Q15678 (PTN14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1187 AA.
Sequence status	Complete.
Protein existence	Evidence 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.10 Ref.12 Ref.13 Ref.14
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.10 Ref.12 Ref.14
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton 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.12
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.12
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.12
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.10 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 process	Transcription Transcription regulation
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lymphangiogenesis Inferred from mutant phenotype Ref.10. Source: UniProtKB negative regulation of cell proliferation Inferred from mutant phenotype Ref.12. Source: UniProtKB regulation of protein export from nucleus Inferred from direct assay Ref.12. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay Ref.5Ref.14. Source: UniProtKB cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.5Ref.14. Source: UniProtKB
Molecular_function	protein tyrosine phosphatase activity Inferred from mutant phenotype Ref.14. Source: UniProtKB transcription cofactor activity Inferred from mutant phenotype Ref.14. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1187

1187

Tyrosine-protein phosphatase non-receptor type 14

PRO_0000219437

Regions

Domain

21 – 306

286

FERM

Domain

909 – 1180

272

Tyrosine-protein phosphatase

Region

1121 – 1127

7

Substrate By similarity

Region

1121 – 1127

7

Substrate binding By similarity

Compositional bias

566 – 573

8

Poly-Pro

Compositional bias

709 – 716

8

Poly-Glu

Sites

Active site

1121

1

Phosphocysteine intermediate By similarity

Binding site

1079

1

Substrate By similarity

Binding site

1165

1

Substrate By similarity

Amino acid modifications

Modified residue

486

1

Phosphoserine Ref.8

Modified residue

591

1

Phosphoserine Ref.11

Modified residue

593

1

Phosphoserine By similarity

Modified residue

594

1

Phosphoserine Ref.11

Modified residue

642

1

Phosphoserine Ref.11

Natural variations

Natural variant

159

1

Q → E in a breast cancer sample; somatic mutation. Ref.16

VAR_035849

Natural variant

360

1

H → P in a breast cancer sample; somatic mutation. Ref.16

VAR_035850

Natural variant

505

1

V → F.
Corresponds to variant rs12239356 [ dbSNP | Ensembl ].

VAR_046995

Experimental info

Sequence conflict

392

1

H → D in CAA57993. Ref.1

Secondary structure

1

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1187

Helix Strand Turn

Details...

Helix

896 – 903

8

Helix

909 – 914

6

Turn

926 – 929

4

Helix

931 – 933

3

Helix

946 – 948

3

Beta strand

964 – 972

9

Beta strand

975 – 982

8

Turn

987 – 989

3

Helix

990 – 999

10

Beta strand

1004 – 1007

4

Beta strand

1011 – 1013

3

Beta strand

1032 – 1035

4

Beta strand

1038 – 1047

10

Beta strand

1049 – 1060

12

Turn

1061 – 1063

3

Beta strand

1066 – 1074

9

Beta strand

1079 – 1081

3

Helix

1086 – 1103

18

Helix

1105 – 1107

3

Beta strand

1117 – 1125

9

Helix

1126 – 1142

17

Helix

1149 – 1157

9

Helix

1167 – 1183

17

Sequences

	Sequence		Length	Mass (Da)
	Q15678 [UniParc]. Last modified October 14, 2008. Version 2. Checksum: 1D22F1C8ED06C096	FASTA	1,187	135,261
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"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].
[10]	"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.
[11]	"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, MASS SPECTROMETRY.
[12]	"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.
[13]	"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. , 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.
[14]	"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, MASS SPECTROMETRY.
[15]	"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.
[16]	"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. , 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 , 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.

IPI

IPI00018914.

PIR

JC4155.

RefSeq

NP_005392.2. NM_005401.4.

UniGene

Hs.193557.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BZL	X-ray	1.65	A	886-1187	[»]

ProteinModelPortal

Q15678.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15678. 2 interactions.

STRING

9606.ENSP00000355923.

PTM databases

PhosphoSite

Q15678.

Polymorphism databases

DMDM

209572662.

Proteomic databases

PaxDb

Q15678.

PRIDE

Q15678.

Protocols and materials databases

DNASU

5784.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000366956; ENSP00000355923; ENSG00000152104.

GeneID

5784.

KEGG

hsa:5784.

UCSC

uc001hkk.2. human.

Organism-specific databases

CTD

5784.

GeneCards

GC01M214523.

HGNC

HGNC:9647. PTPN14.

HPA

CAB011469.

MIM

603155. gene.
613611. phenotype.

neXtProt

NX_Q15678.

PharmGKB

PA33989.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5599.

HOGENOM

HOG000115775.

HOVERGEN

HBG053757.

InParanoid

Q15678.

KO

K01104.

OMA

TTKFRTD.

OrthoDB

EOG4320X9.

PhylomeDB

Q15678.

Gene expression databases

ArrayExpress

Q15678.

Bgee

Q15678.

CleanEx

HS_PTPN14.

Genevestigator

Q15678.

GermOnline

ENSG00000152104. Homo sapiens.

Family and domain databases

Gene3D

1.20.80.10. 1 hit.
2.30.29.30. 1 hit.

InterPro

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.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR014392. Tyr_Pase_non-rcpt_typ-14/21.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]

Pfam

PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]

PIRSF

PIRSF000934. Tyr-Ptase_nr14. 1 hit.

PRINTS

PR00935. BAND41.
PR00700. PRTYPHPHTASE.

SMART

SM00295. B41. 1 hit.
SM00194. PTPc. 1 hit.
[Graphical view]

SUPFAM

SSF47031. FERM_3-hlx. 1 hit.

PROSITE

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]

ProtoNet

Search...

Other

ChiTaRS

PTPN14. human.

EvolutionaryTrace

Q15678.

GenomeRNAi

5784.

NextBio

22502.

SOURCE

Search...

Entry information

Entry name

PTN14_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.