Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q15678

- PTN14_HUMAN

UniProt

Q15678 - PTN14_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Tyrosine-protein phosphatase non-receptor type 14

Gene

PTPN14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.7 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1079 – 10791SubstrateBy similarity
Active sitei1121 – 11211Phosphocysteine intermediatePROSITE-ProRule annotation
Binding sitei1165 – 11651SubstrateBy similarity

GO - Molecular functioni

  1. protein tyrosine phosphatase activity Source: UniProtKB
  2. receptor tyrosine kinase binding Source: UniProtKB
  3. transcription cofactor activity Source: UniProtKB

GO - Biological processi

  1. lymphangiogenesis Source: UniProtKB
  2. negative regulation of cell proliferation Source: UniProtKB
  3. peptidyl-tyrosine dephosphorylation Source: GOC
  4. protein dephosphorylation Source: ProtInc
  5. regulation of protein export from nucleus Source: UniProtKB
  6. regulation of transcription, DNA-templated Source: UniProtKB-KW
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase non-receptor type 14 (EC:3.1.3.48)
Alternative name(s):
Protein-tyrosine phosphatase pez
Gene namesi
Name:PTPN14
Synonyms:PEZ, PTPD2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9647. PTPN14.

Subcellular locationi

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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-KW
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
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.
Influence clinical severity of hereditary haemorragic telagiectasia (HHT).
Frequently mutated in a variety of human cancers.

Organism-specific databases

MIMi613611. phenotype.
PharmGKBiPA33989.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11871187Tyrosine-protein phosphatase non-receptor type 14PRO_0000219437Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei486 – 4861Phosphoserine1 Publication
Modified residuei591 – 5911Phosphoserine1 Publication
Modified residuei594 – 5941Phosphoserine1 Publication
Modified residuei642 – 6421Phosphoserine1 Publication

Post-translational modificationi

Ubiquitinated by the ECS (Elongin BC-CUL2/5-SOCS-box protein)/LRR1 E3 ligase complex and subsequently targeted to proteasomal degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ15678.
PaxDbiQ15678.
PRIDEiQ15678.

PTM databases

PhosphoSiteiQ15678.

Expressioni

Tissue specificityi

Ubiquitous.

Inductioni

Up-regulated at protein level by cell density. However, at the mRNA level remains the same regardless of the status of cell density.1 Publication

Gene expression databases

BgeeiQ15678.
CleanExiHS_PTPN14.
ExpressionAtlasiQ15678. baseline and differential.
GenevestigatoriQ15678.

Organism-specific databases

HPAiCAB011469.
HPA053864.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
YAP1P469376EBI-1237156,EBI-1044059

Protein-protein interaction databases

BioGridi111748. 34 interactions.
IntActiQ15678. 10 interactions.
STRINGi9606.ENSP00000355923.

Structurei

Secondary structure

1
1187
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi896 – 9038Combined sources
Helixi909 – 9146Combined sources
Turni926 – 9294Combined sources
Helixi931 – 9333Combined sources
Helixi946 – 9483Combined sources
Beta strandi964 – 9729Combined sources
Beta strandi975 – 9828Combined sources
Turni987 – 9893Combined sources
Helixi990 – 99910Combined sources
Beta strandi1004 – 10074Combined sources
Beta strandi1011 – 10133Combined sources
Beta strandi1032 – 10354Combined sources
Beta strandi1038 – 104710Combined sources
Beta strandi1049 – 106012Combined sources
Turni1061 – 10633Combined sources
Beta strandi1066 – 10749Combined sources
Beta strandi1079 – 10813Combined sources
Helixi1086 – 110318Combined sources
Helixi1105 – 11073Combined sources
Beta strandi1117 – 11259Combined sources
Helixi1126 – 114217Combined sources
Helixi1149 – 11579Combined sources
Helixi1167 – 118317Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BZLX-ray1.65A886-1187[»]
ProteinModelPortaliQ15678.
SMRiQ15678. Positions 24-303, 895-1184.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15678.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 306286FERMPROSITE-ProRule annotationAdd
BLAST
Domaini909 – 1180272Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1121 – 11277Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi566 – 5738Poly-Pro
Compositional biasi709 – 7168Poly-Glu

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation
Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00770000120472.
HOGENOMiHOG000115775.
HOVERGENiHBG053757.
InParanoidiQ15678.
KOiK18025.
OMAiVTTKFRT.
OrthoDBiEOG7PK8XS.
PhylomeDBiQ15678.
TreeFamiTF315900.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR019749. 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]
PfamiPF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF000934. Tyr-Ptase_nr14. 1 hit.
PRINTSiPR00935. BAND41.
PR00700. PRTYPHPHTASE.
SMARTiSM00295. B41. 1 hit.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. 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]

Sequencei

Sequence statusi: Complete.

Q15678-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPFGLKLRRT RRYNVLSKNC FVTRIRLLDS NVIECTLSVE STGQECLEAV
60 70 80 90 100
AQRLELRETH YFGLWFLSKS QQARWVELEK PLKKHLDKFA NEPLLFFGVM
110 120 130 140 150
FYVPNVSWLQ QEATRYQYYL QVKKDVLEGR LRCTLDQVIR LAGLAVQADF
160 170 180 190 200
GDYNQFDSQD FLREYVLFPM DLALEEAVLE ELTQKVAQEH KAHSGILPAE
210 220 230 240 250
AELMYINEVE RLDGFGQEIF PVKDNHGNCV HLGIFFMGIF VRNRIGRQAV
260 270 280 290 300
IYRWNDMGNI THNKSTILVE LINKEETALF HTDDIENAKY ISRLFATRHK
310 320 330 340 350
FYKQNKICTE QSNSPPPIRR QPTWSRSSLP RQQPYILPPV HVQCGEHYSE
360 370 380 390 400
THTSQDSIFH GNEEALYCNS HNSLDLNYLN GTVTNGSVCS VHSVNSLNCS
410 420 430 440 450
QSFIQASPVS SNLSIPGSDI MRADYIPSHR HSAIIVPSYR PTPDYETVMR
460 470 480 490 500
QMKRGILHTD SQSQSLRNLN IINTHAYNQP EDLVYSQPEM RERHPYTVPY
510 520 530 540 550
GPQGVYSNKL VSPSDQRNPK NNVVPSKPGA SAISHTVSTP ELANMQLQGS
560 570 580 590 600
HNYSTAHMLK NYLFRPPPPY PRPRPATSTP DLASHRHKYV SGSSPDLVTR
610 620 630 640 650
KVQLSVKTFQ EDSSPVVHQS LQEVSEPLTA TKHHGTVNKR HSLEVMNSMV
660 670 680 690 700
RGMEAMTLKS LHLPMARRNT LREQGPPEEG SGSHEVPQLP QYHHKKTFSD
710 720 730 740 750
ATMLIHSSES EEEEEEAPES VPQIPMLREK MEYSAQLQAA LARIPNKPPP
760 770 780 790 800
EYPGPRKSVS NGALRQDQAS LPPAMARARV LRHGPAKAIS MSRTDPPAVN
810 820 830 840 850
GASLGPSISE PDLTSVKERV KKEPVKERPV SEMFSLEDSI IEREMMIRNL
860 870 880 890 900
EKQKMAGLEA QKRPLMLAAL NGLSVARVSG REENRVDATR VPMDERFRTL
910 920 930 940 950
KKKLEEGMVF TEYEQIPKKK ANGIFSTAAL PENAERSRIR EVVPYEENRV
960 970 980 990 1000
ELIPTKENNT GYINASHIKV VVGGAEWHYI ATQGPLPHTC HDFWQMVWEQ
1010 1020 1030 1040 1050
GVNVIAMVTA EEEGGRTKSH RYWPKLGSKH SSATYGKFKV TTKFRTDSVC
1060 1070 1080 1090 1100
YATTGLKVKH LLSGQERTVW HLQYTDWPDH GCPEDVQGFL SYLEEIQSVR
1110 1120 1130 1140 1150
RHTNSMLEGT KNRHPPIVVH CSAGVGRTGV LILSELMIYC LEHNEKVEVP
1160 1170 1180
MMLRLLREQR MFMIQTIAQY KFVYQVLIQF LQNSRLI
Length:1,187
Mass (Da):135,261
Last modified:October 14, 2008 - v2
Checksum:i1D22F1C8ED06C096
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti392 – 3921H → D in CAA57993. (PubMed:7733990)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti159 – 1591Q → E in a breast cancer sample; somatic mutation. 1 Publication
VAR_035849
Natural varianti360 – 3601H → P in a breast cancer sample; somatic mutation. 1 Publication
VAR_035850
Natural varianti505 – 5051V → F.
Corresponds to variant rs12239356 [ dbSNP | Ensembl ].
VAR_046995

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82676 mRNA. Translation: CAA57993.1.
AL929236
, AL445305, AL592216, AL603838 Genomic DNA. Translation: CAH70919.1.
AL603838
, AL445305, AL592216, AL929236 Genomic DNA. Translation: CAH72982.1.
AL445305
, AL592216, AL603838, AL929236 Genomic DNA. Translation: CAH73027.1.
AL592216
, AL445305, AL603838, AL929236 Genomic DNA. Translation: CAH73479.1.
CH471100 Genomic DNA. Translation: EAW93351.1.
BC101754 mRNA. Translation: AAI01755.1.
BC104803 mRNA. Translation: AAI04804.1.
CCDSiCCDS1514.1.
PIRiJC4155.
RefSeqiNP_005392.2. NM_005401.4.
UniGeneiHs.193557.

Genome annotation databases

EnsembliENST00000366956; ENSP00000355923; ENSG00000152104.
GeneIDi5784.
KEGGihsa:5784.
UCSCiuc001hkk.2. human.

Polymorphism databases

DMDMi209572662.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82676 mRNA. Translation: CAA57993.1 .
AL929236
, AL445305 , AL592216 , AL603838 Genomic DNA. Translation: CAH70919.1 .
AL603838
, AL445305 , AL592216 , AL929236 Genomic DNA. Translation: CAH72982.1 .
AL445305
, AL592216 , AL603838 , AL929236 Genomic DNA. Translation: CAH73027.1 .
AL592216
, AL445305 , AL603838 , AL929236 Genomic DNA. Translation: CAH73479.1 .
CH471100 Genomic DNA. Translation: EAW93351.1 .
BC101754 mRNA. Translation: AAI01755.1 .
BC104803 mRNA. Translation: AAI04804.1 .
CCDSi CCDS1514.1.
PIRi JC4155.
RefSeqi NP_005392.2. NM_005401.4.
UniGenei Hs.193557.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BZL X-ray 1.65 A 886-1187 [» ]
ProteinModelPortali Q15678.
SMRi Q15678. Positions 24-303, 895-1184.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111748. 34 interactions.
IntActi Q15678. 10 interactions.
STRINGi 9606.ENSP00000355923.

PTM databases

PhosphoSitei Q15678.

Polymorphism databases

DMDMi 209572662.

Proteomic databases

MaxQBi Q15678.
PaxDbi Q15678.
PRIDEi Q15678.

Protocols and materials databases

DNASUi 5784.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366956 ; ENSP00000355923 ; ENSG00000152104 .
GeneIDi 5784.
KEGGi hsa:5784.
UCSCi uc001hkk.2. human.

Organism-specific databases

CTDi 5784.
GeneCardsi GC01M214523.
HGNCi HGNC:9647. PTPN14.
HPAi CAB011469.
HPA053864.
MIMi 603155. gene.
613611. phenotype.
neXtProti NX_Q15678.
PharmGKBi PA33989.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
GeneTreei ENSGT00770000120472.
HOGENOMi HOG000115775.
HOVERGENi HBG053757.
InParanoidi Q15678.
KOi K18025.
OMAi VTTKFRT.
OrthoDBi EOG7PK8XS.
PhylomeDBi Q15678.
TreeFami TF315900.

Miscellaneous databases

ChiTaRSi PTPN14. human.
EvolutionaryTracei Q15678.
GeneWikii PTPN14.
GenomeRNAii 5784.
NextBioi 22502.
PROi Q15678.
SOURCEi Search...

Gene expression databases

Bgeei Q15678.
CleanExi HS_PTPN14.
ExpressionAtlasi Q15678. baseline and differential.
Genevestigatori Q15678.

Family and domain databases

Gene3Di 1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR019749. 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 ]
Pfami PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000934. Tyr-Ptase_nr14. 1 hit.
PRINTSi PR00935. BAND41.
PR00700. PRTYPHPHTASE.
SMARTi SM00295. B41. 1 hit.
SM00194. PTPc. 1 hit.
[Graphical view ]
SUPFAMi SSF47031. SSF47031. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEi PS00660. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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. 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. Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-159 AND PRO-360.

Entry informationi

Entry nameiPTN14_HUMAN
AccessioniPrimary (citable) accession number: Q15678
Secondary accession number(s): Q5VSI0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 14, 2008
Last modified: November 26, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3