ID PTN4_HUMAN Reviewed; 926 AA. AC P29074; B2RBV8; Q9UDA7; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 15-FEB-2017, entry version 165. DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 4; DE EC=3.1.3.48; DE AltName: Full=Protein-tyrosine phosphatase MEG1; DE Short=MEG; DE Short=PTPase-MEG1; GN Name=PTPN4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1648233; DOI=10.1073/pnas.88.13.5867; RA Gu M., York J.D., Warshawsky I., Majerus P.W.; RT "Identification, cloning, and expression of a cytosolic megakaryocyte RT protein-tyrosine-phosphatase with sequence homology to cytoskeletal RT protein 4.1."; RL Proc. Natl. Acad. Sci. U.S.A. 88:5867-5871(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 745-858. RC TISSUE=Leukemia; RX PubMed=8483328; RA Honda H., Shibuya M., Chiba S., Yazaki Y., Hirai H.; RT "Identification of novel protein-tyrosine phosphatases in a human RT leukemia cell line, F-36P."; RL Leukemia 7:742-746(1993). RN [5] RP STRUCTURE BY NMR OF 507-612. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of PDZ domain of protein tyrosine phosphatase, RT non-receptor type 4."; RL Submitted (NOV-2005) to the PDB data bank. CC -!- FUNCTION: May act at junctions between the membrane and the CC cytoskeleton. CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein CC tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}. CC -!- INTERACTION: CC P46108:CRK; NbExp=3; IntAct=EBI-710431, EBI-886; CC Q92993:KAT5; NbExp=2; IntAct=EBI-710431, EBI-399080; CC P53778:MAPK12; NbExp=2; IntAct=EBI-710431, EBI-602406; CC P16333:NCK1; NbExp=3; IntAct=EBI-710431, EBI-389883; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. CC Cytoplasm, cytoskeleton {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. CC Non-receptor class subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M68941; AAA36530.1; -; mRNA. DR EMBL; AK314836; BAG37355.1; -; mRNA. DR EMBL; BC010674; AAH10674.1; -; mRNA. DR CCDS; CCDS2129.1; -. DR PIR; A41105; A41105. DR RefSeq; NP_002821.1; NM_002830.3. DR RefSeq; XP_016860089.1; XM_017004600.1. DR UniGene; Hs.469809; -. DR PDB; 2CS5; NMR; -; A=507-612. DR PDB; 2I75; X-ray; 2.45 A; A=611-926. DR PDB; 2VPH; X-ray; 1.90 A; A/B=513-606. DR PDB; 3NFK; X-ray; 1.43 A; A/B=499-604. DR PDB; 3NFL; X-ray; 1.91 A; A/B/C/D=499-604. DR PDB; 5EYZ; X-ray; 2.09 A; A/B/C/D=499-604. DR PDB; 5EZ0; X-ray; 2.35 A; A/B/C/D=499-604. DR PDBsum; 2CS5; -. DR PDBsum; 2I75; -. DR PDBsum; 2VPH; -. DR PDBsum; 3NFK; -. DR PDBsum; 3NFL; -. DR PDBsum; 5EYZ; -. DR PDBsum; 5EZ0; -. DR ProteinModelPortal; P29074; -. DR SMR; P29074; -. DR BioGrid; 111741; 12. DR DIP; DIP-34634N; -. DR IntAct; P29074; 14. DR MINT; MINT-1367896; -. DR STRING; 9606.ENSP00000263708; -. DR BindingDB; P29074; -. DR ChEMBL; CHEMBL3165; -. DR DrugBank; DB00630; Alendronate. DR DEPOD; P29074; -. DR iPTMnet; P29074; -. DR PhosphoSitePlus; P29074; -. DR BioMuta; PTPN4; -. DR DMDM; 131531; -. DR EPD; P29074; -. DR PaxDb; P29074; -. DR PeptideAtlas; P29074; -. DR PRIDE; P29074; -. DR DNASU; 5775; -. DR Ensembl; ENST00000263708; ENSP00000263708; ENSG00000088179. DR GeneID; 5775; -. DR KEGG; hsa:5775; -. DR UCSC; uc002tmf.3; human. DR CTD; 5775; -. DR DisGeNET; 5775; -. DR GeneCards; PTPN4; -. DR HGNC; HGNC:9656; PTPN4. DR HPA; HPA019351; -. DR MIM; 176878; gene. DR neXtProt; NX_P29074; -. DR OpenTargets; ENSG00000088179; -. DR PharmGKB; PA34000; -. DR eggNOG; ENOG410KDUQ; Eukaryota. DR eggNOG; COG5599; LUCA. DR GeneTree; ENSGT00760000118823; -. DR HOGENOM; HOG000007048; -. DR HOVERGEN; HBG008322; -. DR InParanoid; P29074; -. DR KO; K18037; -. DR OMA; RKLMDWE; -. DR OrthoDB; EOG091G016K; -. DR PhylomeDB; P29074; -. DR TreeFam; TF315900; -. DR BRENDA; 3.1.3.48; 2681. DR Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade. DR ChiTaRS; PTPN4; human. DR EvolutionaryTrace; P29074; -. DR GeneWiki; PTPN4; -. DR GenomeRNAi; 5775; -. DR PMAP-CutDB; P29074; -. DR PRO; PR:P29074; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000088179; -. DR CleanEx; HS_PTPN4; -. DR ExpressionAtlas; P29074; baseline and differential. DR Genevisible; P29074; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; TAS:ProtInc. DR GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc. DR Gene3D; 1.20.80.10; -; 1. DR Gene3D; 2.30.29.30; -; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 3.90.190.10; -; 1. DR InterPro; IPR019749; Band_41_domain. DR InterPro; IPR014847; FERM-adjacent. DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx. DR InterPro; IPR019748; FERM_central. DR InterPro; IPR019747; FERM_CS. DR InterPro; IPR000299; FERM_domain. DR InterPro; IPR018979; FERM_N. DR InterPro; IPR018980; FERM_PH-like_C. DR InterPro; IPR001478; PDZ. DR InterPro; IPR011993; PH_dom-like. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR000242; PTPase_domain. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR003595; Tyr_Pase_cat. DR InterPro; IPR012151; Tyr_Pase_non-rcpt_typ-3/4. DR InterPro; IPR000387; TYR_PHOSPHATASE_dom. DR InterPro; IPR029071; Ubiquitin-rel_dom. DR Pfam; PF08736; FA; 1. DR Pfam; PF09380; FERM_C; 1. DR Pfam; PF00373; FERM_M; 1. DR Pfam; PF09379; FERM_N; 1. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF00102; Y_phosphatase; 1. DR PIRSF; PIRSF000927; Tyr-Ptase_nr3; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00295; B41; 1. DR SMART; SM01195; FA; 1. DR SMART; SM01196; FERM_C; 1. DR SMART; SM00228; PDZ; 1. DR SMART; SM00194; PTPc; 1. DR SMART; SM00404; PTPc_motif; 1. DR SUPFAM; SSF47031; SSF47031; 1. DR SUPFAM; SSF50156; SSF50156; 1. DR SUPFAM; SSF50729; SSF50729; 1. DR SUPFAM; SSF52799; SSF52799; 1. DR SUPFAM; SSF54236; SSF54236; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Cytoplasm; KW Cytoskeleton; Hydrolase; Membrane; Phosphoprotein; Polymorphism; KW Protein phosphatase; Reference proteome. FT CHAIN 1 926 Tyrosine-protein phosphatase non-receptor FT type 4. FT /FTId=PRO_0000219434. FT DOMAIN 29 312 FERM. {ECO:0000255|PROSITE- FT ProRule:PRU00084}. FT DOMAIN 517 589 PDZ. {ECO:0000255|PROSITE- FT ProRule:PRU00143}. FT DOMAIN 655 911 Tyrosine-protein phosphatase. FT {ECO:0000255|PROSITE-ProRule:PRU00160}. FT REGION 852 858 Substrate binding. {ECO:0000250}. FT ACT_SITE 852 852 Phosphocysteine intermediate. FT {ECO:0000255|PROSITE-ProRule:PRU00160, FT ECO:0000255|PROSITE-ProRule:PRU10044}. FT BINDING 820 820 Substrate. {ECO:0000250}. FT BINDING 896 896 Substrate. {ECO:0000250}. FT MOD_RES 474 474 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9WU22}. FT VARIANT 924 924 T -> S (in dbSNP:rs3189128). FT /FTId=VAR_061033. FT CONFLICT 131 131 K -> E (in Ref. 2; BAG37355). FT {ECO:0000305}. FT CONFLICT 772 772 G -> K (in Ref. 4; no nucleotide entry). FT {ECO:0000305}. FT CONFLICT 863 863 I -> V (in Ref. 2; BAG37355). FT {ECO:0000305}. FT STRAND 516 520 {ECO:0000244|PDB:3NFK}. FT STRAND 524 526 {ECO:0000244|PDB:2CS5}. FT STRAND 530 535 {ECO:0000244|PDB:3NFK}. FT HELIX 536 538 {ECO:0000244|PDB:3NFK}. FT STRAND 540 547 {ECO:0000244|PDB:3NFK}. FT STRAND 549 551 {ECO:0000244|PDB:2CS5}. FT HELIX 552 555 {ECO:0000244|PDB:3NFK}. FT STRAND 556 558 {ECO:0000244|PDB:3NFK}. FT STRAND 565 569 {ECO:0000244|PDB:3NFK}. FT HELIX 579 587 {ECO:0000244|PDB:3NFK}. FT HELIX 589 591 {ECO:0000244|PDB:3NFK}. FT STRAND 596 602 {ECO:0000244|PDB:3NFK}. FT HELIX 639 651 {ECO:0000244|PDB:2I75}. FT HELIX 654 661 {ECO:0000244|PDB:2I75}. FT TURN 677 679 {ECO:0000244|PDB:2I75}. FT HELIX 680 682 {ECO:0000244|PDB:2I75}. FT HELIX 692 694 {ECO:0000244|PDB:2I75}. FT STRAND 695 697 {ECO:0000244|PDB:2I75}. FT STRAND 704 713 {ECO:0000244|PDB:2I75}. FT STRAND 720 726 {ECO:0000244|PDB:2I75}. FT HELIX 731 733 {ECO:0000244|PDB:2I75}. FT HELIX 734 743 {ECO:0000244|PDB:2I75}. FT STRAND 748 751 {ECO:0000244|PDB:2I75}. FT STRAND 755 757 {ECO:0000244|PDB:2I75}. FT STRAND 773 776 {ECO:0000244|PDB:2I75}. FT STRAND 779 783 {ECO:0000244|PDB:2I75}. FT STRAND 790 801 {ECO:0000244|PDB:2I75}. FT TURN 802 805 {ECO:0000244|PDB:2I75}. FT STRAND 806 815 {ECO:0000244|PDB:2I75}. FT STRAND 820 823 {ECO:0000244|PDB:2I75}. FT HELIX 828 841 {ECO:0000244|PDB:2I75}. FT STRAND 848 851 {ECO:0000244|PDB:2I75}. FT STRAND 853 857 {ECO:0000244|PDB:2I75}. FT HELIX 858 873 {ECO:0000244|PDB:2I75}. FT HELIX 880 888 {ECO:0000244|PDB:2I75}. FT HELIX 898 911 {ECO:0000244|PDB:2I75}. SQ SEQUENCE 926 AA; 105911 MW; 4DAC6A87A675CFB0 CRC64; MTSRFRLPAG RTYNVRASEL ARDRQHTEVV CNILLLDNTV QAFKVNKHDQ GQVLLDVVFK HLDLTEQDYF GLQLADDSTD NPRWLDPNKP IRKQLKRGSP YSLNFRVKFF VSDPNKLQEE YTRYQYFLQI KQDILTGRLP CPSNTAALLA SFAVQSELGD YDQSENLSGY LSDYSFIPNQ PQDFEKEIAK LHQQHIGLSP AEAEFNYLNT ARTLELYGVE FHYARDQSNN EIMIGVMSGG ILIYKNRVRM NTFPWLKIVK ISFKCKQFFI QLRKELHESR ETLLGFNMVN YRACKNLWKA CVEHHTFFRL DRPLPPQKNF FAHYFTLGSK FRYCGRTEVQ SVQYGKEKAN KDRVFARSPS KPLARKLMDW EVVSRNSISD DRLETQSLPS RSPPGTPNHR NSTFTQEGTR LRPSSVGHLV DHMVHTSPSE VFVNQRSPSS TQANSIVLES SPSQETPGDG KPPALPPKQS KKNSWNQIHY SHSQQDLESH INETFDIPSS PEKPTPNGGI PHDNLVLIRM KPDENGRFGF NVKGGYDQKM PVIVSRVAPG TPADLCVPRL NEGDQVVLIN GRDIAEHTHD QVVLFIKASC ERHSGELMLL VRPNAVYDVV EEKLENEPDF QYIPEKAPLD SVHQDDHSLR ESMIQLAEGL ITGTVLTQFD QLYRKKPGMT MSCAKLPQNI SKNRYRDISP YDATRVILKG NEDYINANYI NMEIPSSSII NQYIACQGPL PHTCTDFWQM TWEQGSSMVV MLTTQVERGR VKCHQYWPEP TGSSSYGCYQ VTCHSEEGNT AYIFRKMTLF NQEKNESRPL TQIQYIAWPD HGVPDDSSDF LDFVCHVRNK RAGKEEPVVV HCSAGIGRTG VLITMETAMC LIECNQPVYP LDIVRTMRDQ RAMMIQTPSQ YRFVCEAILK VYEEGFVKPL TTSTNK //