Q92729 (PTPRU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Receptor-type tyrosine-protein phosphatase U
Short name=R-PTP-U
EC=3.1.3.48

Alternative name(s):
Pancreatic carcinoma phosphatase 2
Short name=PCP-2
Protein-tyrosine phosphatase J
Short name=PTP-J
Short name=hPTP-J
Protein-tyrosine phosphatase pi
Short name=PTP pi
Protein-tyrosine phosphatase receptor omicron
Short name=PTP-RO
Receptor-type protein-tyrosine phosphatase psi
Short name=R-PTP-psi

Gene names

Name:	PTPRU
Synonyms:	FMI, PCP2, PTPRO

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	1446 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	Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis. Ref.11 Ref.12 Ref.13
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.2
Subunit structure	Forms homooligomeric complexes which mediate cell homotypic adhesion Probable. Interacts (via the cytoplasmic juxtamembrane domain) with CTNNB1; may mediate interaction with the cadherin/catenin adhesion complex. Interacts with KIT. May interact with AP3B1. Ref.11 Ref.12 Ref.13 Ref.14
Subcellular location	Cell junction. Cell membrane; Single-pass type I membrane protein Ref.2.
Tissue specificity	High levels in brain, pancreas, and skeletal muscle; less in colon, kidney, liver, stomach, and uterus; not expressed in placenta and spleen. Also detected in heart, prostate, lung, thymus, testis and ovary. Ubiquitously expressed in brain. Expressed by hematopoietic stem cells. Ref.1 Ref.2 Ref.3 Ref.4
Developmental stage	Expressed in fetal brain, lung and kidney. Ref.4
Induction	Up-regulated upon cell contact (at protein level). Down-regulated by phorbol ester (at protein level) and calcium ionophore but up-regulated by phorbol ester in megakaryocytic cells (Ref.11). Ref.3 Ref.10 Ref.11 Ref.12
Post-translational modification	The extracellular domain is proteolytically processed through cleavage within the fibronectin type-III 4 domain By similarity. Beside the 190 kDa full-length protein, proteolytic products of 100 kDa, 80 kDa and 73 kDa are observed. N-glycosylated. Ref.2 Phosphorylated on tyrosine residues upon activation of KIT with stem cell factor (SCF). The 73 kDa proteolytic product is not phosphorylated. Ref.11
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Receptor class 2B subfamily. Contains 4 fibronectin type-III domains. Contains 1 Ig-like C2-type (immunoglobulin-like) domain. Contains 1 MAM domain. Contains 2 tyrosine-protein phosphatase domains.
Sequence caution	The sequence CAA65016.1 differs from that shown. Reason: Several sequencing problems. The sequence CAA65832.1 differs from that shown. Reason: Several sequencing problems.

Ontologies

Keywords
Biological process	Cell adhesion Differentiation
Cellular component	Cell junction Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Hydrolase Protein phosphatase Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	canonical Wnt receptor signaling pathway Inferred from direct assay Ref.13. Source: UniProtKB cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW cell-cell adhesion Inferred from direct assay Ref.13. Source: UniProtKB homotypic cell-cell adhesion Inferred from electronic annotation. Source: Compara negative regulation of cell migration Inferred from direct assay Ref.12Ref.13. Source: UniProtKB negative regulation of cell proliferation Inferred from direct assay Ref.13. Source: UniProtKB protein localization to cell surface Inferred from direct assay Ref.13. Source: UniProtKB transmembrane receptor protein tyrosine phosphatase signaling pathway Non-traceable author statement Ref.2. Source: UniProtKB
Cellular_component	cell-cell junction Inferred from direct assay Ref.12. Source: UniProtKB integral to plasma membrane Non-traceable author statement Ref.2. Source: UniProtKB
Molecular_function	transmembrane receptor protein tyrosine phosphatase activity Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92729-1)

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: Q92729-2)

The sequence of this isoform differs from the canonical sequence as follows:
     774-783: Missing.

Isoform 3 (identifier: Q92729-3)

The sequence of this isoform differs from the canonical sequence as follows:
     774-783: Missing.
     993-995: Missing.

Isoform 4 (identifier: Q92729-4)

Also known as: PTPRO;

The sequence of this isoform differs from the canonical sequence as follows:
     774-783: Missing.
     950-950: D → DIRINRE
     1329-1330: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Chain	19 – 1446	1428	Receptor-type tyrosine-protein phosphatase U		PRO_0000371658
Regions
	Topological domain	19 – 749	731	Extracellular Potential
	Transmembrane	750 – 770	21	Helical; Potential
	Topological domain	771 – 1446	676	Cytoplasmic Potential
	Domain	25 – 188	164	MAM
	Domain	190 – 275	86	Ig-like C2-type
	Domain	285 – 377	93	Fibronectin type-III 1
	Domain	383 – 481	99	Fibronectin type-III 2
	Domain	482 – 585	104	Fibronectin type-III 3
	Domain	592 – 674	83	Fibronectin type-III 4
	Domain	888 – 1144	257	Tyrosine-protein phosphatase 1
	Domain	1176 – 1439	264	Tyrosine-protein phosphatase 2
	Region	771 – 887	117	Mediates interaction with CTNNB1 By similarity
	Region	1085 – 1091	7	Substrate binding By similarity
Sites
	Active site	1085	1	Phosphocysteine intermediate By similarity
	Active site	1380	1	Phosphocysteine intermediate By similarity
	Binding site	1053	1	Substrate Potential
	Binding site	1129	1	Substrate By similarity
Amino acid modifications
	Modified residue	848	1	Phosphoserine Ref.15
	Modified residue	853	1	Phosphoserine Ref.15
	Glycosylation	75	1	N-linked (GlcNAc...) Potential
	Glycosylation	410	1	N-linked (GlcNAc...) Potential
	Glycosylation	685	1	N-linked (GlcNAc...) Potential
	Disulfide bond	210 ↔ 264		Potential
Natural variations
	Alternative sequence	774 – 783	10	Missing in isoform 2, isoform 3 and isoform 4.		VSP_037082
	Alternative sequence	950	1	D → DIRINRE in isoform 4.		VSP_037083
	Alternative sequence	993 – 995	3	Missing in isoform 3.		VSP_037084
	Alternative sequence	1329 – 1330	2	Missing in isoform 4.		VSP_037085
	Natural variant	60	1	T → N. Corresponds to variant rs35332573 [ dbSNP | Ensembl ].		VAR_055075
	Natural variant	471	1	R → L. Corresponds to variant rs35745442 [ dbSNP | Ensembl ].		VAR_055076
	Natural variant	830	1	H → Y in a colorectal cancer sample; somatic mutation. Ref.16		VAR_035650
	Natural variant	835	1	R → W in a colorectal cancer sample; somatic mutation. Ref.16		VAR_035651
	Natural variant	856	1	R → C in a colorectal cancer sample; somatic mutation. Ref.16		VAR_035652
	Natural variant	940	1	N → S. Corresponds to variant rs2235937 [ dbSNP | Ensembl ].		VAR_055077
Experimental info
	Mutagenesis	1085	1	C → S: Loss of phosphatase activity toward CTNNB1. Loss of the inhibitory effect on CTNNB1 transcriptional activity without effect on interaction with CTNNB1; when associated with S-1380. Ref.12 Ref.13
	Mutagenesis	1380	1	C → S: No effect on phosphatase activity toward CTNNB1. Loss of the inhibitory effect on CTNNB1 transcriptional activity without effect on interaction with CTNNB1; when associated with S-1085. Ref.12 Ref.13
	Sequence conflict	359 – 360	2	LT → S in AAC51938. Ref.4
	Sequence conflict	401	1	T → A in AAC51938. Ref.4
	Sequence conflict	715	1	E → D in AAB51343. Ref.3
	Sequence conflict	840 – 841	2	SG → GW in AAC51938. Ref.4
	Sequence conflict	1215	1	P → A in AAB07074. Ref.5
	Sequence conflict	1245	1	A → R in AAC51938. Ref.4
	Sequence conflict	1399	1	M → I in AAC51938. Ref.4
	Sequence conflict	1436	1	A → V in AAB07074. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: 76F9BD6EFABE8663	FASTA	1,446	162,423
	10 20 30 40 50 60 MARAQALVLA LTFQLCAPET ETPAAGCTFE EASDPAVPCE YSQAQYDDFQ WEQVRIHPGT 70 80 90 100 110 120 RAPADLPHGS YLMVNTSQHA PGQRAHVIFQ SLSENDTHCV QFSYFLYSRD GHSPGTLGVY 130 140 150 160 170 180 VRVNGGPLGS AVWNMTGSHG RQWHQAELAV STFWPNEYQV LFEALISPDR RGYMGLDDIL 190 200 210 220 230 240 LLSYPCAKAP HFSRLGDVEV NAGQNASFQC MAAGRAAEAE RFLLQRQSGA LVPAAGVRHI 250 260 270 280 290 300 SHRRFLATFP LAAVSRAEQD LYRCVSQAPR GAGVSNFAEL IVKEPPTPIA PPQLLRAGPT 310 320 330 340 350 360 YLIIQLNTNS IIGDGPIVRK EIEYRMARGP WAEVHAVSLQ TYKLWHLDPD TEYEISVLLT 370 380 390 400 410 420 RPGDGGTGRP GPPLISRTKC AEPMRAPKGL AFAEIQARQL TLQWEPLGYN VTRCHTYTVS 430 440 450 460 470 480 LCYHYTLGSS HNQTIRECVK TEQGVSRYTI KNLLPYRNVH VRLVLTNPEG RKEGKEVTFQ 490 500 510 520 530 540 TDEDVPSGIA AESLTFTPLE DMIFLKWEEP QEPNGLITQY EISYQSIESS DPAVNVPGPR 550 560 570 580 590 600 RTISKLRNET YHVFSNLHPG TTYLFSVRAR TGKGFGQAAL TEITTNISAP SFDYADMPSP 610 620 630 640 650 660 LGESENTITV LLRPAQGRGA PISVYQVIVE EERARRLRRE PGGQDCFPVP LTFEAALARG 670 680 690 700 710 720 LVHYFGAELA ASSLPEAMPF TVGDNQTYRG FWNPPLEPRK AYLIYFQAAS HLKGETRLNC 730 740 750 760 770 780 IRIARKAACK ESKRPLEVSQ RSEEMGLILG ICAGGLAVLI LLLGAIIVII RKGRDHYAYS 790 800 810 820 830 840 YYPKPVNMTK ATVNYRQEKT HMMSAVDRSF TDQSTLQEDE RLGLSFMDTH GYSTRGDQRS 850 860 870 880 890 900 GGVTEASSLL GGSPRRPCGR KGSPYHTGQL HPAVRVADLL QHINQMKTAE GYGFKQEYES 910 920 930 940 950 960 FFEGWDATKK KDKVKGSRQE PMPAYDRHRV KLHPMLGDPN ADYINANYID GYHRSNHFIA 970 980 990 1000 1010 1020 TQGPKPEMVY DFWRMVWQEH CSSIVMITKL VEVGRVKCSR YWPEDSDTYG DIKIMLVKTE 1030 1040 1050 1060 1070 1080 TLAEYVVRTF ALERRGYSAR HEVRQFHFTA WPEHGVPYHA TGLLAFIRRV KASTPPDAGP 1090 1100 1110 1120 1130 1140 IVIHCSAGTG RTGCYIVLDV MLDMAECEGV VDIYNCVKTL CSRRVNMIQT EEQYIFIHDA 1150 1160 1170 1180 1190 1200 ILEACLCGET TIPVSEFKAT YKEMIRIDPQ SNSSQLREEF QTLNSVTPPL DVEECSIALL 1210 1220 1230 1240 1250 1260 PRNRDKNRSM DVLPPDRCLP FLISTDGDSN NYINAALTDS YTRSAAFIVT LHPLQSTTPD 1270 1280 1290 1300 1310 1320 FWRLVYDYGC TSIVMLNQLN QSNSAWPCLQ YWPEPGRQQY GLMEVEFMSG TADEDLVARV 1330 1340 1350 1360 1370 1380 FRVQNISRLQ EGHLLVRHFQ FLRWSAYRDT PDSKKAFLHL LAEVDKWQAE SGDGRTIVHC 1390 1400 1410 1420 1430 1440 LNGGGRSGTF CACATVLEMI RCHNLVDVFF AAKTLRNYKP NMVETMDQYH FCYDVALEYL EGLESR
	Isoform 2 [UniParc]. Checksum: F88BB75170BF3676	FASTA	1,436	161,107
	10 20 30 40 50 60 MARAQALVLA LTFQLCAPET ETPAAGCTFE EASDPAVPCE YSQAQYDDFQ WEQVRIHPGT 70 80 90 100 110 120 RAPADLPHGS YLMVNTSQHA PGQRAHVIFQ SLSENDTHCV QFSYFLYSRD GHSPGTLGVY 130 140 150 160 170 180 VRVNGGPLGS AVWNMTGSHG RQWHQAELAV STFWPNEYQV LFEALISPDR RGYMGLDDIL 190 200 210 220 230 240 LLSYPCAKAP HFSRLGDVEV NAGQNASFQC MAAGRAAEAE RFLLQRQSGA LVPAAGVRHI 250 260 270 280 290 300 SHRRFLATFP LAAVSRAEQD LYRCVSQAPR GAGVSNFAEL IVKEPPTPIA PPQLLRAGPT 310 320 330 340 350 360 YLIIQLNTNS IIGDGPIVRK EIEYRMARGP WAEVHAVSLQ TYKLWHLDPD TEYEISVLLT 370 380 390 400 410 420 RPGDGGTGRP GPPLISRTKC AEPMRAPKGL AFAEIQARQL TLQWEPLGYN VTRCHTYTVS 430 440 450 460 470 480 LCYHYTLGSS HNQTIRECVK TEQGVSRYTI KNLLPYRNVH VRLVLTNPEG RKEGKEVTFQ 490 500 510 520 530 540 TDEDVPSGIA AESLTFTPLE DMIFLKWEEP QEPNGLITQY EISYQSIESS DPAVNVPGPR 550 560 570 580 590 600 RTISKLRNET YHVFSNLHPG TTYLFSVRAR TGKGFGQAAL TEITTNISAP SFDYADMPSP 610 620 630 640 650 660 LGESENTITV LLRPAQGRGA PISVYQVIVE EERARRLRRE PGGQDCFPVP LTFEAALARG 670 680 690 700 710 720 LVHYFGAELA ASSLPEAMPF TVGDNQTYRG FWNPPLEPRK AYLIYFQAAS HLKGETRLNC 730 740 750 760 770 780 IRIARKAACK ESKRPLEVSQ RSEEMGLILG ICAGGLAVLI LLLGAIIVII RKGKPVNMTK 790 800 810 820 830 840 ATVNYRQEKT HMMSAVDRSF TDQSTLQEDE RLGLSFMDTH GYSTRGDQRS GGVTEASSLL 850 860 870 880 890 900 GGSPRRPCGR KGSPYHTGQL HPAVRVADLL QHINQMKTAE GYGFKQEYES FFEGWDATKK 910 920 930 940 950 960 KDKVKGSRQE PMPAYDRHRV KLHPMLGDPN ADYINANYID GYHRSNHFIA TQGPKPEMVY 970 980 990 1000 1010 1020 DFWRMVWQEH CSSIVMITKL VEVGRVKCSR YWPEDSDTYG DIKIMLVKTE TLAEYVVRTF 1030 1040 1050 1060 1070 1080 ALERRGYSAR HEVRQFHFTA WPEHGVPYHA TGLLAFIRRV KASTPPDAGP IVIHCSAGTG 1090 1100 1110 1120 1130 1140 RTGCYIVLDV MLDMAECEGV VDIYNCVKTL CSRRVNMIQT EEQYIFIHDA ILEACLCGET 1150 1160 1170 1180 1190 1200 TIPVSEFKAT YKEMIRIDPQ SNSSQLREEF QTLNSVTPPL DVEECSIALL PRNRDKNRSM 1210 1220 1230 1240 1250 1260 DVLPPDRCLP FLISTDGDSN NYINAALTDS YTRSAAFIVT LHPLQSTTPD FWRLVYDYGC 1270 1280 1290 1300 1310 1320 TSIVMLNQLN QSNSAWPCLQ YWPEPGRQQY GLMEVEFMSG TADEDLVARV FRVQNISRLQ 1330 1340 1350 1360 1370 1380 EGHLLVRHFQ FLRWSAYRDT PDSKKAFLHL LAEVDKWQAE SGDGRTIVHC LNGGGRSGTF 1390 1400 1410 1420 1430 CACATVLEMI RCHNLVDVFF AAKTLRNYKP NMVETMDQYH FCYDVALEYL EGLESR
	Isoform 3 [UniParc]. Checksum: BA085FF7C36BB2A8	FASTA	1,433	160,795
	10 20 30 40 50 60 MARAQALVLA LTFQLCAPET ETPAAGCTFE EASDPAVPCE YSQAQYDDFQ WEQVRIHPGT 70 80 90 100 110 120 RAPADLPHGS YLMVNTSQHA PGQRAHVIFQ SLSENDTHCV QFSYFLYSRD GHSPGTLGVY 130 140 150 160 170 180 VRVNGGPLGS AVWNMTGSHG RQWHQAELAV STFWPNEYQV LFEALISPDR RGYMGLDDIL 190 200 210 220 230 240 LLSYPCAKAP HFSRLGDVEV NAGQNASFQC MAAGRAAEAE RFLLQRQSGA LVPAAGVRHI 250 260 270 280 290 300 SHRRFLATFP LAAVSRAEQD LYRCVSQAPR GAGVSNFAEL IVKEPPTPIA PPQLLRAGPT 310 320 330 340 350 360 YLIIQLNTNS IIGDGPIVRK EIEYRMARGP WAEVHAVSLQ TYKLWHLDPD TEYEISVLLT 370 380 390 400 410 420 RPGDGGTGRP GPPLISRTKC AEPMRAPKGL AFAEIQARQL TLQWEPLGYN VTRCHTYTVS 430 440 450 460 470 480 LCYHYTLGSS HNQTIRECVK TEQGVSRYTI KNLLPYRNVH VRLVLTNPEG RKEGKEVTFQ 490 500 510 520 530 540 TDEDVPSGIA AESLTFTPLE DMIFLKWEEP QEPNGLITQY EISYQSIESS DPAVNVPGPR 550 560 570 580 590 600 RTISKLRNET YHVFSNLHPG TTYLFSVRAR TGKGFGQAAL TEITTNISAP SFDYADMPSP 610 620 630 640 650 660 LGESENTITV LLRPAQGRGA PISVYQVIVE EERARRLRRE PGGQDCFPVP LTFEAALARG 670 680 690 700 710 720 LVHYFGAELA ASSLPEAMPF TVGDNQTYRG FWNPPLEPRK AYLIYFQAAS HLKGETRLNC 730 740 750 760 770 780 IRIARKAACK ESKRPLEVSQ RSEEMGLILG ICAGGLAVLI LLLGAIIVII RKGKPVNMTK 790 800 810 820 830 840 ATVNYRQEKT HMMSAVDRSF TDQSTLQEDE RLGLSFMDTH GYSTRGDQRS GGVTEASSLL 850 860 870 880 890 900 GGSPRRPCGR KGSPYHTGQL HPAVRVADLL QHINQMKTAE GYGFKQEYES FFEGWDATKK 910 920 930 940 950 960 KDKVKGSRQE PMPAYDRHRV KLHPMLGDPN ADYINANYID GYHRSNHFIA TQGPKPEMVY 970 980 990 1000 1010 1020 DFWRMVWQEH CSSIVMITKL VEVKCSRYWP EDSDTYGDIK IMLVKTETLA EYVVRTFALE 1030 1040 1050 1060 1070 1080 RRGYSARHEV RQFHFTAWPE HGVPYHATGL LAFIRRVKAS TPPDAGPIVI HCSAGTGRTG 1090 1100 1110 1120 1130 1140 CYIVLDVMLD MAECEGVVDI YNCVKTLCSR RVNMIQTEEQ YIFIHDAILE ACLCGETTIP 1150 1160 1170 1180 1190 1200 VSEFKATYKE MIRIDPQSNS SQLREEFQTL NSVTPPLDVE ECSIALLPRN RDKNRSMDVL 1210 1220 1230 1240 1250 1260 PPDRCLPFLI STDGDSNNYI NAALTDSYTR SAAFIVTLHP LQSTTPDFWR LVYDYGCTSI 1270 1280 1290 1300 1310 1320 VMLNQLNQSN SAWPCLQYWP EPGRQQYGLM EVEFMSGTAD EDLVARVFRV QNISRLQEGH 1330 1340 1350 1360 1370 1380 LLVRHFQFLR WSAYRDTPDS KKAFLHLLAE VDKWQAESGD GRTIVHCLNG GGRSGTFCAC 1390 1400 1410 1420 1430 ATVLEMIRCH NLVDVFFAAK TLRNYKPNMV ETMDQYHFCY DVALEYLEGL ESR
	Isoform 4 (PTPRO) [UniParc]. Checksum: EDE5C3CF8C8C9DA0	FASTA	1,440	161,648
	10 20 30 40 50 60 MARAQALVLA LTFQLCAPET ETPAAGCTFE EASDPAVPCE YSQAQYDDFQ WEQVRIHPGT 70 80 90 100 110 120 RAPADLPHGS YLMVNTSQHA PGQRAHVIFQ SLSENDTHCV QFSYFLYSRD GHSPGTLGVY 130 140 150 160 170 180 VRVNGGPLGS AVWNMTGSHG RQWHQAELAV STFWPNEYQV LFEALISPDR RGYMGLDDIL 190 200 210 220 230 240 LLSYPCAKAP HFSRLGDVEV NAGQNASFQC MAAGRAAEAE RFLLQRQSGA LVPAAGVRHI 250 260 270 280 290 300 SHRRFLATFP LAAVSRAEQD LYRCVSQAPR GAGVSNFAEL IVKEPPTPIA PPQLLRAGPT 310 320 330 340 350 360 YLIIQLNTNS IIGDGPIVRK EIEYRMARGP WAEVHAVSLQ TYKLWHLDPD TEYEISVLLT 370 380 390 400 410 420 RPGDGGTGRP GPPLISRTKC AEPMRAPKGL AFAEIQARQL TLQWEPLGYN VTRCHTYTVS 430 440 450 460 470 480 LCYHYTLGSS HNQTIRECVK TEQGVSRYTI KNLLPYRNVH VRLVLTNPEG RKEGKEVTFQ 490 500 510 520 530 540 TDEDVPSGIA AESLTFTPLE DMIFLKWEEP QEPNGLITQY EISYQSIESS DPAVNVPGPR 550 560 570 580 590 600 RTISKLRNET YHVFSNLHPG TTYLFSVRAR TGKGFGQAAL TEITTNISAP SFDYADMPSP 610 620 630 640 650 660 LGESENTITV LLRPAQGRGA PISVYQVIVE EERARRLRRE PGGQDCFPVP LTFEAALARG 670 680 690 700 710 720 LVHYFGAELA ASSLPEAMPF TVGDNQTYRG FWNPPLEPRK AYLIYFQAAS HLKGETRLNC 730 740 750 760 770 780 IRIARKAACK ESKRPLEVSQ RSEEMGLILG ICAGGLAVLI LLLGAIIVII RKGKPVNMTK 790 800 810 820 830 840 ATVNYRQEKT HMMSAVDRSF TDQSTLQEDE RLGLSFMDTH GYSTRGDQRS GGVTEASSLL 850 860 870 880 890 900 GGSPRRPCGR KGSPYHTGQL HPAVRVADLL QHINQMKTAE GYGFKQEYES FFEGWDATKK 910 920 930 940 950 960 KDKVKGSRQE PMPAYDRHRV KLHPMLGDPN ADYINANYID IRINREGYHR SNHFIATQGP 970 980 990 1000 1010 1020 KPEMVYDFWR MVWQEHCSSI VMITKLVEVG RVKCSRYWPE DSDTYGDIKI MLVKTETLAE 1030 1040 1050 1060 1070 1080 YVVRTFALER RGYSARHEVR QFHFTAWPEH GVPYHATGLL AFIRRVKAST PPDAGPIVIH 1090 1100 1110 1120 1130 1140 CSAGTGRTGC YIVLDVMLDM AECEGVVDIY NCVKTLCSRR VNMIQTEEQY IFIHDAILEA 1150 1160 1170 1180 1190 1200 CLCGETTIPV SEFKATYKEM IRIDPQSNSS QLREEFQTLN SVTPPLDVEE CSIALLPRNR 1210 1220 1230 1240 1250 1260 DKNRSMDVLP PDRCLPFLIS TDGDSNNYIN AALTDSYTRS AAFIVTLHPL QSTTPDFWRL 1270 1280 1290 1300 1310 1320 VYDYGCTSIV MLNQLNQSNS AWPCLQYWPE PGRQQYGLME VEFMSGTADE DLVARVFRVQ 1330 1340 1350 1360 1370 1380 NISREGHLLV RHFQFLRWSA YRDTPDSKKA FLHLLAEVDK WQAESGDGRT IVHCLNGGGR 1390 1400 1410 1420 1430 1440 SGTFCACATV LEMIRCHNLV DVFFAAKTLR NYKPNMVETM DQYHFCYDVA LEYLEGLESR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of PTP pi, a novel receptor-like protein-tyrosine phosphatase." Crossland S., Smith P.D., Crompton M.R. Biochem. J. 319:249-254(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Mammary gland.
[2]	"Characterization of PCP-2, a novel receptor protein tyrosine phosphatase of the MAM domain family." Wang H.-Y., Lian Z., Lerch M.M., Chen Z., Xie W., Ullrich A. Oncogene 12:2555-2562(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CATALYTIC ACTIVITY, GLYCOSYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Pancreas.
[3]	"Molecular cloning and characterization of a novel human receptor protein tyrosine phosphatase gene, hPTP-J: down-regulation of gene expression by PMA and calcium ionophore in Jurkat T lymphoma cells." Wang B., Kishihara K., Zhang D., Hara H., Nomoto K. Biochem. Biophys. Res. Commun. 231:77-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, INDUCTION. Tissue: Skeletal muscle.
[4]	"Characterization and chromosomal localization of PTPRO, a novel receptor protein tyrosine phosphatase, expressed in hematopoietic stem cells." Avraham S., London R., Tulloch G.A., Ellis M., Fu Y., Jiang S., White R.A., Painter C., Steinberger A.A., Avraham H. Gene 204:5-16(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Tissue: Brain.
[5]	"Cloning and expression of R-PTP-psi, a novel receptor protein tyrosine phosphatase related to the homophilic binding R-PTP-kappa and -mu." Banville D., Masson S., L'Abbe D., Stocco R., Shen S.-H. Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
[6]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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 3).
[9]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 194-1446 (ISOFORM 2). Tissue: Brain.
[10]	"Transcriptional regulation of a receptor protein tyrosine phosphatase gene hPTP-J by PKC-mediated signaling pathways in Jurkat and Molt-4 T lymphoma cells." Wang B., Kishihara K., Zhang D., Sakamoto T., Nomoto K. Biochim. Biophys. Acta 1450:331-340(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[11]	"The receptor protein tyrosine phosphatase, PTP-RO, is upregulated during megakaryocyte differentiation and is associated with the c-Kit receptor." Taniguchi Y., London R., Schinkmann K., Jiang S., Avraham H. Blood 94:539-549(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH KIT, PHOSPHORYLATION, PROTEOLYTIC PROCESSING, INDUCTION BY PHORBOL ESTER.
[12]	"Physical and functional interaction between receptor-like protein tyrosine phosphatase PCP-2 and beta-catenin." Yan H.-X., He Y.-Q., Dong H., Zhang P., Zeng J.-Z., Cao H.-F., Wu M.-C., Wang H.-Y. Biochemistry 41:15854-15860(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CTNNB1, INDUCTION, MUTAGENESIS OF CYS-1085 AND CYS-1380.
[13]	"Protein-tyrosine phosphatase PCP-2 inhibits beta-catenin signaling and increases E-cadherin-dependent cell adhesion." Yan H.-X., Yang W., Zhang R., Chen L., Tang L., Zhai B., Liu S.-Q., Cao H.-F., Man X.-B., Wu H.-P., Wu M.-C., Wang H.-Y. J. Biol. Chem. 281:15423-15433(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CTNNB1, MUTAGENESIS OF CYS-1085 AND CYS-1380.
[14]	"Involvement of beta3A subunit of adaptor protein-3 in intracellular trafficking of receptor-like protein tyrosine phosphatase PCP-2." Dong H., Yuan H., Jin W., Shen Y., Xu X., Wang H.-Y. Acta Biochim. Biophys. Sin. 39:540-546(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AP3B1.
[15]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-848 AND SER-853, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] TYR-830; TRP-835 AND CYS-856.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X95712 mRNA. Translation: CAA65016.1. Sequence problems. X97198 mRNA. Translation: CAA65832.1. Sequence problems. U73727 mRNA. Translation: AAB51343.1. U71075 mRNA. Translation: AAC51938.1. U60289 Genomic DNA. Translation: AAB07074.1. AL645859, AL049570, AL590729 Genomic DNA. Translation: CAH72393.1. AL645859, AL049570, AL590729 Genomic DNA. Translation: CAH72394.1. AL590729, AL049570, AL645859 Genomic DNA. Translation: CAI14331.1. AL590729, AL049570, AL645859 Genomic DNA. Translation: CAI14332.1. AL049570, AL590729, AL645859 Genomic DNA. Translation: CAI20946.1. AL049570, AL590729, AL645859 Genomic DNA. Translation: CAI20947.1. CH471059 Genomic DNA. Translation: EAX07651.1. CH471059 Genomic DNA. Translation: EAX07652.1. BC146655 mRNA. Translation: AAI46656.1. AB208855 mRNA. Translation: BAD92092.1.
IPI	IPI00023197. IPI00107472. IPI00384563. IPI00943208.
PIR	JC5290. S72441.
RefSeq	NP_001181930.1. NM_001195001.1. NP_005695.3. NM_005704.4. NP_573438.3. NM_133177.3. NP_573439.2. NM_133178.3.
UniGene	Hs.19718.
3D structure databases
ProteinModelPortal	Q92729.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1349420.
Polymorphism databases
DMDM	229462800.
Proteomic databases
PaxDb	Q92729.
PRIDE	Q92729.
Protocols and materials databases
DNASU	10076.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000345512; ENSP00000334941; ENSG00000060656. ENST00000373779; ENSP00000362884; ENSG00000060656. ENST00000428026; ENSP00000392332; ENSG00000060656. ENST00000460170; ENSP00000432906; ENSG00000060656.
GeneID	10076.
KEGG	hsa:10076.
UCSC	uc001bru.3. human. uc001brw.3. human. uc009vtq.3. human. uc009vtr.3. human.
Organism-specific databases
CTD	10076.
GeneCards	GC01P029569.
H-InvDB	HIX0000346.
HGNC	HGNC:9683. PTPRU.
HPA	CAB011476. HPA039832.
MIM	602454. gene.
neXtProt	NX_Q92729.
PharmGKB	PA34028.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5599.
HOVERGEN	HBG062785.
KO	K16662.
OMA	SAPSFDY.
PhylomeDB	Q92729.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	Q92729.
Bgee	Q92729.
CleanEx	HS_PCP2. HS_PTPRU.
Genevestigator	Q92729.
GermOnline	ENSG00000060656. Homo sapiens.
Family and domain databases
Gene3D	2.60.40.10. 4 hits.
InterPro	IPR008985. ConA-like_lec_gl_sf. IPR003961. Fibronectin_type3. IPR013783. Ig-like_fold. IPR003599. Ig_sub. IPR000998. MAM_dom. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. IPR000242. Tyr_Pase_rcpt/non-rcpt. [Graphical view]
Pfam	PF00041. fn3. 2 hits. PF00629. MAM. 1 hit. PF00102. Y_phosphatase. 2 hits. [Graphical view]
PRINTS	PR00020. MAMDOMAIN. PR00700. PRTYPHPHTASE.
SMART	SM00060. FN3. 3 hits. SM00409. IG. 1 hit. SM00137. MAM. 1 hit. SM00194. PTPc. 2 hits. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit. SSF49265. FN_III-like. 3 hits.
PROSITE	PS50853. FN3. 3 hits. PS50835. IG_LIKE. False negative. PS00740. MAM_1. 1 hit. PS50060. MAM_2. 1 hit. PS00383. TYR_PHOSPHATASE_1. 2 hits. PS50056. TYR_PHOSPHATASE_2. 2 hits. PS50055. TYR_PHOSPHATASE_PTP. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL1961785.
ChiTaRS	PTPRU. human.
GenomeRNAi	10076.
NextBio	38089.
SOURCE	Search...

Entry information

Entry name

PTPRU_HUMAN

Accession

Primary (citable) accession number: Q92729
Secondary accession number(s): A6H8L1 , O00197, P78399, Q59HA4, Q5SYU4, Q5SYU5, Q92735, Q92850

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 5, 2009
Last modified:	May 1, 2013
This is version 130 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.