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Q9H3S7

- PTN23_HUMAN

UniProt

Q9H3S7 - PTN23_HUMAN

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Protein

Tyrosine-protein phosphatase non-receptor type 23

Gene

PTPN23

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

Functioni

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.3 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1392 – 13921Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. protein kinase binding Source: UniProtKB
  2. protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. cilium morphogenesis Source: UniProtKB
  2. negative regulation of epithelial cell migration Source: UniProtKB
  3. peptidyl-tyrosine dephosphorylation Source: GOC
  4. positive regulation of adherens junction organization Source: UniProtKB
  5. positive regulation of early endosome to late endosome transport Source: UniProtKB
  6. positive regulation of homophilic cell adhesion Source: UniProtKB
  7. protein transport Source: UniProtKB-KW
  8. ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cilium biogenesis/degradation, Protein transport, Transport

Names & Taxonomyi

Protein namesi
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 namesi
Name:PTPN23
Synonyms:KIAA1471
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:14406. PTPN23.

Subcellular locationi

GO - Cellular componenti

  1. ciliary basal body Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytoplasmic vesicle Source: UniProtKB-KW
  4. early endosome Source: UniProtKB
  5. endosome Source: UniProtKB
  6. extracellular vesicular exosome Source: UniProt
  7. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Endosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi202 – 2021L → D: Nearly abolishes interaction with CHMP4B. Abolishes interaction with CHMP4B; when associated with D-206. 1 Publication
Mutagenesisi206 – 2061I → D: Abolishes interaction with CHMP4B; when associated with D-202. 1 Publication
Mutagenesisi678 – 6781F → D: Abolishes interaction with UBAP1. 1 Publication

Organism-specific databases

PharmGKBiPA33996.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16361636Tyrosine-protein phosphatase non-receptor type 23PRO_0000094777Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1123 – 11231Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H3S7.
PaxDbiQ9H3S7.
PeptideAtlasiQ9H3S7.
PRIDEiQ9H3S7.

PTM databases

PhosphoSiteiQ9H3S7.

Expressioni

Gene expression databases

BgeeiQ9H3S7.
CleanExiHS_PTPN23.
ExpressionAtlasiQ9H3S7. baseline and differential.
GenevestigatoriQ9H3S7.

Organism-specific databases

HPAiHPA016845.

Interactioni

Subunit structurei

Interacts with GRAP2 and GRB2. Interacts with UBAP1 and CHMP4B.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CHMP4BQ9H4442EBI-724478,EBI-749627
GRAP2O757918EBI-724478,EBI-740418
Grap2O891002EBI-724478,EBI-642151From a different organism.
GRB2P629936EBI-724478,EBI-401755
PDCD6O753403EBI-724478,EBI-352915
PTK2Q053974EBI-724478,EBI-702142
SH3GL2Q999622EBI-724478,EBI-77938
TSG101Q998162EBI-724478,EBI-346882

Protein-protein interaction databases

BioGridi117430. 29 interactions.
DIPiDIP-29923N.
IntActiQ9H3S7. 14 interactions.
MINTiMINT-1425077.
STRINGi9606.ENSP00000265562.

Structurei

Secondary structure

1
1636
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 204Combined sources
Helixi23 – 3210Combined sources
Turni38 – 414Combined sources
Helixi42 – 5615Combined sources
Helixi62 – 8120Combined sources
Beta strandi94 – 974Combined sources
Turni99 – 1013Combined sources
Beta strandi104 – 1085Combined sources
Helixi110 – 13122Combined sources
Helixi137 – 16024Combined sources
Helixi167 – 1693Combined sources
Helixi171 – 19525Combined sources
Helixi200 – 22122Combined sources
Helixi224 – 2307Combined sources
Helixi233 – 26230Combined sources
Helixi266 – 28621Combined sources
Turni287 – 2893Combined sources
Helixi292 – 31827Combined sources
Helixi327 – 3293Combined sources
Helixi349 – 3524Combined sources
Turni356 – 3594Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RAUX-ray1.95A/B2-361[»]
ProteinModelPortaliQ9H3S7.
SMRiQ9H3S7. Positions 4-697, 1142-1459.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H3S7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 394387BRO1PROSITE-ProRule annotationAdd
BLAST
Repeati250 – 28334TPR 1Add
BLAST
Repeati374 – 40734TPR 2Add
BLAST
Repeati953 – 95421
Repeati955 – 95622
Repeati957 – 95823
Repeati959 – 96024
Repeati961 – 96225
Repeati963 – 96426
Domaini1192 – 1452261Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni770 – 1130361HisAdd
BLAST
Regioni953 – 964126 X 2 AA approximate tandem repeats of P-QAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili550 – 62374Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi716 – 1108393Pro-richAdd
BLAST
Compositional biasi1509 – 157365Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 BRO1 domain.PROSITE-ProRule annotation
Contains 2 TPR repeats.Curated
Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00770000120582.
HOVERGENiHBG082231.
InParanoidiQ9H3S7.
KOiK18040.
OMAiIARCYTM.
OrthoDBiEOG72C4ZH.
PhylomeDBiQ9H3S7.
TreeFamiTF323502.

Family and domain databases

Gene3Di1.25.40.280. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR025304. ALIX_V_dom.
IPR004328. BRO1_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR028770. PTPN23.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PANTHERiPTHR19134:SF27. PTHR19134:SF27. 1 hit.
PfamiPF13949. ALIX_LYPXL_bnd. 1 hit.
PF03097. BRO1. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM01041. BRO1. 1 hit.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS51180. BRO1. 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.

Q9H3S7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEAVPRMPMI WLDLKEAGDF HFQPAVKKFV LKNYGENPEA YNEELKKLEL
60 70 80 90 100
LRQNAVRVPR DFEGCSVLRK YLGQLHYLQS RVPMGSGQEA AVPVTWTEIF
110 120 130 140 150
SGKSVAHEDI KYEQACILYN LGALHSMLGA MDKRVSEEGM KVSCTHFQCA
160 170 180 190 200
AGAFAYLREH FPQAYSVDMS RQILTLNVNL MLGQAQECLL EKSMLDNRKS
210 220 230 240 250
FLVARISAQV VDYYKEACRA LENPDTASLL GRIQKDWKKL VQMKIYYFAA
260 270 280 290 300
VAHLHMGKQA EEQQKFGERV AYFQSALDKL NEAIKLAKGQ PDTVQDALRF
310 320 330 340 350
TMDVIGGKYN SAKKDNDFIY HEAVPALDTL QPVKGAPLVK PLPVNPTDPA
360 370 380 390 400
VTGPDIFAKL VPMAAHEASS LYSEEKAKLL REMMAKIEDK NEVLDQFMDS
410 420 430 440 450
MQLDPETVDN LDAYSHIPPQ LMEKCAALSV RPDTVRNLVQ SMQVLSGVFT
460 470 480 490 500
DVEASLKDIR DLLEEDELLE QKFQEAVGQA GAISITSKAE LAEVRREWAK
510 520 530 540 550
YMEVHEKASF TNSELHRAMN LHVGNLRLLS GPLDQVRAAL PTPALSPEDK
560 570 580 590 600
AVLQNLKRIL AKVQEMRDQR VSLEQQLREL IQKDDITASL VTTDHSEMKK
610 620 630 640 650
LFEEQLKKYD QLKVYLEQNL AAQDRVLCAL TEANVQYAAV RRVLSDLDQK
660 670 680 690 700
WNSTLQTLVA SYEAYEDLMK KSQEGRDFYA DLESKVAALL ERTQSTCQAR
710 720 730 740 750
EAARQQLLDR ELKKKPPPRP TAPKPLLPRR EESEAVEAGD PPEELRSLPP
760 770 780 790 800
DMVAGPRLPD TFLGSATPLH FPPSPFPSST GPGPHYLSGP LPPGTYSGPT
810 820 830 840 850
QLIQPRAPGP HAMPVAPGPA LYPAPAYTPE LGLVPRSSPQ HGVVSSPYVG
860 870 880 890 900
VGPAPPVAGL PSAPPPQFSG PELAMAVRPA TTTVDSIQAP IPSHTAPRPN
910 920 930 940 950
PTPAPPPPCF PVPPPQPLPT PYTYPAGAKQ PIPAQHHFSS GIPAGFPAPR
960 970 980 990 1000
IGPQPQPHPQ PHPSQAFGPQ PPQQPLPLQH PHLFPPQAPG LLPPQSPYPY
1010 1020 1030 1040 1050
APQPGVLGQP PPPLHTQLYP GPAQDPLPAH SGALPFPSPG PPQPPHPPLA
1060 1070 1080 1090 1100
YGPAPSTRPM GPQAAPLTIR GPSSAGQSTP SPHLVPSPAP SPGPGPVPPR
1110 1120 1130 1140 1150
PPAAEPPPCL RRGAAAADLL SSSPESQHGG TQSPGGGQPL LQPTKVDAAE
1160 1170 1180 1190 1200
GRRPQALRLI ERDPYEHPER LRQLQQELEA FRGQLGDVGA LDTVWRELQD
1210 1220 1230 1240 1250
AQEHDARGRS IAIARCYSLK NRHQDVMPYD SNRVVLRSGK DDYINASCVE
1260 1270 1280 1290 1300
GLSPYCPPLV ATQAPLPGTA ADFWLMVHEQ KVSVIVMLVS EAEMEKQKVA
1310 1320 1330 1340 1350
RYFPTERGQP MVHGALSLAL SSVRSTETHV ERVLSLQFRD QSLKRSLVHL
1360 1370 1380 1390 1400
HFPTWPELGL PDSPSNLLRF IQEVHAHYLH QRPLHTPIIV HCSSGVGRTG
1410 1420 1430 1440 1450
AFALLYAAVQ EVEAGNGIPE LPQLVRRMRQ QRKHMLQEKL HLRFCYEAVV
1460 1470 1480 1490 1500
RHVEQVLQRH GVPPPCKPLA SASISQKNHL PQDSQDLVLG GDVPISSIQA
1510 1520 1530 1540 1550
TIAKLSIRPP GGLESPVASL PGPAEPPGLP PASLPESTPI PSSSPPPLSS
1560 1570 1580 1590 1600
PLPEAPQPKE EPPVPEAPSS GPPSSSLELL ASLTPEAFSL DSSLRGKQRM
1610 1620 1630
SKHNFLQAHN GQGLRATRPS DDPLSLLDPL WTLNKT
Length:1,636
Mass (Da):178,974
Last modified:March 1, 2001 - v1
Checksum:i536BDDF9D3DC95C0
GO

Sequence cautioni

The sequence BAA95995.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti647 – 6471L → G in CAB53676. (PubMed:17974005)Curated
Sequence conflicti1087 – 10871S → P in CAB53676. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti944 – 9441A → T.2 Publications
Corresponds to variant rs6780013 [ dbSNP | Ensembl ].
VAR_022682
Natural varianti1099 – 10991P → S in a lung cancer cell line; may be a common polymorphism. 1 Publication
Corresponds to variant rs149563514 [ dbSNP | Ensembl ].
VAR_022683

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2754.1.
PIRiT14756.
RefSeqiNP_056281.1. NM_015466.2.
UniGeneiHs.25524.

Genome annotation databases

EnsembliENST00000265562; ENSP00000265562; ENSG00000076201.
GeneIDi25930.
KEGGihsa:25930.
UCSCiuc003crf.1. human.

Polymorphism databases

DMDMi68053318.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS2754.1.
PIRi T14756.
RefSeqi NP_056281.1. NM_015466.2.
UniGenei Hs.25524.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3RAU X-ray 1.95 A/B 2-361 [» ]
ProteinModelPortali Q9H3S7.
SMRi Q9H3S7. Positions 4-697, 1142-1459.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117430. 29 interactions.
DIPi DIP-29923N.
IntActi Q9H3S7. 14 interactions.
MINTi MINT-1425077.
STRINGi 9606.ENSP00000265562.

PTM databases

PhosphoSitei Q9H3S7.

Polymorphism databases

DMDMi 68053318.

Proteomic databases

MaxQBi Q9H3S7.
PaxDbi Q9H3S7.
PeptideAtlasi Q9H3S7.
PRIDEi Q9H3S7.

Protocols and materials databases

DNASUi 25930.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265562 ; ENSP00000265562 ; ENSG00000076201 .
GeneIDi 25930.
KEGGi hsa:25930.
UCSCi uc003crf.1. human.

Organism-specific databases

CTDi 25930.
GeneCardsi GC03P047397.
HGNCi HGNC:14406. PTPN23.
HPAi HPA016845.
MIMi 606584. gene.
neXtProti NX_Q9H3S7.
PharmGKBi PA33996.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
GeneTreei ENSGT00770000120582.
HOVERGENi HBG082231.
InParanoidi Q9H3S7.
KOi K18040.
OMAi IARCYTM.
OrthoDBi EOG72C4ZH.
PhylomeDBi Q9H3S7.
TreeFami TF323502.

Miscellaneous databases

ChiTaRSi PTPN23. human.
EvolutionaryTracei Q9H3S7.
GeneWikii PTPN23.
GenomeRNAii 25930.
NextBioi 47476.
PROi Q9H3S7.
SOURCEi Search...

Gene expression databases

Bgeei Q9H3S7.
CleanExi HS_PTPN23.
ExpressionAtlasi Q9H3S7. baseline and differential.
Genevestigatori Q9H3S7.

Family and domain databases

Gene3Di 1.25.40.280. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR025304. ALIX_V_dom.
IPR004328. BRO1_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR028770. PTPN23.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view ]
PANTHERi PTHR19134:SF27. PTHR19134:SF27. 1 hit.
Pfami PF13949. ALIX_LYPXL_bnd. 1 hit.
PF03097. BRO1. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view ]
PRINTSi PR00700. PRTYPHPHTASE.
SMARTi SM01041. BRO1. 1 hit.
SM00194. PTPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS51180. BRO1. 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. "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. 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. 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. 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. 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.

Entry informationi

Entry nameiPTN23_HUMAN
AccessioniPrimary (citable) accession number: Q9H3S7
Secondary accession number(s): A8K0D7
, Q7KZF8, Q8N6Z5, Q9BSR5, Q9P257, Q9UG03, Q9UMZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: March 1, 2001
Last modified: November 26, 2014
This is version 119 of the entry and version 1 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 3
    Human chromosome 3: 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