Q16827 (PTPRO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1216 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 renal disease characterized clinically by proteinuria, 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 component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Hydrolase Protein phosphatase Receptor
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Inferred from sequence or structural similarity. Source: UniProtKB glomerular visceral epithelial cell differentiation Inferred from sequence or structural similarity. 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 receptor 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 slit diaphragm assembly Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	apical 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 growth cone Inferred from sequence or structural similarity. Source: UniProtKB integral to 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
Molecular_function	Wnt-protein binding Inferred from sequence or structural similarity. Source: UniProtKB protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB transmembrane receptor protein tyrosine phosphatase activity Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERBB2	P04626	2	EBI-723739,EBI-641062
TEK	Q02763	2	EBI-723739,EBI-2257090

Alternative products

This entry describes 4 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Potential

Chain

30 – 1216

1187

Receptor-type tyrosine-protein phosphatase O

PRO_0000025458

Regions

Topological domain

30 – 822

793

Extracellular Potential

Transmembrane

823 – 843

21

Helical; Potential

Topological domain

844 – 1216

373

Cytoplasmic Potential

Domain

50 – 124

75

Fibronectin type-III 1

Domain

142 – 211

70

Fibronectin type-III 2

Domain

246 – 306

61

Fibronectin type-III 3

Domain

327 – 399

73

Fibronectin type-III 4

Domain

434 – 508

75

Fibronectin type-III 5

Domain

528 – 608

81

Fibronectin type-III 6

Domain

630 – 703

74

Fibronectin type-III 7

Domain

723 – 793

71

Fibronectin type-III 8

Domain

938 – 1195

258

Tyrosine-protein phosphatase

Region

1136 – 1142

7

Substrate binding By similarity

Sites

Active site

1136

1

Phosphocysteine intermediate By similarity

Binding site

1102

1

Substrate By similarity

Binding site

1180

1

Substrate By similarity

Amino acid modifications

Glycosylation

26

1

N-linked (GlcNAc...) Potential

Glycosylation

75

1

N-linked (GlcNAc...) Potential

Glycosylation

154

1

N-linked (GlcNAc...) Potential

Glycosylation

189

1

N-linked (GlcNAc...) Potential

Glycosylation

201

1

N-linked (GlcNAc...) Potential

Glycosylation

227

1

N-linked (GlcNAc...) Potential

Glycosylation

278

1

N-linked (GlcNAc...) Potential

Glycosylation

287

1

N-linked (GlcNAc...) Potential

Glycosylation

323

1

N-linked (GlcNAc...) Potential

Glycosylation

324

1

N-linked (GlcNAc...) Potential

Glycosylation

370

1

N-linked (GlcNAc...) Potential

Glycosylation

461

1

N-linked (GlcNAc...) Potential

Glycosylation

490

1

N-linked (GlcNAc...) Potential

Glycosylation

700

1

N-linked (GlcNAc...) Potential

Glycosylation

712

1

N-linked (GlcNAc...) Potential

Glycosylation

733

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

1 – 811

811

Missing in isoform 3 and isoform 4.

VSP_043136

Alternative sequence

876 – 903

28

Missing in isoform 2 and isoform 4.

VSP_035586

Experimental info

Sequence conflict

159

1

E → G in CAA88425. Ref.1

Sequence conflict

159

1

E → G in AAA82892. Ref.2

Sequence conflict

196

1

S → C in CAA88425. Ref.1

Sequence conflict

205

1

L → V in CAA88425. Ref.1

Sequence conflict

314

1

V → F in CAA88425. Ref.1

Sequence conflict

441

1

V → F in CAA88425. Ref.1

Sequence conflict

672

1

A → T in CAA88425. Ref.1

Sequence conflict

698

1

I → T in CAA88425. Ref.1

Sequence conflict

705

1

A → T in CAA88425. Ref.1

Sequence conflict

753

1

E → K in CAA88425. Ref.1

Sequence conflict

756 – 758

3

CQQ → FQH in CAA88425. Ref.1

Sequence conflict

775

1

S → P in CAA88425. Ref.1

Sequence conflict

790

1

N → S in CAA88425. Ref.1

Sequence conflict

861 – 863

3

VNF → ANC in CAA88425. Ref.1

Sequence conflict

876

1

W → C in CAA88425. Ref.1

Sequence conflict

876

1

W → C in AAA82892. Ref.2

Sequence conflict

896

1

L → P in CAA88425. Ref.1

Sequence conflict

896

1

L → P in AAA82892. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1216

Helix Strand Turn

Details...

Helix

920 – 922

3

Helix

923 – 946

24

Turn

947 – 951

5

Helix

956 – 958

3

Helix

960 – 965

6

Turn

975 – 977

3

Beta strand

978 – 980

3

Turn

988 – 991

4

Beta strand

992 – 998

7

Beta strand

1007 – 1010

4

Helix

1015 – 1017

3

Helix

1018 – 1027

10

Beta strand

1032 – 1035

4

Beta strand

1039 – 1041

3

Beta strand

1053 – 1056

4

Beta strand

1058 – 1060

3

Beta strand

1063 – 1072

10

Beta strand

1074 – 1085

12

Beta strand

1088 – 1097

10

Beta strand

1103 – 1105

3

Helix

1108 – 1127

20

Beta strand

1132 – 1140

9

Helix

1141 – 1158

18

Beta strand

1160 – 1162

3

Helix

1164 – 1172

9

Helix

1182 – 1202

21

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 14, 2008. Version 2. Checksum: C902B48D1A73BFE1	FASTA	1,216	138,344
	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
	Isoform 2 [UniParc]. Checksum: C27FCA3BDFA0D1EF	FASTA	1,188	134,941
	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 KLPYNWSKNG LKKRKLTNPV QLDDFDAYIK 910 920 930 940 950 960 DMAKDSDYKF SLQFEELKLI GLDIPHFAAD LPLNRCKNRY TNILPYDFSR VRLVSMNEEE 970 980 990 1000 1010 1020 GADYINANYI PGYNSPQEYI ATQGPLPETR NDFWKMVLQQ KSQIIVMLTQ CNEKRRVKCD 1030 1040 1050 1060 1070 1080 HYWPFTEEPI AYGDITVEMI SEEEQDDWAC RHFRINYADE MQDVMHFNYT AWPDHGVPTA 1090 1100 1110 1120 1130 1140 NAAESILQFV HMVRQQATKS KGPMIIHCSA GVGRTGTFIA LDRLLQHIRD HEFVDILGLV 1150 1160 1170 1180 SEMRSYRMSM VQTEEQYIFI HQCVQLMWMK KKQQFCISDV IYENVSKS
	Isoform 3 (PTPROt) [UniParc]. Checksum: D7BED5FFF7312782	FASTA	405	47,163
	10 20 30 40 50 60 MVTEMNPNVV VISVLAILST LLIGLLLVTL IILRKKHLQM ARECGAGTFV NFASLERDGK 70 80 90 100 110 120 LPYNWRRSIF AFLTLLPSCL WTDYLLAFYI NPWSKNGLKK RKLTNPVQLD DFDAYIKDMA 130 140 150 160 170 180 KDSDYKFSLQ FEELKLIGLD IPHFAADLPL NRCKNRYTNI LPYDFSRVRL VSMNEEEGAD 190 200 210 220 230 240 YINANYIPGY NSPQEYIATQ GPLPETRNDF WKMVLQQKSQ IIVMLTQCNE KRRVKCDHYW 250 260 270 280 290 300 PFTEEPIAYG DITVEMISEE EQDDWACRHF RINYADEMQD VMHFNYTAWP DHGVPTANAA 310 320 330 340 350 360 ESILQFVHMV RQQATKSKGP MIIHCSAGVG RTGTFIALDR LLQHIRDHEF VDILGLVSEM 370 380 390 400 RSYRMSMVQT EEQYIFIHQC VQLMWMKKKQ QFCISDVIYE NVSKS
	Isoform 4 [UniParc]. Checksum: 42E10120DBF2D1EF	FASTA	377	43,760
	10 20 30 40 50 60 MVTEMNPNVV VISVLAILST LLIGLLLVTL IILRKKHLQM ARECGAGTFV NFASLERDGK 70 80 90 100 110 120 LPYNWSKNGL KKRKLTNPVQ LDDFDAYIKD MAKDSDYKFS LQFEELKLIG LDIPHFAADL 130 140 150 160 170 180 PLNRCKNRYT NILPYDFSRV RLVSMNEEEG ADYINANYIP GYNSPQEYIA TQGPLPETRN 190 200 210 220 230 240 DFWKMVLQQK SQIIVMLTQC NEKRRVKCDH YWPFTEEPIA YGDITVEMIS EEEQDDWACR 250 260 270 280 290 300 HFRINYADEM QDVMHFNYTA WPDHGVPTAN AAESILQFVH MVRQQATKSK GPMIIHCSAG 310 320 330 340 350 360 VGRTGTFIAL DRLLQHIRDH EFVDILGLVS EMRSYRMSMV QTEEQYIFIH QCVQLMWMKK 370 KQQFCISDVI YENVSKS

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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] (ISOFORM 1). Tissue: Brain.
[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. , 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.
BC126201 mRNA. Translation: AAI26202.1.
BC126203 mRNA. Translation: AAI26204.1.

IPI

IPI00001767.
IPI00001769.
IPI00884189.

PIR

A57064.
S60613.

RefSeq

NP_002839.1. NM_002848.3.
NP_109592.1. NM_030667.2.
NP_109593.1. NM_030668.2.
NP_109594.1. NM_030669.2.
NP_109595.1. NM_030670.2.
NP_109596.1. NM_030671.2.

UniGene

Hs.160871.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q16827.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q16827. 20 interactions.

MINT

MINT-1349488.

STRING

9606.ENSP00000281171.

PTM databases

PhosphoSite

Q16827.

Polymorphism databases

DMDM

209572663.

Proteomic databases

PaxDb

Q16827.

PRIDE

Q16827.

Protocols and materials databases

DNASU

5800.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000281171; ENSP00000281171; ENSG00000151490.
ENST00000348962; ENSP00000343434; ENSG00000151490.
ENST00000442921; ENSP00000404188; ENSG00000151490.
ENST00000445537; ENSP00000393449; ENSG00000151490.
ENST00000542557; ENSP00000437571; ENSG00000151490.
ENST00000544244; ENSP00000439234; ENSG00000151490.

GeneID

5800.

KEGG

hsa:5800.

UCSC

uc001rcv.2. human.
uc001rcw.2. human.

Organism-specific databases

CTD

5800.

GeneCards

GC12P015375.

HGNC

HGNC:9678. PTPRO.

HPA

HPA034525.

MIM

600579. gene.
614196. phenotype.

neXtProt

NX_Q16827.

Orphanet

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.

PharmGKB

PA34023.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5599.

HOGENOM

HOG000243992.

HOVERGEN

HBG053763.

InParanoid

Q16827.

KO

K01104.

OMA

FFEVFCQ.

PhylomeDB

Q16827.

Enzyme and pathway databases

Pathway_Interaction_DB

kitpathway. Signaling events mediated by Stem cell factor receptor (c-Kit).

Gene expression databases

ArrayExpress

Q16827.

Bgee

Q16827.

CleanEx

HS_PTPRO.

Genevestigator

Q16827.

GermOnline

ENSG00000151490. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 3 hits.

InterPro

IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]

Pfam

PF00041. fn3. 2 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]

PRINTS

PR00700. PRTYPHPHTASE.

SMART

SM00060. FN3. 4 hits.
SM00194. PTPc. 1 hit.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 3 hits.

PROSITE

PS50853. FN3. 6 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q16827.

GenomeRNAi

5800.

NextBio

22592.

SOURCE

Search...

Entry information

Entry name

PTPRO_HUMAN

Accession

Primary (citable) accession number: Q16827
Secondary accession number(s): A0AV39 , Q13101, Q9UBF0, Q9UBT5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2003
Last sequence update:	October 14, 2008
Last modified:	May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.