Reviewed, UniProtKB/Swiss-Prot P26045 (PTN3_HUMAN)

Names and origin

Protein names

Recommended name:
    Tyrosine-protein phosphatase non-receptor type 3
    EC=3.1.3.48
Alternative name(s):
    Protein-tyrosine phosphatase H1
      Short name=PTP-H1

Gene names

Name:	PTPN3
Synonyms:	PTPH1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	913 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May act at junctions between the membrane and the cytoskeleton.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cytoskeleton.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily. Contains 1 FERM domain. Contains 1 PDZ (DHR) domain. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	negative regulation of membrane protein ectodomain proteolysis Inferred from mutant phenotype. Source: UniProtKB protein amino acid dephosphorylation Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membrane Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cytoskeletal protein binding Inferred from electronic annotation. Source: InterPro protein tyrosine phosphatase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERBB2	P04626	1	EBI-1047946,EBI-641062
GHR	P10912	2	EBI-1047946,EBI-286316
MET	P08581	1	EBI-1047946,EBI-1039152

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 913

913

Tyrosine-protein phosphatase non-receptor type 3

PRO_0000219433

Regions

Domain

29 – 312

284

FERM

Domain

510 – 582

73

PDZ

Domain

646 – 901

256

Tyrosine-protein phosphatase

Sites

Active site

842

1

Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue

359

1

Phosphoserine Ref.7

Modified residue

367

1

Phosphoserine Ref.7

Modified residue

370

1

Phosphoserine Ref.7

Modified residue

372

1

Phosphoserine Ref.7

Modified residue

376

1

Phosphothreonine Ref.7

Modified residue

381

1

Phosphoserine Ref.7

Natural variations

Natural variant

77

1

D → N: dbSNP rs35285139.

VAR_055252

Natural variant

90

1

A → P: dbSNP rs3793524.

VAR_055253

Natural variant

409

1

T → A: dbSNP rs10979858.

VAR_055254

Natural variant

605

1

F → L: dbSNP rs7859962.

VAR_055255

Natural variant

763

1

D → N: dbSNP rs10116806.

VAR_055256

Experimental info

Sequence conflict

814

1

V → I in AAA35647. Ref.1

Sequence conflict

814

1

V → I in AAB22439. Ref.5

Secondary structure

1

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913

Helix Strand Turn

Details...

Helix

649 – 652

4

Helix

664 – 666

3

Helix

668 – 673

6

Turn

683 – 685

3

Beta strand

686 – 688

3

Beta strand

690 – 692

3

Beta strand

695 – 705

11

Helix

706 – 708

3

Beta strand

710 – 717

8

Turn

722 – 724

3

Helix

725 – 734

10

Beta strand

739 – 742

4

Beta strand

746 – 748

3

Beta strand

764 – 767

4

Beta strand

770 – 779

10

Beta strand

781 – 792

12

Turn

793 – 795

3

Beta strand

798 – 806

9

Beta strand

811 – 813

3

Helix

819 – 831

13

Beta strand

838 – 841

4

Beta strand

843 – 846

4

Helix

847 – 863

17

Helix

870 – 878

9

Helix

888 – 903

16

Sequences

	Sequence		Length	Mass (Da)
	P26045-1 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: 44FBBFA35A5F2AFF	FASTA	913	103,990
	10 20 30 40 50 60 MTSRLRALGG RINNIRTSEL PKEKTRSEVI CSIHFLDGVV QTFKVTKQDT GQVLLDMVHN 70 80 90 100 110 120 HLGVTEKEYF GLQHDDDSVD SPRWLEASKA IRKQLKGGFP CTLHFRVRFF IPDPNTLQQE 130 140 150 160 170 180 QTRHLYFLQL KMDICEGRLT CPLNSAVVLA SYAVQSHFGD YNSSIHHPGY LSDSHFIPDQ 190 200 210 220 230 240 NEDFLTKVES LHEQHSGLKQ SEAESCYINI ARTLDFYGVE LHSGRDLHNL DLMIGIASAG 250 260 270 280 290 300 VAVYRKYICT SFYPWVNILK ISFKRKKFFI HQRQKQAESR EHIVAFNMLN YRSCKNLWKS 310 320 330 340 350 360 CVEHHTFFQA KKLLPQEKNV LSQYWTMGSR NTKKSVNNQY CKKVIGGMVW NPAMRRSLSV 370 380 390 400 410 420 EHLETKSLPS RSPPITPNWR SPRLRHEIRK PRHSSADNLA NEMTYITETE DVFYTYKGSL 430 440 450 460 470 480 APQDSDSEVS QNRSPHQESL SENNPAQSYL TQKSSSSVSP SSNAPGSCSP DGVDQQLLDD 490 500 510 520 530 540 FHRVTKGGST EDASQYYCDK NDNGDSYLVL IRITPDEDGK FGFNLKGGVD QKMPLVVSRI 550 560 570 580 590 600 NPESPADTCI PKLNEGDQIV LINGRDISEH THDQVVMFIK ASRESHSREL ALVIRRRAVR 610 620 630 640 650 660 SFADFKSEDE LNQLFPEAIF PMCPEGGDTL EGSMAQLKKG LESGTVLIQF EQLYRKKPGL 670 680 690 700 710 720 AITFAKLPQN LDKNRYKDVL PYDTTRVLLQ GNEDYINASY VNMEIPAANL VNKYIATQGP 730 740 750 760 770 780 LPHTCAQFWQ VVWDQKLSLI VMLTTLTERG RTKCHQYWPD PPDVMNHGGF HIQCQSEDCT 790 800 810 820 830 840 IAYVSREMLV TNTQTGEEHT VTHLQYVAWP DHGVPDDSSD FLEFVNYVRS LRVDSEPVLV 850 860 870 880 890 900 HCSAGIGRTG VLVTMETAMC LTERNLPIYP LDIVRKMRDQ RAMMVQTSSQ YKFVCEAILR 910 VYEEGLVQML DPS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of a cDNA clone encoding a human protein-tyrosine phosphatase with homology to the cytoskeletal-associated proteins band 4.1, ezrin, and talin." Yang Q., Tonks N.K. Proc. Natl. Acad. Sci. U.S.A. 88:5949-5953(1991) [PubMed: 1648725] [Abstract] Cited for: NUCLOTIDE SEQUENCE [MRNA], VARIANT PRO-90.
[2]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [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 (JUL-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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"cDNA cloning of new protein tyrosine phosphatases in the human colon." Arimura Y., Hinoda Y., Itoh F., Takekawa M., Tsujisaki M., Adachi M., Imai K., Yachi A. Tumor Biol. 13:180-186(1992) [PubMed: 1626183] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 194-896. Tissue: Colon.
[6]	"Expression of cytoskeletal-associated protein tyrosine phosphatase PTPH1 mRNA in human hepatocellular carcinoma." Ikuta S., Itoh F., Hinoda Y., Toyota M., Makiguchi Y., Imai K., Yachi A. J. Gastroenterol. 29:727-732(1994) [PubMed: 7874267] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 899-913.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359; SER-367; SER-370; SER-372; THR-376 AND SER-381, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M64572 mRNA. Translation: AAA35647.1.
AL359963, AL162733, AL450025 Genomic DNA. Translation: CAH71094.1.
AL450025, AL162733, AL359963 Genomic DNA. Translation: CAH73252.1.
AL162733, AL359963, AL450025 Genomic DNA. Translation: CAH73386.1.
CH471105 Genomic DNA. Translation: EAW59046.1.
BC126117 mRNA. Translation: AAI26118.1.
S39392 mRNA. Translation: AAB22439.2.
S76309 mRNA. Translation: AAB33583.1.

IPI

IPI00289649.

PIR

A41109.

RefSeq

NP_002820.3.

UniGene

Hs.436429

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2B49	X-ray	1.54	A	628-913	[»]

SMR

P26045. Positions 508-599.

ModBase

Search...

Protein-protein interaction databases

IntAct

P26045. 5 interactions.

PTM databases

PhosphoSite

P26045.

Proteomic databases

PRIDE

P26045.

Genome annotation databases

Ensembl

ENSG00000070159. Homo sapiens. [Contig view]

GeneID

5774.

KEGG

hsa:5774.

Organism-specific databases

GeneCards

GC09M111177.

H-InvDB

HIX0025742.

HGNC

HGNC:9655. PTPN3.

MIM

176877. gene.

PharmGKB

PA33999.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P26045.

HOVERGEN

P26045.

Enzyme and pathway databases

BRENDA

3.1.3.48. 247.

Gene expression databases

ArrayExpress

P26045.

Bgee

P26045.

CleanEx

HS_PTPN3.

GermOnline

ENSG00000070159. Homo sapiens.

Family and domain databases

InterPro

IPR019749. Band_41_domain.
IPR019750. Band_41_sg.
IPR000798. Ez/rad/moesin.
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.
IPR001478. PDZ/DHR/GLGF.
IPR011993. PH_type.
IPR000387. Tyr_Pase.
IPR016130. Tyr_Pase_AS.
IPR012151. Tyr_Pase_non-rcpt_typ-3/4.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]

Gene3D

G3DSA:1.20.80.10. ACBP. 1 hit.
G3DSA:2.30.29.30. PH_type. 1 hit.

Pfam

PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF00595. PDZ. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]

PIRSF

PIRSF000927. Tyr-Ptase_nr3. 1 hit.

PRINTS

PR00935. BAND41.
PR00661. ERMFAMILY.
PR00700. PRTYPHPHTASE.

SMART

SM00295. B41. 1 hit.
SM00228. PDZ. 1 hit.
SM00194. PTPc. 1 hit.
[Graphical view]

PROSITE

PS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
PS50106. PDZ. 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 Resources

NextBio

22458.

SOURCE

Search...

Entry information

Entry name

PTN3_HUMAN

Accession

Primary (citable) accession number: P26045
Secondary accession number(s): A0AUW9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 5, 2009
Last modified:	June 16, 2009
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)