ID PTN3_HUMAN Reviewed; 913 AA.
AC P26045; A0AUW9; E7EN99; E9PGU7;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 01-MAY-2013, entry version 133.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 3;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphatase H1;
DE Short=PTP-H1;
GN Name=PTPN3; Synonyms=PTPH1;
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] (ISOFORM 1), AND VARIANT PRO-90.
RX PubMed=1648725; DOI=10.1073/pnas.88.14.5949;
RA Yang Q., Tonks N.K.;
RT "Isolation of a cDNA clone encoding a human protein-tyrosine
RT phosphatase with homology to the cytoskeletal-associated proteins band
RT 4.1, ezrin, and talin.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:5949-5953(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Fetal kidney, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 194-896 (ISOFORM 1).
RC TISSUE=Colon;
RX PubMed=1626183;
RA Arimura Y., Hinoda Y., Itoh F., Takekawa M., Tsujisaki M., Adachi M.,
RA Imai K., Yachi A.;
RT "cDNA cloning of new protein tyrosine phosphatases in the human
RT colon.";
RL Tumor Biol. 13:180-186(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 899-913 (ISOFORM 1).
RX PubMed=7874267; DOI=10.1007/BF02349278;
RA Ikuta S., Itoh F., Hinoda Y., Toyota M., Makiguchi Y., Imai K.,
RA Yachi A.;
RT "Expression of cytoskeletal-associated protein tyrosine phosphatase
RT PTPH1 mRNA in human hepatocellular carcinoma.";
RL J. Gastroenterol. 29:727-732(1994).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359; SER-367; THR-376
RP AND SER-381, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 628-913.
RX PubMed=19167335; DOI=10.1016/j.cell.2008.11.038;
RA Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P.,
RA Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.;
RT "Large-scale structural analysis of the classical human protein
RT tyrosine phosphatome.";
RL Cell 136:352-363(2009).
CC -!- FUNCTION: May act at junctions between the membrane and the
CC cytoskeleton. Possesses tyrosine phosphatase activity.
CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- INTERACTION:
CC P10912:GHR; NbExp=4; IntAct=EBI-1047946, EBI-286316;
CC P11473:VDR; NbExp=4; IntAct=EBI-1047946, EBI-286357;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P26045-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P26045-2; Sequence=VSP_046309;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P26045-3; Sequence=VSP_046309, VSP_046310;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Non-receptor class subfamily.
CC -!- SIMILARITY: Contains 1 FERM domain.
CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
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DR EMBL; M64572; AAA35647.1; -; mRNA.
DR EMBL; BX648253; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX648735; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL359963; CAH71094.1; -; Genomic_DNA.
DR EMBL; AL162733; CAH71094.1; JOINED; Genomic_DNA.
DR EMBL; AL450025; CAH71094.1; JOINED; Genomic_DNA.
DR EMBL; AL450025; CAH73252.1; -; Genomic_DNA.
DR EMBL; AL162733; CAH73252.1; JOINED; Genomic_DNA.
DR EMBL; AL359963; CAH73252.1; JOINED; Genomic_DNA.
DR EMBL; AL162733; CAH73386.1; -; Genomic_DNA.
DR EMBL; AL359963; CAH73386.1; JOINED; Genomic_DNA.
DR EMBL; AL450025; CAH73386.1; JOINED; Genomic_DNA.
DR EMBL; CH471105; EAW59046.1; -; Genomic_DNA.
DR EMBL; BC126117; AAI26118.1; -; mRNA.
DR EMBL; S39392; AAB22439.2; -; mRNA.
DR EMBL; S76309; AAB33583.1; -; mRNA.
DR IPI; IPI00289649; -.
DR IPI; IPI00480052; -.
DR IPI; IPI00922112; -.
DR PIR; A41109; A41109.
DR RefSeq; NP_001138840.1; NM_001145368.1.
DR RefSeq; NP_001138841.1; NM_001145369.1.
DR RefSeq; NP_001138842.1; NM_001145370.1.
DR RefSeq; NP_001138843.1; NM_001145371.1.
DR RefSeq; NP_002820.3; NM_002829.3.
DR UniGene; Hs.436429; -.
DR PDB; 2B49; X-ray; 1.54 A; A=628-913.
DR PDBsum; 2B49; -.
DR ProteinModelPortal; P26045; -.
DR IntAct; P26045; 5.
DR MINT; MINT-246110; -.
DR STRING; 9606.ENSP00000262539; -.
DR PhosphoSite; P26045; -.
DR DMDM; 229462761; -.
DR PaxDb; P26045; -.
DR PRIDE; P26045; -.
DR DNASU; 5774; -.
DR Ensembl; ENST00000374541; ENSP00000363667; ENSG00000070159.
DR Ensembl; ENST00000394831; ENSP00000378308; ENSG00000070159.
DR Ensembl; ENST00000412145; ENSP00000416654; ENSG00000070159.
DR Ensembl; ENST00000446349; ENSP00000395384; ENSG00000070159.
DR GeneID; 5774; -.
DR KEGG; hsa:5774; -.
DR UCSC; uc004beb.2; human.
DR CTD; 5774; -.
DR GeneCards; GC09M112138; -.
DR H-InvDB; HIX0025742; -.
DR HGNC; HGNC:9655; PTPN3.
DR HPA; HPA038343; -.
DR MIM; 176877; gene.
DR neXtProt; NX_P26045; -.
DR PharmGKB; PA33999; -.
DR eggNOG; COG5599; -.
DR HOGENOM; HOG000007048; -.
DR HOVERGEN; HBG008322; -.
DR InParanoid; P26045; -.
DR KO; K01104; -.
DR OMA; RSEVICS; -.
DR OrthoDB; EOG4RNB7S; -.
DR PhylomeDB; P26045; -.
DR ChiTaRS; PTPN3; human.
DR EvolutionaryTrace; P26045; -.
DR GenomeRNAi; 5774; -.
DR NextBio; 22458; -.
DR ArrayExpress; P26045; -.
DR Bgee; P26045; -.
DR CleanEx; HS_PTPN3; -.
DR Genevestigator; P26045; -.
DR GermOnline; ENSG00000070159; Homo sapiens.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0009898; C:internal side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IMP:BHF-UCL.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:BHF-UCL.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR019750; Band_41_fam.
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_like_dom.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR012151; Tyr_Pase_non-rcpt_typ-3/4.
DR InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
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; SM00228; PDZ; 1.
DR SMART; SM00194; PTPc; 1.
DR SUPFAM; SSF47031; FERM_3-hlx; 1.
DR SUPFAM; SSF50156; PDZ; 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; Alternative splicing; Cell membrane; Complete proteome;
KW Cytoplasm; Cytoskeleton; Hydrolase; Membrane; Phosphoprotein;
KW Polymorphism; Protein phosphatase; Reference proteome.
FT CHAIN 1 913 Tyrosine-protein phosphatase non-receptor
FT type 3.
FT /FTId=PRO_0000219433.
FT DOMAIN 29 312 FERM.
FT DOMAIN 510 582 PDZ.
FT DOMAIN 646 901 Tyrosine-protein phosphatase.
FT REGION 842 848 Substrate binding (By similarity).
FT ACT_SITE 842 842 Phosphocysteine intermediate (By
FT similarity).
FT BINDING 811 811 Substrate (By similarity).
FT BINDING 886 886 Substrate (By similarity).
FT MOD_RES 359 359 Phosphoserine.
FT MOD_RES 367 367 Phosphoserine.
FT MOD_RES 376 376 Phosphothreonine.
FT MOD_RES 381 381 Phosphoserine.
FT VAR_SEQ 1 131 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_046309.
FT VAR_SEQ 335 379 Missing (in isoform 3).
FT /FTId=VSP_046310.
FT VARIANT 77 77 D -> N (in dbSNP:rs35285139).
FT /FTId=VAR_055252.
FT VARIANT 90 90 A -> P (in dbSNP:rs3793524).
FT /FTId=VAR_055253.
FT VARIANT 409 409 T -> A (in dbSNP:rs10979858).
FT /FTId=VAR_055254.
FT VARIANT 605 605 F -> L (in dbSNP:rs7859962).
FT /FTId=VAR_055255.
FT VARIANT 763 763 D -> N (in dbSNP:rs10116806).
FT /FTId=VAR_055256.
FT CONFLICT 814 814 V -> I (in Ref. 1; AAA35647 and 6;
FT AAB22439).
FT HELIX 649 652
FT HELIX 664 666
FT HELIX 668 673
FT TURN 683 685
FT STRAND 686 688
FT STRAND 690 692
FT STRAND 695 705
FT HELIX 706 708
FT STRAND 710 717
FT TURN 722 724
FT HELIX 725 734
FT STRAND 739 742
FT STRAND 746 748
FT STRAND 764 767
FT STRAND 770 779
FT STRAND 781 792
FT TURN 793 795
FT STRAND 798 806
FT STRAND 811 813
FT HELIX 819 831
FT STRAND 838 841
FT STRAND 843 846
FT HELIX 847 863
FT HELIX 870 878
FT HELIX 888 903
SQ SEQUENCE 913 AA; 103990 MW; 44FBBFA35A5F2AFF CRC64;
MTSRLRALGG RINNIRTSEL PKEKTRSEVI CSIHFLDGVV QTFKVTKQDT GQVLLDMVHN
HLGVTEKEYF GLQHDDDSVD SPRWLEASKA IRKQLKGGFP CTLHFRVRFF IPDPNTLQQE
QTRHLYFLQL KMDICEGRLT CPLNSAVVLA SYAVQSHFGD YNSSIHHPGY LSDSHFIPDQ
NEDFLTKVES LHEQHSGLKQ SEAESCYINI ARTLDFYGVE LHSGRDLHNL DLMIGIASAG
VAVYRKYICT SFYPWVNILK ISFKRKKFFI HQRQKQAESR EHIVAFNMLN YRSCKNLWKS
CVEHHTFFQA KKLLPQEKNV LSQYWTMGSR NTKKSVNNQY CKKVIGGMVW NPAMRRSLSV
EHLETKSLPS RSPPITPNWR SPRLRHEIRK PRHSSADNLA NEMTYITETE DVFYTYKGSL
APQDSDSEVS QNRSPHQESL SENNPAQSYL TQKSSSSVSP SSNAPGSCSP DGVDQQLLDD
FHRVTKGGST EDASQYYCDK NDNGDSYLVL IRITPDEDGK FGFNLKGGVD QKMPLVVSRI
NPESPADTCI PKLNEGDQIV LINGRDISEH THDQVVMFIK ASRESHSREL ALVIRRRAVR
SFADFKSEDE LNQLFPEAIF PMCPEGGDTL EGSMAQLKKG LESGTVLIQF EQLYRKKPGL
AITFAKLPQN LDKNRYKDVL PYDTTRVLLQ GNEDYINASY VNMEIPAANL VNKYIATQGP
LPHTCAQFWQ VVWDQKLSLI VMLTTLTERG RTKCHQYWPD PPDVMNHGGF HIQCQSEDCT
IAYVSREMLV TNTQTGEEHT VTHLQYVAWP DHGVPDDSSD FLEFVNYVRS LRVDSEPVLV
HCSAGIGRTG VLVTMETAMC LTERNLPIYP LDIVRKMRDQ RAMMVQTSSQ YKFVCEAILR
VYEEGLVQML DPS
//
