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P14621 (ACYP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acylphosphatase-2

EC=3.6.1.7
Alternative name(s):
Acylphosphatase, muscle type isozyme
Acylphosphate phosphohydrolase 2
Gene names
Name:ACYP2
Synonyms:ACYP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length99 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Its physiological role is not yet clear.

Catalytic activity

An acylphosphate + H2O = a carboxylate + phosphate.

Sequence similarities

Belongs to the acylphosphatase family.

Contains 1 acylphosphatase-like domain.

Ontologies

Keywords
   Molecular functionHydrolase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processphosphate-containing compound metabolic process

Traceable author statement PubMed 8268218. Source: ProtInc

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionacylphosphatase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.5
Chain2 – 9998Acylphosphatase-2
PRO_0000158542

Regions

Domain9 – 9991Acylphosphatase-like

Sites

Active site241 Potential
Active site421 Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.5

Sequences

Sequence LengthMass (Da)Tools
P14621 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: AEDE40E45B6207A0

FASTA9911,140
        10         20         30         40         50         60 
MSTAQSLKSV DYEVFGRVQG VCFRMYTEDE ARKIGVVGWV KNTSKGTVTG QVQGPEDKVN 

        70         80         90 
SMKSWLSKVG SPSSRIDRTN FSNEKTISKL EYSNFSIRY 

« Hide

References

« Hide 'large scale' references
[1]"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: Ovary.
[2]"Human skeletal muscle acylphosphatase: the primary structure."
Manao G., Camici G., Modesti A., Liguri G., Berti A., Setfani M., Cappugi G., Ramponi G.
Mol. Biol. Med. 2:369-378(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-99.
Tissue: Muscle.
[3]"Cloning and expression of the cDNA coding for the erythrocyte isoenzyme of human acylphosphatase."
Fiaschi T., Raugei G., Marzocchini R., Chiarugi P., Cirri P., Ramponi G.
FEBS Lett. 367:145-148(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-99.
Tissue: Heart.
[4]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC012290 mRNA. Translation: AAH12290.1.
X84195 mRNA. Translation: CAA58988.1.
PIRS52327. S59138.
RefSeqNP_612457.1. NM_138448.3.
UniGeneHs.516173.
Hs.642983.

3D structure databases

ProteinModelPortalP14621.
SMRP14621. Positions 2-99.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106613. 1 interaction.
DIPDIP-48449N.
STRING9606.ENSP00000378161.

Proteomic databases

PaxDbP14621.
PRIDEP14621.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000394666; ENSP00000378161; ENSG00000170634.
GeneID98.
KEGGhsa:98.
UCSCuc002rxq.4. human.

Organism-specific databases

CTD98.
GeneCardsGC02P054199.
HGNCHGNC:180. ACYP2.
HPAHPA035301.
MIM102595. gene.
neXtProtNX_P14621.
PharmGKBPA24500.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1254.
HOGENOMHOG000292688.
HOVERGENHBG050454.
InParanoidP14621.
KOK01512.
OMAKVNSMMS.
PhylomeDBP14621.
TreeFamTF300288.

Enzyme and pathway databases

SABIO-RKP14621.

Gene expression databases

ArrayExpressP14621.
BgeeP14621.
CleanExHS_ACYP2.
GenevestigatorP14621.

Family and domain databases

InterProIPR020456. Acylphosphatase.
IPR027147. Acylphosphatase-2.
IPR001792. Acylphosphatase-like_dom.
IPR017968. Acylphosphatase_CS.
[Graphical view]
PANTHERPTHR10029:SF1. PTHR10029:SF1. 1 hit.
PfamPF00708. Acylphosphatase. 1 hit.
[Graphical view]
PRINTSPR00112. ACYLPHPHTASE.
SUPFAMSSF54975. SSF54975. 1 hit.
PROSITEPS00150. ACYLPHOSPHATASE_1. 1 hit.
PS00151. ACYLPHOSPHATASE_2. 1 hit.
PS51160. ACYLPHOSPHATASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACYP2. human.
GeneWikiACYP2.
GenomeRNAi98.
NextBio373.
PROP14621.
SOURCESearch...

Entry information

Entry nameACYP2_HUMAN
AccessionPrimary (citable) accession number: P14621
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM