Skip Header

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

Q9NPJ3

- ACO13_HUMAN

UniProt

Q9NPJ3 - ACO13_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

Acyl-coenzyme A thioesterase 13

Gene

ACOT13

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

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequences (2)
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

Functioni

Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Can also hydrolyze 3-hydroxyphenylacetyl-CoA and 3,4-dihydroxyphenylacetyl-CoA (in vitro). May play a role in controlling adaptive thermogenesis (By similarity).By similarity

Kineticsi

  1. KM=4.9 µM for n-decanoyl-CoA1 Publication
  2. KM=26 µM for n-octanoyl-CoA1 Publication
  3. KM=5 µM for myristoyl-CoA1 Publication
  4. KM=9 µM for palmitoyl-CoA1 Publication
  5. KM=9 µM for oleoyl-CoA1 Publication
  6. KM=10 µM for 3,4-dihydroxyphenylacetyl-CoA1 Publication
  7. KM=40 µM for 3-hydroxyphenylacetyl-CoA1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei50 – 501Substrate

GO - Molecular functioni

  1. acyl-CoA hydrolase activity Source: UniProtKB

GO - Biological processi

  1. metabolic process Source: GOC
  2. protein homotetramerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

SABIO-RKQ9NPJ3.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-coenzyme A thioesterase 13 (EC:3.1.2.-)
Short name:
Acyl-CoA thioesterase 13
Alternative name(s):
Thioesterase superfamily member 2
Cleaved into the following chain:
Acyl-coenzyme A thioesterase 13, N-terminally processed
Gene namesi
Name:ACOT13
Synonyms:THEM2
ORF Names:HT012, PNAS-27
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:20999. ACOT13.

Subcellular locationi

Cytoplasm › cytosol By similarity. Mitochondrion By similarity. Nucleus By similarity. Cytoplasm › cytoskeleton › spindle By similarity
Note: During interphase, found both in the nucleus and in the cytoplasm. At mitosis, localizes to the spindle. Colocalizes with tubulin (By similarity).By similarity

GO - Cellular componenti

  1. cytosol Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: UniProtKB
  3. mitochondrion Source: UniProtKB-SubCell
  4. nucleus Source: UniProtKB
  5. spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi50 – 501N → A: Reduced activity. 1 Publication
Mutagenesisi56 – 561H → A: Decreases affinity for substrate. 1 Publication
Mutagenesisi65 – 651D → A: Loss of activity. 2 Publications
Mutagenesisi65 – 651D → E or N: Reduced activity. 2 Publications
Mutagenesisi83 – 831S → A: Reduced activity. 1 Publication

Organism-specific databases

PharmGKBiPA165617655.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 140140Acyl-coenzyme A thioesterase 13PRO_0000156697Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 140139Acyl-coenzyme A thioesterase 13, N-terminally processedPRO_0000424501Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine; in Acyl-coenzyme A thioesterase 13; alternate2 Publications
Modified residuei2 – 21N-acetylthreonine; in Acyl-coenzyme A thioesterase 13, N-terminally processed3 Publications
Modified residuei27 – 271N6-acetyllysineBy similarity
Modified residuei37 – 371N6-acetyllysineBy similarity
Modified residuei43 – 431N6-acetyllysineBy similarity
Modified residuei108 – 1081N6-acetyllysineBy similarity
Modified residuei127 – 1271N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NPJ3.
PaxDbiQ9NPJ3.
PeptideAtlasiQ9NPJ3.
PRIDEiQ9NPJ3.

PTM databases

PhosphoSiteiQ9NPJ3.

Expressioni

Gene expression databases

BgeeiQ9NPJ3.
CleanExiHS_THEM2.
GenevestigatoriQ9NPJ3.

Organism-specific databases

HPAiHPA019881.

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

BioGridi120958. 13 interactions.
IntActiQ9NPJ3. 3 interactions.
STRINGi9606.ENSP00000230048.

Structurei

Secondary structure

1
140
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1513Combined sources
Beta strandi18 – 203Combined sources
Helixi21 – 255Combined sources
Beta strandi29 – 346Combined sources
Beta strandi37 – 437Combined sources
Helixi46 – 483Combined sources
Beta strandi53 – 553Combined sources
Helixi57 – 7317Combined sources
Beta strandi75 – 773Combined sources
Beta strandi82 – 909Combined sources
Beta strandi99 – 10911Combined sources
Beta strandi111 – 12212Combined sources
Turni123 – 1253Combined sources
Beta strandi128 – 13710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F0XX-ray2.30A/B/C/D/E/F/G/H1-140[»]
2H4UX-ray2.20A/B/C/D19-140[»]
3F5OX-ray1.70A/B/C/D/E/F/G/H1-140[»]
ProteinModelPortaliQ9NPJ3.
SMRiQ9NPJ3. Positions 2-139.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NPJ3.

Family & Domainsi

Sequence similaritiesi

Belongs to the thioesterase PaaI family.Curated

Phylogenomic databases

eggNOGiCOG2050.
GeneTreeiENSGT00390000013934.
HOGENOMiHOG000170540.
InParanoidiQ9NPJ3.
KOiK17362.
OMAiMNITYMS.
OrthoDBiEOG7Q8CQ4.
PhylomeDBiQ9NPJ3.
TreeFamiTF315062.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
InterProiIPR029069. HotDog_dom.
IPR003736. PAAI_dom.
IPR006683. Thioestr_supf.
[Graphical view]
PfamiPF03061. 4HBT. 1 hit.
[Graphical view]
SUPFAMiSSF54637. SSF54637. 1 hit.
TIGRFAMsiTIGR00369. unchar_dom_1. 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: Q9NPJ3-1) [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

        10         20         30         40         50
MTSMTQSLRE VIKAMTKARN FERVLGKITL VSAAPGKVIC EMKVEEEHTN 
        60         70         80         90        100
AIGTLHGGLT ATLVDNISTM ALLCTERGAP GVSVDMNITY MSPAKLGEDI 
       110        120        130        140
VITAHVLKQG KTLAFTSVDL TNKATGKLIA QGRHTKHLGN
Length:140
Mass (Da):14,960
Last modified:October 1, 2000 - v1
Checksum:i084E36EFEE715A18
GO
Isoform 2 (identifier: Q9NPJ3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MTSMTQSLREVIKAMTKARNFERVLG → MVR

Note: No experimental confirmation available.

Show »
Length:117
Mass (Da):12,366
Checksum:iA6F50AA63A00583A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2626MTSMT…ERVLG → MVR in isoform 2. 1 PublicationVSP_046101Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF155649 mRNA. Translation: AAF67006.1.
AF220186 mRNA. Translation: AAF67651.1.
AF274952 mRNA. Translation: AAK07529.1.
AK000508 mRNA. Translation: BAA91215.1.
AK309738 mRNA. No translation available.
AL031775 Genomic DNA. Translation: CAD92509.1.
BC000894 mRNA. Translation: AAH00894.1.
CCDSiCCDS4558.1. [Q9NPJ3-1]
CCDS54972.1. [Q9NPJ3-2]
RefSeqiNP_001153566.1. NM_001160094.1. [Q9NPJ3-2]
NP_060943.1. NM_018473.3. [Q9NPJ3-1]
UniGeneiHs.731605.

Genome annotation databases

EnsembliENST00000230048; ENSP00000230048; ENSG00000112304. [Q9NPJ3-1]
ENST00000537591; ENSP00000445552; ENSG00000112304. [Q9NPJ3-2]
GeneIDi55856.
KEGGihsa:55856.
UCSCiuc003nek.3. human. [Q9NPJ3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 AF155649 mRNA. Translation: AAF67006.1 .
AF220186 mRNA. Translation: AAF67651.1 .
AF274952 mRNA. Translation: AAK07529.1 .
AK000508 mRNA. Translation: BAA91215.1 .
AK309738 mRNA. No translation available.
AL031775 Genomic DNA. Translation: CAD92509.1 .
BC000894 mRNA. Translation: AAH00894.1 .
CCDSi CCDS4558.1. [Q9NPJ3-1 ]
CCDS54972.1. [Q9NPJ3-2 ]
RefSeqi NP_001153566.1. NM_001160094.1. [Q9NPJ3-2 ]
NP_060943.1. NM_018473.3. [Q9NPJ3-1 ]
UniGenei Hs.731605.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2F0X X-ray 2.30 A/B/C/D/E/F/G/H 1-140 [» ]
2H4U X-ray 2.20 A/B/C/D 19-140 [» ]
3F5O X-ray 1.70 A/B/C/D/E/F/G/H 1-140 [» ]
ProteinModelPortali Q9NPJ3.
SMRi Q9NPJ3. Positions 2-139.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120958. 13 interactions.
IntActi Q9NPJ3. 3 interactions.
STRINGi 9606.ENSP00000230048.

PTM databases

PhosphoSitei Q9NPJ3.

Proteomic databases

MaxQBi Q9NPJ3.
PaxDbi Q9NPJ3.
PeptideAtlasi Q9NPJ3.
PRIDEi Q9NPJ3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000230048 ; ENSP00000230048 ; ENSG00000112304 . [Q9NPJ3-1 ]
ENST00000537591 ; ENSP00000445552 ; ENSG00000112304 . [Q9NPJ3-2 ]
GeneIDi 55856.
KEGGi hsa:55856.
UCSCi uc003nek.3. human. [Q9NPJ3-1 ]

Organism-specific databases

CTDi 55856.
GeneCardsi GC06P024667.
H-InvDB HIX0005627.
HGNCi HGNC:20999. ACOT13.
HPAi HPA019881.
MIMi 615652. gene.
neXtProti NX_Q9NPJ3.
PharmGKBi PA165617655.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2050.
GeneTreei ENSGT00390000013934.
HOGENOMi HOG000170540.
InParanoidi Q9NPJ3.
KOi K17362.
OMAi MNITYMS.
OrthoDBi EOG7Q8CQ4.
PhylomeDBi Q9NPJ3.
TreeFami TF315062.

Enzyme and pathway databases

SABIO-RK Q9NPJ3.

Miscellaneous databases

ChiTaRSi ACOT13. human.
EvolutionaryTracei Q9NPJ3.
GenomeRNAii 55856.
NextBioi 61135.
PROi Q9NPJ3.
SOURCEi Search...

Gene expression databases

Bgeei Q9NPJ3.
CleanExi HS_THEM2.
Genevestigatori Q9NPJ3.

Family and domain databases

Gene3Di 3.10.129.10. 1 hit.
InterProi IPR029069. HotDog_dom.
IPR003736. PAAI_dom.
IPR006683. Thioestr_supf.
[Graphical view ]
Pfami PF03061. 4HBT. 1 hit.
[Graphical view ]
SUPFAMi SSF54637. SSF54637. 1 hit.
TIGRFAMsi TIGR00369. unchar_dom_1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Adrenal gland and Hypothalamus.
  2. "Human acute promyelocytic leukemia cell line NB4's apoptosis related genes."
    Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W., Yang H., Zhao Z.-L.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Promyelocytic leukemia.
  3. "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] (ISOFORMS 1 AND 2).
    Tissue: Teratocarcinoma.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    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 1).
    Tissue: Cervix.
  6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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 MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF ASP-65, SUBUNIT.
  11. "The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis."
    Cao J., Xu H., Zhao H., Gong W., Dunaway-Mariano D.
    Biochemistry 48:1293-1304(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-50; HIS-56; ASP-65 AND SER-83, SUBUNIT.
  12. "The crystal structure of human thioesterase superfamily member 2."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Entry informationi

Entry nameiACO13_HUMAN
AccessioniPrimary (citable) accession number: Q9NPJ3
Secondary accession number(s): F5H2L4, O95549
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: October 1, 2000
Last modified: January 7, 2015
This is version 117 of the entry and version 1 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 6
    Human chromosome 6: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.
© 2002– 2015 UniProt Consortium | License & Disclaimer