Reviewed, UniProtKB/Swiss-Prot P24666 (PPAC_HUMAN)

Names and origin

Protein names

Recommended name:
    Low molecular weight phosphotyrosine protein phosphatase
      Short name=LMW-PTPase
      Short name=LMW-PTP
    EC=3.1.3.48
Alternative name(s):
    Low molecular weight cytosolic acid phosphatase
    EC=3.1.3.2
    Red cell acid phosphatase 1
    Adipocyte acid phosphatase

Gene names

Name:

ACP1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	158 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.15
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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	protein amino acid dephosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fraction Ref.3 Traceable author statement. Source: ProtInc
Molecular function	acid phosphatase activity Ref.3 Traceable author statement. Source: ProtInc identical protein binding Inferred from physical interaction. Source: IntAct non-membrane spanning protein tyrosine phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-717701,EBI-717701

Alternative products

This entry describes 3 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 158

157

Low molecular weight phosphotyrosine protein phosphatase

PRO_0000046558

Sites

Active site

13

1

Nucleophile By similarity

Active site

19

1

By similarity

Active site

130

1

Proton donor By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.1

Modified residue

132

1

Phosphotyrosine Ref.6 Ref.16 Ref.17

Modified residue

133

1

Phosphotyrosine Ref.6

Modified residue

156

1

N6-acetyllysine Ref.19

Natural variations

Alternative sequence

41 – 74

34

RVDSA…PMSHV → VIDSGAVSDWNVGRSPDPRA VSCLRNHGIHTAHK in isoform 2.

VSP_010087

Alternative sequence

41 – 74

34

Missing in isoform 3.

VSP_010088

Natural variant

7

1

K → N: dbSNP rs11691572.

VAR_050526

Natural variant

106

1

Q → R in allele ACP1*A. dbSNP rs7576247. Ref.12

VAR_006171

Natural variant

137

1

S → F: dbSNP rs35569198.

VAR_050527

Experimental info

Mutagenesis

13

1

C → S: Inactive. Ref.6

Mutagenesis

132

1

Y → F: Reduced phosphorylation and activity. Ref.6

Mutagenesis

133

1

Y → F: Reduced phosphorylation. No effect on activity. Ref.6

Sequence conflict

2 – 6

5

AEQAT → PRRGR in AAB27086. Ref.5

Sequence conflict

13 – 20

8

CLGNICRS → PARREAAR in AAB27085. Ref.5

Sequence conflict

32

1

T → W Ref.1

Sequence conflict

32

1

T → W Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

158

Helix Strand Turn

Details...

Beta strand

7 – 18

12

Helix

19 – 33

15

Helix

37 – 39

3

Beta strand

40 – 49

10

Turn

50 – 53

4

Helix

58 – 66

9

Helix

80 – 85

6

Beta strand

87 – 93

7

Helix

94 – 105

12

Beta strand

113 – 116

4

Helix

117 – 120

4

Helix

136 – 156

21

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (F) (A) (Alpha) (LMPTP-A) (HCPTP-A) [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 46617BD799313EED	FASTA	158	18,042
	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
	Isoform 2 (S) (B) (Beta) (LMPTP-B) (HCPTP-B) [UniParc] [UniParc]. Checksum: A137F38F06F39161	FASTA	158	17,977
	10 20 30 40 50 60 MAEQATKSVL FVCLGNICRS PIAEAVFRKL VTDQNISENW VIDSGAVSDW NVGRSPDPRA 70 80 90 100 110 120 VSCLRNHGIH TAHKARQITK EDFATFDYIL CMDESNLRDL NRKSNQVKTC KAKIELLGSY 130 140 150 DPQKQLIIED PYYGNDSDFE TVYQQCVRCC RAFLEKAH
	Isoform 3 (C) (LMPTP-C). Checksum: D68ED15D431D2484	FASTA	124	14,342
	10 20 30 40 50 60 MAEQATKSVL FVCLGNICRS PIAEAVFRKL VTDQNISENW ARQITKEDFA TFDYILCMDE 70 80 90 100 110 120 SNLRDLNRKS NQVKTCKAKI ELLGSYDPQK QLIIEDPYYG NDSDFETVYQ QCVRCCRAFL EKAH

References

	« Hide 'large scale' referencesShow '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: 1939112] [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: 1627603] [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: 1587862] [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: 8586411] [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: 1304913] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (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: 9038134] [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: 10336608] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 3).
[8]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Hippocampus and Skeletal muscle.
[9]	"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).
[10]	"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. , 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: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	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. , 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].
[12]	"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] (ISOFORMS 1 AND 2), VARIANT ARG-106. Tissue: Muscle and Placenta.
[13]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 42-59, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[14]	"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: 8364553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-158 (ISOFORMS 1/2). Tissue: Blood.
[15]	"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: 11971983] [Abstract] Cited for: INTERACTION WITH SPTAN1.
[16]	"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M. Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-132, MASS SPECTROMETRY. Tissue: Epithelium.
[17]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-132, MASS SPECTROMETRY.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-156, MASS SPECTROMETRY.
[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: 9705307] [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.
AK289934 mRNA. Translation: BAF82623.1.
AK291861 mRNA. Translation: BAF84550.1.
BT007136 mRNA. Translation: AAP35800.1.
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.

IPI

IPI00218847.
IPI00219861.
IPI00410615.

PIR

A38148.
B38148.

RefSeq

NP_004291.1.
NP_009030.1.

UniGene

Hs.558296

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XWW	X-ray	1.63	A	2-158	[»]
5PNT	X-ray	2.20	A	2-158	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P24666. 11 interactions.

STRING

P24666.

PTM databases

PhosphoSite

P24666.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00218847.
IPI00219861.

Proteomic databases

PRIDE

P24666.

Genome annotation databases

Ensembl

ENST00000272065; ENSP00000272065; ENSG00000143727; Homo sapiens. [Genome view]

GeneID

52.

UCSC

uc002qwf.1. human.
uc002qwg.1. human.

Organism-specific databases

CTD

52.

GeneCards

GC02P000254.

H-InvDB

HIX0001778.

HGNC

HGNC:122. ACP1.

HPA

HPA016754.

MIM

171500. gene.

PharmGKB

PA24446.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P24666.

InParanoid

P24666.

OMA

HRGTQAI.

OrthoDB

EOG9SJ80C.

PhylomeDB

P24666.

Enzyme and pathway databases

BRENDA

3.1.3.2. 247.
3.1.3.48. 247.

Pathway_Interaction_DB

epha2_fwdpathway. EPHA2 forward signaling.
pdgfrbpathway. PDGFR-beta signaling pathway.

Gene expression databases

ArrayExpress

P24666.

Bgee

P24666.

CleanEx

HS_ACP1.

Genevestigator

P24666.

GermOnline

ENSG00000143727. Homo sapiens.

Family and domain databases

InterPro

IPR002115. Tyr_Pase_low_mol_wt_mml.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]

PANTHER

PTHR11717. Low_mwt_PTPase. 1 hit.

Pfam

PF01451. LMWPc. 1 hit.
[Graphical view]

PRINTS

PR00719. LMWPTPASE.
PR00720. MAMMALPTPASE.

SMART

SM00226. LMWPc. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

205.

SOURCE

Search...

Entry information

Entry name

PPAC_HUMAN

Accession

Primary (citable) accession number: P24666
Secondary accession number(s): A8K1L9 , P24667, Q16035, Q16036, Q16725, Q3KQX8, Q53RU0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.