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Protein

Receptor-type tyrosine-protein phosphatase U

Gene

PTPRU

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1053 – 10531SubstrateSequence Analysis
Active sitei1085 – 10851Phosphocysteine intermediateBy similarity
Binding sitei1129 – 11291SubstrateBy similarity
Active sitei1380 – 13801Phosphocysteine intermediateBy similarity

GO - Molecular functioni

  • beta-catenin binding Source: UniProtKB
  • protein tyrosine phosphatase activity Source: UniProtKB
  • transmembrane receptor protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  • canonical Wnt signaling pathway Source: UniProtKB
  • cell adhesion Source: UniProtKB
  • cell differentiation Source: UniProtKB-KW
  • homotypic cell-cell adhesion Source: Ensembl
  • negative regulation of cell migration Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • organ regeneration Source: Ensembl
  • peptidyl-tyrosine dephosphorylation Source: GOC
  • protein dephosphorylation Source: UniProtKB
  • protein localization to cell surface Source: UniProtKB
  • response to glucocorticoid Source: Ensembl
  • single organismal cell-cell adhesion Source: UniProtKB
  • transmembrane receptor protein tyrosine phosphatase signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase, Receptor

Keywords - Biological processi

Cell adhesion, Differentiation

Enzyme and pathway databases

BRENDAi3.1.3.48. 2681.
ReactomeiREACT_111040. Signaling by SCF-KIT.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-type tyrosine-protein phosphatase U (EC:3.1.3.48)
Short name:
R-PTP-U
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 namesi
Name:PTPRU
Synonyms:FMI, PCP2, PTPRO
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9683. PTPRU.

Subcellular locationi

  • Cell junction 1 Publication
  • Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 749731ExtracellularSequence AnalysisAdd
BLAST
Transmembranei750 – 77021HelicalSequence AnalysisAdd
BLAST
Topological domaini771 – 1446676CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cell-cell junction Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1085 – 10851C → 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. 2 Publications
Mutagenesisi1380 – 13801C → 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. 2 Publications

Organism-specific databases

PharmGKBiPA34028.

Polymorphism and mutation databases

BioMutaiPTPRU.
DMDMi229462800.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 14461428Receptor-type tyrosine-protein phosphatase UPRO_0000371658Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi210 ↔ 264Sequence Analysis
Glycosylationi410 – 4101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi685 – 6851N-linked (GlcNAc...)Sequence Analysis
Modified residuei848 – 8481Phosphoserine1 Publication
Modified residuei853 – 8531Phosphoserine1 Publication

Post-translational modificationi

The extracellular domain is proteolytically processed through cleavage within the fibronectin type-III 4 domain (By similarity). In addition to the 190 kDa full-length protein, proteolytic products of 100 kDa, 80 kDa and 73 kDa are observed.By similarity1 Publication
N-glycosylated.1 Publication
Phosphorylated on tyrosine residues upon activation of KIT with stem cell factor (SCF). The 73 kDa proteolytic product is not phosphorylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ92729.
PaxDbiQ92729.
PRIDEiQ92729.

PTM databases

DEPODiQ92729.

Expressioni

Tissue specificityi

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.4 Publications

Developmental stagei

Expressed in fetal brain, lung and kidney.1 Publication

Inductioni

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 (PubMed:10397721).4 Publications

Gene expression databases

BgeeiQ92729.
CleanExiHS_PCP2.
HS_PTPRU.
GenevisibleiQ92729. HS.

Organism-specific databases

HPAiCAB011476.
HPA039832.

Interactioni

Subunit structurei

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.Curated4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KITP107212EBI-7052301,EBI-1379503

Protein-protein interaction databases

BioGridi115386. 5 interactions.
IntActiQ92729. 1 interaction.
MINTiMINT-1349420.
STRINGi9606.ENSP00000334941.

Structurei

3D structure databases

ProteinModelPortaliQ92729.
SMRiQ92729. Positions 872-1157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 188164MAMPROSITE-ProRule annotationAdd
BLAST
Domaini190 – 27586Ig-like C2-typeAdd
BLAST
Domaini288 – 38396Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini386 – 48499Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini485 – 591107Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini592 – 67483Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini888 – 1144257Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
BLAST
Domaini1176 – 1439264Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni771 – 887117Mediates interaction with CTNNB1By similarityAdd
BLAST
Regioni1085 – 10917Substrate bindingBy similarity

Sequence similaritiesi

Contains 4 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 MAM domain.PROSITE-ProRule annotation
Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00760000118900.
HOVERGENiHBG062785.
InParanoidiQ92729.
KOiK16662.
OMAiASFQCMA.
OrthoDBiEOG70KGNP.
PhylomeDBiQ92729.
TreeFamiTF312900.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
3.90.190.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR000998. MAM_dom.
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.
PF00629. MAM. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSiPR00020. MAMDOMAIN.
PR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 3 hits.
SM00409. IG. 1 hit.
SM00137. MAM. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF52799. SSF52799. 2 hits.
PROSITEiPS50853. FN3. 3 hits.
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]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q92729-1) [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
MARAQALVLA LTFQLCAPET ETPAAGCTFE EASDPAVPCE YSQAQYDDFQ
60 70 80 90 100
WEQVRIHPGT RAPADLPHGS YLMVNTSQHA PGQRAHVIFQ SLSENDTHCV
110 120 130 140 150
QFSYFLYSRD GHSPGTLGVY VRVNGGPLGS AVWNMTGSHG RQWHQAELAV
160 170 180 190 200
STFWPNEYQV LFEALISPDR RGYMGLDDIL LLSYPCAKAP HFSRLGDVEV
210 220 230 240 250
NAGQNASFQC MAAGRAAEAE RFLLQRQSGA LVPAAGVRHI SHRRFLATFP
260 270 280 290 300
LAAVSRAEQD LYRCVSQAPR GAGVSNFAEL IVKEPPTPIA PPQLLRAGPT
310 320 330 340 350
YLIIQLNTNS IIGDGPIVRK EIEYRMARGP WAEVHAVSLQ TYKLWHLDPD
360 370 380 390 400
TEYEISVLLT RPGDGGTGRP GPPLISRTKC AEPMRAPKGL AFAEIQARQL
410 420 430 440 450
TLQWEPLGYN VTRCHTYTVS LCYHYTLGSS HNQTIRECVK TEQGVSRYTI
460 470 480 490 500
KNLLPYRNVH VRLVLTNPEG RKEGKEVTFQ TDEDVPSGIA AESLTFTPLE
510 520 530 540 550
DMIFLKWEEP QEPNGLITQY EISYQSIESS DPAVNVPGPR RTISKLRNET
560 570 580 590 600
YHVFSNLHPG TTYLFSVRAR TGKGFGQAAL TEITTNISAP SFDYADMPSP
610 620 630 640 650
LGESENTITV LLRPAQGRGA PISVYQVIVE EERARRLRRE PGGQDCFPVP
660 670 680 690 700
LTFEAALARG LVHYFGAELA ASSLPEAMPF TVGDNQTYRG FWNPPLEPRK
710 720 730 740 750
AYLIYFQAAS HLKGETRLNC IRIARKAACK ESKRPLEVSQ RSEEMGLILG
760 770 780 790 800
ICAGGLAVLI LLLGAIIVII RKGRDHYAYS YYPKPVNMTK ATVNYRQEKT
810 820 830 840 850
HMMSAVDRSF TDQSTLQEDE RLGLSFMDTH GYSTRGDQRS GGVTEASSLL
860 870 880 890 900
GGSPRRPCGR KGSPYHTGQL HPAVRVADLL QHINQMKTAE GYGFKQEYES
910 920 930 940 950
FFEGWDATKK KDKVKGSRQE PMPAYDRHRV KLHPMLGDPN ADYINANYID
960 970 980 990 1000
GYHRSNHFIA TQGPKPEMVY DFWRMVWQEH CSSIVMITKL VEVGRVKCSR
1010 1020 1030 1040 1050
YWPEDSDTYG DIKIMLVKTE TLAEYVVRTF ALERRGYSAR HEVRQFHFTA
1060 1070 1080 1090 1100
WPEHGVPYHA TGLLAFIRRV KASTPPDAGP IVIHCSAGTG RTGCYIVLDV
1110 1120 1130 1140 1150
MLDMAECEGV VDIYNCVKTL CSRRVNMIQT EEQYIFIHDA ILEACLCGET
1160 1170 1180 1190 1200
TIPVSEFKAT YKEMIRIDPQ SNSSQLREEF QTLNSVTPPL DVEECSIALL
1210 1220 1230 1240 1250
PRNRDKNRSM DVLPPDRCLP FLISTDGDSN NYINAALTDS YTRSAAFIVT
1260 1270 1280 1290 1300
LHPLQSTTPD FWRLVYDYGC TSIVMLNQLN QSNSAWPCLQ YWPEPGRQQY
1310 1320 1330 1340 1350
GLMEVEFMSG TADEDLVARV FRVQNISRLQ EGHLLVRHFQ FLRWSAYRDT
1360 1370 1380 1390 1400
PDSKKAFLHL LAEVDKWQAE SGDGRTIVHC LNGGGRSGTF CACATVLEMI
1410 1420 1430 1440
RCHNLVDVFF AAKTLRNYKP NMVETMDQYH FCYDVALEYL EGLESR
Length:1,446
Mass (Da):162,423
Last modified:May 5, 2009 - v2
Checksum:i76F9BD6EFABE8663
GO
Isoform 2 (identifier: Q92729-2) [UniParc]FASTAAdd to basket

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

Show »
Length:1,436
Mass (Da):161,107
Checksum:iF88BB75170BF3676
GO
Isoform 3 (identifier: Q92729-3) [UniParc]FASTAAdd to basket

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

Show »
Length:1,433
Mass (Da):160,795
Checksum:iBA085FF7C36BB2A8
GO
Isoform 4 (identifier: Q92729-4) [UniParc]FASTAAdd to basket

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.
Show »
Length:1,440
Mass (Da):161,648
Checksum:iEDE5C3CF8C8C9DA0
GO

Sequence cautioni

The sequence CAA65016.1 differs from that shown.Several sequencing problems.Curated
The sequence CAA65832.1 differs from that shown.Several sequencing problems.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti359 – 3602LT → S in AAC51938 (PubMed:9434160).Curated
Sequence conflicti401 – 4011T → A in AAC51938 (PubMed:9434160).Curated
Sequence conflicti715 – 7151E → D in AAB51343 (PubMed:9070223).Curated
Sequence conflicti840 – 8412SG → GW in AAC51938 (PubMed:9434160).Curated
Sequence conflicti1215 – 12151P → A in AAB07074 (Ref. 5) Curated
Sequence conflicti1245 – 12451A → R in AAC51938 (PubMed:9434160).Curated
Sequence conflicti1399 – 13991M → I in AAC51938 (PubMed:9434160).Curated
Sequence conflicti1436 – 14361A → V in AAB07074 (Ref. 5) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601T → N.
Corresponds to variant rs35332573 [ dbSNP | Ensembl ].
VAR_055075
Natural varianti471 – 4711R → L.
Corresponds to variant rs35745442 [ dbSNP | Ensembl ].
VAR_055076
Natural varianti830 – 8301H → Y in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035650
Natural varianti835 – 8351R → W in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035651
Natural varianti856 – 8561R → C in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035652
Natural varianti940 – 9401N → S.
Corresponds to variant rs2235937 [ dbSNP | Ensembl ].
VAR_055077

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei774 – 78310Missing in isoform 2, isoform 3 and isoform 4. 5 PublicationsVSP_037082
Alternative sequencei950 – 9501D → DIRINRE in isoform 4. 1 PublicationVSP_037083
Alternative sequencei993 – 9953Missing in isoform 3. 1 PublicationVSP_037084
Alternative sequencei1329 – 13302Missing in isoform 4. 1 PublicationVSP_037085

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS334.1. [Q92729-1]
CCDS335.1. [Q92729-2]
CCDS44098.2. [Q92729-4]
CCDS53290.1. [Q92729-3]
PIRiJC5290.
S72441.
RefSeqiNP_001181930.1. NM_001195001.1. [Q92729-3]
NP_005695.3. NM_005704.4. [Q92729-1]
NP_573438.3. NM_133177.3. [Q92729-4]
NP_573439.2. NM_133178.3. [Q92729-2]
UniGeneiHs.19718.

Genome annotation databases

EnsembliENST00000345512; ENSP00000334941; ENSG00000060656.
ENST00000373779; ENSP00000362884; ENSG00000060656. [Q92729-2]
ENST00000428026; ENSP00000392332; ENSG00000060656. [Q92729-3]
ENST00000460170; ENSP00000432906; ENSG00000060656. [Q92729-4]
GeneIDi10076.
KEGGihsa:10076.
UCSCiuc001bru.3. human. [Q92729-1]
uc001brw.3. human. [Q92729-2]
uc009vtq.3. human. [Q92729-4]
uc009vtr.3. human. [Q92729-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS334.1. [Q92729-1]
CCDS335.1. [Q92729-2]
CCDS44098.2. [Q92729-4]
CCDS53290.1. [Q92729-3]
PIRiJC5290.
S72441.
RefSeqiNP_001181930.1. NM_001195001.1. [Q92729-3]
NP_005695.3. NM_005704.4. [Q92729-1]
NP_573438.3. NM_133177.3. [Q92729-4]
NP_573439.2. NM_133178.3. [Q92729-2]
UniGeneiHs.19718.

3D structure databases

ProteinModelPortaliQ92729.
SMRiQ92729. Positions 872-1157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115386. 5 interactions.
IntActiQ92729. 1 interaction.
MINTiMINT-1349420.
STRINGi9606.ENSP00000334941.

Chemistry

ChEMBLiCHEMBL1961785.

PTM databases

DEPODiQ92729.

Polymorphism and mutation databases

BioMutaiPTPRU.
DMDMi229462800.

Proteomic databases

MaxQBiQ92729.
PaxDbiQ92729.
PRIDEiQ92729.

Protocols and materials databases

DNASUi10076.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000345512; ENSP00000334941; ENSG00000060656.
ENST00000373779; ENSP00000362884; ENSG00000060656. [Q92729-2]
ENST00000428026; ENSP00000392332; ENSG00000060656. [Q92729-3]
ENST00000460170; ENSP00000432906; ENSG00000060656. [Q92729-4]
GeneIDi10076.
KEGGihsa:10076.
UCSCiuc001bru.3. human. [Q92729-1]
uc001brw.3. human. [Q92729-2]
uc009vtq.3. human. [Q92729-4]
uc009vtr.3. human. [Q92729-3]

Organism-specific databases

CTDi10076.
GeneCardsiGC01P029569.
H-InvDBHIX0000346.
HGNCiHGNC:9683. PTPRU.
HPAiCAB011476.
HPA039832.
MIMi602454. gene.
neXtProtiNX_Q92729.
PharmGKBiPA34028.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00760000118900.
HOVERGENiHBG062785.
InParanoidiQ92729.
KOiK16662.
OMAiASFQCMA.
OrthoDBiEOG70KGNP.
PhylomeDBiQ92729.
TreeFamiTF312900.

Enzyme and pathway databases

BRENDAi3.1.3.48. 2681.
ReactomeiREACT_111040. Signaling by SCF-KIT.

Miscellaneous databases

ChiTaRSiPTPRU. human.
GeneWikiiPTPRU.
GenomeRNAii10076.
NextBioi38089.
PROiQ92729.
SOURCEiSearch...

Gene expression databases

BgeeiQ92729.
CleanExiHS_PCP2.
HS_PTPRU.
GenevisibleiQ92729. HS.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
3.90.190.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR000998. MAM_dom.
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.
PF00629. MAM. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSiPR00020. MAMDOMAIN.
PR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 3 hits.
SM00409. IG. 1 hit.
SM00137. MAM. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF52799. SSF52799. 2 hits.
PROSITEiPS50853. FN3. 3 hits.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. Cited for: VARIANTS [LARGE SCALE ANALYSIS] TYR-830; TRP-835 AND CYS-856.

Entry informationi

Entry nameiPTPRU_HUMAN
AccessioniPrimary (citable) accession number: Q92729
Secondary accession number(s): A6H8L1
, O00197, P78399, Q59HA4, Q5SYU4, Q5SYU5, Q92735, Q92850
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 5, 2009
Last modified: July 22, 2015
This is version 151 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.