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Q16827

- PTPRO_HUMAN

UniProt

Q16827 - PTPRO_HUMAN

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Protein
Receptor-type tyrosine-protein phosphatase O
Gene
PTPRO, GLEPP1, PTPU2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Possesses tyrosine phosphatase activity. Plays a role in regulating the glomerular pressure/filtration rate relationship through an effect on podocyte structure and function By similarity.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1102 – 11021Substrate By similarity
Active sitei1136 – 11361Phosphocysteine intermediate By similarity
Binding sitei1180 – 11801Substrate By similarity

GO - Molecular functioni

  1. Wnt-protein binding Source: UniProtKB
  2. phosphatase activity Source: UniProtKB
  3. protein binding Source: IntAct
  4. protein homodimerization activity Source: UniProtKB
  5. protein tyrosine phosphatase activity Source: UniProtKB
  6. transmembrane receptor protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. axon guidance Source: UniProtKB
  2. cell morphogenesis Source: UniProtKB
  3. glomerular visceral epithelial cell differentiation Source: UniProtKB
  4. glomerulus development Source: UniProtKB
  5. lamellipodium assembly Source: UniProtKB
  6. monocyte chemotaxis Source: UniProtKB
  7. negative regulation of canonical Wnt signaling pathway Source: UniProtKB
  8. negative regulation of cell-substrate adhesion Source: UniProtKB
  9. negative regulation of glomerular filtration Source: UniProtKB
  10. negative regulation of neuron projection development Source: UniProtKB
  11. negative regulation of retinal ganglion cell axon guidance Source: UniProtKB
  12. peptidyl-tyrosine dephosphorylation Source: UniProtKB
  13. protein dephosphorylation Source: UniProtKB
  14. regulation of glomerular filtration Source: UniProtKB
  15. slit diaphragm assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase, Receptor

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-type tyrosine-protein phosphatase O (EC:3.1.3.48)
Short name:
R-PTP-O
Alternative name(s):
Glomerular epithelial protein 1
Protein tyrosine phosphatase U2
Short name:
PTP-U2
Short name:
PTPase U2
Gene namesi
Name:PTPRO
Synonyms:GLEPP1, PTPU2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:9678. PTPRO.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini30 – 822793Extracellular Reviewed prediction
Add
BLAST
Transmembranei823 – 84321Helical; Reviewed prediction
Add
BLAST
Topological domaini844 – 1216373Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. axon Source: UniProtKB
  3. dendritic spine Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProt
  5. growth cone Source: UniProtKB
  6. integral component of membrane Source: UniProtKB
  7. integral component of plasma membrane Source: UniProtKB
  8. lamellipodium Source: UniProtKB
  9. lateral plasma membrane Source: UniProtKB
  10. neuron projection Source: UniProtKB
  11. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Nephrotic syndrome 6 (NPHS6) [MIM:614196]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

Organism-specific databases

MIMi614196. phenotype.
Orphaneti93214. Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial proliferation.
93217. Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial sclerosis.
93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
93216. Familial idiopathic steroid-resistant nephrotic syndrome with minimal changes.
PharmGKBiPA34023.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929 Reviewed prediction
Add
BLAST
Chaini30 – 12161187Receptor-type tyrosine-protein phosphatase O
PRO_0000025458Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi26 – 261N-linked (GlcNAc...) Reviewed prediction
Glycosylationi75 – 751N-linked (GlcNAc...) Reviewed prediction
Glycosylationi154 – 1541N-linked (GlcNAc...) Reviewed prediction
Glycosylationi189 – 1891N-linked (GlcNAc...) Reviewed prediction
Glycosylationi201 – 2011N-linked (GlcNAc...) Reviewed prediction
Glycosylationi227 – 2271N-linked (GlcNAc...) Reviewed prediction
Glycosylationi278 – 2781N-linked (GlcNAc...) Reviewed prediction
Glycosylationi287 – 2871N-linked (GlcNAc...) Reviewed prediction
Glycosylationi323 – 3231N-linked (GlcNAc...) Reviewed prediction
Glycosylationi324 – 3241N-linked (GlcNAc...) Reviewed prediction
Glycosylationi370 – 3701N-linked (GlcNAc...) Reviewed prediction
Glycosylationi461 – 4611N-linked (GlcNAc...) Reviewed prediction
Glycosylationi490 – 4901N-linked (GlcNAc...) Reviewed prediction
Glycosylationi700 – 7001N-linked (GlcNAc...) Reviewed prediction
Glycosylationi712 – 7121N-linked (GlcNAc...) Reviewed prediction
Glycosylationi733 – 7331N-linked (GlcNAc...) Reviewed prediction
Modified residuei865 – 8651Phosphoserine By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ16827.
PaxDbiQ16827.
PRIDEiQ16827.

PTM databases

PhosphoSiteiQ16827.

Expressioni

Tissue specificityi

Glomerulus of kidney. Also detected in brain, lung and placenta.1 Publication

Inductioni

By various differentiation-inducing agents.

Gene expression databases

ArrayExpressiQ16827.
BgeeiQ16827.
CleanExiHS_PTPRO.
GenevestigatoriQ16827.

Organism-specific databases

HPAiHPA034525.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ERBB2P046262EBI-723739,EBI-641062
TEKQ027632EBI-723739,EBI-2257090

Protein-protein interaction databases

BioGridi111764. 7 interactions.
IntActiQ16827. 25 interactions.
MINTiMINT-1415956.
STRINGi9606.ENSP00000281171.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi920 – 9223
Helixi923 – 94624
Turni947 – 9515
Helixi956 – 9583
Helixi960 – 9656
Turni975 – 9773
Beta strandi978 – 9803
Turni988 – 9914
Beta strandi992 – 9987
Beta strandi1007 – 10104
Helixi1015 – 10173
Helixi1018 – 102710
Beta strandi1032 – 10354
Beta strandi1039 – 10413
Beta strandi1053 – 10564
Beta strandi1058 – 10603
Beta strandi1063 – 107210
Beta strandi1074 – 108512
Beta strandi1088 – 109710
Beta strandi1103 – 11053
Helixi1108 – 112720
Beta strandi1132 – 11409
Helixi1141 – 115818
Beta strandi1160 – 11623
Helixi1164 – 11729
Helixi1182 – 120221

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G59X-ray2.19A/B914-1200[»]
2GJTX-ray2.15A/B916-1208[»]
ProteinModelPortaliQ16827.
SMRiQ16827. Positions 916-1208.

Miscellaneous databases

EvolutionaryTraceiQ16827.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 12475Fibronectin type-III 1
Add
BLAST
Domaini142 – 21170Fibronectin type-III 2
Add
BLAST
Domaini246 – 30661Fibronectin type-III 3
Add
BLAST
Domaini329 – 42597Fibronectin type-III 4
Add
BLAST
Domaini435 – 53197Fibronectin type-III 5
Add
BLAST
Domaini532 – 62897Fibronectin type-III 6
Add
BLAST
Domaini631 – 72494Fibronectin type-III 7
Add
BLAST
Domaini725 – 81793Fibronectin type-III 8
Add
BLAST
Domaini938 – 1195258Tyrosine-protein phosphatase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1136 – 11427Substrate binding By similarity

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5599.
HOGENOMiHOG000243992.
HOVERGENiHBG053763.
InParanoidiQ16827.
KOiK18035.
OMAiSTMVTEM.
OrthoDBiEOG7PCJFZ.
PhylomeDBiQ16827.
TreeFamiTF351926.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
3.90.190.10. 1 hit.
InterProiIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00041. fn3. 2 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 4 hits.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
SSF52799. SSF52799. 1 hit.
PROSITEiPS50853. FN3. 5 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q16827-1) [UniParc]FASTAAdd to Basket

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

MGHLPTGIHG ARRLLPLLWL FVLFKNATAF HVTVQDDNNI VVSLEASDVI     50
SPASVYVVKI TGESKNYFFE FEEFNSTLPP PVIFKASYHG LYYIITLVVV 100
NGNVVTKPSR SITVLTKPLP VTSVSIYDYK PSPETGVLFE IHYPEKYNVF 150
TRVNISYWEG KDFRTMLYKD FFKGKTVFNH WLPGMCYSNI TFQLVSEATF 200
NKSTLVEYSG VSHEPKQHRT APYPPQNISV RIVNLNKNNW EEQSGNFPEE 250
SFMRSQDTIG KEKLFHFTEE TPEIPSGNIS SGWPDFNSSD YETTSQPYWW 300
DSASAAPESE DEFVSVLPME YENNSTLSET EKSTSGSFSF FPVQMILTWL 350
PPKPPTAFDG FHIHIEREEN FTEYLMVDEE AHEFVAELKE PGKYKLSVTT 400
FSSSGSCETR KSQSAKSLSF YISPSGEWIE ELTEKPQHVS VHVLSSTTAL 450
MSWTSSQENY NSTIVSVVSL TCQKQKESQR LEKQYCTQVN SSKPIIENLV 500
PGAQYQVVIY LRKGPLIGPP SDPVTFAIVP TGIKDLMLYP LGPTAVVLSW 550
TRPYLGVFRK YVVEMFYFNP ATMTSEWTTY YEIAATVSLT ASVRIANLLP 600
AWYYNFRVTM VTWGDPELSC CDSSTISFIT APVAPEITSV EYFNSLLYIS 650
WTYGDDTTDL SHSRMLHWMV VAEGKKKIKK SVTRNVMTAI LSLPPGDIYN 700
LSVTACTERG SNTSMLRLVK LEPAPPKSLF AVNKTQTSVT LLWVEEGVAD 750
FFEVFCQQVG SSQKTKLQEP VAVSSHVVTI SSLLPATAYN CSVTSFSHDS 800
PSVPTFIAVS TMVTEMNPNV VVISVLAILS TLLIGLLLVT LIILRKKHLQ 850
MARECGAGTF VNFASLERDG KLPYNWRRSI FAFLTLLPSC LWTDYLLAFY 900
INPWSKNGLK KRKLTNPVQL DDFDAYIKDM AKDSDYKFSL QFEELKLIGL 950
DIPHFAADLP LNRCKNRYTN ILPYDFSRVR LVSMNEEEGA DYINANYIPG 1000
YNSPQEYIAT QGPLPETRND FWKMVLQQKS QIIVMLTQCN EKRRVKCDHY 1050
WPFTEEPIAY GDITVEMISE EEQDDWACRH FRINYADEMQ DVMHFNYTAW 1100
PDHGVPTANA AESILQFVHM VRQQATKSKG PMIIHCSAGV GRTGTFIALD 1150
RLLQHIRDHE FVDILGLVSE MRSYRMSMVQ TEEQYIFIHQ CVQLMWMKKK 1200
QQFCISDVIY ENVSKS 1216
Length:1,216
Mass (Da):138,344
Last modified:October 14, 2008 - v2
Checksum:iC902B48D1A73BFE1
GO
Isoform 2 (identifier: Q16827-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     876-903: Missing.

Show »
Length:1,188
Mass (Da):134,941
Checksum:iC27FCA3BDFA0D1EF
GO
Isoform 3 (identifier: Q16827-3) [UniParc]FASTAAdd to Basket

Also known as: PTPROt

The sequence of this isoform differs from the canonical sequence as follows:
     1-811: Missing.

Note: Predominantly expressed in B-lymphoid tissues.

Show »
Length:405
Mass (Da):47,163
Checksum:iD7BED5FFF7312782
GO
Isoform 4 (identifier: Q16827-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-811: Missing.
     876-903: Missing.

Show »
Length:377
Mass (Da):43,760
Checksum:i42E10120DBF2D1EF
GO
Isoform 5 (identifier: Q16827-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     594-597: RIAN → VIFP
     598-1216: Missing.

Note: No experimental confirmation available.

Show »
Length:597
Mass (Da):67,672
Checksum:iC0B2674199E893AA
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 811811Missing in isoform 3 and isoform 4.
VSP_043136Add
BLAST
Alternative sequencei594 – 5974RIAN → VIFP in isoform 5.
VSP_054481
Alternative sequencei598 – 1216619Missing in isoform 5.
VSP_054482Add
BLAST
Alternative sequencei876 – 90328Missing in isoform 2 and isoform 4.
VSP_035586Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1591E → G in CAA88425. 1 Publication
Sequence conflicti159 – 1591E → G in AAA82892. 1 Publication
Sequence conflicti196 – 1961S → C in CAA88425. 1 Publication
Sequence conflicti205 – 2051L → V in CAA88425. 1 Publication
Sequence conflicti314 – 3141V → F in CAA88425. 1 Publication
Sequence conflicti441 – 4411V → F in CAA88425. 1 Publication
Sequence conflicti672 – 6721A → T in CAA88425. 1 Publication
Sequence conflicti698 – 6981I → T in CAA88425. 1 Publication
Sequence conflicti705 – 7051A → T in CAA88425. 1 Publication
Sequence conflicti753 – 7531E → K in CAA88425. 1 Publication
Sequence conflicti756 – 7583CQQ → FQH in CAA88425. 1 Publication
Sequence conflicti775 – 7751S → P in CAA88425. 1 Publication
Sequence conflicti790 – 7901N → S in CAA88425. 1 Publication
Sequence conflicti861 – 8633VNF → ANC in CAA88425. 1 Publication
Sequence conflicti876 – 8761W → C in CAA88425. 1 Publication
Sequence conflicti876 – 8761W → C in AAA82892. 1 Publication
Sequence conflicti896 – 8961L → P in CAA88425. 1 Publication
Sequence conflicti896 – 8961L → P in AAA82892. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z48541 mRNA. Translation: CAA88425.1.
U20489 mRNA. Translation: AAA82892.1.
AF187043 mRNA. Translation: AAF04086.1.
AF187044 mRNA. Translation: AAF04087.1.
AK290982 mRNA. Translation: BAF83671.1.
AC007542 Genomic DNA. No translation available.
AC022334 Genomic DNA. No translation available.
AC092183 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96349.1.
CH471094 Genomic DNA. Translation: EAW96350.1.
CH471094 Genomic DNA. Translation: EAW96351.1.
BC035960 mRNA. Translation: AAH35960.1.
BC126201 mRNA. Translation: AAI26202.1.
BC126203 mRNA. Translation: AAI26204.1.
CCDSiCCDS44837.1. [Q16827-3]
CCDS53754.1. [Q16827-4]
CCDS8674.1. [Q16827-2]
CCDS8675.1. [Q16827-1]
PIRiA57064.
S60613.
RefSeqiNP_002839.1. NM_002848.3. [Q16827-2]
NP_109592.1. NM_030667.2. [Q16827-1]
NP_109593.1. NM_030668.2. [Q16827-4]
NP_109594.1. NM_030669.2. [Q16827-3]
NP_109595.1. NM_030670.2. [Q16827-4]
NP_109596.1. NM_030671.2. [Q16827-3]
UniGeneiHs.160871.

Genome annotation databases

EnsembliENST00000281171; ENSP00000281171; ENSG00000151490. [Q16827-1]
ENST00000348962; ENSP00000343434; ENSG00000151490. [Q16827-2]
ENST00000442921; ENSP00000404188; ENSG00000151490. [Q16827-3]
ENST00000445537; ENSP00000393449; ENSG00000151490. [Q16827-3]
ENST00000542557; ENSP00000437571; ENSG00000151490. [Q16827-4]
ENST00000543886; ENSP00000444173; ENSG00000151490.
ENST00000544244; ENSP00000439234; ENSG00000151490. [Q16827-4]
GeneIDi5800.
KEGGihsa:5800.
UCSCiuc001rcv.2. human. [Q16827-1]
uc001rcw.2. human. [Q16827-2]
uc001rcx.2. human. [Q16827-3]
uc001rcz.2. human. [Q16827-4]

Polymorphism databases

DMDMi209572663.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z48541 mRNA. Translation: CAA88425.1 .
U20489 mRNA. Translation: AAA82892.1 .
AF187043 mRNA. Translation: AAF04086.1 .
AF187044 mRNA. Translation: AAF04087.1 .
AK290982 mRNA. Translation: BAF83671.1 .
AC007542 Genomic DNA. No translation available.
AC022334 Genomic DNA. No translation available.
AC092183 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96349.1 .
CH471094 Genomic DNA. Translation: EAW96350.1 .
CH471094 Genomic DNA. Translation: EAW96351.1 .
BC035960 mRNA. Translation: AAH35960.1 .
BC126201 mRNA. Translation: AAI26202.1 .
BC126203 mRNA. Translation: AAI26204.1 .
CCDSi CCDS44837.1. [Q16827-3 ]
CCDS53754.1. [Q16827-4 ]
CCDS8674.1. [Q16827-2 ]
CCDS8675.1. [Q16827-1 ]
PIRi A57064.
S60613.
RefSeqi NP_002839.1. NM_002848.3. [Q16827-2 ]
NP_109592.1. NM_030667.2. [Q16827-1 ]
NP_109593.1. NM_030668.2. [Q16827-4 ]
NP_109594.1. NM_030669.2. [Q16827-3 ]
NP_109595.1. NM_030670.2. [Q16827-4 ]
NP_109596.1. NM_030671.2. [Q16827-3 ]
UniGenei Hs.160871.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2G59 X-ray 2.19 A/B 914-1200 [» ]
2GJT X-ray 2.15 A/B 916-1208 [» ]
ProteinModelPortali Q16827.
SMRi Q16827. Positions 916-1208.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111764. 7 interactions.
IntActi Q16827. 25 interactions.
MINTi MINT-1415956.
STRINGi 9606.ENSP00000281171.

PTM databases

PhosphoSitei Q16827.

Polymorphism databases

DMDMi 209572663.

Proteomic databases

MaxQBi Q16827.
PaxDbi Q16827.
PRIDEi Q16827.

Protocols and materials databases

DNASUi 5800.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000281171 ; ENSP00000281171 ; ENSG00000151490 . [Q16827-1 ]
ENST00000348962 ; ENSP00000343434 ; ENSG00000151490 . [Q16827-2 ]
ENST00000442921 ; ENSP00000404188 ; ENSG00000151490 . [Q16827-3 ]
ENST00000445537 ; ENSP00000393449 ; ENSG00000151490 . [Q16827-3 ]
ENST00000542557 ; ENSP00000437571 ; ENSG00000151490 . [Q16827-4 ]
ENST00000543886 ; ENSP00000444173 ; ENSG00000151490 .
ENST00000544244 ; ENSP00000439234 ; ENSG00000151490 . [Q16827-4 ]
GeneIDi 5800.
KEGGi hsa:5800.
UCSCi uc001rcv.2. human. [Q16827-1 ]
uc001rcw.2. human. [Q16827-2 ]
uc001rcx.2. human. [Q16827-3 ]
uc001rcz.2. human. [Q16827-4 ]

Organism-specific databases

CTDi 5800.
GeneCardsi GC12P015375.
HGNCi HGNC:9678. PTPRO.
HPAi HPA034525.
MIMi 600579. gene.
614196. phenotype.
neXtProti NX_Q16827.
Orphaneti 93214. Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial proliferation.
93217. Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial sclerosis.
93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
93216. Familial idiopathic steroid-resistant nephrotic syndrome with minimal changes.
PharmGKBi PA34023.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
HOGENOMi HOG000243992.
HOVERGENi HBG053763.
InParanoidi Q16827.
KOi K18035.
OMAi STMVTEM.
OrthoDBi EOG7PCJFZ.
PhylomeDBi Q16827.
TreeFami TF351926.

Miscellaneous databases

EvolutionaryTracei Q16827.
GeneWikii PTPRO.
GenomeRNAii 5800.
NextBioi 22592.
PROi Q16827.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q16827.
Bgeei Q16827.
CleanExi HS_PTPRO.
Genevestigatori Q16827.

Family and domain databases

Gene3Di 2.60.40.10. 3 hits.
3.90.190.10. 1 hit.
InterProi IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view ]
Pfami PF00041. fn3. 2 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view ]
PRINTSi PR00700. PRTYPHPHTASE.
SMARTi SM00060. FN3. 4 hits.
SM00194. PTPc. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 2 hits.
SSF52799. SSF52799. 1 hit.
PROSITEi PS50853. FN3. 5 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression and chromosomal localization of a novel gene for protein tyrosine phosphatase (PTP-U2) induced by various differentiation-inducing agents."
    Seimiya H., Sawabe T., Inazawa J., Tsuruo T.
    Oncogene 10:1731-1738(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  2. "Molecular cloning of cDNAs encoding human GLEPP1, a membrane protein tyrosine phosphatase: characterization of the GLEPP1 protein distribution in human kidney and assignment of the GLEPP1 gene to human chromosome 12p12-p13."
    Wiggins R.C., Wiggins J.E., Goyal M., Wharram B.L., Thomas P.E.
    Genomics 27:174-181(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Kidney.
  3. "PTPROt: an alternatively spliced and developmentally regulated B-lymphoid phosphatase that promotes G0/G1 arrest."
    Aguiar R.C., Yakushijin Y., Kharbanda S., Tiwari S., Freeman G.J., Shipp M.A.
    Blood 94:2403-2413(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY.
  4. "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] (ISOFORM 4).
  5. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 5).
    Tissue: Brain and Kidney.
  8. Cited for: INVOLVEMENT IN NPHS6.
  9. "Large-scale structural analysis of the classical human protein tyrosine phosphatome."
    Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P., Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.
    Cell 136:352-363(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 916-1208, FUNCTION.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 914-1200.

Entry informationi

Entry nameiPTPRO_HUMAN
AccessioniPrimary (citable) accession number: Q16827
Secondary accession number(s): A0AV39
, Q13101, Q8IYG3, Q9UBF0, Q9UBT5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: October 14, 2008
Last modified: July 9, 2014
This is version 137 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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