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P23470 (PTPRG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. 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 gamma

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

Protein attributes

Sequence length1445 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Possesses tyrosine phosphatase activity. Ref.12

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.12

Subunit structure

Monomer; active form. Homodimer; inactive form Probable. Interacts with CNTN3, CNTN4, CNTN5 and CNTN6. Ref.12 Ref.15

Subcellular location

Membrane; Single-pass type I membrane protein Probable.

Tissue specificity

Found in a variety of tissues.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 5 subfamily.

Contains 1 alpha-carbonic anhydrase domain.

Contains 1 fibronectin type-III domain.

Contains 2 tyrosine-protein phosphatase domains.

Sequence caution

The sequence BAD93108.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CTNNB1P352222EBI-2258115,EBI-491549

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P23470-1)

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: P23470-2)

The sequence of this isoform differs from the canonical sequence as follows:
     764-792: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919
Chain20 – 14451426Receptor-type tyrosine-protein phosphatase gamma
PRO_0000025441

Regions

Topological domain20 – 736717Extracellular Potential
Transmembrane737 – 76226Helical; Potential
Topological domain763 – 1445683Cytoplasmic Potential
Domain58 – 321264Alpha-carbonic anhydrase
Domain349 – 448100Fibronectin type-III
Domain848 – 1119272Tyrosine-protein phosphatase 1
Domain1150 – 1410261Tyrosine-protein phosphatase 2
Region1060 – 10667Substrate binding By similarity

Sites

Active site10601Phosphocysteine intermediate By similarity
Binding site10281Substrate By similarity
Binding site11041Substrate By similarity
Site13511Ancestral active site

Amino acid modifications

Modified residue11821Phosphoserine Ref.11
Glycosylation1091N-linked (GlcNAc...) Potential
Glycosylation1131N-linked (GlcNAc...) Ref.10
Glycosylation1561N-linked (GlcNAc...) Potential
Glycosylation3591N-linked (GlcNAc...) Potential
Glycosylation4441N-linked (GlcNAc...) Ref.10
Glycosylation6191N-linked (GlcNAc...) Potential
Glycosylation6311N-linked (GlcNAc...) Potential
Glycosylation7221N-linked (GlcNAc...) Potential
Disulfide bond78 ↔ 261 Ref.15

Natural variations

Alternative sequence764 – 79229Missing in isoform 2.
VSP_024353
Natural variant921Y → H. Ref.2 Ref.6
Corresponds to variant rs62620047 [ dbSNP | Ensembl ].
VAR_070892
Natural variant5741G → S.
Corresponds to variant rs2292245 [ dbSNP | Ensembl ].
VAR_020301
Natural variant6391Q → R.
Corresponds to variant rs9870460 [ dbSNP | Ensembl ].
VAR_031562

Experimental info

Mutagenesis9581R → E: Loss of dimerization; when associated with E-960. Ref.12
Mutagenesis9601K → E: Loss of dimerization; when associated with E-958. Ref.12
Mutagenesis13051D → K: Loss of dimerization; when associated with K-1306. Ref.12
Mutagenesis13061D → K: Loss of dimerization; when associated with K-1305. Ref.12
Sequence conflict801G → S in AAA60224. Ref.1
Sequence conflict5491A → V in AAC50439. Ref.2
Sequence conflict7561I → T in AAC50439. Ref.2
Sequence conflict8051S → R in CAH18125. Ref.7
Sequence conflict13161C → Y in CAH18125. Ref.7
Sequence conflict14071M → R in AAA60224. Ref.1
Sequence conflict14071M → R in AAC50439. Ref.2

Secondary structure

.................................................................................................................................... 1445
Helix Strand Turn

Details...

Sequences

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

Last modified May 5, 2009. Version 4.
Checksum: A48A007BA14082BC

FASTA1,445162,003
        10         20         30         40         50         60 
MRRLLEPCWW ILFLKITSSV LHYVVCFPAL TEGYVGALHE NRHGSAVQIR RRKASGDPYW 

        70         80         90        100        110        120 
AYSGAYGPEH WVTSSVSCGG RHQSPIDILD QYARVGEEYQ ELQLDGFDNE SSNKTWMKNT 

       130        140        150        160        170        180 
GKTVAILLKD DYFVSGAGLP GRFKAEKVEF HWGHSNGSAG SEHSINGRRF PVEMQIFFYN 

       190        200        210        220        230        240 
PDDFDSFQTA ISENRIIGAM AIFFQVSPRD NSALDPIIHG LKGVVHHEKE TFLDPFVLRD 

       250        260        270        280        290        300 
LLPASLGSYY RYTGSLTTPP CSEIVEWIVF RRPVPISYHQ LEAFYSIFTT EQQDHVKSVE 

       310        320        330        340        350        360 
YLRNNFRPQQ RLHDRVVSKS AVRDSWNHDM TDFLENPLGT EASKVCSSPP IHMKVQPLNQ 

       370        380        390        400        410        420 
TALQVSWSQP ETIYHPPIMN YMISYSWTKN EDEKEKTFTK DSDKDLKATI SHVSPDSLYL 

       430        440        450        460        470        480 
FRVQAVCRND MRSDFSQTML FQANTTRIFQ GTRIVKTGVP TASPASSADM APISSGSSTW 

       490        500        510        520        530        540 
TSSGIPFSFV SMATGMGPSS SGSQATVASV VTSTLLAGLG FGGGGISSFP STVWPTRLPT 

       550        560        570        580        590        600 
AASASKQAAR PVLATTEALA SPGPDGDSSP TKDGEGTEEG EKDEKSESED GEREHEEDGE 

       610        620        630        640        650        660 
KDSEKKEKSG VTHAAEERNQ TEPSPTPSSP NRTAEGGHQT IPGHEQDHTA VPTDQTGGRR 

       670        680        690        700        710        720 
DAGPGLDPDM VTSTQVPPTA TEEQYAGSDP KRPEMPSKKP MSRGDRFSED SRFITVNPAE 

       730        740        750        760        770        780 
KNTSGMISRP APGRMEWIIP LIVVSALTFV CLILLIAVLV YWRGCNKIKS KGFPRRFREV 

       790        800        810        820        830        840 
PSSGERGEKG SRKCFQTAHF YVEDSSSPRV VPNESIPIIP IPDDMEAIPV KQFVKHIGEL 

       850        860        870        880        890        900 
YSNNQHGFSE DFEEVQRCTA DMNITAEHSN HPENKHKNRY INILAYDHSR VKLRPLPGKD 

       910        920        930        940        950        960 
SKHSDYINAN YVDGYNKAKA YIATQGPLKS TFEDFWRMIW EQNTGIIVMI TNLVEKGRRK 

       970        980        990       1000       1010       1020 
CDQYWPTENS EEYGNIIVTL KSTKIHACYT VRRFSIRNTK VKKGQKGNPK GRQNERVVIQ 

      1030       1040       1050       1060       1070       1080 
YHYTQWPDMG VPEYALPVLT FVRRSSAARM PETGPVLVHC SAGVGRTGTY IVIDSMLQQI 

      1090       1100       1110       1120       1130       1140 
KDKSTVNVLG FLKHIRTQRN YLVQTEEQYI FIHDALLEAI LGKETEVSSN QLHSYVNSIL 

      1150       1160       1170       1180       1190       1200 
IPGVGGKTRL EKQFKLVTQC NAKYVECFSA QKECNKEKNR NSSVVPSERA RVGLAPLPGM 

      1210       1220       1230       1240       1250       1260 
KGTDYINASY IMGYYRSNEF IITQHPLPHT TKDFWRMIWD HNAQIIVMLP DNQSLAEDEF 

      1270       1280       1290       1300       1310       1320 
VYWPSREESM NCEAFTVTLI SKDRLCLSNE EQIIIHDFIL EATQDDYVLE VRHFQCPKWP 

      1330       1340       1350       1360       1370       1380 
NPDAPISSTF ELINVIKEEA LTRDGPTIVH DEYGAVSAGM LCALTTLSQQ LENENAVDVF 

      1390       1400       1410       1420       1430       1440 
QVAKMINLMR PGVFTDIEQY QFIYKAMLSL VSTKENGNGP MTVDKNGAVL IADESDPAES 


MESLV 

« Hide

Isoform 2 [UniParc].

Checksum: 8DFA46915A799CFD
Show »

FASTA1,416158,771

References

« Hide 'large scale' references
[1]"Identification of a carbonic anhydrase-like domain in the extracellular region of RPTP gamma defines a new subfamily of receptor tyrosine phosphatases."
Barnea G., Silvennoinen O., Shaanan B., Honegger A.M., Canoll P.D., D'Eustachio P., Morse B., Levy J.B., Laforgia S., Huebner K., Musacchio J.M., Sap J., Schlessinger J.
Mol. Cell. Biol. 13:1497-1506(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Structure of the human receptor tyrosine phosphatase gamma gene (PTPRG) and relation to the familial RCC t(3;8) chromosome translocation."
Kastury K., Ohta M., Lasota J., Moir D., Dorman T., Laforgia S., Druck T., Huebner K.
Genomics 32:225-235(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-92.
[3]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] (ISOFORM 1).
Tissue: Aortic endothelium.
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 1 AND 2), VARIANT HIS-92.
Tissue: Brain.
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 711-1445 (ISOFORM 2).
Tissue: Prostate.
[8]"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 836-1445.
Tissue: Placenta.
[9]"Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain."
Kaplan R., Morse B., Huebner K., Croce C., Howk R., Ravera M., Ricca G., Jaye M., Schlessinger J.
Proc. Natl. Acad. Sci. U.S.A. 87:7000-7004(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 874-1118 AND 1175-1409.
Tissue: Brain.
[10]"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-113 AND ASN-444.
Tissue: Plasma.
[11]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Large-scale structural analysis of the classical human protein tyrosine phosphatome."
Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P., Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.
Cell 136:352-363(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 827-1445, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF ARG-958; LYS-960; ASP-1305 AND ASP-1306.
[13]"Crystal structure of the human receptor phosphatase PTPRG."
Structural genomics consortium (SGC)
Submitted (JUL-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 830-1127.
[14]"Structural genomics of protein phosphatases."
New York structural genomix research consortium (NYSGXRC)
Submitted (MAR-2008) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 819-1130.
[15]"The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members of the contactin family of neural recognition molecules."
Bouyain S., Watkins D.J.
Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 56-320, INTERACTION WITH CNTN3; CNTN4; CNTN5 AND CNTN6, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L09247 mRNA. Translation: AAA60224.1.
U46116 expand/collapse EMBL AC list , U46089, U46090, U46091, U46092, U46093, U46094, U46095, U46096, U46097, U46098, U46099, U46100, U46101, U46102, U46103, U46104, U46105, U46106, U46107, U46108, U46109, U46110, U46111, U46112, U46113, U46114, U46115 Genomic DNA. Translation: AAC50439.1.
AB209871 mRNA. Translation: BAD93108.1. Different initiation.
AC004695 Genomic DNA. No translation available.
AC092502 Genomic DNA. No translation available.
AC096919 Genomic DNA. No translation available.
AC098482 Genomic DNA. No translation available.
AC103587 Genomic DNA. No translation available.
AC103921 Genomic DNA. No translation available.
AC104849 Genomic DNA. No translation available.
AC105939 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW65397.1.
BC140904 mRNA. Translation: AAI40905.1.
BC144110 mRNA. Translation: AAI44111.1.
CR749269 mRNA. Translation: CAH18125.1.
X54132 mRNA. Translation: CAA38067.1.
CCDSCCDS2895.1. [P23470-1]
PIRA48148.
RefSeqNP_002832.3. NM_002841.3. [P23470-1]
XP_005265410.1. XM_005265353.2. [P23470-2]
UniGeneHs.595541.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2H4VX-ray1.55A/B831-1127[»]
2HY3X-ray2.60A/B820-1130[»]
2NLKX-ray2.40A827-1445[»]
2PBNX-ray1.70A820-1130[»]
3JXHX-ray1.70C56-320[»]
3QCBX-ray2.10A/B825-1128[»]
3QCCX-ray2.10A/B825-1128[»]
3QCDX-ray1.80A825-1128[»]
3QCEX-ray2.10A/B825-1128[»]
3QCFX-ray2.50A/B825-1128[»]
3QCGX-ray2.05A825-1128[»]
3QCHX-ray2.40A825-1128[»]
3QCIX-ray2.27A825-1128[»]
3QCJX-ray2.26A825-1128[»]
3QCKX-ray2.05A825-1128[»]
3QCLX-ray2.40A825-1128[»]
3QCMX-ray2.40A/B825-1128[»]
3QCNX-ray2.41A825-1128[»]
ProteinModelPortalP23470.
SMRP23470. Positions 58-320, 347-445, 826-1412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111757. 6 interactions.
IntActP23470. 22 interactions.
MINTMINT-1349880.
STRING9606.ENSP00000418112.

Chemistry

BindingDBP23470.
ChEMBLCHEMBL4905.

PTM databases

PhosphoSiteP23470.

Polymorphism databases

DMDM229463033.

Proteomic databases

MaxQBP23470.
PaxDbP23470.
PRIDEP23470.

Protocols and materials databases

DNASU5793.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295874; ENSP00000295874; ENSG00000144724. [P23470-2]
ENST00000474889; ENSP00000418112; ENSG00000144724. [P23470-1]
GeneID5793.
KEGGhsa:5793.
UCSCuc003dlb.3. human. [P23470-1]
uc003dlc.3. human. [P23470-2]

Organism-specific databases

CTD5793.
GeneCardsGC03P061522.
H-InvDBHIX0024329.
HGNCHGNC:9671. PTPRG.
MIM176886. gene.
neXtProtNX_P23470.
PharmGKBPA34016.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000060222.
HOVERGENHBG053760.
KOK16667.
OMAWRGCNKI.
OrthoDBEOG7K6PT4.
PhylomeDBP23470.
TreeFamTF351978.

Enzyme and pathway databases

SignaLinkP23470.

Gene expression databases

ArrayExpressP23470.
BgeeP23470.
CleanExHS_PTPRG.
GenevestigatorP23470.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.10.200.10. 1 hit.
3.90.190.10. 2 hits.
InterProIPR001148. Carbonic_anhydrase_a.
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]
PfamPF00194. Carb_anhydrase. 1 hit.
PF00041. fn3. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM01057. Carb_anhydrase. 1 hit.
SM00060. FN3. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 1 hit.
SSF51069. SSF51069. 1 hit.
SSF52799. SSF52799. 2 hits.
PROSITEPS51144. ALPHA_CA_2. 1 hit.
PS50853. FN3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPRG. human.
EvolutionaryTraceP23470.
GeneWikiPTPRG.
GenomeRNAi5793.
NextBio22556.
PROP23470.
SOURCESearch...

Entry information

Entry namePTPRG_HUMAN
AccessionPrimary (citable) accession number: P23470
Secondary accession number(s): B2RU12 expand/collapse secondary AC list , B7ZLX5, Q15623, Q59EE0, Q68DU5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 158 of the entry and version 4 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 3

Human chromosome 3: entries, gene names and cross-references to MIM