi146 – 1527ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. choline kinase activity Source: UniProtKB
  3. ethanolamine kinase activity Source: UniProtKB

GO - Biological processi

  1. CDP-choline pathway Source: GOC
  2. glycerophospholipid biosynthetic process Source: Reactome
  3. phosphatidylcholine biosynthetic process Source: Reactome
  4. phosphatidylethanolamine biosynthetic process Source: UniProtKB
  5. phospholipid metabolic process Source: Reactome
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.32. 2681.
ReactomeiREACT_120919. Synthesis of PE.
REACT_121238. Synthesis of PC.
SABIO-RKQ9Y259.
UniPathwayiUPA00558; UER00741.

Names & Taxonomyi

Protein namesi
Recommended name:
Choline/ethanolamine kinase
Alternative name(s):
Choline kinase beta (EC:2.7.1.32)
Short name:
CK
Short name:
CKB
Choline kinase-like protein
Ethanolamine kinase (EC:2.7.1.82)
Short name:
EK
Ethanolamine kinase beta
Short name:
EKB
choline/ethanolamine kinase beta
Short name:
CKEKB
Gene namesi
Name:CHKB
Synonyms:CHETK, CHKL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Organism-specific databases

HGNCiHGNC:1938. CHKB.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

Orphaneti280671. Congenital muscular dystrophy due to phosphatidylcholine biosynthesis defect.
PharmGKBiPA26469.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 395394Choline/ethanolamine kinasePRO_0000206222Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9Y259.
PaxDbiQ9Y259.
PRIDEiQ9Y259.

PTM databases

PhosphoSiteiQ9Y259.

Expressioni

Gene expression databases

BgeeiQ9Y259.
CleanExiHS_CHKB.
GenevestigatoriQ9Y259.

Organism-specific databases

HPAiHPA018797.

Interactioni

Subunit structurei

Homodimer, and heterodimer with CHKA.1 Publication

Protein-protein interaction databases

BioGridi107544. 2 interactions.
IntActiQ9Y259. 1 interaction.
STRINGi9606.ENSP00000384400.

Structurei

Secondary structure

1
395
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi43 – 5715
Helixi59 – 635
Helixi66 – 683
Beta strandi70 – 745
Turni77 – 793
Beta strandi82 – 865
Beta strandi94 – 963
Beta strandi99 – 1057
Helixi108 – 1103
Helixi113 – 12816
Beta strandi135 – 1395
Beta strandi142 – 1465
Beta strandi149 – 1524
Helixi155 – 1595
Helixi161 – 17515
Helixi187 – 20115
Helixi212 – 2154
Helixi218 – 23013
Beta strandi236 – 2394
Helixi245 – 2473
Beta strandi248 – 2525
Beta strandi260 – 2623
Helixi265 – 2673
Beta strandi269 – 2724
Helixi273 – 28311
Helixi300 – 3023
Helixi306 – 32015
Turni321 – 3233
Helixi328 – 36134
Beta strandi365 – 3684
Helixi370 – 38617

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IG7X-ray1.80A/B14-395[»]
3FEGX-ray1.30A35-395[»]
3LQ3X-ray1.42A14-395[»]
ProteinModelPortaliQ9Y259.
SMRiQ9Y259. Positions 42-388.

Miscellaneous databases

EvolutionaryTraceiQ9Y259.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni77 – 793Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0510.
HOGENOMiHOG000041274.
HOVERGENiHBG050943.
InParanoidiQ9Y259.
KOiK14156.
OMAiYKAQPAN.
OrthoDBiEOG72VH68.
PhylomeDBiQ9Y259.
TreeFamiTF313549.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y259-1) [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

MAAEATAVAG SGAVGGCLAK DGLQQSKCPD TTPKRRRASS LSRDAERRAY    50
QWCREYLGGA WRRVQPEELR VYPVSGGLSN LLFRCSLPDH LPSVGEEPRE 100
VLLRLYGAIL QGVDSLVLES VMFAILAERS LGPQLYGVFP EGRLEQYIPS 150
RPLKTQELRE PVLSAAIATK MAQFHGMEMP FTKEPHWLFG TMERYLKQIQ 200
DLPPTGLPEM NLLEMYSLKD EMGNLRKLLE STPSPVVFCH NDIQEGNILL 250
LSEPENADSL MLVDFEYSSY NYRGFDIGNH FCEWVYDYTH EEWPFYKARP 300
TDYPTQEQQL HFIRHYLAEA KKGETLSQEE QRKLEEDLLV EVSRYALASH 350
FFWGLWSILQ ASMSTIEFGY LDYAQSRFQF YFQQKGQLTS VHSSS 395
Length:395
Mass (Da):45,271
Last modified:January 23, 2007 - v3
Checksum:i18367468B22FB9CE
GO
Isoform 2 (identifier: Q9Y259-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     75-127: SGGLSNLLFR...LESVMFAILA → RWEVRGQPLR...WPGGGRGRGR
     128-395: Missing.

Show »
Length:127
Mass (Da):13,506
Checksum:i1C3DBAB66A5D1637
GO

Sequence cautioni

The sequence AAB03342.2 differs from that shown. Reason: Erroneous gene model prediction.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei75 – 12753SGGLS…FAILA → RWEVRGQPLRCADRGQGSAA GPSGCSMFSPPSCARAWGGA GPAWPGGGRGRGR in isoform 2. VSP_034248Add
BLAST
Alternative sequencei128 – 395268Missing in isoform 2. VSP_034249Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB029885 Genomic DNA. Translation: BAA82511.1.
AB029886 mRNA. Translation: BAA82512.1.
AL096780 mRNA. Translation: CAB46629.1.
AL096781 mRNA. Translation: CAB46630.1.
CR456419 mRNA. Translation: CAG30305.1.
AK314324 mRNA. Translation: BAG36972.1.
U62317 Genomic DNA. Translation: AAB03342.2. Sequence problems.
CH471138 Genomic DNA. Translation: EAW73573.1.
BC082263 mRNA. Translation: AAH82263.1.
BC101488 mRNA. Translation: AAI01489.1.
BC113521 mRNA. Translation: AAI13522.2.
CCDSiCCDS14099.1. [Q9Y259-1]
RefSeqiNP_005189.2. NM_005198.4. [Q9Y259-1]
UniGeneiHs.654827.

Genome annotation databases

EnsembliENST00000406938; ENSP00000384400; ENSG00000100288. [Q9Y259-1]
GeneIDi1120.
KEGGihsa:1120.
UCSCiuc003bmu.3. human. [Q9Y259-1]

Polymorphism databases

DMDMi6685604.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB029885 Genomic DNA. Translation: BAA82511.1 .
AB029886 mRNA. Translation: BAA82512.1 .
AL096780 mRNA. Translation: CAB46629.1 .
AL096781 mRNA. Translation: CAB46630.1 .
CR456419 mRNA. Translation: CAG30305.1 .
AK314324 mRNA. Translation: BAG36972.1 .
U62317 Genomic DNA. Translation: AAB03342.2 . Sequence problems.
CH471138 Genomic DNA. Translation: EAW73573.1 .
BC082263 mRNA. Translation: AAH82263.1 .
BC101488 mRNA. Translation: AAI01489.1 .
BC113521 mRNA. Translation: AAI13522.2 .
CCDSi CCDS14099.1. [Q9Y259-1 ]
RefSeqi NP_005189.2. NM_005198.4. [Q9Y259-1 ]
UniGenei Hs.654827.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2IG7 X-ray 1.80 A/B 14-395 [» ]
3FEG X-ray 1.30 A 35-395 [» ]
3LQ3 X-ray 1.42 A 14-395 [» ]
ProteinModelPortali Q9Y259.
SMRi Q9Y259. Positions 42-388.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107544. 2 interactions.
IntActi Q9Y259. 1 interaction.
STRINGi 9606.ENSP00000384400.

Chemistry

DrugBanki DB00122. Choline.

PTM databases

PhosphoSitei Q9Y259.

Polymorphism databases

DMDMi 6685604.

Proteomic databases

MaxQBi Q9Y259.
PaxDbi Q9Y259.
PRIDEi Q9Y259.

Protocols and materials databases

DNASUi 1120.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000406938 ; ENSP00000384400 ; ENSG00000100288 . [Q9Y259-1 ]
GeneIDi 1120.
KEGGi hsa:1120.
UCSCi uc003bmu.3. human. [Q9Y259-1 ]

Organism-specific databases

CTDi 1120.
GeneCardsi GC22M051017.
GeneReviewsi CHKB.
HGNCi HGNC:1938. CHKB.
HPAi HPA018797.
MIMi 612395. gene.
neXtProti NX_Q9Y259.
Orphaneti 280671. Congenital muscular dystrophy due to phosphatidylcholine biosynthesis defect.
PharmGKBi PA26469.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0510.
HOGENOMi HOG000041274.
HOVERGENi HBG050943.
InParanoidi Q9Y259.
KOi K14156.
OMAi YKAQPAN.
OrthoDBi EOG72VH68.
PhylomeDBi Q9Y259.
TreeFami TF313549.

Enzyme and pathway databases

UniPathwayi UPA00558 ; UER00741 .
BRENDAi 2.7.1.32. 2681.
Reactomei REACT_120919. Synthesis of PE.
REACT_121238. Synthesis of PC.
SABIO-RK Q9Y259.

Miscellaneous databases

EvolutionaryTracei Q9Y259.
GeneWikii CHKB_(gene).
GenomeRNAii 1120.
NextBioi 4648.
PROi Q9Y259.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y259.
CleanExi HS_CHKB.
Genevestigatori Q9Y259.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Novel expression of equivocal messages containing both regions of choline/ethanolamine kinase and muscle type carnitine palmitoyltransferase I."
    Yamazaki N., Shinohara Y., Kajimoto K., Shindo M., Terada H.
    J. Biol. Chem. 275:31739-31746(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
  2. Smink L.J., Huckle E.J.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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].
    Tissue: Brain.
  5. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 1).
    Tissue: Brain and Lung.
  8. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
    Submitted (MAY-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-19, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: T-cell.
  9. "Differential role of human choline kinase alpha and beta enzymes in lipid metabolism: implications in cancer onset and treatment."
    Gallego-Ortega D., Ramirez de Molina A., Ramos M.A., Valdes-Mora F., Barderas M.G., Sarmentero-Estrada J., Lacal J.C.
    PLoS ONE 4:E7819-E7819(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Crystal structure of human choline kinase beta in complex with phosphorylated hemicholinium-3 and adenosine nucleotide."
    Structural genomics consortium (SGC)
    Submitted (SEP-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 14-395 IN COMPLEX WITH ADP; MAGNESIUM IONS AND HEMICHOLINIUM-3.

Entry informationi

Entry nameiCHKB_HUMAN
AccessioniPrimary (citable) accession number: Q9Y259
Secondary accession number(s): A0PJM6, Q13388
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: October 1, 2014
This is version 120 of the entry and version 3 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

Miscellaneous

This protein is produced by a bicistronic gene which also produces the CPT1B protein from a non-overlapping reading frame.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi