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P07311 (ACYP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 117. 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·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)
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
   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. Source: ProtInc

   Molecular functionacylphosphatase activity

Traceable author statement. Source: ProtInc

Complete GO annotation...

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

Secondary structure

........... 99
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07311 [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

References

« Hide 'large scale' references
[1]Raugei G.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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: 12508121] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: 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: 3026468] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-99.
[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: 7796909] [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: 21269460] [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: 16511269] [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: 19196981] [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.
CH471061 Genomic DNA. Translation: EAW81216.1.
BC035568 mRNA. Translation: AAH35568.1.
IPIIPI00221117.
PIRQPHUE. S66187.
RefSeqNP_001098.1. NM_001107.3.
NP_982355.1. NM_203488.1.
UniGeneHs.18573.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K7JNMR-A2-99[»]
2K7KNMR-A2-99[»]
2VH7X-ray1.45A1-99[»]
2W4CX-ray1.52A1-98[»]
2W4PX-ray1.70A1-98[»]
ProteinModelPortalP07311.
SMRP07311. Positions 6-99.
ModBaseSearch...

Protein-protein interaction databases

STRINGP07311.

Polymorphism databases

DMDM2507560.

Proteomic databases

PRIDEP07311.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000238618; ENSP00000238618; ENSG00000119640.
GeneID97.
KEGGhsa:97.
UCSCuc001xrg.1. human.

Organism-specific databases

CTD97.
GeneCardsGC14M075519.
H-InvDBHIX0202094.
HGNCHGNC:179. ACYP1.
HPAHPA034944.
MIM600875. gene.
neXtProtNX_P07311.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG20949.
GeneTreeENSGT00390000011103.
HOGENOMHBG750266.
HOVERGENHBG050454.
InParanoidP07311.
OMAASFNNEK.
OrthoDBEOG4XD3SN.
PhylomeDBP07311.

Gene expression databases

CleanExHS_ACYP1.
GenevestigatorP07311.
GermOnlineENSG00000119640. Homo sapiens.

Family and domain databases

InterProIPR020456. Acylphosphatase.
IPR001792. Acylphosphatase-like.
IPR017968. Acylphosphatase_CS.
[Graphical view]
KOK01512.
PfamPF00708. Acylphosphatase. 1 hit.
[Graphical view]
PRINTSPR00112. ACYLPHPHTASE.
SUPFAMSSF54975. Acylphosphatase. 1 hit.
PROSITEPS00150. ACYLPHOSPHATASE_1. 1 hit.
PS00151. ACYLPHOSPHATASE_2. 1 hit.
PS51160. ACYLPHOSPHATASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio367.
SOURCESearch...

Entry information

Entry nameACYP1_HUMAN
AccessionPrimary (citable) accession number: P07311
Secondary accession number(s): B2R590
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 117 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

Human chromosome 14

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families