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Q12913

- PTPRJ_HUMAN

UniProt

Q12913 - PTPRJ_HUMAN

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Protein

Receptor-type tyrosine-protein phosphatase eta

Gene

PTPRJ

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

Functioni

Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, RET (variant MEN2A), KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2. Plays a role in cell adhesion, migration, proliferation and differentiation. Involved in vascular development. Regulator of macrophage adhesion and spreading. Positively affects cell-matrix adhesion. Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation. Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR. Positive regulator of endothelial cell survival, as well as of VEGF-induced SRC and AKT activation; through KDR dephosphorylation. Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation. Enhances the barrier function of epithelial junctions during reassembly. Negatively regulates T-cell receptor (TCR) signaling. Upon T-cell TCR activation, it is up-regulated and excluded from the immunological synapses, while upon T-cell-antigen presenting cells (APC) disengagement, it is no longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate prolongation of signaling.19 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1205 – 12051SubstrateBy similarity
Active sitei1239 – 12391Phosphocysteine intermediatePROSITE-ProRule annotation
Binding sitei1283 – 12831SubstrateBy similarity

GO - Molecular functioni

  1. beta-catenin binding Source: UniProtKB
  2. delta-catenin binding Source: UniProtKB
  3. gamma-catenin binding Source: UniProtKB
  4. mitogen-activated protein kinase binding Source: UniProtKB
  5. phosphatase activity Source: UniProtKB
  6. platelet-derived growth factor receptor binding Source: UniProtKB
  7. protein kinase binding Source: UniProtKB
  8. protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. contact inhibition Source: UniProtKB
  2. heart development Source: Ensembl
  3. negative regulation of cell growth Source: UniProtKB
  4. negative regulation of cell migration Source: UniProtKB
  5. negative regulation of cell proliferation Source: UniProtKB
  6. negative regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  7. negative regulation of MAP kinase activity Source: UniProtKB
  8. negative regulation of platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  9. negative regulation of protein kinase B signaling Source: UniProtKB
  10. negative regulation of T cell receptor signaling pathway Source: UniProtKB
  11. negative regulation of vascular permeability Source: UniProtKB
  12. oligodendrocyte differentiation Source: Ensembl
  13. peptidyl-tyrosine dephosphorylation Source: UniProtKB
  14. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  15. positive chemotaxis Source: UniProtKB
  16. positive regulation of cell adhesion Source: UniProtKB
  17. positive regulation of focal adhesion assembly Source: UniProtKB
  18. positive regulation of protein kinase B signaling Source: UniProtKB
  19. regulation of cell adhesion Source: UniProtKB
  20. vasculogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

SignaLinkiQ12913.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-type tyrosine-protein phosphatase eta (EC:3.1.3.48)
Short name:
Protein-tyrosine phosphatase eta
Short name:
R-PTP-eta
Alternative name(s):
Density-enhanced phosphatase 1
Short name:
DEP-1
HPTP eta
Protein-tyrosine phosphatase receptor type J
Short name:
R-PTP-J
CD_antigen: CD148
Gene namesi
Name:PTPRJ
Synonyms:DEP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:9673. PTPRJ.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein. Cell projectionruffle membrane By similarity. Cell junction
Note: After T-cell stimulation, it is temporarily excluded from immunological synapses.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini36 – 975940ExtracellularSequence AnalysisAdd
BLAST
Transmembranei976 – 99621HelicalSequence AnalysisAdd
BLAST
Topological domaini997 – 1337341CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell-cell junction Source: UniProtKB
  2. cell projection Source: UniProtKB-KW
  3. cell surface Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. immunological synapse Source: UniProtKB
  6. integral component of plasma membrane Source: ProtInc
  7. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1016 – 10161K → A: 80% decrease in interaction with MAPK1 and MAPK3. 1 Publication
Mutagenesisi1205 – 12051D → A: Substrate trapping with much higher affinity for substrate. 9 Publications
Mutagenesisi1239 – 12391C → S: Catalytically inactive and substrate trapping with higher affinity for substrate. 6 Publications

Organism-specific databases

PharmGKBiPA34018.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535Sequence AnalysisAdd
BLAST
Chaini36 – 13371302Receptor-type tyrosine-protein phosphatase etaPRO_0000025444Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi72 – 721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi82 – 821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi142 – 1421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi192 – 1921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi231 – 2311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi278 – 2781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi342 – 3421N-linked (GlcNAc...)1 Publication
Glycosylationi351 – 3511N-linked (GlcNAc...)1 Publication
Glycosylationi376 – 3761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi391 – 3911N-linked (GlcNAc...)1 Publication
Glycosylationi396 – 3961N-linked (GlcNAc...)1 Publication
Glycosylationi413 – 4131N-linked (GlcNAc...)1 Publication
Glycosylationi431 – 4311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi501 – 5011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi525 – 5251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi536 – 5361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi582 – 5821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi603 – 6031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi618 – 6181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi628 – 6281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi637 – 6371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi666 – 6661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi669 – 6691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi761 – 7611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi772 – 7721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi784 – 7841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi790 – 7901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi824 – 8241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi910 – 9101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi937 – 9371N-linked (GlcNAc...)1 Publication

Post-translational modificationi

N- and O-glycosylated.3 Publications

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ12913.
PaxDbiQ12913.
PRIDEiQ12913.

PTM databases

PhosphoSiteiQ12913.

Expressioni

Tissue specificityi

Expressed in the promyelocytic cell line HL-60, the granulocyte-macrophage colony-stimulating factor-dependent leukemic cell line F-36P, and the IL3 and erythropoietin-dependent leukemic cell line F-36E. Expressed predominantly in epithelial cells and lymphocytes. Enhanced expression at high cell density.3 Publications

Gene expression databases

BgeeiQ12913.
CleanExiHS_PTPRJ.
ExpressionAtlasiQ12913. baseline and differential.
GenevestigatoriQ12913.

Organism-specific databases

HPAiHPA006026.

Interactioni

Subunit structurei

Monomer. Interacts with CTNNB1 (phosphorylated) and JUP (phosphorylated). Interacts with FLT3 (phosphorylated). Interacts with GAB1 and GRB2.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTNNB1P352222EBI-2264500,EBI-491549
CTNND1O607165EBI-2264500,EBI-701927
ERBB2P046262EBI-2264500,EBI-641062
FLT1P179482EBI-2264500,EBI-1026718
FLT3P368883EBI-2264500,EBI-3946257
GAB1Q134802EBI-2264500,EBI-517684
GHRP109122EBI-2264500,EBI-286316
KDRP359684EBI-2264500,EBI-1005487
MAPK1P284827EBI-2264500,EBI-959949
MAPK3P273615EBI-2264500,EBI-73995
METP085815EBI-2264500,EBI-1039152
PDGFRBP096194EBI-2264500,EBI-641237
TEKQ027632EBI-2264500,EBI-2257090

Protein-protein interaction databases

BioGridi111759. 13 interactions.
IntActiQ12913. 39 interactions.
MINTiMINT-1349281.
STRINGi9606.ENSP00000400010.

Structurei

Secondary structure

1
1337
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi368 – 37710Combined sources
Beta strandi382 – 3898Combined sources
Beta strandi398 – 4047Combined sources
Beta strandi409 – 42012Combined sources
Beta strandi429 – 44012Combined sources
Beta strandi446 – 4516Combined sources
Helixi1023 – 104725Combined sources
Turni1048 – 10547Combined sources
Turni1058 – 10614Combined sources
Helixi1063 – 10686Combined sources
Turni1078 – 10803Combined sources
Beta strandi1087 – 10893Combined sources
Helixi1090 – 10934Combined sources
Beta strandi1096 – 11005Combined sources
Beta strandi1108 – 11136Combined sources
Turni1117 – 11193Combined sources
Helixi1120 – 112910Combined sources
Beta strandi1134 – 11385Combined sources
Beta strandi1155 – 11573Combined sources
Beta strandi1159 – 11613Combined sources
Beta strandi1164 – 117310Combined sources
Beta strandi1175 – 118612Combined sources
Turni1187 – 11893Combined sources
Beta strandi1192 – 12009Combined sources
Helixi1212 – 122514Combined sources
Beta strandi1235 – 12439Combined sources
Helixi1244 – 126118Combined sources
Beta strandi1262 – 12654Combined sources
Helixi1267 – 12759Combined sources
Helixi1285 – 130218Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CFVX-ray2.50A1019-1311[»]
2DLENMR-A366-456[»]
2NZ6X-ray2.30A1019-1311[»]
ProteinModelPortaliQ12913.
SMRiQ12913. Positions 169-195, 210-279, 319-714, 721-812, 1018-1303.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12913.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini121 – 20989Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini207 – 29185Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini271 – 36494Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini368 – 45689Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini457 – 54185Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini542 – 62382Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST
Domaini625 – 72096Fibronectin type-III 7PROSITE-ProRule annotationAdd
BLAST
Domaini721 – 81797Fibronectin type-III 8PROSITE-ProRule annotationAdd
BLAST
Domaini816 – 90287Fibronectin type-III 9PROSITE-ProRule annotationAdd
BLAST
Domaini1041 – 1298258Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1239 – 12457Substrate bindingBy similarity

Sequence similaritiesi

Contains 9 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000232054.
HOVERGENiHBG053761.
InParanoidiQ12913.
KOiK05698.
OMAiSYVSFSR.
OrthoDBiEOG7PCJFZ.
PhylomeDBiQ12913.
TreeFamiTF351926.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
3.90.190.10. 1 hit.
InterProiIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00041. fn3. 4 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 8 hits.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 4 hits.
SSF52799. SSF52799. 1 hit.
PROSITEiPS50853. FN3. 6 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q12913-1) [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
MKPAAREARL PPRSPGLRWA LPLLLLLLRL GQILCAGGTP SPIPDPSVAT
60 70 80 90 100
VATGENGITQ ISSTAESFHK QNGTGTPQVE TNTSEDGESS GANDSLRTPE
110 120 130 140 150
QGSNGTDGAS QKTPSSTGPS PVFDIKAVSI SPTNVILTWK SNDTAASEYK
160 170 180 190 200
YVVKHKMENE KTITVVHQPW CNITGLRPAT SYVFSITPGI GNETWGDPRV
210 220 230 240 250
IKVITEPIPV SDLRVALTGV RKAALSWSNG NGTASCRVLL ESIGSHEELT
260 270 280 290 300
QDSRLQVNIS GLKPGVQYNI NPYLLQSNKT KGDPLGTEGG LDASNTERSR
310 320 330 340 350
AGSPTAPVHD ESLVGPVDPS SGQQSRDTEV LLVGLEPGTR YNATVYSQAA
360 370 380 390 400
NGTEGQPQAI EFRTNAIQVF DVTAVNISAT SLTLIWKVSD NESSSNYTYK
410 420 430 440 450
IHVAGETDSS NLNVSEPRAV IPGLRSSTFY NITVCPVLGD IEGTPGFLQV
460 470 480 490 500
HTPPVPVSDF RVTVVSTTEI GLAWSSHDAE SFQMHITQEG AGNSRVEITT
510 520 530 540 550
NQSIIIGGLF PGTKYCFEIV PKGPNGTEGA SRTVCNRTVP SAVFDIHVVY
560 570 580 590 600
VTTTEMWLDW KSPDGASEYV YHLVIESKHG SNHTSTYDKA ITLQGLIPGT
610 620 630 640 650
LYNITISPEV DHVWGDPNST AQYTRPSNVS NIDVSTNTTA ATLSWQNFDD
660 670 680 690 700
ASPTYSYCLL IEKAGNSSNA TQVVTDIGIT DATVTELIPG SSYTVEIFAQ
710 720 730 740 750
VGDGIKSLEP GRKSFCTDPA SMASFDCEVV PKEPALVLKW TCPPGANAGF
760 770 780 790 800
ELEVSSGAWN NATHLESCSS ENGTEYRTEV TYLNFSTSYN ISITTVSCGK
810 820 830 840 850
MAAPTRNTCT TGITDPPPPD GSPNITSVSH NSVKVKFSGF EASHGPIKAY
860 870 880 890 900
AVILTTGEAG HPSADVLKYT YEDFKKGASD TYVTYLIRTE EKGRSQSLSE
910 920 930 940 950
VLKYEIDVGN ESTTLGYYNG KLEPLGSYRA CVAGFTNITF HPQNKGLIDG
960 970 980 990 1000
AESYVSFSRY SDAVSLPQDP GVICGAVFGC IFGALVIVTV GGFIFWRKKR
1010 1020 1030 1040 1050
KDAKNNEVSF SQIKPKKSKL IRVENFEAYF KKQQADSNCG FAEEYEDLKL
1060 1070 1080 1090 1100
VGISQPKYAA ELAENRGKNR YNNVLPYDIS RVKLSVQTHS TDDYINANYM
1110 1120 1130 1140 1150
PGYHSKKDFI ATQGPLPNTL KDFWRMVWEK NVYAIIMLTK CVEQGRTKCE
1160 1170 1180 1190 1200
EYWPSKQAQD YGDITVAMTS EIVLPEWTIR DFTVKNIQTS ESHPLRQFHF
1210 1220 1230 1240 1250
TSWPDHGVPD TTDLLINFRY LVRDYMKQSP PESPILVHCS AGVGRTGTFI
1260 1270 1280 1290 1300
AIDRLIYQIE NENTVDVYGI VYDLRMHRPL MVQTEDQYVF LNQCVLDIVR
1310 1320 1330
SQKDSKVDLI YQNTTAMTIY ENLAPVTTFG KTNGYIA
Length:1,337
Mass (Da):145,941
Last modified:February 5, 2008 - v3
Checksum:iB44F4343FC8FD1B4
GO
Isoform 2 (identifier: Q12913-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     539-539: V → G
     540-1337: Missing.

Note: No experimental confirmation available.

Show »
Length:539
Mass (Da):57,190
Checksum:iE970DA55A6B2E38D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti261 – 2611G → D in AAB36687. (PubMed:7937872)Curated
Sequence conflicti918 – 92912YNGKL…LGSYR → LQWEAGTSGLLP in BAA07035. (PubMed:7994032)CuratedAdd
BLAST
Sequence conflicti1130 – 11301K → Q no nucleotide entry (PubMed:8483328)Curated
Sequence conflicti1234 – 12341P → E no nucleotide entry (PubMed:8483328)Curated
Sequence conflicti1243 – 12431V → I no nucleotide entry (PubMed:8483328)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti214 – 2141R → C in a colon cancer sample; somatic mutation. 1 Publication
VAR_015905
Natural varianti276 – 2761Q → P in a colon cancer sample; somatic mutation. 2 Publications
Corresponds to variant rs1566734 [ dbSNP | Ensembl ].
VAR_015906
Natural varianti293 – 2931A → T.
Corresponds to variant rs2229701 [ dbSNP | Ensembl ].
VAR_038414
Natural varianti326 – 3261R → Q.1 Publication
Corresponds to variant rs1503185 [ dbSNP | Ensembl ].
VAR_024582
Natural varianti372 – 3721V → I.
Corresponds to variant rs2229703 [ dbSNP | Ensembl ].
VAR_038415
Natural varianti872 – 8721E → D.4 Publications
Corresponds to variant rs4752904 [ dbSNP | Ensembl ].
VAR_038416
Natural varianti1235 – 12351I → T.
Corresponds to variant rs11039554 [ dbSNP | Ensembl ].
VAR_038417

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei539 – 5391V → G in isoform 2. 1 PublicationVSP_043652
Alternative sequencei540 – 1337798Missing in isoform 2. 1 PublicationVSP_043653Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10886 mRNA. Translation: AAB36687.1.
D37781 mRNA. Translation: BAA07035.1.
AC026975 Genomic DNA. No translation available.
AC103828 Genomic DNA. No translation available.
BC063417 mRNA. Translation: AAH63417.1.
AH011675 Genomic DNA. Translation: AAM69432.1.
CCDSiCCDS44596.1. [Q12913-2]
CCDS7945.1. [Q12913-1]
PIRiI38670.
RefSeqiNP_001091973.1. NM_001098503.1. [Q12913-2]
NP_002834.3. NM_002843.3. [Q12913-1]
UniGeneiHs.318547.

Genome annotation databases

EnsembliENST00000418331; ENSP00000400010; ENSG00000149177. [Q12913-1]
ENST00000440289; ENSP00000409733; ENSG00000149177. [Q12913-2]
GeneIDi5795.
KEGGihsa:5795.
UCSCiuc001ngo.4. human. [Q12913-2]
uc001ngp.4. human. [Q12913-1]

Polymorphism databases

DMDMi166899088.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10886 mRNA. Translation: AAB36687.1 .
D37781 mRNA. Translation: BAA07035.1 .
AC026975 Genomic DNA. No translation available.
AC103828 Genomic DNA. No translation available.
BC063417 mRNA. Translation: AAH63417.1 .
AH011675 Genomic DNA. Translation: AAM69432.1 .
CCDSi CCDS44596.1. [Q12913-2 ]
CCDS7945.1. [Q12913-1 ]
PIRi I38670.
RefSeqi NP_001091973.1. NM_001098503.1. [Q12913-2 ]
NP_002834.3. NM_002843.3. [Q12913-1 ]
UniGenei Hs.318547.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CFV X-ray 2.50 A 1019-1311 [» ]
2DLE NMR - A 366-456 [» ]
2NZ6 X-ray 2.30 A 1019-1311 [» ]
ProteinModelPortali Q12913.
SMRi Q12913. Positions 169-195, 210-279, 319-714, 721-812, 1018-1303.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111759. 13 interactions.
IntActi Q12913. 39 interactions.
MINTi MINT-1349281.
STRINGi 9606.ENSP00000400010.

Chemistry

BindingDBi Q12913.
ChEMBLi CHEMBL3692.

PTM databases

PhosphoSitei Q12913.

Polymorphism databases

DMDMi 166899088.

Proteomic databases

MaxQBi Q12913.
PaxDbi Q12913.
PRIDEi Q12913.

Protocols and materials databases

DNASUi 5795.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000418331 ; ENSP00000400010 ; ENSG00000149177 . [Q12913-1 ]
ENST00000440289 ; ENSP00000409733 ; ENSG00000149177 . [Q12913-2 ]
GeneIDi 5795.
KEGGi hsa:5795.
UCSCi uc001ngo.4. human. [Q12913-2 ]
uc001ngp.4. human. [Q12913-1 ]

Organism-specific databases

CTDi 5795.
GeneCardsi GC11P048002.
H-InvDB HIX0035923.
HGNCi HGNC:9673. PTPRJ.
HPAi HPA006026.
MIMi 600925. gene.
neXtProti NX_Q12913.
PharmGKBi PA34018.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
GeneTreei ENSGT00770000120452.
HOGENOMi HOG000232054.
HOVERGENi HBG053761.
InParanoidi Q12913.
KOi K05698.
OMAi SYVSFSR.
OrthoDBi EOG7PCJFZ.
PhylomeDBi Q12913.
TreeFami TF351926.

Enzyme and pathway databases

SignaLinki Q12913.

Miscellaneous databases

ChiTaRSi PTPRJ. human.
EvolutionaryTracei Q12913.
GeneWikii PTPRJ.
GenomeRNAii 5795.
NextBioi 22564.
PROi Q12913.
SOURCEi Search...

Gene expression databases

Bgeei Q12913.
CleanExi HS_PTPRJ.
ExpressionAtlasi Q12913. baseline and differential.
Genevestigatori Q12913.

Family and domain databases

Gene3Di 2.60.40.10. 5 hits.
3.90.190.10. 1 hit.
InterProi IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view ]
Pfami PF00041. fn3. 4 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view ]
PRINTSi PR00700. PRTYPHPHTASE.
SMARTi SM00060. FN3. 8 hits.
SM00194. PTPc. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 4 hits.
SSF52799. SSF52799. 1 hit.
PROSITEi PS50853. FN3. 6 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density."
    Oestman A., Yang Q., Tonks N.K.
    Proc. Natl. Acad. Sci. U.S.A. 91:9680-9684(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-872.
  2. "Molecular cloning, characterization, and chromosomal localization of a novel protein-tyrosine phosphatase, HPTP eta."
    Honda H., Inazawa J., Nishida J., Yazaki Y., Hirai H.
    Blood 84:4186-4194(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-872.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 2).
    Tissue: Pancreas.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-1337, VARIANTS CYS-214; PRO-276 AND ASP-872.
    Tissue: Colon.
  6. "Identification of novel protein-tyrosine phosphatases in a human leukemia cell line, F-36P."
    Honda H., Shibuya M., Chiba S., Yazaki Y., Hirai H.
    Leukemia 7:742-746(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1124-1245 (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Leukemia.
  7. "CD148 is a membrane protein tyrosine phosphatase present in all hematopoietic lineages and is involved in signal transduction on lymphocytes."
    de la Fuente-Garcia M.A., Nicolas J.M., Freed J.H., Palou E., Thomas A.P., Vilella R., Vives J., Gaya A.
    Blood 91:2800-2809(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 36-49; 485-502 AND 723-739, FUNCTION, TISSUE SPECIFICITY, GLYCOSYLATION, SUBCELLULAR LOCATION.
  8. "Negative regulation of human T cell activation by the receptor-type protein tyrosine phosphatase CD148."
    Tangye S.G., Wu J., Aversa G., de Vries J.E., Lanier L.L., Phillips J.H.
    J. Immunol. 161:3803-3807(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1."
    Kovalenko M., Denner K., Sandstrom J., Persson C., Gross S., Jandt E., Vilella R., Bohmer F., Ostman A.
    J. Biol. Chem. 275:16219-16226(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylation."
    Baker J.E., Majeti R., Tangye S.G., Weiss A.
    Mol. Cell. Biol. 21:2393-2403(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Primary sequence determinants responsible for site-selective dephosphorylation of the PDGF beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1."
    Persson C., Engstrom U., Mowbray S.L., Ostman A.
    FEBS Lett. 517:27-31(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn)."
    Holsinger L.J., Ward K., Duffield B., Zachwieja J., Jallal B.
    Oncogene 21:7067-7076(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CTNNB1 AND JUP, MUTAGENESIS OF ASP-1205 AND CYS-1239, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  13. "Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1."
    Palka H.L., Park M., Tonks N.K.
    J. Biol. Chem. 278:5728-5735(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CTNNB1; GRB2; GAB1 AND JUP, MUTAGENESIS OF ASP-1205 AND CYS-1239.
  14. "The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling."
    Lin J., Weiss A.
    J. Cell Biol. 162:673-682(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  15. "The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation."
    Kellie S., Craggs G., Bird I.N., Jones G.E.
    J. Cell Sci. 117:609-618(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-342; ASN-351; ASN-391 AND ASN-396.
    Tissue: Plasma.
  17. "The receptor-type protein tyrosine phosphatase J antagonizes the biochemical and biological effects of RET-derived oncoproteins."
    Iervolino A., Iuliano R., Trapasso F., Viglietto G., Melillo R.M., Carlomagno F., Santoro M., Fusco A.
    Cancer Res. 66:6280-6287(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-1205.
  18. "DEP-1 protein tyrosine phosphatase inhibits proliferation and migration of colon carcinoma cells and is upregulated by protective nutrients."
    Balavenkatraman K.K., Jandt E., Friedrich K., Kautenburger T., Pool-Zobel B.L., Ostman A., Bohmer F.D.
    Oncogene 25:6319-6324(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "The tyrosine phosphatase CD148 interacts with the p85 regulatory subunit of phosphoinositide 3-kinase."
    Tsuboi N., Utsunomiya T., Roberts R.L., Ito H., Takahashi K., Noda M., Takahashi T.
    Biochem. J. 413:193-200(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-1205, SUBCELLULAR LOCATION.
  20. "The tyrosine phosphatase CD148 is an essential positive regulator of platelet activation and thrombosis."
    Senis Y.A., Tomlinson M.G., Ellison S., Mazharian A., Lim J., Zhao Y., Kornerup K.N., Auger J.M., Thomas S.G., Dhanjal T., Kalia N., Zhu J.W., Weiss A., Watson S.P.
    Blood 113:4942-4954(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  21. "An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase controlling EGFR endocytosis."
    Tarcic G., Boguslavsky S.K., Wakim J., Kiuchi T., Liu A., Reinitz F., Nathanson D., Takahashi T., Mischel P.S., Ng T., Yarden Y.
    Curr. Biol. 19:1788-1798(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN EGFR REGULATION, MUTAGENESIS OF ASP-1205 AND CYS-1239, SUBCELLULAR LOCATION.
  22. "Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells."
    Sallee J.L., Burridge K.
    J. Biol. Chem. 284:14997-15006(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-1205 AND CYS-1239, SUBCELLULAR LOCATION.
  23. "Tumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the RAS pathway by direct dephosphorylation of ERK1/2 kinases."
    Sacco F., Tinti M., Palma A., Ferrari E., Nardozza A.P., Hooft van Huijsduijnen R., Takahashi T., Castagnoli L., Cesareni G.
    J. Biol. Chem. 284:22048-22058(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-1016 AND ASP-1205.
  24. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-413 AND ASN-937.
    Tissue: Liver.
  25. "New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival."
    Chabot C., Spring K., Gratton J.P., Elchebly M., Royal I.
    Mol. Cell. Biol. 29:241-253(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-1205 AND CYS-1239.
  26. "Loss of the protein-tyrosine phosphatase DEP-1/PTPRJ drives meningioma cell motility."
    Petermann A., Haase D., Wetzel A., Balavenkatraman K.K., Tenev T., Guhrs K.H., Friedrich S., Nakamura M., Mawrin C., Bohmer F.D.
    Brain Pathol. 21:405-418(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  27. "Phosphatome profiling reveals PTPN2, PTPRJ and PTEN as potent negative regulators of PKB/Akt activation in Ras-mutated cancer cells."
    Omerovic J., Clague M.J., Prior I.A.
    Biochem. J. 426:65-72(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  28. Cited for: FUNCTION, INTERACTION WITH FLT3, MUTAGENESIS OF ASP-1205 AND CYS-1239.
  29. "Solution structure of the fourth FN3 domain of human receptor-type tyrosine-protein phosphatase eta."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 366-456.
  30. "The tyrosine phosphatase PTPRJ/DEP-1 genotype affects thyroid carcinogenesis."
    Iuliano R., Le Pera I., Cristofaro C., Baudi F., Arturi F., Pallante P., Martelli M.L., Trapasso F., Chiariotti L., Fusco A.
    Oncogene 23:8432-8438(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PRO-276; GLN-326 AND ASP-872.

Entry informationi

Entry nameiPTPRJ_HUMAN
AccessioniPrimary (citable) accession number: Q12913
Secondary accession number(s): Q15255
, Q6P4H4, Q8NHM2, Q9UDA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 5, 2008
Last modified: November 26, 2014
This is version 155 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3