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P24666 (PPAC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Low molecular weight phosphotyrosine protein phosphatase

Short name=LMW-PTP
Short name=LMW-PTPase
EC=3.1.3.48
Alternative name(s):
Adipocyte acid phosphatase
Low molecular weight cytosolic acid phosphatase
EC=3.1.3.2
Red cell acid phosphatase 1
Gene names
Name:ACP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Isoform 3 does not possess phosphatase activity.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

A phosphate monoester + H2O = an alcohol + phosphate.

Enzyme regulation

Inhibited by sulfhydryl reagents.

Subunit structure

Isoform 1 interacts with the SH3 domain of SPTAN1. There is no interaction observed for isoforms 2 or 3. Interacts with EPHA2; dephosphorylates EPHA2. Interacts with EPHB1. Ref.16 Ref.17 Ref.18

Subcellular location

Cytoplasm.

Tissue specificity

T-lymphocytes express only isoform 2. Ref.6

Polymorphism

ACP1 is genetically polymorphic. Three common alleles are known in Caucasians: ACP1*A, ACP1*B and ACP1*C. They give rise to six different phenotypes. Each allele appears to encode two electrophoretically different isozymes, F and S, which are produced in allele-specific ratios. The sequence shown is that of allele ACP1*B and allele ACP1*C.

Sequence similarities

Belongs to the low molecular weight phosphotyrosine protein phosphatase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself1EBI-717701,EBI-717701

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: The ratio of isoform 1 to isoform 2 is 2:1 in allele A, 4:1 in allele B and 1:4 in allele C.
Isoform 1 (identifier: P24666-1)

Also known as: F; A; Alpha; LMPTP-A; HCPTP-A;

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: P24666-2)

Also known as: S; B; Beta; LMPTP-B; HCPTP-B;

The sequence of this isoform differs from the canonical sequence as follows:
     41-74: RVDSAATSGYEIGNPPDYRGQSCMKRHGIPMSHV → VIDSGAVSDWNVGRSPDPRAVSCLRNHGIHTAHK
Isoform 3 (identifier: P24666-3)

Also known as: C; LMPTP-C;

The sequence of this isoform differs from the canonical sequence as follows:
     41-74: Missing.
Isoform 4 (identifier: P24666-4)

The sequence of this isoform differs from the canonical sequence as follows:
     78-112: ITKEDFATFDYILCMDESNLRDLNRKSNQVKTCKA → VPSLDLKLCVLCFSGSLTAVLFLTGTWAGPQTQEL
     113-158: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 158157Low molecular weight phosphotyrosine protein phosphatase
PRO_0000046558

Sites

Active site131Nucleophile By similarity
Active site191 By similarity
Active site1301Proton donor By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.1
Modified residue1321Phosphotyrosine Ref.6
Modified residue1331Phosphotyrosine Ref.6

Natural variations

Alternative sequence41 – 7434RVDSA…PMSHV → VIDSGAVSDWNVGRSPDPRA VSCLRNHGIHTAHK in isoform 2.
VSP_010087
Alternative sequence41 – 7434Missing in isoform 3.
VSP_010088
Alternative sequence78 – 11235ITKED…KTCKA → VPSLDLKLCVLCFSGSLTAV LFLTGTWAGPQTQEL in isoform 4.
VSP_054074
Alternative sequence113 – 15846Missing in isoform 4.
VSP_054075
Natural variant71K → N.
Corresponds to variant rs11691572 [ dbSNP | Ensembl ].
VAR_050526
Natural variant1061Q → R in allele ACP1*A. Ref.13
Corresponds to variant rs7576247 [ dbSNP | Ensembl ].
VAR_006171
Natural variant1371S → F.
Corresponds to variant rs35569198 [ dbSNP | Ensembl ].
VAR_050527

Experimental info

Mutagenesis131C → S: Inactive. Ref.6
Mutagenesis1321Y → F: Reduced phosphorylation and activity. Ref.6
Mutagenesis1331Y → F: Reduced phosphorylation. No effect on activity. Ref.6
Sequence conflict2 – 65AEQAT → PRRGR in AAB27086. Ref.5
Sequence conflict21A → P in BP363227. Ref.10
Sequence conflict13 – 208CLGNICRS → PARREAAR in AAB27085. Ref.5
Sequence conflict321T → W AA sequence Ref.1
Sequence conflict321T → W AA sequence Ref.2

Secondary structure

.................... 158
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (F) (A) (Alpha) (LMPTP-A) (HCPTP-A) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 46617BD799313EED

FASTA15818,042
        10         20         30         40         50         60 
MAEQATKSVL FVCLGNICRS PIAEAVFRKL VTDQNISENW RVDSAATSGY EIGNPPDYRG 

        70         80         90        100        110        120 
QSCMKRHGIP MSHVARQITK EDFATFDYIL CMDESNLRDL NRKSNQVKTC KAKIELLGSY 

       130        140        150 
DPQKQLIIED PYYGNDSDFE TVYQQCVRCC RAFLEKAH 

« Hide

Isoform 2 (S) (B) (Beta) (LMPTP-B) (HCPTP-B) [UniParc] [UniParc].

Checksum: A137F38F06F39161
Show »

FASTA15817,977
Isoform 3 (C) (LMPTP-C) [UniParc].

Checksum: D68ED15D431D2484
Show »

FASTA12414,342
Isoform 4 [UniParc].

Checksum: 805DBFA90F43D732
Show »

FASTA11212,230

References

« Hide 'large scale' references
[1]"Human red cell acid phosphatase (ACP1). The amino acid sequence of the two isozymes Bf and Bs encoded by the ACP1*B allele."
Dissing J., Johnsen A.H., Sensabaugh G.F.
J. Biol. Chem. 266:20619-20625(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE (ALLELE B; ISOFORMS 1 AND 2).
[2]"Human red cell acid phosphatase (ACP1): the primary structure of the two pairs of isozymes encoded by the ACP1*A and ACP1*C alleles."
Dissing J., Johnsen A.H.
Biochim. Biophys. Acta 1121:261-268(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE (ALLELES A AND C; ISOFORMS 1 AND 2).
[3]"Sequencing, cloning, and expression of human red cell-type acid phosphatase, a cytoplasmic phosphotyrosyl protein phosphatase."
Wo Y.-Y.P., McCormack A.L., Shabonowitz J., Hunt D.F., Davis J.P., Mitchell G.L., van Etten R.L.
J. Biol. Chem. 267:10856-10865(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[4]"Gene structure, sequence, and chromosomal localization of the human red cell-type low-molecular-weight acid phosphotyrosyl phosphatase gene, ACP1."
Bryson G.L.M., Massa H., Trask B.J., van Etten R.L.
Genomics 30:133-140(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Identification of the adipocyte acid phosphatase as a PAO-sensitive tyrosyl phosphatase."
Shekels L.L., Smith A.J., van Etten R.L., Bernlohr D.A.
Protein Sci. 1:710-721(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Adipocyte.
[6]"Regulation of the low molecular weight phosphotyrosine phosphatase by phosphorylation at tyrosines 131 and 132."
Tailor P., Gilman J., Williams S., Couture C., Mustelin T.
J. Biol. Chem. 272:5371-5374(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2), TISSUE SPECIFICITY, PHOSPHORYLATION AT TYR-132 AND TYR-133, MUTAGENESIS OF CYS-13; TYR-132 AND TYR-133.
[7]"A novel isoform of the low molecular weight phosphotyrosine phosphatase, LMPTP-C, arising from alternative mRNA splicing."
Tailor P., Gilman J., Williams S., Mustelin T.
Eur. J. Biochem. 262:277-282(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 3).
[8]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[9]"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] (ISOFORMS 1 AND 2).
Tissue: Hippocampus and Skeletal muscle.
[10]"Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes."
Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T., Yamashita R., Yamamoto J., Sekine M., Tsuritani K., Wakaguri H., Ishii S., Sugiyama T., Saito K., Isono Y., Irie R., Kushida N., Yoneyama T., Otsuka R. expand/collapse author list , Kanda K., Yokoi T., Kondo H., Wagatsuma M., Murakawa K., Ishida S., Ishibashi T., Takahashi-Fujii A., Tanase T., Nagai K., Kikuchi H., Nakai K., Isogai T., Sugano S.
Genome Res. 16:55-65(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
[11]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]"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), VARIANT ARG-106.
Tissue: Muscle and Placenta.
[14]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 42-59, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[15]"A TaqI site identifies the *A allele at the ACP1 locus."
Sensabaugh G.F., Lazaruk K.A.
Hum. Mol. Genet. 2:1079-1079(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-158 (ISOFORMS 1/2).
Tissue: Blood.
[16]"Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses."
Stein E., Lane A.A., Cerretti D.P., Schoecklmann H.O., Schroff A.D., Van Etten R.L., Daniel T.O.
Genes Dev. 12:667-678(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPHB1.
[17]"Regulation of the EphA2 kinase by the low molecular weight tyrosine phosphatase induces transformation."
Kikawa K.D., Vidale D.R., Van Etten R.L., Kinch M.S.
J. Biol. Chem. 277:39274-39279(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPHA2.
[18]"Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain."
Nicolas G., Fournier C.M., Galand C., Malbert-Colas L., Bournier O., Kroviarski Y., Bourgeois M., Camonis J.H., Dhermy D., Grandchamp B., Lecomte M.-C.
Mol. Cell. Biol. 22:3527-3536(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPTAN1.
[19]"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].
[20]"Crystal structure of a human low molecular weight phosphotyrosyl phosphatase. Implications for substrate specificity."
Zhang M., Stauffacher C.V., Lin D., van Etten R.L.
J. Biol. Chem. 273:21714-21720(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M83653 mRNA. Translation: AAB59354.1.
M83654 mRNA. Translation: AAB59355.1.
U25849, U25847, U25848 Genomic DNA. Translation: AAC52067.1.
S62884 mRNA. Translation: AAB27085.1.
S62885 mRNA. Translation: AAB27086.1.
M87545 mRNA. No translation available.
BT007136 mRNA. Translation: AAP35800.1.
AK289934 mRNA. Translation: BAF82623.1.
AK291861 mRNA. Translation: BAF84550.1.
BP363227 mRNA. No translation available.
AC079779 Genomic DNA. Translation: AAY14958.1.
CH471053 Genomic DNA. Translation: EAX01112.1.
CH471053 Genomic DNA. Translation: EAX01116.1.
BC007422 mRNA. Translation: AAH07422.1.
BC106011 mRNA. Translation: AAI06012.1.
L06508 Genomic DNA. Translation: AAB59628.1.
PIRA38148.
B38148.
RefSeqNP_004291.1. NM_004300.3.
NP_009030.1. NM_007099.3.
UniGeneHs.558296.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XWWX-ray1.63A2-158[»]
3N8IX-ray1.50A2-158[»]
5PNTX-ray2.20A2-158[»]
ProteinModelPortalP24666.
SMRP24666. Positions 5-158.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106568. 19 interactions.
IntActP24666. 6 interactions.
STRING9606.ENSP00000272065.

Chemistry

BindingDBP24666.
ChEMBLCHEMBL4903.

PTM databases

PhosphoSiteP24666.

Polymorphism databases

DMDM1709543.

2D gel databases

REPRODUCTION-2DPAGEIPI00218847.
IPI00219861.

Proteomic databases

PaxDbP24666.
PRIDEP24666.

Protocols and materials databases

DNASU52.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000272065; ENSP00000272065; ENSG00000143727. [P24666-1]
ENST00000272067; ENSP00000272067; ENSG00000143727. [P24666-2]
ENST00000407983; ENSP00000385404; ENSG00000143727.
GeneID52.
KEGGhsa:52.
UCSCuc002qwf.3. human. [P24666-1]
uc002qwg.3. human. [P24666-2]

Organism-specific databases

CTD52.
GeneCardsGC02P000254.
HGNCHGNC:122. ACP1.
HPAHPA016754.
MIM171500. gene.
neXtProtNX_P24666.
PharmGKBPA24446.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0394.
HOGENOMHOG000074091.
HOVERGENHBG007540.
InParanoidP24666.
KOK14394.
OMAIDITVDS.
OrthoDBEOG7QZGCG.
PhylomeDBP24666.
TreeFamTF353727.

Enzyme and pathway databases

SignaLinkP24666.

Gene expression databases

ArrayExpressP24666.
BgeeP24666.
CleanExHS_ACP1.
GenevestigatorP24666.

Family and domain databases

InterProIPR023485. Ptyr_pPase_SF.
IPR002115. Tyr_Pase_low_mol_wt_mml.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERPTHR11717. PTHR11717. 1 hit.
PfamPF01451. LMWPc. 1 hit.
[Graphical view]
PRINTSPR00719. LMWPTPASE.
PR00720. MAMMALPTPASE.
SMARTSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMSSF52788. SSF52788. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP24666.
GeneWikiACP1.
GenomeRNAi52.
NextBio205.
PROP24666.
SOURCESearch...

Entry information

Entry namePPAC_HUMAN
AccessionPrimary (citable) accession number: P24666
Secondary accession number(s): A8K1L9 expand/collapse secondary AC list , B5MCC7, P24667, Q16035, Q16036, Q16725, Q3KQX8, Q53RU0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 156 of the entry and version 3 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

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