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Protein

Low molecular weight phosphotyrosine protein phosphatase

Gene

ACP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 – 131NucleophileBy similarity
Active sitei19 – 191By similarity
Active sitei130 – 1301Proton donorBy similarity

GO - Molecular functioni

  1. acid phosphatase activity Source: ProtInc
  2. non-membrane spanning protein tyrosine phosphatase activity Source: InterPro
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: UniProtKB
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

DEPODiP24666.
PhosphoSiteiP24666.

Expressioni

Tissue specificityi

T-lymphocytes express only isoform 2.1 Publication

Gene expression databases

BgeeiP24666.
CleanExiHS_ACP1.
ExpressionAtlasiP24666. baseline and differential.
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 – 1812Combined sources
Helixi19 – 3315Combined sources
Helixi37 – 393Combined sources
Beta strandi40 – 4910Combined sources
Turni50 – 534Combined sources
Helixi58 – 669Combined sources
Helixi80 – 856Combined sources
Beta strandi87 – 937Combined sources
Helixi94 – 10411Combined sources
Beta strandi113 – 1164Combined sources
Helixi117 – 1204Combined sources
Helixi136 – 15520Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP24666.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0394.
GeneTreeiENSGT00500000044891.
HOGENOMiHOG000074091.
HOVERGENiHBG007540.
InParanoidiP24666.
KOiK14394.
OMAiCEIAPEM.
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:SF15. PTHR11717:SF15. 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

        10         20         30         40         50
MAEQATKSVL FVCLGNICRS PIAEAVFRKL VTDQNISENW RVDSAATSGY
60 70 80 90 100
EIGNPPDYRG QSCMKRHGIP MSHVARQITK EDFATFDYIL CMDESNLRDL
110 120 130 140 150
NRKSNQVKTC KAKIELLGSY DPQKQLIIED PYYGNDSDFE TVYQQCVRCC

RAFLEKAH
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 65AEQAT → PRRGR in AAB27086. (PubMed:1304913)Curated
Sequence conflicti2 – 21A → P in BP363227. (PubMed:16344560)Curated
Sequence conflicti13 – 208CLGNICRS → PARREAAR in AAB27085. (PubMed:1304913)Curated
Sequence conflicti32 – 321T → W AA sequence (PubMed:1939112)Curated
Sequence conflicti32 – 321T → W AA sequence (PubMed:1627603)Curated

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. 5 PublicationsVSP_010087Add
BLAST
Alternative sequencei41 – 7434Missing in isoform 3. CuratedVSP_010088Add
BLAST
Alternative sequencei78 – 11235ITKED…KTCKA → VPSLDLKLCVLCFSGSLTAV LFLTGTWAGPQTQEL in isoform 4. 1 PublicationVSP_054074Add
BLAST
Alternative sequencei113 – 15846Missing in isoform 4. 1 PublicationVSP_054075Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [P24666-4]
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

BindingDBiP24666.
ChEMBLiCHEMBL4903.
DrugBankiDB00173. Adenine.

PTM databases

DEPODiP24666.
PhosphoSiteiP24666.

Polymorphism databases

DMDMi1709543.

2D gel databases

REPRODUCTION-2DPAGEIPI00218847.
IPI00219861.

Proteomic databases

MaxQBiP24666.
PaxDbiP24666.
PRIDEiP24666.

Protocols and materials databases

DNASUi52.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000272065; ENSP00000272065; ENSG00000143727. [P24666-1]
ENST00000272067; ENSP00000272067; ENSG00000143727. [P24666-2]
ENST00000407983; ENSP00000385404; ENSG00000143727. [P24666-4]
GeneIDi52.
KEGGihsa:52.
UCSCiuc002qwf.3. human. [P24666-1]
uc002qwg.3. human. [P24666-2]

Organism-specific databases

CTDi52.
GeneCardsiGC02P000254.
HGNCiHGNC:122. ACP1.
HPAiHPA016754.
MIMi171500. gene.
neXtProtiNX_P24666.
PharmGKBiPA24446.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0394.
GeneTreeiENSGT00500000044891.
HOGENOMiHOG000074091.
HOVERGENiHBG007540.
InParanoidiP24666.
KOiK14394.
OMAiCEIAPEM.
OrthoDBiEOG7QZGCG.
PhylomeDBiP24666.
TreeFamiTF353727.

Enzyme and pathway databases

SignaLinkiP24666.

Miscellaneous databases

EvolutionaryTraceiP24666.
GeneWikiiACP1.
GenomeRNAii52.
NextBioi205.
PROiP24666.
SOURCEiSearch...

Gene expression databases

BgeeiP24666.
CleanExiHS_ACP1.
ExpressionAtlasiP24666. baseline and differential.
GenevestigatoriP24666.

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:SF15. PTHR11717:SF15. 1 hit.
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
PRINTSiPR00719. LMWPTPASE.
PR00720. MAMMALPTPASE.
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMiSSF52788. SSF52788. 1 hit.
ProtoNetiSearch...

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: January 7, 2015
This is version 164 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.