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P23468 (PTPRD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Short name=Protein-tyrosine phosphatase delta
Short name=R-PTP-delta
EC=3.1.3.48
Gene names
Name:PTPRD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1912 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Interacts with IL1RAPL1 (via extracellular region); interaction is required for IL1RAPL1-mediated synapse formation By similarity. Interacts with PPFIA1, PPFIA2 and PPFIA3. Ref.5

Subcellular location

Membrane; Single-pass type I membrane protein.

Post-translational modification

A cleavage occurs, separating the extracellular domain from the transmembrane segment. This process called 'ectodomain shedding' is thought to be involved in receptor desensitization, signal transduction and/or membrane localization.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 2A subfamily.

Contains 8 fibronectin type-III domains.

Contains 3 Ig-like C2-type (immunoglobulin-like) domains.

Contains 2 tyrosine-protein phosphatase domains.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protein phosphatase
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processheterophilic cell-cell adhesion

Inferred from sequence or structural similarity. Source: BHF-UCL

neuron differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

peptidyl-tyrosine dephosphorylation

Traceable author statement Ref.1. Source: GOC

phosphate-containing compound metabolic process

Non-traceable author statement Ref.1. Source: ProtInc

positive regulation of dendrite morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

presynaptic membrane assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

protein dephosphorylation

Traceable author statement Ref.1. Source: ProtInc

transmembrane receptor protein tyrosine phosphatase signaling pathway

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentintegral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functioncell adhesion molecule binding

Inferred from sequence or structural similarity. Source: BHF-UCL

receptor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

transmembrane receptor protein tyrosine phosphatase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

STAT3Q9BXH23EBI-2682990,EBI-7021400

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P23468-1)

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.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 2 (identifier: P23468-2)

Also known as: Kidney;

The sequence of this isoform differs from the canonical sequence as follows:
     181-189: Missing.
     226-229: Missing.
     775-783: Missing.
Isoform 3 (identifier: P23468-3)

Also known as: Fetal brain;

The sequence of this isoform differs from the canonical sequence as follows:
     609-1137: Missing.
Isoform 4 (identifier: P23468-4)

The sequence of this isoform differs from the canonical sequence as follows:
     184-189: Missing.
     227-230: Missing.
     608-608: K → M
     609-1019: Missing.
     1330-1330: G → GSDDSGYPGNLHSSS
Note: No experimental confirmation available.
Isoform 5 (identifier: P23468-5)

The sequence of this isoform differs from the canonical sequence as follows:
     608-608: K → M
     609-1019: Missing.
     1291-1291: K → KSKPD
Note: No experimental confirmation available.
Isoform 6 (identifier: P23468-6)

The sequence of this isoform differs from the canonical sequence as follows:
     608-608: K → M
     609-1019: Missing.
     1291-1291: K → KSSKPD
Note: No experimental confirmation available.
Isoform 7 (identifier: P23468-7)

The sequence of this isoform differs from the canonical sequence as follows:
     181-183: Missing.
     608-1019: KPSAPPQDIS...QFRTLPVDQV → M
     1291-1291: K → KSKPD

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 19121892Receptor-type tyrosine-protein phosphatase delta
PRO_0000025437

Regions

Topological domain21 – 12651245Extracellular Potential
Transmembrane1266 – 129025Helical; Potential
Topological domain1291 – 1912622Cytoplasmic Potential
Domain24 – 11491Ig-like C2-type 1
Domain126 – 22499Ig-like C2-type 2
Domain236 – 31883Ig-like C2-type 3
Domain325 – 41591Fibronectin type-III 1
Domain420 – 51697Fibronectin type-III 2
Domain518 – 60790Fibronectin type-III 3
Domain612 – 70998Fibronectin type-III 4
Domain714 – 822109Fibronectin type-III 5
Domain823 – 91694Fibronectin type-III 6
Domain921 – 101696Fibronectin type-III 7
Domain1020 – 110687Fibronectin type-III 8
Domain1357 – 1612256Tyrosine-protein phosphatase 1
Domain1644 – 1903260Tyrosine-protein phosphatase 2
Region180 – 18910Interaction with IL1RAPL1 By similarity
Region1553 – 15597Substrate binding By similarity

Sites

Active site15531Phosphocysteine intermediate By similarity
Active site18441Phosphocysteine intermediate By similarity
Binding site15211Substrate By similarity
Binding site15971Substrate By similarity
Site1181 – 11822Cleavage Probable

Amino acid modifications

Glycosylation2541N-linked (GlcNAc...) Potential
Glycosylation2991N-linked (GlcNAc...) Potential
Glycosylation7241N-linked (GlcNAc...) Potential
Glycosylation8321N-linked (GlcNAc...) Potential
Disulfide bond45 ↔ 98 Potential
Disulfide bond147 ↔ 207 Potential
Disulfide bond257 ↔ 302 Potential

Natural variations

Alternative sequence181 – 1899Missing in isoform 2.
VSP_005147
Alternative sequence181 – 1833Missing in isoform 7.
VSP_054220
Alternative sequence184 – 1896Missing in isoform 4.
VSP_043384
Alternative sequence226 – 2294Missing in isoform 2.
VSP_005148
Alternative sequence227 – 2304Missing in isoform 4.
VSP_043385
Alternative sequence608 – 1019412KPSAP…PVDQV → M in isoform 7.
VSP_054221
Alternative sequence6081K → M in isoform 4, isoform 5 and isoform 6.
VSP_043386
Alternative sequence609 – 1137529Missing in isoform 3.
VSP_005150
Alternative sequence609 – 1019411Missing in isoform 4, isoform 5 and isoform 6.
VSP_043387
Alternative sequence775 – 7839Missing in isoform 2.
VSP_005149
Alternative sequence12911K → KSKPD in isoform 5 and isoform 7.
VSP_043388
Alternative sequence12911K → KSSKPD in isoform 6.
VSP_043389
Alternative sequence13301G → GSDDSGYPGNLHSSS in isoform 4.
VSP_043390
Natural variant281R → Q in a colorectal cancer sample; somatic mutation. Ref.8
VAR_035645
Natural variant2761L → P in a colorectal cancer sample; somatic mutation. Ref.8
VAR_035646
Natural variant4471Q → E.
Corresponds to variant rs10977171 [ dbSNP | Ensembl ].
VAR_024581
Natural variant9011V → A in a colorectal cancer sample; somatic mutation. Ref.8
VAR_035647
Natural variant9951R → C.
Corresponds to variant rs35929428 [ dbSNP | Ensembl ].
VAR_061761
Natural variant10781E → D.
Corresponds to variant rs7869444 [ dbSNP | Ensembl ].
VAR_051761

Experimental info

Mutagenesis11781R → A: 2.5-fold reduction in cleavage. 10-fold reduction in cleavage; when associated with A-1181. Ref.1
Mutagenesis11811R → A: No reduction in cleavage. 10-fold reduction in cleavage; when associated with A-1178. Ref.1

Secondary structure

............................................................................ 1912
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 1996. Version 2.
Checksum: 3AE8CBCD32182E26

FASTA1,912214,760
        10         20         30         40         50         60 
MVHVARLLLL LLTFFLRTDA ETPPRFTRTP VDQTGVSGGV ASFICQATGD PRPKIVWNKK 

        70         80         90        100        110        120 
GKKVSNQRFE VIEFDDGSGS VLRIQPLRTP RDEAIYECVA SNNVGEISVS TRLTVLREDQ 

       130        140        150        160        170        180 
IPRGFPTIDM GPQLKVVERT RTATMLCAAS GNPDPEITWF KDFLPVDTSN NNGRIKQLRS 

       190        200        210        220        230        240 
ESIGGTPIRG ALQIEQSEES DQGKYECVAT NSAGTRYSAP ANLYVRELRE VRRVPPRFSI 

       250        260        270        280        290        300 
PPTNHEIMPG GSVNITCVAV GSPMPYVKWM LGAEDLTPED DMPIGRNVLE LNDVRQSANY 

       310        320        330        340        350        360 
TCVAMSTLGV IEAIAQITVK ALPKPPGTPV VTESTATSIT LTWDSGNPEP VSYYIIQHKP 

       370        380        390        400        410        420 
KNSEELYKEI DGVATTRYSV AGLSPYSDYE FRVVAVNNIG RGPPSEPVLT QTSEQAPSSA 

       430        440        450        460        470        480 
PRDVQARMLS STTILVQWKE PEEPNGQIQG YRVYYTMDPT QHVNNWMKHN VADSQITTIG 

       490        500        510        520        530        540 
NLVPQKTYSV KVLAFTSIGD GPLSSDIQVI TQTGVPGQPL NFKAEPESET SILLSWTPPR 

       550        560        570        580        590        600 
SDTIANYELV YKDGEHGEEQ RITIEPGTSY RLQGLKPNSL YYFRLAARSP QGLGASTAEI 

       610        620        630        640        650        660 
SARTMQSKPS APPQDISCTS PSSTSILVSW QPPPVEKQNG IITEYSIKYT AVDGEDDKPH 

       670        680        690        700        710        720 
EILGIPSDTT KYLLEQLEKW TEYRITVTAH TDVGPGPESL SVLIRTNEDV PSGPPRKVEV 

       730        740        750        760        770        780 
EAVNSTSVKV SWRSPVPNKQ HGQIRGYQVH YVRMENGEPK GQPMLKDVML ADAQWEFDDT 

       790        800        810        820        830        840 
TEHDMIISGL QPETSYSLTV TAYTTKGDGA RSKPKLVSTT GAVPGKPRLV INHTQMNTAL 

       850        860        870        880        890        900 
IQWHPPVDTF GPLQGYRLKF GRKDMEPLTT LEFSEKEDHF TATDIHKGAS YVFRLSARNK 

       910        920        930        940        950        960 
VGFGEEMVKE ISIPEEVPTG FPQNLHSEGT TSTSVQLSWQ PPVLAERNGI ITKYTLLYRD 

       970        980        990       1000       1010       1020 
INIPLLPMEQ LIVPADTTMT LTGLKPDTTY DVKVRAHTSK GPGPYSPSVQ FRTLPVDQVF 

      1030       1040       1050       1060       1070       1080 
AKNFHVKAVM KTSVLLSWEI PENYNSAMPF KILYDDGKMV EEVDGRATQK LIVNLKPEKS 

      1090       1100       1110       1120       1130       1140 
YSFVLTNRGN SAGGLQHRVT AKTAPDVLRT KPAFIGKTNL DGMITVQLPE VPANENIKGY 

      1150       1160       1170       1180       1190       1200 
YIIIVPLKKS RGKFIKPWES PDEMELDELL KEISRKRRSI RYGREVELKP YIAAHFDVLP 

      1210       1220       1230       1240       1250       1260 
TEFTLGDDKH YGGFTNKQLQ SGQEYVFFVL AVMEHAESKM YATSPYSDPV VSMDLDPQPI 

      1270       1280       1290       1300       1310       1320 
TDEEEGLIWV VGPVLAVVFI ICIVIAILLY KRKRAESDSR KSSIPNNKEI PSHHPTDPVE 

      1330       1340       1350       1360       1370       1380 
LRRLNFQTPG MASHPPIPIL ELADHIERLK ANDNLKFSQE YESIDPGQQF TWEHSNLEVN 

      1390       1400       1410       1420       1430       1440 
KPKNRYANVI AYDHSRVLLS AIEGIPGSDY VNANYIDGYR KQNAYIATQG SLPETFGDFW 

      1450       1460       1470       1480       1490       1500 
RMIWEQRSAT VVMMTKLEER SRVKCDQYWP SRGTETHGLV QVTLLDTVEL ATYCVRTFAL 

      1510       1520       1530       1540       1550       1560 
YKNGSSEKRE VRQFQFTAWP DHGVPEHPTP FLAFLRRVKT CNPPDAGPMV VHCSAGVGRT 

      1570       1580       1590       1600       1610       1620 
GCFIVIDAML ERIKHEKTVD IYGHVTLMRA QRNYMVQTED QYIFIHDALL EAVTCGNTEV 

      1630       1640       1650       1660       1670       1680 
PARNLYAYIQ KLTQIETGEN VTGMELEFKR LASSKAHTSR FISANLPCNK FKNRLVNIMP 

      1690       1700       1710       1720       1730       1740 
YESTRVCLQP IRGVEGSDYI NASFIDGYRQ QKAYIATQGP LAETTEDFWR MLWEHNSTIV 

      1750       1760       1770       1780       1790       1800 
VMLTKLREMG REKCHQYWPA ERSARYQYFV VDPMAEYNMP QYILREFKVT DARDGQSRTV 

      1810       1820       1830       1840       1850       1860 
RQFQFTDWPE QGVPKSGEGF IDFIGQVHKT KEQFGQDGPI SVHCSAGVGR TGVFITLSIV 

      1870       1880       1890       1900       1910 
LERMRYEGVV DIFQTVKMLR TQRPAMVQTE DQYQFSYRAA LEYLGSFDHY AT 

« Hide

Isoform 2 (Kidney) [UniParc].

Checksum: F67473E6C295C0D3
Show »

FASTA1,890212,133
Isoform 3 (Fetal brain) [UniParc].

Checksum: 6FA7F02992F7AEFF
Show »

FASTA1,383156,088
Isoform 4 [UniParc].

Checksum: 737878C2930FBF68
Show »

FASTA1,505169,474
Isoform 5 [UniParc].

Checksum: 7F25884835F91CDB
Show »

FASTA1,505169,606
Isoform 6 [UniParc].

Checksum: 136D13489D0BEA56
Show »

FASTA1,506169,693
Isoform 7 [UniParc].

Checksum: CDEDB66CFBBE5D0D
Show »

FASTA1,502169,277

References

« Hide 'large scale' references
[1]"Molecular characterization of the human transmembrane protein-tyrosine phosphatase delta. Evidence for tissue-specific expression of alternative human transmembrane protein-tyrosine phosphatase delta isoforms."
Pulido R., Krueger N.X., Serra-Pages C., Saito H., Streuli M.
J. Biol. Chem. 270:6722-6728(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CLEAVAGE SITE, MUTAGENESIS OF ARG-1178 AND ARG-1181.
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
[4]"Structural diversity and evolution of human receptor-like protein tyrosine phosphatases."
Krueger N.X., Streuli M., Saito H.
EMBO J. 9:3241-3252(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 390-1912.
Tissue: Placenta.
[5]"Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins."
Serra-Pages C., Medley Q.G., Tang M., Hart A., Streuli M.
J. Biol. Chem. 273:15611-15620(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPFIA1; PPFIA2 AND PPFIA3.
[6]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[7]"Solution structure of the second and third FN3 domain of human receptor-type tyrosine-protein phosphatase delta."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 405-607.
[8]"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. expand/collapse author list , 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] GLN-28; PRO-276 AND ALA-901.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L38929 mRNA. Translation: AAC41749.1.
AL137125 expand/collapse EMBL AC list , AL356584, AL445926, AL583805, AL590397 Genomic DNA. Translation: CAH70912.2.
AL356584 expand/collapse EMBL AC list , AL137125, AL445926, AL583805, AL590397 Genomic DNA. Translation: CAI16146.2.
AL445926 expand/collapse EMBL AC list , AL137125, AL356584, AL583805, AL590397 Genomic DNA. Translation: CAH73847.2.
AL583805 expand/collapse EMBL AC list , AL137125, AL356584, AL445926, AL590397 Genomic DNA. Translation: CAH70443.2.
AL590397 expand/collapse EMBL AC list , AL137125, AL356584, AL445926, AL583805 Genomic DNA. Translation: CAH73128.2.
AL133479 Genomic DNA. No translation available.
AL135790 Genomic DNA. No translation available.
AL137069 Genomic DNA. No translation available.
AL137851 Genomic DNA. No translation available.
AL157826 Genomic DNA. No translation available.
AL353638 Genomic DNA. No translation available.
AL353733 Genomic DNA. No translation available.
AL354722 Genomic DNA. No translation available.
AL356054 Genomic DNA. No translation available.
AL390723 Genomic DNA. No translation available.
AL391864 Genomic DNA. No translation available.
AL441884 Genomic DNA. No translation available.
AL451130 Genomic DNA. No translation available.
AL513422 Genomic DNA. No translation available.
AL590307 Genomic DNA. No translation available.
AL591133 Genomic DNA. No translation available.
AL591622 Genomic DNA. No translation available.
AL596451 Genomic DNA. No translation available.
AL669908 Genomic DNA. No translation available.
BC106713 mRNA. Translation: AAI06714.1.
BC106714 mRNA. Translation: AAI06715.1.
BC106715 mRNA. Translation: AAI06716.1.
X54133 mRNA. Translation: CAA38068.1.
PIRA56178.
RefSeqNP_001164496.1. NM_001171025.1.
NP_002830.1. NM_002839.3.
NP_569075.2. NM_130391.3.
NP_569076.2. NM_130392.3.
UniGeneHs.446083.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X5ZNMR-A506-607[»]
2DLHNMR-A407-514[»]
2YD6X-ray1.35A21-226[»]
2YD7X-ray1.98A/B21-226[»]
ProteinModelPortalP23468.
SMRP23468. Positions 21-318, 323-719, 921-1016, 1331-1906.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111753. 3 interactions.
DIPDIP-17023N.
IntActP23468. 3 interactions.
MINTMINT-1350159.
STRING9606.ENSP00000348812.

PTM databases

PhosphoSiteP23468.

Polymorphism databases

DMDM1709906.

Proteomic databases

PaxDbP23468.
PRIDEP23468.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355233; ENSP00000347373; ENSG00000153707. [P23468-6]
ENST00000356435; ENSP00000348812; ENSG00000153707. [P23468-1]
ENST00000381196; ENSP00000370593; ENSG00000153707. [P23468-1]
ENST00000397606; ENSP00000380731; ENSG00000153707. [P23468-4]
ENST00000397611; ENSP00000380735; ENSG00000153707.
ENST00000486161; ENSP00000417093; ENSG00000153707. [P23468-5]
ENST00000540109; ENSP00000438164; ENSG00000153707. [P23468-1]
GeneID5789.
KEGGhsa:5789.
UCSCuc003zkk.3. human. [P23468-1]
uc003zkp.3. human. [P23468-6]
uc003zkq.3. human. [P23468-5]
uc003zks.3. human. [P23468-4]

Organism-specific databases

CTD5789.
GeneCardsGC09M008307.
HGNCHGNC:9668. PTPRD.
HPACAB026474.
MIM601598. gene.
neXtProtNX_P23468.
PharmGKBPA34013.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000010250.
HOVERGENHBG053758.
InParanoidP23468.
KOK06777.
OMAGYYIVIV.
OrthoDBEOG7M98FB.
PhylomeDBP23468.
TreeFamTF312900.

Enzyme and pathway databases

SignaLinkP23468.

Gene expression databases

ArrayExpressP23468.
BgeeP23468.
CleanExHS_PTPRD.
GenevestigatorP23468.

Family and domain databases

Gene3D2.60.40.10. 11 hits.
InterProIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00041. fn3. 7 hits.
PF07679. I-set. 3 hits.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 8 hits.
SM00408. IGc2. 3 hits.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 6 hits.
PROSITEPS50853. FN3. 8 hits.
PS50835. IG_LIKE. 3 hits.
PS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPRD. human.
EvolutionaryTraceP23468.
GeneWikiPTPRD.
GenomeRNAi5789.
NextBio22528.
PROP23468.
SOURCESearch...

Entry information

Entry namePTPRD_HUMAN
AccessionPrimary (citable) accession number: P23468
Secondary accession number(s): B1ALA0 expand/collapse secondary AC list , F5GWT7, Q3KPJ0, Q3KPJ1, Q3KPJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM