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Q16827

- PTPRO_HUMAN

UniProt

Q16827 - PTPRO_HUMAN

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Protein

Receptor-type tyrosine-protein phosphatase O

Gene

PTPRO

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).By similarity

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1102 – 11021SubstrateBy similarity
Active sitei1136 – 11361Phosphocysteine intermediatePROSITE-ProRule annotation
Binding sitei1180 – 11801SubstrateBy similarity

GO - Molecular functioni

  1. phosphatase activity Source: UniProtKB
  2. protein homodimerization activity Source: UniProtKB
  3. protein tyrosine phosphatase activity Source: UniProtKB
  4. transmembrane receptor protein tyrosine phosphatase activity Source: UniProtKB
  5. Wnt-protein binding 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 – 822793ExtracellularSequence AnalysisAdd
BLAST
Transmembranei823 – 84321HelicalSequence AnalysisAdd
BLAST
Topological domaini844 – 1216373CytoplasmicSequence AnalysisAdd
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

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 – 2929Sequence AnalysisAdd
BLAST
Chaini30 – 12161187Receptor-type tyrosine-protein phosphatase OPRO_0000025458Add
BLAST

Amino acid modifications

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

BgeeiQ16827.
CleanExiHS_PTPRO.
ExpressionAtlasiQ16827. baseline and differential.
GenevestigatoriQ16827.

Organism-specific databases

HPAiHPA034525.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi111764. 11 interactions.
IntActiQ16827. 25 interactions.
MINTiMINT-1415956.
STRINGi9606.ENSP00000281171.

Structurei

Secondary structure

1
1216
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi920 – 9223Combined sources
Helixi923 – 94624Combined sources
Turni947 – 9515Combined sources
Helixi956 – 9583Combined sources
Helixi960 – 9656Combined sources
Turni975 – 9773Combined sources
Beta strandi978 – 9803Combined sources
Turni988 – 9914Combined sources
Beta strandi992 – 9987Combined sources
Beta strandi1007 – 10104Combined sources
Helixi1015 – 10173Combined sources
Helixi1018 – 102710Combined sources
Beta strandi1032 – 10354Combined sources
Beta strandi1039 – 10413Combined sources
Beta strandi1053 – 10564Combined sources
Beta strandi1058 – 10603Combined sources
Beta strandi1063 – 107210Combined sources
Beta strandi1074 – 108512Combined sources
Beta strandi1088 – 109710Combined sources
Beta strandi1103 – 11053Combined sources
Helixi1108 – 112720Combined sources
Beta strandi1132 – 11409Combined sources
Helixi1141 – 115818Combined sources
Beta strandi1160 – 11623Combined sources
Helixi1164 – 11729Combined sources
Helixi1182 – 120221Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ16827.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Contains 8 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00770000120452.
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

        10         20         30         40         50
MGHLPTGIHG ARRLLPLLWL FVLFKNATAF HVTVQDDNNI VVSLEASDVI
60 70 80 90 100
SPASVYVVKI TGESKNYFFE FEEFNSTLPP PVIFKASYHG LYYIITLVVV
110 120 130 140 150
NGNVVTKPSR SITVLTKPLP VTSVSIYDYK PSPETGVLFE IHYPEKYNVF
160 170 180 190 200
TRVNISYWEG KDFRTMLYKD FFKGKTVFNH WLPGMCYSNI TFQLVSEATF
210 220 230 240 250
NKSTLVEYSG VSHEPKQHRT APYPPQNISV RIVNLNKNNW EEQSGNFPEE
260 270 280 290 300
SFMRSQDTIG KEKLFHFTEE TPEIPSGNIS SGWPDFNSSD YETTSQPYWW
310 320 330 340 350
DSASAAPESE DEFVSVLPME YENNSTLSET EKSTSGSFSF FPVQMILTWL
360 370 380 390 400
PPKPPTAFDG FHIHIEREEN FTEYLMVDEE AHEFVAELKE PGKYKLSVTT
410 420 430 440 450
FSSSGSCETR KSQSAKSLSF YISPSGEWIE ELTEKPQHVS VHVLSSTTAL
460 470 480 490 500
MSWTSSQENY NSTIVSVVSL TCQKQKESQR LEKQYCTQVN SSKPIIENLV
510 520 530 540 550
PGAQYQVVIY LRKGPLIGPP SDPVTFAIVP TGIKDLMLYP LGPTAVVLSW
560 570 580 590 600
TRPYLGVFRK YVVEMFYFNP ATMTSEWTTY YEIAATVSLT ASVRIANLLP
610 620 630 640 650
AWYYNFRVTM VTWGDPELSC CDSSTISFIT APVAPEITSV EYFNSLLYIS
660 670 680 690 700
WTYGDDTTDL SHSRMLHWMV VAEGKKKIKK SVTRNVMTAI LSLPPGDIYN
710 720 730 740 750
LSVTACTERG SNTSMLRLVK LEPAPPKSLF AVNKTQTSVT LLWVEEGVAD
760 770 780 790 800
FFEVFCQQVG SSQKTKLQEP VAVSSHVVTI SSLLPATAYN CSVTSFSHDS
810 820 830 840 850
PSVPTFIAVS TMVTEMNPNV VVISVLAILS TLLIGLLLVT LIILRKKHLQ
860 870 880 890 900
MARECGAGTF VNFASLERDG KLPYNWRRSI FAFLTLLPSC LWTDYLLAFY
910 920 930 940 950
INPWSKNGLK KRKLTNPVQL DDFDAYIKDM AKDSDYKFSL QFEELKLIGL
960 970 980 990 1000
DIPHFAADLP LNRCKNRYTN ILPYDFSRVR LVSMNEEEGA DYINANYIPG
1010 1020 1030 1040 1050
YNSPQEYIAT QGPLPETRND FWKMVLQQKS QIIVMLTQCN EKRRVKCDHY
1060 1070 1080 1090 1100
WPFTEEPIAY GDITVEMISE EEQDDWACRH FRINYADEMQ DVMHFNYTAW
1110 1120 1130 1140 1150
PDHGVPTANA AESILQFVHM VRQQATKSKG PMIIHCSAGV GRTGTFIALD
1160 1170 1180 1190 1200
RLLQHIRDHE FVDILGLVSE MRSYRMSMVQ TEEQYIFIHQ CVQLMWMKKK
1210
QQFCISDVIY ENVSKS
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1591E → G in CAA88425. (PubMed:7753550)Curated
Sequence conflicti159 – 1591E → G in AAA82892. (PubMed:7665166)Curated
Sequence conflicti196 – 1961S → C in CAA88425. (PubMed:7753550)Curated
Sequence conflicti205 – 2051L → V in CAA88425. (PubMed:7753550)Curated
Sequence conflicti314 – 3141V → F in CAA88425. (PubMed:7753550)Curated
Sequence conflicti441 – 4411V → F in CAA88425. (PubMed:7753550)Curated
Sequence conflicti672 – 6721A → T in CAA88425. (PubMed:7753550)Curated
Sequence conflicti698 – 6981I → T in CAA88425. (PubMed:7753550)Curated
Sequence conflicti705 – 7051A → T in CAA88425. (PubMed:7753550)Curated
Sequence conflicti753 – 7531E → K in CAA88425. (PubMed:7753550)Curated
Sequence conflicti756 – 7583CQQ → FQH in CAA88425. (PubMed:7753550)Curated
Sequence conflicti775 – 7751S → P in CAA88425. (PubMed:7753550)Curated
Sequence conflicti790 – 7901N → S in CAA88425. (PubMed:7753550)Curated
Sequence conflicti861 – 8633VNF → ANC in CAA88425. (PubMed:7753550)Curated
Sequence conflicti876 – 8761W → C in CAA88425. (PubMed:7753550)Curated
Sequence conflicti876 – 8761W → C in AAA82892. (PubMed:7665166)Curated
Sequence conflicti896 – 8961L → P in CAA88425. (PubMed:7753550)Curated
Sequence conflicti896 – 8961L → P in AAA82892. (PubMed:7665166)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 811811Missing in isoform 3 and isoform 4. 2 PublicationsVSP_043136Add
BLAST
Alternative sequencei594 – 5974RIAN → VIFP in isoform 5. 1 PublicationVSP_054481
Alternative sequencei598 – 1216619Missing in isoform 5. 1 PublicationVSP_054482Add
BLAST
Alternative sequencei876 – 90328Missing in isoform 2 and isoform 4. 3 PublicationsVSP_035586Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [Q16827-5]
ENST00000544244; ENSP00000439234; ENSG00000151490. [Q16827-4]
GeneIDi5800.
KEGGihsa:5800.
UCSCiuc001rcu.2. human.
uc001rcv.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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 11 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 . [Q16827-5 ]
ENST00000544244 ; ENSP00000439234 ; ENSG00000151490 . [Q16827-4 ]
GeneIDi 5800.
KEGGi hsa:5800.
UCSCi uc001rcu.2. human.
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 GC12P015476.
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.
GeneTreei ENSGT00770000120452.
HOGENOMi HOG000243992.
HOVERGENi HBG053763.
InParanoidi Q16827.
KOi K18035.
OMAi STMVTEM.
OrthoDBi EOG7PCJFZ.
PhylomeDBi Q16827.
TreeFami TF351926.

Miscellaneous databases

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

Gene expression databases

Bgeei Q16827.
CleanExi HS_PTPRO.
ExpressionAtlasi Q16827. baseline and differential.
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: November 26, 2014
This is version 140 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