Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P07311 (ACYP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acylphosphatase-1

EC=3.6.1.7
Alternative name(s):
Acylphosphatase, erythrocyte isozyme
Acylphosphatase, organ-common type isozyme
Acylphosphate phosphohydrolase 1
Gene names
Name:ACYP1
Synonyms:ACYPE
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.

Tissue specificity

Organ-common type isozyme is found in many different tissues.

Sequence similarities

Belongs to the acylphosphatase family.

Contains 1 acylphosphatase-like domain.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   Molecular functionHydrolase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processphosphate-containing compound metabolic process

Traceable author statement Ref.6. Source: ProtInc

   Molecular_functionacylphosphatase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P07311-1)

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 2 (identifier: P07311-2)

The sequence of this isoform differs from the canonical sequence as follows:
     29-99: AEGKKLGLVG...LDYSDFQIVK → EMTVENRIAETHSKSCVPVSFATSYAG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 9998Acylphosphatase-1
PRO_0000158535

Regions

Domain9 – 9991Acylphosphatase-like

Sites

Active site241 Potential
Active site421 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.6

Natural variations

Alternative sequence29 – 9971AEGKK…FQIVK → EMTVENRIAETHSKSCVPVS FATSYAG in isoform 2.
VSP_045688

Secondary structure

................... 99
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F9F787E490BC8296

FASTA9911,261
        10         20         30         40         50         60 
MAEGNTLISV DYEIFGKVQG VFFRKHTQAE GKKLGLVGWV QNTDRGTVQG QLQGPISKVR 

        70         80         90 
HMQEWLETRG SPKSHIDKAN FNNEKVILKL DYSDFQIVK 

« Hide

Isoform 2 [UniParc].

Checksum: 37822D3FA5EF8F81
Show »

FASTA556,113

References

« Hide 'large scale' references
[1]Raugei G.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]"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. expand/collapse author list , 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] (ISOFORM 1).
Tissue: Testis.
[3]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [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. expand/collapse author list , 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 (JUL-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] (ISOFORMS 1 AND 2).
Tissue: Embryonic carcinoma and Mammary gland.
[6]"A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure."
Liguri G., Camici G., Manao G., Cappugi G., Nassi P., Modesti A., Ramponi G.
Biochemistry 25:8089-8094(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-99, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2.
[7]"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: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 10-86.
Tissue: Placenta.
[8]"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].
[9]"Crystallization and preliminary crystallographic analysis of human common-type acylphosphatase."
Yeung R.C., Lam S.Y., Wong K.B.
Acta Crystallogr. F 62:80-82(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
[10]"Rational stabilization of enzymes by computational redesign of surface charge-charge interactions."
Gribenko A.V., Patel M.M., Liu J., McCallum S.A., Wang C., Makhatadze G.I.
Proc. Natl. Acad. Sci. U.S.A. 106:2601-2606(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 2-99.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X84194 mRNA. Translation: CAA58987.1.
AK312101 mRNA. Translation: BAG35037.1.
AC007055 Genomic DNA. Translation: AAD31937.1.
AL049780 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81216.1.
BC035568 mRNA. Translation: AAH35568.1.
BG614847 mRNA. No translation available.
CCDSCCDS45137.1. [P07311-2]
CCDS9838.1. [P07311-1]
PIRQPHUE. S66187.
RefSeqNP_001098.1. NM_001107.3. [P07311-1]
NP_982355.1. NM_203488.1. [P07311-2]
UniGeneHs.18573.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K7JNMR-A2-99[»]
2K7KNMR-A2-99[»]
2VH7X-ray1.45A1-99[»]
2W4CX-ray1.52A1-99[»]
2W4PX-ray1.70A1-99[»]
3TOQX-ray2.00A1-99[»]
ProteinModelPortalP07311.
SMRP07311. Positions 6-99.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106612. 2 interactions.
STRING9606.ENSP00000238618.

PTM databases

PhosphoSiteP07311.

Proteomic databases

MaxQBP07311.
PaxDbP07311.
PRIDEP07311.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000238618; ENSP00000238618; ENSG00000119640. [P07311-1]
ENST00000357971; ENSP00000350655; ENSG00000119640. [P07311-2]
ENST00000555694; ENSP00000451581; ENSG00000119640. [P07311-1]
GeneID97.
KEGGhsa:97.
UCSCuc001xrg.3. human. [P07311-1]

Organism-specific databases

CTD97.
GeneCardsGC14M075519.
HGNCHGNC:179. ACYP1.
HPAHPA034944.
MIM600875. gene.
neXtProtNX_P07311.
PharmGKBPA24499.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG289322.
HOGENOMHOG000292688.
HOVERGENHBG050454.
InParanoidP07311.
KOK01512.
OrthoDBEOG7ZGX55.
PhylomeDBP07311.
TreeFamTF300288.

Enzyme and pathway databases

SABIO-RKP07311.

Gene expression databases

ArrayExpressP07311.
BgeeP07311.
CleanExHS_ACYP1.
GenevestigatorP07311.

Family and domain databases

InterProIPR020456. Acylphosphatase.
IPR001792. Acylphosphatase-like_dom.
IPR017968. Acylphosphatase_CS.
[Graphical view]
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

EvolutionaryTraceP07311.
GeneWikiACYP1.
GenomeRNAi97.
NextBio367.
PROP07311.
SOURCESearch...

Entry information

Entry nameACYP1_HUMAN
AccessionPrimary (citable) accession number: P07311
Secondary accession number(s): A6NDV8, B2R590
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 140 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM