Statistics
241 human active and 13 inactive phosphatases in total;
194 phosphatases have substrate data;
--------------------------------
336 protein substrates;
83 non-protein substrates;
1215 dephosphorylation interactions;
--------------------------------
299 KEGG pathways;
876 Reactome pathways;
--------------------------------
last scientific update:
11 Mar, 2019
194 phosphatases have substrate data;
--------------------------------
336 protein substrates;
83 non-protein substrates;
1215 dephosphorylation interactions;
--------------------------------
299 KEGG pathways;
876 Reactome pathways;
--------------------------------
last scientific update:
11 Mar, 2019
Top
PTPRQ
Gene Name  | PTPRQ (QuickGO) | (A quick tutorial to explore the interactive visualization) |
| Synonyms | PTPRQ | |
| Protein Name | PTPRQ |
|
|
Alternative Name(s) |
Phosphatidylinositol phosphatase PTPRQ;3.1.3.-;Receptor-type tyrosine-protein phosphatase Q;PTP-RQ;R-PTP-Q;3.1.3.48; | |
| EntrezGene ID | NA (Comparative Toxicogenomics) | |
| UniProt AC (Human) | Q9UMZ3 (protein sequence) | |
| Enzyme Class | EC 3.1.3.48 (BRENDA ) | |
| Molecular Weight | 260924 Dalton | |
| Protein Length | 2332 amino acids (AA) | |
| Genome Browsers | NCBI | ENSG00000139304 (Ensembl) | UCSC | |
| Crosslinking annotations | Query our ID-mapping table | |
| Orthologues | Quest For Orthologues (QFO) | GeneTree | |
| Classification | Superfamily: Class I Cys-based PTPs --> Family: R-PTP | Historic class: Class I Cys-based PTPs --> Classical PTPs --> Receptor-type PTPs (R-PTPs) | CATH ID: 3.90.190.10 | SCOP Fold: CC1 | |
| Phosphatase activity | active | Catalytic signature motif: HCSAGVGR | |
| Domain organization, Expression, Diseases | (show / hide) |
| Protein Domain | InterPro | Pfam | SMART | 3D Structure | PDB | DrugPort | ModBase | SwissModel |
| Polypeptide organization (Pfam) | No Pfam domain found | ||
| Catalytic Site | Mechanism and Catalytic Site Atlas | ||
| Gene Expression | Gene Expression Atlas | Diseases | OMIM | ClinVar |
| Protein-protein interactions | STRING | IntAct | MINT | BioGRID | ||
| Phosphosites | Phospho.ELM | PhosphoSitePlus | ||
| Localization, Function, Catalytic activity and Sequence | (show / hide) |
| Localization (UniProt annotation) | |||
| Membrane | |||
| Function (UniProt annotation) | |||
| Phosphatidylinositol phosphatase required for auditoryfunction May act by regulating the level of phosphatidylinositol4,5-bisphosphate (PIP2) level in the basal region of hair bundlesCan dephosphorylate a broad range of phosphatidylinositolphosphates, including phosphatidylinositol 3,4,5-trisphosphate andmost phosphatidylinositol monophosphates and diphosphatesPhosphate can be hydrolyzed from the D3 and D5 positions in theinositol ring Has low tyrosine-protein phosphatase activity;however, the relevance of such activity in vivo is unclear Playsan important role in adipogenesis of mesenchymal stem cells(MSCs) Regulates the phosphorylation state of AKT1 by suppressingthe phosphatidylinositol 3,4,5-trisphosphate (PIP3) level in MSCsand preadipocyte cells | |||
| Catalytic Activity (UniProt annotation) | |||
| Protein tyrosine phosphate + H(2)O = proteintyrosine + phosphate | |||
| Protein Sequence | |||
| MKKVPIKPEQPEKLRAFNISTHSFSLHWSLPSGHVERYQVDLVPDSGFVTIRDLGGGEYQVDVSNVVPGTRYDITISSIS TTYTSPVTRIVTTNVTKPGPPVFLAGERVGSAGILLSWNTPPNPNGRIISYIVKYKEVCPWMQTVYTQVRSKPDSLEVLL TNLNPGTTYEIKVAAENSAGIGVFSDPFLFQTAESAPGKVVNLTVEAYNASAVKLIWYLPRQPNGKITSFKISVKHARSG IVVKDVSIRVEDILTGKLPECNENSESFLWSTASPSPTLGRVTPPSRTTHSSSTLTQNEISSVWKEPISFVVTHLRPYTT YLFEVSAVTTEAGYIDSTIVRTPESVPEGPPQNCVTGNITGKSFSILWDPPTIVTGKFSYRVELYGPSGRILDNSTKDLK FAFTNLTPFTMYDVYIAAETSAGTGPKSNISVFTPPDVPGAVFDLQLAEVESTQVRITWKKPRQPNGIINQYRVKVLVPE TGIILENTLLTGNNEYINDPMAPEIVNIVEPMVGLYEGSAEMSSDLHSLATFIYNSHPDKNFPARNRAEDQTSPVVTTRN QYITDIAAEQLSYVIRRLVPFTEHMISVSAFTIMGEGPPTVLSVRTRQQVPSSIKIINYKNISSSSILLYWDPPEYPNGK ITHYTIYAMELDTNRAFQITTIDNSFLITGLKKYTKYKMRVAASTHVGESSLSEENDIFVRTSEDEPESSPQDVEVIDVT ADEIRLKWSPPEKPNGIIIAYEVLYKNIDTLYMKNTSTTDIILRNLRPHTLYNISVRSYTRFGHGNQVSSLLSVRTSETV PDSAPENITYKNISSGEIELSFLPPSSPNGIIKKYTIYLKRSNGNEERTINTTSLTQNIKVLKKYTQYIIEVSASTLKGE GVRSAPISILTEEDAPDSPPQDFSVKQLSGVTVKLSWQPPLEPNGIILYYTVYVWNRSSLKTINVTETSLELSDLDYNVE YSAYVTASTRFGDGKTRSNIISFQTPEGAPSDPPKDVYYANLSSSSIILFWTPPSKPNGIIQYYSVYYRNTSGTFMQNFT LHEVTNDFDNMTVSTIIDKLTIFSYYTFWLTASTSVGNGNKSSDIIEVYTDQDIPEGFVGNLTYESISSTAINVSWVPPA QPNGLVFYYVSLILQQTPRHVRPPLVTYERSIYFDNLEKYTDYILKITPSTEKGFSDTYTAQLYIKTEEDVPETSPIINT FKNLSSTSVLLSWDPPVKPNGAIISYDLTLQGPNENYSFITSDNYIILEELSPFTLYSFFAAARTRKGLGPSSILFFYTD ESVPLAPPQNLTLINCTSDFVWLKWSPSPLPGGIVKVYSFKIHEHETDTIYYKNISGFKTEAKLVGLEPVSTYSIRVSAF TKVGNGNQFSNVVKFTTQESVPDVVQNMQCMATSWQSVLVKWDPPKKANGIITQYMVTVERNSTKVSPQDHMYTFIKLLA NTSYVFKVRASTSAGEGDESTCHVSTLPETVPSVPTNIAFSDVQSTSATLTWIRPDTILGYFQNYKITTQLRAQKCKEWE SEECVEYQKIQYLYEAHLTEETVYGLKKFRWYRFQVAASTNAGYGNASNWISTKTLPGPPDGPPENVHVVATSPFSISIS WSEPAVITGPTCYLIDVKSVDNDEFNISFIKSNEENKTIEIKDLEIFTRYSVVITAFTGNISAAYVEGKSSAEMIVTTLE SAPKDPPNNMTFQKIPDEVTKFQLTFLPPSQPNGNIQVYQALVYREDDPTAVQIHNLSIIQKTNTFVIAMLEGLKGGHTY NISVYAVNSAGAGPKVPMRITMDIKAPARPKTKPTPIYDATGKLLVTSTTITIRMPICYYSDDHGPIKNVQVLVTETGAQ HDGNVTKWYDAYFNKARPYFTNEGFPNPPCTEGKTKFSGNEEIYIIGADNACMIPGNEDKICNGPLKPKKQYLFKFRATN IMGQFTDSDYSDPVKTLGEGLSERTVEIILSVTLCILSIILLGTAIFAFARIRQKQKEGGTYSPQDAEIIDTKLKLDQLI TVADLELKDERLTRPISKKSFLQHVEELCTNNNLKFQEEFSELPKFLQDLSSTDADLPWNRAKNRFPNIKPYNNNRVKLI ADASVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTLVMLTQCFEKGRIRCHQYWPEDNKPVTVFG DIVITKLMEDVQIDWTIRDLKIERHGDCMTVRQCNFTAWPEHGVPENSAPLIHFVKLVRASRAHDTTPMIVHCSAGVGRT GVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQCILDLLSNKGSNQPICFVNYSALQKMDSLDAME GDVELEWEETTM |
| Motif information from Eukaryotic Linear Motif atlas (ELM) | (show / hide) |
ELM Motif | Motif Instance | Description | Motif Regex |
| NA | NA | NA | NA |
| Gene Ontology (P: Process; F: Function and C: Component terms) | (show / hide) | |
| GO:0004725 | F:protein tyrosine phosphatase activity |
| GO:0016021 | C:integral component of membrane |
| GO:0045598 | P:regulation of fat cell differentiation |
