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Q15678 (PTN14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein phosphatase non-receptor type 14

EC=3.1.3.48
Alternative name(s):
Protein-tyrosine phosphatase pez
Gene names
Name:PTPN14
Synonyms:PEZ, PTPD2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1187 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein tyrosine phosphatase which may play a role in the regulation of lymphangiogenesis, cell-cell adhesion, cell-matrix adhesion, cell migration, cell growth and also regulates TGF-beta gene expression, thereby modulating epithelial-mesenchymal transition. Mediates beta-catenin dephosphorylation at adhesion junctions. Acts as a negative regulator of the oncogenic property of YAP, a downstream target of the hippo pathway, in a cell density-dependent manner. May function as a tumor suppressor. Ref.5 Ref.6 Ref.7 Ref.11 Ref.13 Ref.14 Ref.15

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Interacts with FLT4; the interaction is enhanced by stimulation with VEGFC. Interacts (via PPxY motifs) with YAP1 (via WW domains); this interaction leads to the cytoplasmic sequestration of YAP1 and inhibits its transcriptional co-activator activity. Ref.11 Ref.13 Ref.15

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton By similarity. Nucleus. Note: Translocation into the nucleus is associated with induction of cell proliferation. Partially colocalized with actin filaments at the plasma membrane. Ref.5 Ref.13

Tissue specificity

Ubiquitous.

Induction

Up-regulated at protein level by cell density. However, at the mRNA level remains the same regardless of the status of cell density. Ref.13

Post-translational modification

Ubiquitinated by the ECS (Elongin BC-CUL2/5-SOCS-box protein)/LRR1 E3 ligase complex and subsequently targeted to proteasomal degradation. Ref.13

Involvement in disease

Choanal atresia and lymphedema (CHATLY) [MIM:613611]: A disease characterized by posterior choanal atresia and lymphedema. Additional features are a high-arched palate, hypoplastic nipples, and mild pectus excavatum.
Note: The disease is caused by mutations affecting the gene represented in this entry. A homozygous deletion in PTPN14 predicted to result in frameshift and premature truncation, has been shown to be the cause of choanal atresia and lymphedema in one family. Ref.11

Influence clinical severity of hereditary haemorragic telagiectasia (HHT).

Frequently mutated in a variety of human cancers (PubMed:15155950).

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily.

Contains 1 FERM domain.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityPolymorphism
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlymphangiogenesis

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype Ref.13. Source: UniProtKB

peptidyl-tyrosine dephosphorylation

Inferred from mutant phenotype Ref.15. Source: GOC

protein dephosphorylation

Traceable author statement Ref.1. Source: ProtInc

regulation of protein export from nucleus

Inferred from direct assay Ref.13. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay Ref.5Ref.15. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.5Ref.15. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.15Ref.13. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from mutant phenotype Ref.15. Source: UniProtKB

receptor tyrosine kinase binding

Inferred from physical interaction Ref.11. Source: UniProtKB

transcription cofactor activity

Inferred from mutant phenotype Ref.15. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11871187Tyrosine-protein phosphatase non-receptor type 14
PRO_0000219437

Regions

Domain21 – 306286FERM
Domain909 – 1180272Tyrosine-protein phosphatase
Region1121 – 11277Substrate binding By similarity
Compositional bias566 – 5738Poly-Pro
Compositional bias709 – 7168Poly-Glu

Sites

Active site11211Phosphocysteine intermediate By similarity
Binding site10791Substrate By similarity
Binding site11651Substrate By similarity

Amino acid modifications

Modified residue4861Phosphoserine Ref.8
Modified residue5911Phosphoserine Ref.12
Modified residue5941Phosphoserine Ref.12
Modified residue6421Phosphoserine Ref.12

Natural variations

Natural variant1591Q → E in a breast cancer sample; somatic mutation. Ref.17
VAR_035849
Natural variant3601H → P in a breast cancer sample; somatic mutation. Ref.17
VAR_035850
Natural variant5051V → F.
Corresponds to variant rs12239356 [ dbSNP | Ensembl ].
VAR_046995

Experimental info

Sequence conflict3921H → D in CAA57993. Ref.1

Secondary structure

............................................ 1187
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15678 [UniParc].

Last modified October 14, 2008. Version 2.
Checksum: 1D22F1C8ED06C096

FASTA1,187135,261
        10         20         30         40         50         60 
MPFGLKLRRT RRYNVLSKNC FVTRIRLLDS NVIECTLSVE STGQECLEAV AQRLELRETH 

        70         80         90        100        110        120 
YFGLWFLSKS QQARWVELEK PLKKHLDKFA NEPLLFFGVM FYVPNVSWLQ QEATRYQYYL 

       130        140        150        160        170        180 
QVKKDVLEGR LRCTLDQVIR LAGLAVQADF GDYNQFDSQD FLREYVLFPM DLALEEAVLE 

       190        200        210        220        230        240 
ELTQKVAQEH KAHSGILPAE AELMYINEVE RLDGFGQEIF PVKDNHGNCV HLGIFFMGIF 

       250        260        270        280        290        300 
VRNRIGRQAV IYRWNDMGNI THNKSTILVE LINKEETALF HTDDIENAKY ISRLFATRHK 

       310        320        330        340        350        360 
FYKQNKICTE QSNSPPPIRR QPTWSRSSLP RQQPYILPPV HVQCGEHYSE THTSQDSIFH 

       370        380        390        400        410        420 
GNEEALYCNS HNSLDLNYLN GTVTNGSVCS VHSVNSLNCS QSFIQASPVS SNLSIPGSDI 

       430        440        450        460        470        480 
MRADYIPSHR HSAIIVPSYR PTPDYETVMR QMKRGILHTD SQSQSLRNLN IINTHAYNQP 

       490        500        510        520        530        540 
EDLVYSQPEM RERHPYTVPY GPQGVYSNKL VSPSDQRNPK NNVVPSKPGA SAISHTVSTP 

       550        560        570        580        590        600 
ELANMQLQGS HNYSTAHMLK NYLFRPPPPY PRPRPATSTP DLASHRHKYV SGSSPDLVTR 

       610        620        630        640        650        660 
KVQLSVKTFQ EDSSPVVHQS LQEVSEPLTA TKHHGTVNKR HSLEVMNSMV RGMEAMTLKS 

       670        680        690        700        710        720 
LHLPMARRNT LREQGPPEEG SGSHEVPQLP QYHHKKTFSD ATMLIHSSES EEEEEEAPES 

       730        740        750        760        770        780 
VPQIPMLREK MEYSAQLQAA LARIPNKPPP EYPGPRKSVS NGALRQDQAS LPPAMARARV 

       790        800        810        820        830        840 
LRHGPAKAIS MSRTDPPAVN GASLGPSISE PDLTSVKERV KKEPVKERPV SEMFSLEDSI 

       850        860        870        880        890        900 
IEREMMIRNL EKQKMAGLEA QKRPLMLAAL NGLSVARVSG REENRVDATR VPMDERFRTL 

       910        920        930        940        950        960 
KKKLEEGMVF TEYEQIPKKK ANGIFSTAAL PENAERSRIR EVVPYEENRV ELIPTKENNT 

       970        980        990       1000       1010       1020 
GYINASHIKV VVGGAEWHYI ATQGPLPHTC HDFWQMVWEQ GVNVIAMVTA EEEGGRTKSH 

      1030       1040       1050       1060       1070       1080 
RYWPKLGSKH SSATYGKFKV TTKFRTDSVC YATTGLKVKH LLSGQERTVW HLQYTDWPDH 

      1090       1100       1110       1120       1130       1140 
GCPEDVQGFL SYLEEIQSVR RHTNSMLEGT KNRHPPIVVH CSAGVGRTGV LILSELMIYC 

      1150       1160       1170       1180 
LEHNEKVEVP MMLRLLREQR MFMIQTIAQY KFVYQVLIQF LQNSRLI 

« Hide

References

« Hide 'large scale' references
[1]"Pez: a novel human cDNA encoding protein tyrosine phosphatase- and ezrin-like domains."
Smith A.L., Mitchell P.J., Shipley J., Gusterson B.A., Rogers M.V., Crompton M.R.
Biochem. Biophys. Res. Commun. 209:959-965(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary carcinoma.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart and Lung.
[5]"Translocation of protein tyrosine phosphatase Pez/PTPD2/PTP36 to the nucleus is associated with induction of cell proliferation."
Wadham C., Gamble J.R., Vadas M.A., Khew-Goodall Y.
J. Cell Sci. 113:3117-3123(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION.
[6]"The protein tyrosine phosphatase Pez is a major phosphatase of adherens junctions and dephosphorylates beta-catenin."
Wadham C., Gamble J.R., Vadas M.A., Khew-Goodall Y.
Mol. Biol. Cell 14:2520-2529(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"The protein tyrosine phosphatase Pez regulates TGFbeta, epithelial-mesenchymal transition, and organ development."
Wyatt L., Wadham C., Crocker L.A., Lardelli M., Khew-Goodall Y.
J. Cell Biol. 178:1223-1235(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Protein tyrosine phosphatase PTPN14 is a regulator of lymphatic function and choanal development in humans."
Au A.C., Hernandez P.A., Lieber E., Nadroo A.M., Shen Y.M., Kelley K.A., Gelb B.D., Diaz G.A.
Am. J. Hum. Genet. 87:436-444(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FLT4, INVOLVEMENT IN CHATLY.
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-591; SER-594 AND SER-642, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"PTPN14 is required for the density-dependent control of YAP1."
Wang W., Huang J., Wang X., Yuan J., Li X., Feng L., Park J.I., Chen J.
Genes Dev. 26:1959-1971(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INDUCTION, FUNCTION, INTERACTION WITH YAP1; CUL2 AND LRR1, UBIQUITINATION.
[14]"Mouse and human strategies identify PTPN14 as a modifier of angiogenesis and hereditary haemorrhagic telangiectasia."
Benzinou M., Clermont F.F., Letteboer T.G., Kim J.H., Espejel S., Harradine K.A., Arbelaez J., Luu M.T., Roy R., Quigley D., Higgins M.N., Zaid M., Aouizerat B.E., van Amstel J.K., Giraud S., Dupuis-Girod S., Lesca G., Plauchu H. expand/collapse author list , Hughes C.C., Westermann C.J., Akhurst R.J.
Nat. Commun. 3:616-616(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HEREDITARY HAEMORRAGIC TELAGIECTASIA, FUNCTION.
[15]"PTPN14 interacts with and negatively regulates the oncogenic function of YAP."
Liu X., Yang N., Figel S.A., Wilson K.E., Morrison C.D., Gelman I.H., Zhang J.
Oncogene 32:1266-1273(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH YAP1, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
[16]"Crystal structure of human protein tyrosine phosphatase 14 (PTPN14) at 1.65-A resolution."
Barr A.J., Debreczeni J.E., Eswaran J., Knapp S.
Proteins 63:1132-1136(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 886-1187.
[17]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-159 AND PRO-360.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X82676 mRNA. Translation: CAA57993.1.
AL929236 expand/collapse EMBL AC list , AL445305, AL592216, AL603838 Genomic DNA. Translation: CAH70919.1.
AL603838 expand/collapse EMBL AC list , AL445305, AL592216, AL929236 Genomic DNA. Translation: CAH72982.1.
AL445305 expand/collapse EMBL AC list , AL592216, AL603838, AL929236 Genomic DNA. Translation: CAH73027.1.
AL592216 expand/collapse EMBL AC list , AL445305, AL603838, AL929236 Genomic DNA. Translation: CAH73479.1.
CH471100 Genomic DNA. Translation: EAW93351.1.
BC101754 mRNA. Translation: AAI01755.1.
BC104803 mRNA. Translation: AAI04804.1.
CCDSCCDS1514.1.
PIRJC4155.
RefSeqNP_005392.2. NM_005401.4.
UniGeneHs.193557.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BZLX-ray1.65A886-1187[»]
ProteinModelPortalQ15678.
SMRQ15678. Positions 24-303, 895-1184.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111748. 33 interactions.
IntActQ15678. 10 interactions.
STRING9606.ENSP00000355923.

PTM databases

PhosphoSiteQ15678.

Polymorphism databases

DMDM209572662.

Proteomic databases

MaxQBQ15678.
PaxDbQ15678.
PRIDEQ15678.

Protocols and materials databases

DNASU5784.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366956; ENSP00000355923; ENSG00000152104.
GeneID5784.
KEGGhsa:5784.
UCSCuc001hkk.2. human.

Organism-specific databases

CTD5784.
GeneCardsGC01M214523.
HGNCHGNC:9647. PTPN14.
HPACAB011469.
HPA053864.
MIM603155. gene.
613611. phenotype.
neXtProtNX_Q15678.
PharmGKBPA33989.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000115775.
HOVERGENHBG053757.
InParanoidQ15678.
KOK18025.
OMAVTTKFRT.
OrthoDBEOG7PK8XS.
PhylomeDBQ15678.
TreeFamTF315900.

Gene expression databases

ArrayExpressQ15678.
BgeeQ15678.
CleanExHS_PTPN14.
GenevestigatorQ15678.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
3.90.190.10. 1 hit.
InterProIPR019749. Band_41_domain.
IPR019750. Band_41_fam.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR011993. PH_like_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR014392. Tyr_Pase_non-rcpt_typ-14/21.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamPF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFPIRSF000934. Tyr-Ptase_nr14. 1 hit.
PRINTSPR00935. BAND41.
PR00700. PRTYPHPHTASE.
SMARTSM00295. B41. 1 hit.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPN14. human.
EvolutionaryTraceQ15678.
GeneWikiPTPN14.
GenomeRNAi5784.
NextBio22502.
PROQ15678.
SOURCESearch...

Entry information

Entry namePTN14_HUMAN
AccessionPrimary (citable) accession number: Q15678
Secondary accession number(s): Q5VSI0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 14, 2008
Last modified: July 9, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM