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Q16827 (PTPRO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Receptor-type tyrosine-protein phosphatase O

Short name=R-PTP-O
EC=3.1.3.48
Alternative name(s):
Glomerular epithelial protein 1
Protein tyrosine phosphatase U2
Short name=PTP-U2
Short name=PTPase U2
Gene names
Name:PTPRO
Synonyms:GLEPP1, PTPU2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1216 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Glomerulus of kidney. Also detected in brain, lung and placenta. Ref.3

Induction

By various differentiation-inducing agents.

Involvement in disease

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. Ref.8

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 3 subfamily.

Contains 8 fibronectin type-III domains.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protein phosphatase
Receptor
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Inferred from sequence or structural similarity. Source: UniProtKB

cell morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

glomerular visceral epithelial cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

glomerulus development

Inferred from mutant phenotype Ref.8. Source: UniProtKB

lamellipodium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

monocyte chemotaxis

Inferred from mutant phenotype PubMed 19233845. Source: UniProtKB

negative regulation of canonical Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell-substrate adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of glomerular filtration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of retinal ganglion cell axon guidance

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-tyrosine dephosphorylation

Inferred from mutant phenotype PubMed 19233845. Source: UniProtKB

protein dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of glomerular filtration

Inferred from sequence or structural similarity. Source: UniProtKB

slit diaphragm assembly

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentapical plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

axon

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic spine

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

growth cone

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Traceable author statement Ref.3. Source: UniProtKB

integral component of plasma membrane

Non-traceable author statement Ref.2. Source: UniProtKB

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

lateral plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionWnt-protein binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.9. Source: IntAct

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from direct assay Ref.9. Source: UniProtKB

transmembrane receptor protein tyrosine phosphatase activity

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16827-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q16827-2)

The sequence of this isoform differs from the canonical sequence as follows:
     876-903: Missing.
Isoform 3 (identifier: Q16827-3)

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.
Isoform 4 (identifier: Q16827-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-811: Missing.
     876-903: Missing.
Isoform 5 (identifier: Q16827-5)

The sequence of this isoform differs from the canonical sequence as follows:
     594-597: RIAN → VIFP
     598-1216: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 12161187Receptor-type tyrosine-protein phosphatase O
PRO_0000025458

Regions

Topological domain30 – 822793Extracellular Potential
Transmembrane823 – 84321Helical; Potential
Topological domain844 – 1216373Cytoplasmic Potential
Domain50 – 12475Fibronectin type-III 1
Domain142 – 21170Fibronectin type-III 2
Domain246 – 30661Fibronectin type-III 3
Domain329 – 42597Fibronectin type-III 4
Domain435 – 53197Fibronectin type-III 5
Domain532 – 62897Fibronectin type-III 6
Domain631 – 72494Fibronectin type-III 7
Domain725 – 81793Fibronectin type-III 8
Domain938 – 1195258Tyrosine-protein phosphatase
Region1136 – 11427Substrate binding By similarity

Sites

Active site11361Phosphocysteine intermediate By similarity
Binding site11021Substrate By similarity
Binding site11801Substrate By similarity

Amino acid modifications

Modified residue8651Phosphoserine By similarity
Glycosylation261N-linked (GlcNAc...) Potential
Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation1541N-linked (GlcNAc...) Potential
Glycosylation1891N-linked (GlcNAc...) Potential
Glycosylation2011N-linked (GlcNAc...) Potential
Glycosylation2271N-linked (GlcNAc...) Potential
Glycosylation2781N-linked (GlcNAc...) Potential
Glycosylation2871N-linked (GlcNAc...) Potential
Glycosylation3231N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Glycosylation3701N-linked (GlcNAc...) Potential
Glycosylation4611N-linked (GlcNAc...) Potential
Glycosylation4901N-linked (GlcNAc...) Potential
Glycosylation7001N-linked (GlcNAc...) Potential
Glycosylation7121N-linked (GlcNAc...) Potential
Glycosylation7331N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 811811Missing in isoform 3 and isoform 4.
VSP_043136
Alternative sequence594 – 5974RIAN → VIFP in isoform 5.
VSP_054481
Alternative sequence598 – 1216619Missing in isoform 5.
VSP_054482
Alternative sequence876 – 90328Missing in isoform 2 and isoform 4.
VSP_035586

Experimental info

Sequence conflict1591E → G in CAA88425. Ref.1
Sequence conflict1591E → G in AAA82892. Ref.2
Sequence conflict1961S → C in CAA88425. Ref.1
Sequence conflict2051L → V in CAA88425. Ref.1
Sequence conflict3141V → F in CAA88425. Ref.1
Sequence conflict4411V → F in CAA88425. Ref.1
Sequence conflict6721A → T in CAA88425. Ref.1
Sequence conflict6981I → T in CAA88425. Ref.1
Sequence conflict7051A → T in CAA88425. Ref.1
Sequence conflict7531E → K in CAA88425. Ref.1
Sequence conflict756 – 7583CQQ → FQH in CAA88425. Ref.1
Sequence conflict7751S → P in CAA88425. Ref.1
Sequence conflict7901N → S in CAA88425. Ref.1
Sequence conflict861 – 8633VNF → ANC in CAA88425. Ref.1
Sequence conflict8761W → C in CAA88425. Ref.1
Sequence conflict8761W → C in AAA82892. Ref.2
Sequence conflict8961L → P in CAA88425. Ref.1
Sequence conflict8961L → P in AAA82892. Ref.2

Secondary structure

............................................... 1216
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 14, 2008. Version 2.
Checksum: C902B48D1A73BFE1

FASTA1,216138,344
        10         20         30         40         50         60 
MGHLPTGIHG ARRLLPLLWL FVLFKNATAF HVTVQDDNNI VVSLEASDVI SPASVYVVKI 

        70         80         90        100        110        120 
TGESKNYFFE FEEFNSTLPP PVIFKASYHG LYYIITLVVV NGNVVTKPSR SITVLTKPLP 

       130        140        150        160        170        180 
VTSVSIYDYK PSPETGVLFE IHYPEKYNVF TRVNISYWEG KDFRTMLYKD FFKGKTVFNH 

       190        200        210        220        230        240 
WLPGMCYSNI TFQLVSEATF NKSTLVEYSG VSHEPKQHRT APYPPQNISV RIVNLNKNNW 

       250        260        270        280        290        300 
EEQSGNFPEE SFMRSQDTIG KEKLFHFTEE TPEIPSGNIS SGWPDFNSSD YETTSQPYWW 

       310        320        330        340        350        360 
DSASAAPESE DEFVSVLPME YENNSTLSET EKSTSGSFSF FPVQMILTWL PPKPPTAFDG 

       370        380        390        400        410        420 
FHIHIEREEN FTEYLMVDEE AHEFVAELKE PGKYKLSVTT FSSSGSCETR KSQSAKSLSF 

       430        440        450        460        470        480 
YISPSGEWIE ELTEKPQHVS VHVLSSTTAL MSWTSSQENY NSTIVSVVSL TCQKQKESQR 

       490        500        510        520        530        540 
LEKQYCTQVN SSKPIIENLV PGAQYQVVIY LRKGPLIGPP SDPVTFAIVP TGIKDLMLYP 

       550        560        570        580        590        600 
LGPTAVVLSW TRPYLGVFRK YVVEMFYFNP ATMTSEWTTY YEIAATVSLT ASVRIANLLP 

       610        620        630        640        650        660 
AWYYNFRVTM VTWGDPELSC CDSSTISFIT APVAPEITSV EYFNSLLYIS WTYGDDTTDL 

       670        680        690        700        710        720 
SHSRMLHWMV VAEGKKKIKK SVTRNVMTAI LSLPPGDIYN LSVTACTERG SNTSMLRLVK 

       730        740        750        760        770        780 
LEPAPPKSLF AVNKTQTSVT LLWVEEGVAD FFEVFCQQVG SSQKTKLQEP VAVSSHVVTI 

       790        800        810        820        830        840 
SSLLPATAYN CSVTSFSHDS PSVPTFIAVS TMVTEMNPNV VVISVLAILS TLLIGLLLVT 

       850        860        870        880        890        900 
LIILRKKHLQ MARECGAGTF VNFASLERDG KLPYNWRRSI FAFLTLLPSC LWTDYLLAFY 

       910        920        930        940        950        960 
INPWSKNGLK KRKLTNPVQL DDFDAYIKDM AKDSDYKFSL QFEELKLIGL DIPHFAADLP 

       970        980        990       1000       1010       1020 
LNRCKNRYTN ILPYDFSRVR LVSMNEEEGA DYINANYIPG YNSPQEYIAT QGPLPETRND 

      1030       1040       1050       1060       1070       1080 
FWKMVLQQKS QIIVMLTQCN EKRRVKCDHY WPFTEEPIAY GDITVEMISE EEQDDWACRH 

      1090       1100       1110       1120       1130       1140 
FRINYADEMQ DVMHFNYTAW PDHGVPTANA AESILQFVHM VRQQATKSKG PMIIHCSAGV 

      1150       1160       1170       1180       1190       1200 
GRTGTFIALD RLLQHIRDHE FVDILGLVSE MRSYRMSMVQ TEEQYIFIHQ CVQLMWMKKK 

      1210 
QQFCISDVIY ENVSKS 

« Hide

Isoform 2 [UniParc].

Checksum: C27FCA3BDFA0D1EF
Show »

FASTA1,188134,941
Isoform 3 (PTPROt) [UniParc].

Checksum: D7BED5FFF7312782
Show »

FASTA40547,163
Isoform 4 [UniParc].

Checksum: 42E10120DBF2D1EF
Show »

FASTA37743,760
Isoform 5 [UniParc].

Checksum: C0B2674199E893AA
Show »

FASTA59767,672

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Disruption of PTPRO causes childhood-onset nephrotic syndrome."
Ozaltin F., Ibsirlioglu T., Taskiran E.Z., Baydar D.E., Kaymaz F., Buyukcelik M., Kilic B.D., Balat A., Iatropoulos P., Asan E., Akarsu N.A., Schaefer F., Yilmaz E., Bakkaloglu A.
Am. J. Hum. Genet. 89:139-147(2011) [PubMed] [Europe PMC] [Abstract]
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]"Structural genomics of protein phosphatases."
Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P., Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S., Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y., Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R. expand/collapse author list , Sali A., Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K.
J. Struct. Funct. Genomics 8:121-140(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 914-1200.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS44837.1. [Q16827-3]
CCDS53754.1. [Q16827-4]
CCDS8674.1. [Q16827-2]
CCDS8675.1. [Q16827-1]
PIRA57064.
S60613.
RefSeqNP_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]
UniGeneHs.160871.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2G59X-ray2.19A/B914-1200[»]
2GJTX-ray2.15A/B916-1208[»]
ProteinModelPortalQ16827.
SMRQ16827. Positions 916-1208.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111764. 7 interactions.
IntActQ16827. 25 interactions.
MINTMINT-1415956.
STRING9606.ENSP00000281171.

PTM databases

PhosphoSiteQ16827.

Polymorphism databases

DMDM209572663.

Proteomic databases

MaxQBQ16827.
PaxDbQ16827.
PRIDEQ16827.

Protocols and materials databases

DNASU5800.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000281171; 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]
GeneID5800.
KEGGhsa:5800.
UCSCuc001rcv.2. human. [Q16827-1]
uc001rcw.2. human. [Q16827-2]
uc001rcx.2. human. [Q16827-3]
uc001rcz.2. human. [Q16827-4]

Organism-specific databases

CTD5800.
GeneCardsGC12P015375.
HGNCHGNC:9678. PTPRO.
HPAHPA034525.
MIM600579. gene.
614196. phenotype.
neXtProtNX_Q16827.
Orphanet93214. 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.
PharmGKBPA34023.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000243992.
HOVERGENHBG053763.
InParanoidQ16827.
KOK18035.
OMASTMVTEM.
OrthoDBEOG7PCJFZ.
PhylomeDBQ16827.
TreeFamTF351926.

Gene expression databases

ArrayExpressQ16827.
BgeeQ16827.
CleanExHS_PTPRO.
GenevestigatorQ16827.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
3.90.190.10. 1 hit.
InterProIPR003961. 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]
PfamPF00041. fn3. 2 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 4 hits.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
SSF52799. SSF52799. 1 hit.
PROSITEPS50853. FN3. 5 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ16827.
GeneWikiPTPRO.
GenomeRNAi5800.
NextBio22592.
PROQ16827.
SOURCESearch...

Entry information

Entry namePTPRO_HUMAN
AccessionPrimary (citable) accession number: Q16827
Secondary accession number(s): A0AV39 expand/collapse secondary AC list , Q13101, Q8IYG3, Q9UBF0, Q9UBT5
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM