ID PTN14_MOUSE Reviewed; 1189 AA.
AC Q62130; G5E8M1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 2.
DT 27-MAR-2024, entry version 176.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 14;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphatase PTP36;
GN Name=Ptpn14;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CB-17/SCID; TISSUE=Thymus;
RX PubMed=8074693; DOI=10.1006/bbrc.1994.2207;
RA Sawada M., Ogata M., Fujino Y., Hamaoka T.;
RT "cDNA cloning of a novel protein tyrosine phosphatase with homology to
RT cytoskeletal protein 4.1 and its expression in T-lineage cells.";
RL Biochem. Biophys. Res. Commun. 203:479-484(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20826270; DOI=10.1016/j.ajhg.2010.08.008;
RA Au A.C., Hernandez P.A., Lieber E., Nadroo A.M., Shen Y.M., Kelley K.A.,
RA Gelb B.D., Diaz G.A.;
RT "Protein tyrosine phosphatase PTPN14 is a regulator of lymphatic function
RT and choanal development in humans.";
RL Am. J. Hum. Genet. 87:436-444(2010).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-461; SER-486;
RP SER-593; SER-594 AND SER-833, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Protein tyrosine phosphatase which may play a role in the
CC regulation of lymphangiogenesis, cell-cell adhesion, cell-matrix
CC adhesion, cell migration, cell growth and also regulates TGF-beta gene
CC expression, thereby modulating epithelial-mesenchymal transition.
CC Mediates beta-catenin dephosphorylation at adhesion junctions. Acts as
CC a negative regulator of the oncogenic property of YAP, a downstream
CC target of the hippo pathway, in a cell density-dependent manner. May
CC function as a tumor suppressor. {ECO:0000269|PubMed:20826270}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBUNIT: Interacts with FLT4; the interaction is enhanced by
CC stimulation with VEGFC. Interacts (via PPxY motifs) with YAP1 (via WW
CC domains); this interaction leads to the cytoplasmic sequestration of
CC YAP1 and inhibits its transcriptional coactivator activity.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocation into the
CC nucleus is associated with induction of cell proliferation. Partially
CC colocalized with actin filaments at the plasma membrane. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Thymus; in cells of both hematopoietic and non-
CC hematopoietic origins.
CC -!- PTM: Ubiquitinated by the ECS (Elongin BC-CUL2/5-SOCS-box protein)/LRR1
CC E3 ligase complex and subsequently targeted to proteasomal degradation.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: PTPN14 deficient mice have swelling of the limbs
CC or periorbital edema. These mice also show hyperplasia of lymphatic
CC capillaries of the ears. There is no evidence of choanal atresia or any
CC overtly dysmorphic features. {ECO:0000269|PubMed:20826270}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
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DR EMBL; D31842; BAA06628.1; -; mRNA.
DR EMBL; AC140250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC140461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466555; EDL13025.1; -; Genomic_DNA.
DR EMBL; CH466555; EDL13028.1; -; Genomic_DNA.
DR CCDS; CCDS15609.1; -.
DR PIR; JC2366; JC2366.
DR RefSeq; NP_033002.2; NM_008976.2.
DR RefSeq; XP_006497192.1; XM_006497129.3.
DR RefSeq; XP_006497193.1; XM_006497130.3.
DR RefSeq; XP_006497194.1; XM_006497131.3.
DR RefSeq; XP_006497196.1; XM_006497133.3.
DR AlphaFoldDB; Q62130; -.
DR SMR; Q62130; -.
DR BioGRID; 202480; 13.
DR IntAct; Q62130; 1.
DR STRING; 10090.ENSMUSP00000095051; -.
DR iPTMnet; Q62130; -.
DR PhosphoSitePlus; Q62130; -.
DR jPOST; Q62130; -.
DR MaxQB; Q62130; -.
DR PaxDb; 10090-ENSMUSP00000095051; -.
DR PeptideAtlas; Q62130; -.
DR ProteomicsDB; 291628; -.
DR Pumba; Q62130; -.
DR Antibodypedia; 34618; 194 antibodies from 28 providers.
DR DNASU; 19250; -.
DR Ensembl; ENSMUST00000097442.9; ENSMUSP00000095051.3; ENSMUSG00000026604.18.
DR GeneID; 19250; -.
DR KEGG; mmu:19250; -.
DR UCSC; uc007eau.1; mouse.
DR AGR; MGI:102467; -.
DR CTD; 5784; -.
DR MGI; MGI:102467; Ptpn14.
DR VEuPathDB; HostDB:ENSMUSG00000026604; -.
DR eggNOG; KOG0792; Eukaryota.
DR GeneTree; ENSGT00940000156874; -.
DR InParanoid; Q62130; -.
DR OMA; FKKCRQY; -.
DR OrthoDB; 3108587at2759; -.
DR PhylomeDB; Q62130; -.
DR TreeFam; TF315900; -.
DR BRENDA; 3.1.3.48; 3474.
DR BioGRID-ORCS; 19250; 0 hits in 82 CRISPR screens.
DR ChiTaRS; Ptpn14; mouse.
DR PRO; PR:Q62130; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q62130; Protein.
DR Bgee; ENSMUSG00000026604; Expressed in endothelial cell of lymphatic vessel and 187 other cell types or tissues.
DR ExpressionAtlas; Q62130; baseline and differential.
DR Genevisible; Q62130; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0001946; P:lymphangiogenesis; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0046825; P:regulation of protein export from nucleus; ISS:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13188; FERM_C_PTPN14_PTPN21; 1.
DR CDD; cd17191; FERM_F1_PTPN14; 1.
DR CDD; cd14599; PTPc-N14; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR014392; PTP_non-rcpt_14/21.
DR InterPro; IPR041782; PTPN14/21_FERM_C.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45706; TYROSINE-PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR45706:SF6; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 14; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000934; Tyr-Ptase_nr14; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM01196; FERM_C; 1.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 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 Cytoplasm; Cytoskeleton; Hydrolase; Nucleus; Phosphoprotein;
KW Protein phosphatase; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1189
FT /note="Tyrosine-protein phosphatase non-receptor type 14"
FT /id="PRO_0000219438"
FT DOMAIN 21..306
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 911..1182
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 744..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1123
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 1123..1129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1167
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15678"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15678"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 23
FT /note="T -> A (in Ref. 1; BAA06628)"
FT /evidence="ECO:0000305"
FT CONFLICT 887
FT /note="H -> R (in Ref. 1; BAA06628)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1189 AA; 135042 MW; 7FAFED60C5145477 CRC64;
MPFGLKLRRT RRYNVLSKNC FVTRIRLLDS NVIECTLSVE STGQECLEAV AQRLELRETH
YFGLWFLSKS QQARWVELEK PLKKHLDKFA NEPLLFFGVM FYVPNVSRLQ QEATRYQYYL
QVKKDVLEGR LRCSLEQVIR LAGLAVQADF GDYNQFDSQE FLREYVLFPM DLAMEEAALE
ELTQKVAQEH KAHSGILPAE AELMYINEVE RLDGFGQEIF PVKDSHGNSV HLGIFFMGIF
VRNRVGRQAV IYRWNDIGSV THSKAAILLE LIDKEETALF HTDDIENAKY ISRLFTTRHK
FYKQNKICTE QSNSPPPIRR QPTWSRSSLP RQQPYILPPM HVQCSEHYSE THTSQDSIFP
GNEEALYCRS HNSLDLNYLN GTVTNGSVCS VHSVNSLSCS QSFIQASPVS SNLSIPGSDI
MRADYIPSHR HSTIIVPSYR PTPDYETVMR QMKRGLMHAD SQSRSLRNLN IINTHAYNQP
EELVYSQPEM RERHPYTVPY AHQGCYGHKL VSPSDQMNPQ NCAMPIKPGA SSISHTVSTP
ELANMQLQGA QHYSTAHMLK NYLFRPPPPY PRPRPATSTP DLASHRHKYV SGSSPDLVTR
KVQLSVKTFQ EDSSPVVHQS LQEVSEPLTA TKHHGGGGGT VNKRHSLEVM NSMVRGMEAM
TLKSLNIPMA RRNTLREQGP SEETGGHEVH GLPQYHHKKT FSDATMLIHS SESEEEEETL
EAAPQVPVLR EKVEYSAQLQ AALARIPNRP PPEYPGPRKS VSNGALRQDQ GTPLPAMARC
RVLRHGPSKA LSVSRAEQLA VNGASLGPSI SEPDLTSVKE RVKKEPVKER PVSEMFSLED
SIIEREMMIR NLEKQKMTGP QAQKRPLMLA ALNGLSVARV SGREDGHHDA TRVPIDERLR
ALKKKLEDGM VFTEYEQIPN KKANGVFSTA TLPENAERSR IREVVPYEEN RVELIPTKEN
NTGYINASHI KVVVGGSEWH YIATQGPLPH TCHDFWQMVW EQGVNVIAMV TAEEEGGRTK
SHRYWPKLGS KHSSATYGKF KVTTKFRTDS GCYATTGLKV KHLLSGQERT VWHLQYTDWP
HHGCPEDVQG FLSYLEEIQS VRRHTNSVLE GIRTRHPPIV VHCSAGVGRT GVVILSELMI
YCLEHNEKVE VPTMLRFLRE QRMFMIQTIA QYKFVYQVLV QFLQNSRLI
//
