SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P24666

- PPAC_HUMAN

UniProt

P24666 - PPAC_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Low molecular weight phosphotyrosine protein phosphatase

Gene
ACP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
A phosphate monoester + H2O = an alcohol + phosphate.

Enzyme regulationi

Inhibited by sulfhydryl reagents.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei13 – 131Nucleophile By similarity
Active sitei19 – 191 By similarity
Active sitei130 – 1301Proton donor By similarity

GO - Molecular functioni

  1. acid phosphatase activity Source: ProtInc
  2. non-membrane spanning protein tyrosine phosphatase activity Source: InterPro
  3. protein binding Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

SignaLinkiP24666.

Names & Taxonomyi

Protein namesi
Recommended name:
Low molecular weight phosphotyrosine protein phosphatase (EC:3.1.3.48)
Short name:
LMW-PTP
Short name:
LMW-PTPase
Alternative name(s):
Adipocyte acid phosphatase
Low molecular weight cytosolic acid phosphatase (EC:3.1.3.2)
Red cell acid phosphatase 1
Gene namesi
Name:ACP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:122. ACP1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic side of plasma membrane Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131C → S: Inactive. 1 Publication
Mutagenesisi132 – 1321Y → F: Reduced phosphorylation and activity. 1 Publication
Mutagenesisi133 – 1331Y → F: Reduced phosphorylation. No effect on activity. 1 Publication

Organism-specific databases

PharmGKBiPA24446.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 158157Low molecular weight phosphotyrosine protein phosphatasePRO_0000046558Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei132 – 1321Phosphotyrosine1 Publication
Modified residuei133 – 1331Phosphotyrosine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP24666.
PaxDbiP24666.
PRIDEiP24666.

2D gel databases

REPRODUCTION-2DPAGEIPI00218847.
IPI00219861.

PTM databases

PhosphoSiteiP24666.

Expressioni

Tissue specificityi

T-lymphocytes express only isoform 2.1 Publication

Gene expression databases

ArrayExpressiP24666.
BgeeiP24666.
CleanExiHS_ACP1.
GenevestigatoriP24666.

Organism-specific databases

HPAiHPA016754.

Interactioni

Subunit structurei

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 EPHB1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself1EBI-717701,EBI-717701

Protein-protein interaction databases

BioGridi106568. 19 interactions.
IntActiP24666. 6 interactions.
STRINGi9606.ENSP00000272065.

Structurei

Secondary structure

1
158
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 1812
Helixi19 – 3315
Helixi37 – 393
Beta strandi40 – 4910
Turni50 – 534
Helixi58 – 669
Helixi80 – 856
Beta strandi87 – 937
Helixi94 – 10411
Beta strandi113 – 1164
Helixi117 – 1204
Helixi136 – 15520

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XWWX-ray1.63A2-158[»]
3N8IX-ray1.50A2-158[»]
5PNTX-ray2.20A2-158[»]
ProteinModelPortaliP24666.
SMRiP24666. Positions 5-158.

Miscellaneous databases

EvolutionaryTraceiP24666.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0394.
HOGENOMiHOG000074091.
HOVERGENiHBG007540.
InParanoidiP24666.
KOiK14394.
OMAiENQHYIN.
OrthoDBiEOG7QZGCG.
PhylomeDBiP24666.
TreeFamiTF353727.

Family and domain databases

InterProiIPR023485. Ptyr_pPase_SF.
IPR002115. Tyr_Pase_low_mol_wt_mml.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERiPTHR11717. PTHR11717. 1 hit.
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
PRINTSiPR00719. LMWPTPASE.
PR00720. MAMMALPTPASE.
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMiSSF52788. SSF52788. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

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) [UniParc]FASTAAdd to Basket

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.

« Hide

MAEQATKSVL FVCLGNICRS PIAEAVFRKL VTDQNISENW RVDSAATSGY    50
EIGNPPDYRG QSCMKRHGIP MSHVARQITK EDFATFDYIL CMDESNLRDL 100
NRKSNQVKTC KAKIELLGSY DPQKQLIIED PYYGNDSDFE TVYQQCVRCC 150
RAFLEKAH 158
Length:158
Mass (Da):18,042
Last modified:January 23, 2007 - v3
Checksum:i46617BD799313EED
GO
Isoform 2 (identifier: P24666-2) [UniParc] [UniParc]FASTAAdd to Basket

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

Show »
Length:158
Mass (Da):17,977
Checksum:iA137F38F06F39161
GO
Isoform 3 (identifier: P24666-3) [UniParc]FASTAAdd to Basket

Also known as: C, LMPTP-C

The sequence of this isoform differs from the canonical sequence as follows:
     41-74: Missing.

Show »
Length:124
Mass (Da):14,342
Checksum:iD68ED15D431D2484
GO
Isoform 4 (identifier: P24666-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     78-112: ITKEDFATFDYILCMDESNLRDLNRKSNQVKTCKA → VPSLDLKLCVLCFSGSLTAVLFLTGTWAGPQTQEL
     113-158: Missing.

Note: No experimental confirmation available.

Show »
Length:112
Mass (Da):12,230
Checksum:i805DBFA90F43D732
GO

Polymorphismi

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71K → N.
Corresponds to variant rs11691572 [ dbSNP | Ensembl ].
VAR_050526
Natural varianti106 – 1061Q → R in allele ACP1*A. 1 Publication
Corresponds to variant rs7576247 [ dbSNP | Ensembl ].
VAR_006171
Natural varianti137 – 1371S → F.
Corresponds to variant rs35569198 [ dbSNP | Ensembl ].
VAR_050527

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei41 – 7434RVDSA…PMSHV → VIDSGAVSDWNVGRSPDPRA VSCLRNHGIHTAHK in isoform 2. VSP_010087Add
BLAST
Alternative sequencei41 – 7434Missing in isoform 3. VSP_010088Add
BLAST
Alternative sequencei78 – 11235ITKED…KTCKA → VPSLDLKLCVLCFSGSLTAV LFLTGTWAGPQTQEL in isoform 4. VSP_054074Add
BLAST
Alternative sequencei113 – 15846Missing in isoform 4. VSP_054075Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 65AEQAT → PRRGR in AAB27086. 1 Publication
Sequence conflicti2 – 21A → P in BP363227. 1 Publication
Sequence conflicti13 – 208CLGNICRS → PARREAAR in AAB27085. 1 Publication
Sequence conflicti32 – 321T → W AA sequence 1 Publication
Sequence conflicti32 – 321T → W AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1639.1. [P24666-1]
CCDS1640.1. [P24666-2]
CCDS46217.1. [P24666-4]
PIRiA38148.
B38148.
RefSeqiNP_001035739.1. NM_001040649.2. [P24666-4]
NP_004291.1. NM_004300.3. [P24666-1]
NP_009030.1. NM_007099.3. [P24666-2]
UniGeneiHs.558296.

Genome annotation databases

EnsembliENST00000272065; ENSP00000272065; ENSG00000143727. [P24666-1]
ENST00000272067; ENSP00000272067; ENSG00000143727. [P24666-2]
ENST00000407983; ENSP00000385404; ENSG00000143727.
GeneIDi52.
KEGGihsa:52.
UCSCiuc002qwf.3. human. [P24666-1]
uc002qwg.3. human. [P24666-2]

Polymorphism databases

DMDMi1709543.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1639.1. [P24666-1 ]
CCDS1640.1. [P24666-2 ]
CCDS46217.1. [P24666-4 ]
PIRi A38148.
B38148.
RefSeqi NP_001035739.1. NM_001040649.2. [P24666-4 ]
NP_004291.1. NM_004300.3. [P24666-1 ]
NP_009030.1. NM_007099.3. [P24666-2 ]
UniGenei Hs.558296.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XWW X-ray 1.63 A 2-158 [» ]
3N8I X-ray 1.50 A 2-158 [» ]
5PNT X-ray 2.20 A 2-158 [» ]
ProteinModelPortali P24666.
SMRi P24666. Positions 5-158.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106568. 19 interactions.
IntActi P24666. 6 interactions.
STRINGi 9606.ENSP00000272065.

Chemistry

BindingDBi P24666.
ChEMBLi CHEMBL4903.

PTM databases

PhosphoSitei P24666.

Polymorphism databases

DMDMi 1709543.

2D gel databases

REPRODUCTION-2DPAGE IPI00218847.
IPI00219861.

Proteomic databases

MaxQBi P24666.
PaxDbi P24666.
PRIDEi P24666.

Protocols and materials databases

DNASUi 52.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000272065 ; ENSP00000272065 ; ENSG00000143727 . [P24666-1 ]
ENST00000272067 ; ENSP00000272067 ; ENSG00000143727 . [P24666-2 ]
ENST00000407983 ; ENSP00000385404 ; ENSG00000143727 .
GeneIDi 52.
KEGGi hsa:52.
UCSCi uc002qwf.3. human. [P24666-1 ]
uc002qwg.3. human. [P24666-2 ]

Organism-specific databases

CTDi 52.
GeneCardsi GC02P000254.
HGNCi HGNC:122. ACP1.
HPAi HPA016754.
MIMi 171500. gene.
neXtProti NX_P24666.
PharmGKBi PA24446.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0394.
HOGENOMi HOG000074091.
HOVERGENi HBG007540.
InParanoidi P24666.
KOi K14394.
OMAi ENQHYIN.
OrthoDBi EOG7QZGCG.
PhylomeDBi P24666.
TreeFami TF353727.

Enzyme and pathway databases

SignaLinki P24666.

Miscellaneous databases

EvolutionaryTracei P24666.
GeneWikii ACP1.
GenomeRNAii 52.
NextBioi 205.
PROi P24666.
SOURCEi Search...

Gene expression databases

ArrayExpressi P24666.
Bgeei P24666.
CleanExi HS_ACP1.
Genevestigatori P24666.

Family and domain databases

InterProi IPR023485. Ptyr_pPase_SF.
IPR002115. Tyr_Pase_low_mol_wt_mml.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view ]
PANTHERi PTHR11717. PTHR11717. 1 hit.
Pfami PF01451. LMWPc. 1 hit.
[Graphical view ]
PRINTSi PR00719. LMWPTPASE.
PR00720. MAMMALPTPASE.
SMARTi SM00226. LMWPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52788. SSF52788. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-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.
    , 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. 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.
    , 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. 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. Cited for: INTERACTION WITH SPTAN1.
  19. 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).

Entry informationi

Entry nameiPPAC_HUMAN
AccessioniPrimary (citable) accession number: P24666
Secondary accession number(s): A8K1L9
, B5MCC7, P24667, Q16035, Q16036, Q16725, Q3KQX8, Q53RU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 160 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi