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Q9H3S7 (PTN23_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1636 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs) via its interaction with the ESCRT-I complex (endosomal sorting complex required for transport I), and possibly also other ESCRT complexes. May act as a negative regulator of Ras-mediated mitogenic activity. Plays a role in ciliogenesis. Ref.12 Ref.14 Ref.18

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Interacts with GRAP2 and GRB2. Interacts with UBAP1 and CHMP4B. Ref.12 Ref.15 Ref.18

Subcellular location

Nucleus. Cytoplasm. Cytoplasmic vesicle. Endosome. Cytoplasmcytoskeletoncilium basal body. Early endosome Ref.1 Ref.12 Ref.14 Ref.15.

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. Translation N-terminally shortened.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16361636Tyrosine-protein phosphatase non-receptor type 23
PRO_0000094777

Regions

Domain8 – 394387BRO1
Repeat250 – 28334TPR 1
Repeat374 – 40734TPR 2
Repeat953 – 95421
Repeat955 – 95622
Repeat957 – 95823
Repeat959 – 96024
Repeat961 – 96225
Repeat963 – 96426
Domain1192 – 1452261Tyrosine-protein phosphatase
Region770 – 1130361His
Region953 – 964126 X 2 AA approximate tandem repeats of P-Q
Coiled coil550 – 62374 Potential
Compositional bias716 – 1108393Pro-rich
Compositional bias1509 – 157365Pro-rich

Sites

Active site13921Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue11231Phosphoserine Ref.11 Ref.13

Natural variations

Natural variant9441A → T. Ref.6 Ref.8
Corresponds to variant rs6780013 [ dbSNP | Ensembl ].
VAR_022682
Natural variant10991P → S in a lung cancer cell line; may be a common polymorphism. Ref.1
Corresponds to variant rs149563514 [ dbSNP | Ensembl ].
VAR_022683

Experimental info

Mutagenesis2021L → D: Nearly abolishes interaction with CHMP4B. Abolishes interaction with CHMP4B; when associated with D-206. Ref.12
Mutagenesis2061I → D: Abolishes interaction with CHMP4B; when associated with D-202. Ref.12
Mutagenesis6781F → D: Abolishes interaction with UBAP1. Ref.18
Sequence conflict6471L → G in CAB53676. Ref.8
Sequence conflict10871S → P in CAB53676. Ref.8

Secondary structure

......................................... 1636
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9H3S7 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 536BDDF9D3DC95C0

FASTA1,636178,974
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. 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 (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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"The Bro1-related protein HD-PTP/PTPN23 is required for endosomal cargo sorting and multivesicular body morphogenesis."
Doyotte A., Mironov A., McKenzie E., Woodman P.
Proc. Natl. Acad. Sci. U.S.A. 105:6308-6313(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CHMP4B, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-202 AND ILE-206.
[13]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"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.
[15]"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.
[16]"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.
[17]"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].
[18]"UBAP1 is a component of an endosome-specific ESCRT-I complex that is essential for MVB sorting."
Stefani F., Zhang L., Taylor S., Donovan J., Rollinson S., Doyotte A., Brownhill K., Bennion J., Pickering-Brown S., Woodman P.
Curr. Biol. 21:1245-1250(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH UBAP1, SUBCELLULAR LOCTION, MUTAGENESIS OF PHE-678.
[19]"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].
[20]"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.
PIRT14756.
RefSeqNP_056281.1. NM_015466.2.
UniGeneHs.25524.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3RAUX-ray1.95A/B2-361[»]
ProteinModelPortalQ9H3S7.
SMRQ9H3S7. Positions 4-697, 1142-1459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117430. 25 interactions.
DIPDIP-29923N.
IntActQ9H3S7. 14 interactions.
MINTMINT-1425077.
STRING9606.ENSP00000265562.

PTM databases

PhosphoSiteQ9H3S7.

Polymorphism databases

DMDM68053318.

Proteomic databases

PaxDbQ9H3S7.
PeptideAtlasQ9H3S7.
PRIDEQ9H3S7.

Protocols and materials databases

DNASU25930.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265562; ENSP00000265562; ENSG00000076201.
GeneID25930.
KEGGhsa:25930.
UCSCuc003crf.1. human.

Organism-specific databases

CTD25930.
GeneCardsGC03P047397.
HGNCHGNC:14406. PTPN23.
HPAHPA016845.
MIM606584. gene.
neXtProtNX_Q9H3S7.
PharmGKBPA33996.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOVERGENHBG082231.
InParanoidQ9H3S7.
KOK18040.
OMAIARCYTM.
OrthoDBEOG72C4ZH.
PhylomeDBQ9H3S7.
TreeFamTF323502.

Gene expression databases

ArrayExpressQ9H3S7.
BgeeQ9H3S7.
CleanExHS_PTPN23.
GenevestigatorQ9H3S7.

Family and domain databases

Gene3D1.25.40.280. 1 hit.
InterProIPR025304. ALIX_V_dom.
IPR004328. BRO1_dom.
IPR028770. PTPN23.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PANTHERPTHR19134:SF27. PTHR19134:SF27. 1 hit.
PfamPF13949. ALIX_LYPXL_bnd. 1 hit.
PF03097. BRO1. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM01041. BRO1. 1 hit.
SM00194. PTPc. 1 hit.
[Graphical view]
PROSITEPS51180. BRO1. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPN23. human.
EvolutionaryTraceQ9H3S7.
GeneWikiPTPN23.
GenomeRNAi25930.
NextBio47476.
PROQ9H3S7.
SOURCESearch...

Entry information

Entry namePTN23_HUMAN
AccessionPrimary (citable) accession number: Q9H3S7
Secondary accession number(s): A8K0D7 expand/collapse secondary AC list , Q7KZF8, Q8N6Z5, Q9BSR5, Q9P257, Q9UG03, Q9UMZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 112 of the entry and version 1 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 3

Human chromosome 3: entries, gene names and cross-references to MIM