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P23470

- PTPRG_HUMAN

UniProt

P23470 - PTPRG_HUMAN

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Protein

Receptor-type tyrosine-protein phosphatase gamma

Gene

PTPRG

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

Functioni

Possesses tyrosine phosphatase activity.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 PublicationPROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1028 – 10281SubstrateBy similarity
Active sitei1060 – 10601Phosphocysteine intermediatePROSITE-ProRule annotation
Binding sitei1104 – 11041SubstrateBy similarity
Sitei1351 – 13511Ancestral active site

GO - Molecular functioni

  1. identical protein binding Source: UniProtKB
  2. protein tyrosine phosphatase activity Source: UniProtKB
  3. transmembrane receptor protein tyrosine phosphatase activity Source: ProtInc

GO - Biological processi

  1. brain development Source: Ensembl
  2. negative regulation of epithelial cell migration Source: UniProtKB
  3. negative regulation of neuron projection development Source: Ensembl
  4. peptidyl-tyrosine dephosphorylation Source: GOC
  5. transmembrane receptor protein tyrosine kinase signaling pathway Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

SignaLinkiP23470.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-type tyrosine-protein phosphatase gamma (EC:3.1.3.48)
Short name:
Protein-tyrosine phosphatase gamma
Short name:
R-PTP-gamma
Gene namesi
Name:PTPRG
Synonyms:PTPG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:9671. PTPRG.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 736717ExtracellularSequence AnalysisAdd
BLAST
Transmembranei737 – 76226HelicalSequence AnalysisAdd
BLAST
Topological domaini763 – 1445683CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular space Source: Ensembl
  2. extracellular vesicular exosome Source: UniProtKB
  3. integral component of plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi958 – 9581R → E: Loss of dimerization; when associated with E-960. 1 Publication
Mutagenesisi960 – 9601K → E: Loss of dimerization; when associated with E-958. 1 Publication
Mutagenesisi1305 – 13051D → K: Loss of dimerization; when associated with K-1306. 1 Publication
Mutagenesisi1306 – 13061D → K: Loss of dimerization; when associated with K-1305. 1 Publication

Organism-specific databases

PharmGKBiPA34016.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Add
BLAST
Chaini20 – 14451426Receptor-type tyrosine-protein phosphatase gammaPRO_0000025441Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi78 ↔ 2611 Publication
Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi113 – 1131N-linked (GlcNAc...)1 Publication
Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi444 – 4441N-linked (GlcNAc...)1 Publication
Glycosylationi619 – 6191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi631 – 6311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi722 – 7221N-linked (GlcNAc...)Sequence Analysis
Modified residuei1182 – 11821Phosphoserine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP23470.
PaxDbiP23470.
PRIDEiP23470.

PTM databases

PhosphoSiteiP23470.

Expressioni

Tissue specificityi

Found in a variety of tissues.

Gene expression databases

BgeeiP23470.
CleanExiHS_PTPRG.
ExpressionAtlasiP23470. baseline and differential.
GenevestigatoriP23470.

Interactioni

Subunit structurei

Monomer; active form. Homodimer; inactive form (Probable). Interacts with CNTN3, CNTN4, CNTN5 and CNTN6.2 PublicationsCurated

Binary interactionsi

WithEntry#Exp.IntActNotes
CTNNB1P352222EBI-2258115,EBI-491549

Protein-protein interaction databases

BioGridi111757. 11 interactions.
IntActiP23470. 22 interactions.
MINTiMINT-1349880.
STRINGi9606.ENSP00000418112.

Structurei

Secondary structure

1
1445
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi64 – 663Combined sources
Helixi68 – 703Combined sources
Helixi71 – 744Combined sources
Helixi76 – 794Combined sources
Helixi90 – 923Combined sources
Beta strandi103 – 1064Combined sources
Beta strandi116 – 1194Combined sources
Beta strandi124 – 1274Combined sources
Beta strandi133 – 1353Combined sources
Beta strandi143 – 15210Combined sources
Beta strandi162 – 1654Combined sources
Beta strandi171 – 1799Combined sources
Turni181 – 1833Combined sources
Helixi187 – 1926Combined sources
Beta strandi197 – 20913Combined sources
Helixi212 – 2143Combined sources
Helixi215 – 2239Combined sources
Beta strandi230 – 2323Combined sources
Helixi238 – 2414Combined sources
Beta strandi249 – 2546Combined sources
Beta strandi265 – 2728Combined sources
Beta strandi274 – 2774Combined sources
Helixi278 – 2858Combined sources
Beta strandi288 – 2903Combined sources
Beta strandi299 – 3013Combined sources
Helixi831 – 86131Combined sources
Turni867 – 8704Combined sources
Helixi872 – 8776Combined sources
Helixi887 – 8893Combined sources
Beta strandi890 – 8923Combined sources
Turni899 – 9013Combined sources
Helixi902 – 9054Combined sources
Beta strandi906 – 9127Combined sources
Beta strandi915 – 9173Combined sources
Beta strandi921 – 9244Combined sources
Helixi929 – 9313Combined sources
Helixi932 – 94211Combined sources
Beta strandi946 – 9494Combined sources
Beta strandi953 – 9553Combined sources
Beta strandi967 – 9737Combined sources
Beta strandi976 – 98510Combined sources
Beta strandi987 – 99812Combined sources
Beta strandi1016 – 10238Combined sources
Beta strandi1028 – 10314Combined sources
Helixi1036 – 104712Combined sources
Beta strandi1056 – 10649Combined sources
Helixi1065 – 108218Combined sources
Beta strandi1084 – 10863Combined sources
Helixi1088 – 10958Combined sources
Turni1096 – 10983Combined sources
Helixi1106 – 112116Combined sources
Helixi1129 – 11313Combined sources
Helixi1132 – 11398Combined sources
Helixi1149 – 11579Combined sources
Beta strandi1172 – 11743Combined sources
Beta strandi1207 – 12115Combined sources
Beta strandi1219 – 12246Combined sources
Helixi1228 – 12303Combined sources
Helixi1231 – 124111Combined sources
Beta strandi1245 – 12484Combined sources
Beta strandi1270 – 12723Combined sources
Beta strandi1275 – 128612Combined sources
Beta strandi1292 – 130514Combined sources
Beta strandi1308 – 13158Combined sources
Beta strandi1318 – 13203Combined sources
Helixi1326 – 13283Combined sources
Helixi1329 – 134012Combined sources
Beta strandi1347 – 13548Combined sources
Helixi1356 – 137419Combined sources
Beta strandi1375 – 13773Combined sources
Helixi1379 – 138911Combined sources
Helixi1397 – 140812Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP23470.
SMRiP23470. Positions 58-320, 347-445, 826-1412.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23470.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 321264Alpha-carbonic anhydraseAdd
BLAST
Domaini349 – 448100Fibronectin type-IIIPROSITE-ProRule annotationAdd
BLAST
Domaini848 – 1119272Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
BLAST
Domaini1150 – 1410261Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1060 – 10667Substrate bindingBy similarity

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00760000118900.
HOGENOMiHOG000060222.
HOVERGENiHBG053760.
InParanoidiP23470.
KOiK16667.
OMAiWRGCNKI.
OrthoDBiEOG7K6PT4.
PhylomeDBiP23470.
TreeFamiTF351978.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.10.200.10. 1 hit.
3.90.190.10. 2 hits.
InterProiIPR001148. 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]
PfamiPF00194. Carb_anhydrase. 1 hit.
PF00041. fn3. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM01057. Carb_anhydrase. 1 hit.
SM00060. FN3. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF51069. SSF51069. 1 hit.
SSF52799. SSF52799. 2 hits.
PROSITEiPS51144. 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]

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: P23470-1) [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
MRRLLEPCWW ILFLKITSSV LHYVVCFPAL TEGYVGALHE NRHGSAVQIR
60 70 80 90 100
RRKASGDPYW AYSGAYGPEH WVTSSVSCGG RHQSPIDILD QYARVGEEYQ
110 120 130 140 150
ELQLDGFDNE SSNKTWMKNT GKTVAILLKD DYFVSGAGLP GRFKAEKVEF
160 170 180 190 200
HWGHSNGSAG SEHSINGRRF PVEMQIFFYN PDDFDSFQTA ISENRIIGAM
210 220 230 240 250
AIFFQVSPRD NSALDPIIHG LKGVVHHEKE TFLDPFVLRD LLPASLGSYY
260 270 280 290 300
RYTGSLTTPP CSEIVEWIVF RRPVPISYHQ LEAFYSIFTT EQQDHVKSVE
310 320 330 340 350
YLRNNFRPQQ RLHDRVVSKS AVRDSWNHDM TDFLENPLGT EASKVCSSPP
360 370 380 390 400
IHMKVQPLNQ TALQVSWSQP ETIYHPPIMN YMISYSWTKN EDEKEKTFTK
410 420 430 440 450
DSDKDLKATI SHVSPDSLYL FRVQAVCRND MRSDFSQTML FQANTTRIFQ
460 470 480 490 500
GTRIVKTGVP TASPASSADM APISSGSSTW TSSGIPFSFV SMATGMGPSS
510 520 530 540 550
SGSQATVASV VTSTLLAGLG FGGGGISSFP STVWPTRLPT AASASKQAAR
560 570 580 590 600
PVLATTEALA SPGPDGDSSP TKDGEGTEEG EKDEKSESED GEREHEEDGE
610 620 630 640 650
KDSEKKEKSG VTHAAEERNQ TEPSPTPSSP NRTAEGGHQT IPGHEQDHTA
660 670 680 690 700
VPTDQTGGRR DAGPGLDPDM VTSTQVPPTA TEEQYAGSDP KRPEMPSKKP
710 720 730 740 750
MSRGDRFSED SRFITVNPAE KNTSGMISRP APGRMEWIIP LIVVSALTFV
760 770 780 790 800
CLILLIAVLV YWRGCNKIKS KGFPRRFREV PSSGERGEKG SRKCFQTAHF
810 820 830 840 850
YVEDSSSPRV VPNESIPIIP IPDDMEAIPV KQFVKHIGEL YSNNQHGFSE
860 870 880 890 900
DFEEVQRCTA DMNITAEHSN HPENKHKNRY INILAYDHSR VKLRPLPGKD
910 920 930 940 950
SKHSDYINAN YVDGYNKAKA YIATQGPLKS TFEDFWRMIW EQNTGIIVMI
960 970 980 990 1000
TNLVEKGRRK CDQYWPTENS EEYGNIIVTL KSTKIHACYT VRRFSIRNTK
1010 1020 1030 1040 1050
VKKGQKGNPK GRQNERVVIQ YHYTQWPDMG VPEYALPVLT FVRRSSAARM
1060 1070 1080 1090 1100
PETGPVLVHC SAGVGRTGTY IVIDSMLQQI KDKSTVNVLG FLKHIRTQRN
1110 1120 1130 1140 1150
YLVQTEEQYI FIHDALLEAI LGKETEVSSN QLHSYVNSIL IPGVGGKTRL
1160 1170 1180 1190 1200
EKQFKLVTQC NAKYVECFSA QKECNKEKNR NSSVVPSERA RVGLAPLPGM
1210 1220 1230 1240 1250
KGTDYINASY IMGYYRSNEF IITQHPLPHT TKDFWRMIWD HNAQIIVMLP
1260 1270 1280 1290 1300
DNQSLAEDEF VYWPSREESM NCEAFTVTLI SKDRLCLSNE EQIIIHDFIL
1310 1320 1330 1340 1350
EATQDDYVLE VRHFQCPKWP NPDAPISSTF ELINVIKEEA LTRDGPTIVH
1360 1370 1380 1390 1400
DEYGAVSAGM LCALTTLSQQ LENENAVDVF QVAKMINLMR PGVFTDIEQY
1410 1420 1430 1440
QFIYKAMLSL VSTKENGNGP MTVDKNGAVL IADESDPAES MESLV
Length:1,445
Mass (Da):162,003
Last modified:May 5, 2009 - v4
Checksum:iA48A007BA14082BC
GO
Isoform 2 (identifier: P23470-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     764-792: Missing.

Note: No experimental confirmation available.

Show »
Length:1,416
Mass (Da):158,771
Checksum:i8DFA46915A799CFD
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801G → S in AAA60224. (PubMed:8382771)Curated
Sequence conflicti549 – 5491A → V in AAC50439. (PubMed:8833149)Curated
Sequence conflicti756 – 7561I → T in AAC50439. (PubMed:8833149)Curated
Sequence conflicti805 – 8051S → R in CAH18125. (PubMed:17974005)Curated
Sequence conflicti1316 – 13161C → Y in CAH18125. (PubMed:17974005)Curated
Sequence conflicti1407 – 14071M → R in AAA60224. (PubMed:8382771)Curated
Sequence conflicti1407 – 14071M → R in AAC50439. (PubMed:8833149)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti92 – 921Y → H.2 Publications
Corresponds to variant rs62620047 [ dbSNP | Ensembl ].
VAR_070892
Natural varianti574 – 5741G → S.
Corresponds to variant rs2292245 [ dbSNP | Ensembl ].
VAR_020301
Natural varianti639 – 6391Q → R.
Corresponds to variant rs9870460 [ dbSNP | Ensembl ].
VAR_031562

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei764 – 79229Missing in isoform 2. 2 PublicationsVSP_024353Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09247 mRNA. Translation: AAA60224.1.
U46116
, 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.
CCDSiCCDS2895.1. [P23470-1]
PIRiA48148.
RefSeqiNP_002832.3. NM_002841.3. [P23470-1]
XP_005265410.1. XM_005265353.2. [P23470-2]
UniGeneiHs.595541.

Genome annotation databases

EnsembliENST00000295874; ENSP00000295874; ENSG00000144724. [P23470-2]
ENST00000474889; ENSP00000418112; ENSG00000144724. [P23470-1]
GeneIDi5793.
KEGGihsa:5793.
UCSCiuc003dlb.3. human. [P23470-1]
uc003dlc.3. human. [P23470-2]

Polymorphism databases

DMDMi229463033.

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
L09247 mRNA. Translation: AAA60224.1 .
U46116
, 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 .
CCDSi CCDS2895.1. [P23470-1 ]
PIRi A48148.
RefSeqi NP_002832.3. NM_002841.3. [P23470-1 ]
XP_005265410.1. XM_005265353.2. [P23470-2 ]
UniGenei Hs.595541.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2H4V X-ray 1.55 A/B 831-1127 [» ]
2HY3 X-ray 2.60 A/B 820-1130 [» ]
2NLK X-ray 2.40 A 827-1445 [» ]
2PBN X-ray 1.70 A 820-1130 [» ]
3JXH X-ray 1.70 C 56-320 [» ]
3QCB X-ray 2.10 A/B 825-1128 [» ]
3QCC X-ray 2.10 A/B 825-1128 [» ]
3QCD X-ray 1.80 A 825-1128 [» ]
3QCE X-ray 2.10 A/B 825-1128 [» ]
3QCF X-ray 2.50 A/B 825-1128 [» ]
3QCG X-ray 2.05 A 825-1128 [» ]
3QCH X-ray 2.40 A 825-1128 [» ]
3QCI X-ray 2.27 A 825-1128 [» ]
3QCJ X-ray 2.26 A 825-1128 [» ]
3QCK X-ray 2.05 A 825-1128 [» ]
3QCL X-ray 2.40 A 825-1128 [» ]
3QCM X-ray 2.40 A/B 825-1128 [» ]
3QCN X-ray 2.41 A 825-1128 [» ]
ProteinModelPortali P23470.
SMRi P23470. Positions 58-320, 347-445, 826-1412.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111757. 11 interactions.
IntActi P23470. 22 interactions.
MINTi MINT-1349880.
STRINGi 9606.ENSP00000418112.

Chemistry

BindingDBi P23470.
ChEMBLi CHEMBL4905.

PTM databases

PhosphoSitei P23470.

Polymorphism databases

DMDMi 229463033.

Proteomic databases

MaxQBi P23470.
PaxDbi P23470.
PRIDEi P23470.

Protocols and materials databases

DNASUi 5793.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000295874 ; ENSP00000295874 ; ENSG00000144724 . [P23470-2 ]
ENST00000474889 ; ENSP00000418112 ; ENSG00000144724 . [P23470-1 ]
GeneIDi 5793.
KEGGi hsa:5793.
UCSCi uc003dlb.3. human. [P23470-1 ]
uc003dlc.3. human. [P23470-2 ]

Organism-specific databases

CTDi 5793.
GeneCardsi GC03P061522.
H-InvDB HIX0024329.
HGNCi HGNC:9671. PTPRG.
MIMi 176886. gene.
neXtProti NX_P23470.
PharmGKBi PA34016.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
GeneTreei ENSGT00760000118900.
HOGENOMi HOG000060222.
HOVERGENi HBG053760.
InParanoidi P23470.
KOi K16667.
OMAi WRGCNKI.
OrthoDBi EOG7K6PT4.
PhylomeDBi P23470.
TreeFami TF351978.

Enzyme and pathway databases

SignaLinki P23470.

Miscellaneous databases

ChiTaRSi PTPRG. human.
EvolutionaryTracei P23470.
GeneWikii PTPRG.
GenomeRNAii 5793.
NextBioi 22556.
PROi P23470.
SOURCEi Search...

Gene expression databases

Bgeei P23470.
CleanExi HS_PTPRG.
ExpressionAtlasi P23470. baseline and differential.
Genevestigatori P23470.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
3.10.200.10. 1 hit.
3.90.190.10. 2 hits.
InterProi IPR001148. 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 ]
Pfami PF00194. Carb_anhydrase. 1 hit.
PF00041. fn3. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view ]
PRINTSi PR00700. PRTYPHPHTASE.
SMARTi SM01057. Carb_anhydrase. 1 hit.
SM00060. FN3. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 1 hit.
SSF51069. SSF51069. 1 hit.
SSF52799. SSF52799. 2 hits.
PROSITEi PS51144. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiPTPRG_HUMAN
AccessioniPrimary (citable) accession number: P23470
Secondary accession number(s): B2RU12
, B7ZLX5, Q15623, Q59EE0, Q68DU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: May 5, 2009
Last modified: November 26, 2014
This is version 162 of the entry and version 4 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, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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