PTN21_HUMAN
ID PTN21_HUMAN Reviewed; 1174 AA.
AC Q16825;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 21;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphatase D1;
GN Name=PTPN21; Synonyms=PTPD1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PHE-385 AND ALA-936.
RC TISSUE=Skeletal muscle;
RX PubMed=7519780; DOI=10.1073/pnas.91.16.7477;
RA Moeller N.P.H., Moeller K.B., Lammers R., Kharitonenkov A., Sures I.,
RA Ullrich A.;
RT "Src kinase associates with a member of a distinct subfamily of protein-
RT tyrosine phosphatases containing an ezrin-like domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:7477-7481(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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 -!- INTERACTION:
CC Q16825; O95817: BAG3; NbExp=3; IntAct=EBI-2860264, EBI-747185;
CC Q16825; P51813: BMX; NbExp=3; IntAct=EBI-2860264, EBI-696657;
CC Q16825; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-2860264, EBI-744545;
CC Q16825; Q9HCG8: CWC22; NbExp=3; IntAct=EBI-2860264, EBI-373289;
CC Q16825; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-2860264, EBI-745689;
CC Q16825; Q96EF6: FBXO17; NbExp=3; IntAct=EBI-2860264, EBI-2510157;
CC Q16825; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2860264, EBI-618309;
CC Q16825; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-2860264, EBI-746778;
CC Q16825; Q70IA8: MOB3C; NbExp=3; IntAct=EBI-2860264, EBI-9679267;
CC Q16825; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-2860264, EBI-11750983;
CC Q16825; Q6X4W1-2: NSMF; NbExp=3; IntAct=EBI-2860264, EBI-12028784;
CC Q16825; Q9P286: PAK5; NbExp=3; IntAct=EBI-2860264, EBI-741896;
CC Q16825; Q9NPB6-2: PARD6A; NbExp=3; IntAct=EBI-2860264, EBI-10693102;
CC Q16825; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-2860264, EBI-14066006;
CC Q16825; P47897: QARS1; NbExp=3; IntAct=EBI-2860264, EBI-347462;
CC Q16825; Q9Y272: RASD1; NbExp=3; IntAct=EBI-2860264, EBI-740818;
CC Q16825; Q96RF0: SNX18; NbExp=3; IntAct=EBI-2860264, EBI-298169;
CC Q16825; P12931: SRC; NbExp=2; IntAct=EBI-2860264, EBI-621482;
CC Q16825; Q14142: TRIM14; NbExp=3; IntAct=EBI-2860264, EBI-2820256;
CC Q16825; Q8TF42: UBASH3B; NbExp=3; IntAct=EBI-2860264, EBI-1380492;
CC Q16825; O14972: VPS26C; NbExp=3; IntAct=EBI-2860264, EBI-7207091;
CC Q16825; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-2860264, EBI-10486136;
CC Q16825; O08715-5: Akap1; Xeno; NbExp=2; IntAct=EBI-2860264, EBI-9117988;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PTPN21ID41916ch14q21.html";
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DR EMBL; X79510; CAA56042.1; -; mRNA.
DR EMBL; AL162171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS9884.1; -.
DR PIR; I38140; I38140.
DR RefSeq; NP_008970.2; NM_007039.3.
DR RefSeq; XP_005267344.1; XM_005267287.2.
DR RefSeq; XP_011534669.1; XM_011536367.2.
DR AlphaFoldDB; Q16825; -.
DR SMR; Q16825; -.
DR BioGRID; 116280; 89.
DR IntAct; Q16825; 42.
DR MINT; Q16825; -.
DR STRING; 9606.ENSP00000452414; -.
DR BindingDB; Q16825; -.
DR DEPOD; PTPN21; -.
DR iPTMnet; Q16825; -.
DR PhosphoSitePlus; Q16825; -.
DR BioMuta; PTPN21; -.
DR DMDM; 290457654; -.
DR EPD; Q16825; -.
DR jPOST; Q16825; -.
DR MassIVE; Q16825; -.
DR MaxQB; Q16825; -.
DR PaxDb; Q16825; -.
DR PeptideAtlas; Q16825; -.
DR PRIDE; Q16825; -.
DR ProteomicsDB; 61084; -.
DR Antibodypedia; 26302; 139 antibodies from 28 providers.
DR DNASU; 11099; -.
DR Ensembl; ENST00000328736.7; ENSP00000330276.3; ENSG00000070778.13.
DR Ensembl; ENST00000556564.6; ENSP00000452414.1; ENSG00000070778.13.
DR GeneID; 11099; -.
DR KEGG; hsa:11099; -.
DR MANE-Select; ENST00000556564.6; ENSP00000452414.1; NM_007039.4; NP_008970.2.
DR UCSC; uc001xwv.5; human.
DR CTD; 11099; -.
DR DisGeNET; 11099; -.
DR GeneCards; PTPN21; -.
DR HGNC; HGNC:9651; PTPN21.
DR HPA; ENSG00000070778; Low tissue specificity.
DR MIM; 603271; gene.
DR neXtProt; NX_Q16825; -.
DR OpenTargets; ENSG00000070778; -.
DR PharmGKB; PA33994; -.
DR VEuPathDB; HostDB:ENSG00000070778; -.
DR eggNOG; KOG0792; Eukaryota.
DR GeneTree; ENSGT00940000155613; -.
DR HOGENOM; CLU_006456_1_0_1; -.
DR InParanoid; Q16825; -.
DR OMA; LYMQEIE; -.
DR OrthoDB; 144506at2759; -.
DR PhylomeDB; Q16825; -.
DR TreeFam; TF315900; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; Q16825; -.
DR SignaLink; Q16825; -.
DR SIGNOR; Q16825; -.
DR BioGRID-ORCS; 11099; 15 hits in 1073 CRISPR screens.
DR ChiTaRS; PTPN21; human.
DR GeneWiki; PTPN21; -.
DR GenomeRNAi; 11099; -.
DR Pharos; Q16825; Tbio.
DR PRO; PR:Q16825; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q16825; protein.
DR Bgee; ENSG00000070778; Expressed in upper leg skin and 169 other tissues.
DR ExpressionAtlas; Q16825; baseline and differential.
DR Genevisible; Q16825; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13188; FERM_C_PTPN14_PTPN21; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.90.190.10; -; 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 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; SSF47031; SSF47031; 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; 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; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..1174
FT /note="Tyrosine-protein phosphatase non-receptor type 21"
FT /id="PRO_0000219439"
FT DOMAIN 23..308
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 896..1167
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 396..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1108
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 1067
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 1108..1114
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1152
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62136"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62136"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62136"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62136"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62728"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62728"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62136"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62136"
FT MOD_RES 804
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62136"
FT VARIANT 385
FT /note="L -> F (in dbSNP:rs2401751)"
FT /evidence="ECO:0000269|PubMed:7519780"
FT /id="VAR_060341"
FT VARIANT 906
FT /note="K -> N (in dbSNP:rs12879993)"
FT /id="VAR_055539"
FT VARIANT 936
FT /note="V -> A (in dbSNP:rs2274736)"
FT /evidence="ECO:0000269|PubMed:7519780"
FT /id="VAR_060342"
SQ SEQUENCE 1174 AA; 133281 MW; 5B746C824578F117 CRC64;
MPLPFGLKLK RTRRYTVSSK SCLVARIQLL NNEFVEFTLS VESTGQESLE AVAQRLELRE
VTYFSLWYYN KQNQRRWVDL EKPLKKQLDK YALEPTVYFG VVFYVPSVSQ LQQEITRYQY
YLQLKKDILE GSIPCTLEQA IQLAGLAVQA DFGDFDQYES QDFLQKFALF PVGWLQDEKV
LEEATQKVAL LHQKYRGLTA PDAEMLYMQE VERMDGYGEE SYPAKDSQGS DISIGACLEG
IFVKHKNGRH PVVFRWHDIA NMSHNKSFFA LELANKEETI QFQTEDMETA KYIWRLCVAR
HKFYRLNQCN LQTQTVTVNP IRRRSSSRMS LPKPQPYVMP PPPQLHYNGH YTEPYASSQD
NLFVPNQNGY YCHSQTSLDR AQIDLNGRIR NGSVYSAHST NSLNNPQPYL QPSPMSSNPS
ITGSDVMRPD YLPSHRHSAV IPPSYRPTPD YETVMKQLNR GLVHAERQSH SLRNLNIGSS
YAYSRPAALV YSQPEIREHA QLPSPAAAHC PFSLSYSFHS PSPYPYPAER RPVVGAVSVP
ELTNAQLQAQ DYPSPNIMRT QVYRPPPPYP PPRPANSTPD LSRHLYISSS NPDLITRRVH
HSVQTFQEDS LPVAHSLQEV SEPLTAARHA QLHKRNSIEV AGLSHGLEGL RLKERTLSAS
AAEVAPRAVS VGSQPSVFTE RTQREGPEEA EGLRYGHKKS LSDATMLIHS SEEEEDEDFE
EESGARAPPA RAREPRPGLA QDPPGCPRVL LAGPLHILEP KAHVPDAEKR MMDSSPVRTT
AEAQRPWRDG LLMPSMSESD LTTSGRYRAR RDSLKKRPVS DLLSGKKNIV EGLPPLGGMK
KTRVDAKKIG PLKLAALNGL SLSRVPLPDE GKEVATRATN DERCKILEQR LEQGMVFTEY
ERILKKRLVD GECSTARLPE NAERNRFQDV LPYDDVRVEL VPTKENNTGY INASHIKVSV
SGIEWDYIAT QGPLQNTCQD FWQMVWEQGI AIIAMVTAEE EGGREKSFRY WPRLGSRHNT
VTYGRFKITT RFRTDSGCYA TTGLKMKHLL TGQERTVWHL QYTDWPEHGC PEDLKGFLSY
LEEIQSVRRH TNSTSDPQSP NPPLLVHCSA GVGRTGVVIL SEIMIACLEH NEVLDIPRVL
DMLRQQRMML VQTLCQYTFV YRVLIQFLKS SRLI
