Q9H3S7 (PTN23_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein phosphatase non-receptor type 23
EC=3.1.3.48

Alternative name(s):
His domain-containing protein tyrosine phosphatase
Short name=HD-PTP
Protein tyrosine phosphatase TD14
Short name=PTP-TD14

Gene names

Name:	PTPN23
Synonyms:	KIAA1471

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	1636 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May act as a negative regulator of Ras-mediated mitogenic activity. Plays a role in ciliogenesis. Ref.13
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subunit structure	Interacts with GRAP2 and GRB2. Ref.14
Subcellular location	Nucleus. Cytoplasm. Cytoplasmic vesicle. Endosome. Cytoplasm › cytoskeleton › cilium basal body Ref.1 Ref.13 Ref.14.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily. Contains 1 BRO1 domain. Contains 2 TPR repeats. Contains 1 tyrosine-protein phosphatase domain.
Sequence caution	The sequence BAA95995.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cilium biogenesis/degradation
Cellular component	Cell projection Cilium Cytoplasm Cytoplasmic vesicle Cytoskeleton Endosome Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat TPR repeat
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cilium morphogenesis Inferred from mutant phenotype Ref.13. Source: UniProtKB peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	cilium Inferred from electronic annotation. Source: UniProtKB-KW cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell endosome Inferred from direct assay Ref.14. Source: UniProtKB microtubule basal body Inferred from direct assay Ref.13. Source: UniProtKB nucleus Inferred from direct assay Ref.14. Source: UniProtKB
Molecular_function	protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRAP2	O75791	5	EBI-724478,EBI-740418
GRB2	P62993	6	EBI-724478,EBI-401755

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1636

1636

Tyrosine-protein phosphatase non-receptor type 23

PRO_0000094777

Regions

Domain

8 – 394

387

BRO1

Repeat

250 – 283

34

TPR 1

Repeat

374 – 407

34

TPR 2

Repeat

953 – 954

2

1

Repeat

955 – 956

2

2

Repeat

957 – 958

2

3

Repeat

959 – 960

2

4

Repeat

961 – 962

2

5

Repeat

963 – 964

2

6

Domain

1192 – 1452

261

Tyrosine-protein phosphatase

Region

770 – 1130

361

His

Region

953 – 964

12

6 X 2 AA approximate tandem repeats of P-Q

Coiled coil

550 – 623

74

Potential

Compositional bias

716 – 1108

393

Pro-rich

Compositional bias

1509 – 1573

65

Pro-rich

Sites

Active site

1392

1

Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue

1123

1

Phosphoserine Ref.11 Ref.12

Modified residue

1126

1

Phosphoserine By similarity

Natural variations

Natural variant

944

1

A → T. Ref.6 Ref.8
Corresponds to variant rs6780013 [ dbSNP | Ensembl ].

VAR_022682

Natural variant

1099

1

P → S in a lung cancer cell line; may be a common polymorphism. Ref.1

VAR_022683

Experimental info

Sequence conflict

647

1

L → G Ref.8

Sequence conflict

1087

1

S → P Ref.8

Secondary structure

1

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1636

Helix Strand Turn

Details...

Beta strand

17 – 20

4

Helix

23 – 32

10

Turn

38 – 41

4

Helix

42 – 56

15

Helix

62 – 81

20

Beta strand

94 – 97

4

Turn

99 – 101

3

Beta strand

104 – 108

5

Helix

110 – 131

22

Helix

137 – 160

24

Helix

167 – 169

3

Helix

171 – 195

25

Helix

200 – 221

22

Helix

224 – 230

7

Helix

233 – 262

30

Helix

266 – 286

21

Turn

287 – 289

3

Helix

292 – 318

27

Helix

327 – 329

3

Helix

349 – 352

4

Turn

356 – 359

4

Sequences

	Sequence		Length	Mass (Da)
	Q9H3S7 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 536BDDF9D3DC95C0	FASTA	1,636	178,974
	10 20 30 40 50 60 MEAVPRMPMI WLDLKEAGDF HFQPAVKKFV LKNYGENPEA YNEELKKLEL LRQNAVRVPR 70 80 90 100 110 120 DFEGCSVLRK YLGQLHYLQS RVPMGSGQEA AVPVTWTEIF SGKSVAHEDI KYEQACILYN 130 140 150 160 170 180 LGALHSMLGA MDKRVSEEGM KVSCTHFQCA AGAFAYLREH FPQAYSVDMS RQILTLNVNL 190 200 210 220 230 240 MLGQAQECLL EKSMLDNRKS FLVARISAQV VDYYKEACRA LENPDTASLL GRIQKDWKKL 250 260 270 280 290 300 VQMKIYYFAA VAHLHMGKQA EEQQKFGERV AYFQSALDKL NEAIKLAKGQ PDTVQDALRF 310 320 330 340 350 360 TMDVIGGKYN SAKKDNDFIY HEAVPALDTL QPVKGAPLVK PLPVNPTDPA VTGPDIFAKL 370 380 390 400 410 420 VPMAAHEASS LYSEEKAKLL REMMAKIEDK NEVLDQFMDS MQLDPETVDN LDAYSHIPPQ 430 440 450 460 470 480 LMEKCAALSV RPDTVRNLVQ SMQVLSGVFT DVEASLKDIR DLLEEDELLE QKFQEAVGQA 490 500 510 520 530 540 GAISITSKAE LAEVRREWAK YMEVHEKASF TNSELHRAMN LHVGNLRLLS GPLDQVRAAL 550 560 570 580 590 600 PTPALSPEDK AVLQNLKRIL AKVQEMRDQR VSLEQQLREL IQKDDITASL VTTDHSEMKK 610 620 630 640 650 660 LFEEQLKKYD QLKVYLEQNL AAQDRVLCAL TEANVQYAAV RRVLSDLDQK WNSTLQTLVA 670 680 690 700 710 720 SYEAYEDLMK KSQEGRDFYA DLESKVAALL ERTQSTCQAR EAARQQLLDR ELKKKPPPRP 730 740 750 760 770 780 TAPKPLLPRR EESEAVEAGD PPEELRSLPP DMVAGPRLPD TFLGSATPLH FPPSPFPSST 790 800 810 820 830 840 GPGPHYLSGP LPPGTYSGPT QLIQPRAPGP HAMPVAPGPA LYPAPAYTPE LGLVPRSSPQ 850 860 870 880 890 900 HGVVSSPYVG VGPAPPVAGL PSAPPPQFSG PELAMAVRPA TTTVDSIQAP IPSHTAPRPN 910 920 930 940 950 960 PTPAPPPPCF PVPPPQPLPT PYTYPAGAKQ PIPAQHHFSS GIPAGFPAPR IGPQPQPHPQ 970 980 990 1000 1010 1020 PHPSQAFGPQ PPQQPLPLQH PHLFPPQAPG LLPPQSPYPY APQPGVLGQP PPPLHTQLYP 1030 1040 1050 1060 1070 1080 GPAQDPLPAH SGALPFPSPG PPQPPHPPLA YGPAPSTRPM GPQAAPLTIR GPSSAGQSTP 1090 1100 1110 1120 1130 1140 SPHLVPSPAP SPGPGPVPPR PPAAEPPPCL RRGAAAADLL SSSPESQHGG TQSPGGGQPL 1150 1160 1170 1180 1190 1200 LQPTKVDAAE GRRPQALRLI ERDPYEHPER LRQLQQELEA FRGQLGDVGA LDTVWRELQD 1210 1220 1230 1240 1250 1260 AQEHDARGRS IAIARCYSLK NRHQDVMPYD SNRVVLRSGK DDYINASCVE GLSPYCPPLV 1270 1280 1290 1300 1310 1320 ATQAPLPGTA ADFWLMVHEQ KVSVIVMLVS EAEMEKQKVA RYFPTERGQP MVHGALSLAL 1330 1340 1350 1360 1370 1380 SSVRSTETHV ERVLSLQFRD QSLKRSLVHL HFPTWPELGL PDSPSNLLRF IQEVHAHYLH 1390 1400 1410 1420 1430 1440 QRPLHTPIIV HCSSGVGRTG AFALLYAAVQ EVEAGNGIPE LPQLVRRMRQ QRKHMLQEKL 1450 1460 1470 1480 1490 1500 HLRFCYEAVV RHVEQVLQRH GVPPPCKPLA SASISQKNHL PQDSQDLVLG GDVPISSIQA 1510 1520 1530 1540 1550 1560 TIAKLSIRPP GGLESPVASL PGPAEPPGLP PASLPESTPI PSSSPPPLSS PLPEAPQPKE 1570 1580 1590 1600 1610 1620 EPPVPEAPSS GPPSSSLELL ASLTPEAFSL DSSLRGKQRM SKHNFLQAHN GQGLRATRPS 1630 DDPLSLLDPL WTLNKT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"HD-PTP: a novel protein tyrosine phosphatase gene on human chromosome 3p21.3." Toyooka S., Ouchida M., Jitsumori Y., Tsukuda K., Sakai A., Nakamura A., Shimizu N., Shimizu K. Biochem. Biophys. Res. Commun. 278:671-678(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-1099, SUBCELLULAR LOCATION. Tissue: Stomach cancer.
[2]	"Cloning, chromosomal assignment and tissue expression of a novel human protein tyrosine phosphatase (PTP-TD14) gene." Qu X., Zhai Y., Wei H., Zhang C., Xing G., Lu C., Wang M., He F. Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[4]	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].
[5]	"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: Muscle, Ovary and Skin.
[6]	"Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O. DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1383, VARIANT THR-944. Tissue: Brain.
[7]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[8]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 647-1636, VARIANT THR-944. Tissue: Brain.
[9]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1060-1636.
[10]	"Differential expression of PTPase RNAs resulting from K562 differentiation induced by PMA." Dayton M.A., Blanchard K.L. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1351-1493.
[11]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1123, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1123, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"Functional genomic screen for modulators of ciliogenesis and cilium length." Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T., Aza-Blanc P., Gleeson J.G. Nature 464:1048-1051(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]	"Histidine domain-protein tyrosine phosphatase interacts with Grb2 and GrpL." Tanase C.A. PLoS ONE 5:E14339-E14339(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRAP2 AND GRB2, SUBCELLULAR LOCATION.
[15]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"The Phe105 loop of Alix Bro1 domain plays a key role in HIV-1 release." Sette P., Mu R., Dussupt V., Jiang J., Snyder G., Smith P., Xiao T.S., Bouamr F. Structure 19:1485-1495(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 2-361.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB025194 mRNA. Translation: BAB19280.1.
AF290614 mRNA. Translation: AAK28025.1.
AK289502 mRNA. Translation: BAF82191.1.
CH471055 Genomic DNA. Translation: EAW64823.1.
BC004881 mRNA. Translation: AAH04881.2.
BC027711 mRNA. Translation: AAH27711.2.
BC089042 mRNA. Translation: AAH89042.1.
AB040904 mRNA. Translation: BAA95995.2. Different initiation.
AL110210 mRNA. Translation: CAB53676.1.
BT009758 mRNA. Translation: AAP88760.1.
AF169350 mRNA. Translation: AAD50276.1.

IPI

IPI00034006.

PIR

T14756.

RefSeq

NP_056281.1. NM_015466.2.

UniGene

Hs.25524.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3RAU	X-ray	1.95	A/B	2-361	[»]

ProteinModelPortal

Q9H3S7.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29923N.

IntAct

Q9H3S7. 7 interactions.

MINT

MINT-1425077.

STRING

9606.ENSP00000265562.

PTM databases

PhosphoSite

Q9H3S7.

Polymorphism databases

DMDM

68053318.

Proteomic databases

PaxDb

Q9H3S7.

PeptideAtlas

Q9H3S7.

PRIDE

Q9H3S7.

Protocols and materials databases

DNASU

25930.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265562; ENSP00000265562; ENSG00000076201.

GeneID

25930.

KEGG

hsa:25930.

UCSC

uc003crf.1. human.

Organism-specific databases

CTD

25930.

GeneCards

GC03P047397.

HGNC

HGNC:14406. PTPN23.

HPA

HPA016845.

MIM

606584. gene.

neXtProt

NX_Q9H3S7.

PharmGKB

PA33996.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5599.

HOVERGEN

HBG082231.

InParanoid

Q9H3S7.

KO

K01104.

OMA

RFIQEVH.

PhylomeDB

Q9H3S7.

Gene expression databases

ArrayExpress

Q9H3S7.

Bgee

Q9H3S7.

CleanEx

HS_PTPN23.

Genevestigator

Q9H3S7.

GermOnline

ENSG00000076201. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.280. 1 hit.

InterPro

IPR025304. ALIX_V_dom.
IPR004328. BRO1_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]

Pfam

PF13949. ALIX_LYPXL_bnd. 1 hit.
PF03097. BRO1. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]

PRINTS

PR00700. PRTYPHPHTASE.

SMART

SM01041. BRO1. 1 hit.
SM00194. PTPc. 1 hit.
[Graphical view]

PROSITE

PS51180. BRO1. 1 hit.
PS50005. TPR. False negative.
PS50293. TPR_REGION. False negative.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PTPN23. human.

EvolutionaryTrace

Q9H3S7.

GenomeRNAi

25930.

NextBio

47476.

SOURCE

Search...

Entry information

Entry name

PTN23_HUMAN

Accession

Primary (citable) accession number: Q9H3S7
Secondary accession number(s): A8K0D7 , Q7KZF8, Q8N6Z5, Q9BSR5, Q9P257, Q9UG03, Q9UMZ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 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.