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Protein

Tyrosine-protein phosphatase 10D

Gene

Ptp10D

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May have a role in axon outgrowth and guidance.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1436 – 14361SubstrateBy similarity
Active sitei1468 – 14681Phosphocysteine intermediatePROSITE-ProRule annotation
Binding sitei1512 – 15121SubstrateBy similarity

GO - Molecular functioni

  1. phosphoprotein phosphatase activity Source: FlyBase
  2. protein tyrosine phosphatase activity Source: FlyBase
  3. transmembrane receptor protein tyrosine phosphatase activity Source: FlyBase

GO - Biological processi

  1. axon guidance Source: FlyBase
  2. central nervous system development Source: FlyBase
  3. long-term memory Source: FlyBase
  4. motor neuron axon guidance Source: FlyBase
  5. open tracheal system development Source: FlyBase
  6. peptidyl-tyrosine dephosphorylation Source: GOC
  7. protein dephosphorylation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Protein phosphatase

Keywords - Biological processi

Differentiation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase 10D (EC:3.1.3.48)
Alternative name(s):
Receptor-linked protein-tyrosine phosphatase 10D
Short name:
DPTP10D
Gene namesi
Name:Ptp10D
ORF Names:CG1817
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0004370. Ptp10D.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini43 – 11971155ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1198 – 121821HelicalSequence AnalysisAdd
BLAST
Topological domaini1219 – 1990772CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. apical part of cell Source: FlyBase
  2. axon Source: FlyBase
  3. integral component of membrane Source: UniProtKB-KW
  4. plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4242Sequence AnalysisAdd
BLAST
Chaini43 – 19901948Tyrosine-protein phosphatase 10DPRO_0000025427Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi169 – 1691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi212 – 2121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi229 – 2291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi259 – 2591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi317 – 3171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi471 – 4711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi486 – 4861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi512 – 5121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi533 – 5331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi588 – 5881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi668 – 6681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi687 – 6871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi719 – 7191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi723 – 7231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi823 – 8231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi841 – 8411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi874 – 8741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi908 – 9081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi925 – 9251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1001 – 10011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1104 – 11041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1136 – 11361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1195 – 11951N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP35992.
PRIDEiP35992.

Expressioni

Tissue specificityi

In 9-12 hour embryos, expression is specifically seen in the anterior commissure and its junctions with the longitudinal tracts.2 Publications

Developmental stagei

Expressed both maternally and zygotically. Expressed throughout development to adulthood, lowest expression is during second and third larval instars.1 Publication

Gene expression databases

BgeeiP35992.

Interactioni

Protein-protein interaction databases

BioGridi58524. 4 interactions.
IntActiP35992. 5 interactions.

Structurei

Secondary structure

1
1990
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1254 – 12563Combined sources
Helixi1257 – 127721Combined sources
Turni1278 – 12858Combined sources
Helixi1290 – 12923Combined sources
Turni1294 – 12963Combined sources
Helixi1297 – 12993Combined sources
Helixi1309 – 13113Combined sources
Beta strandi1312 – 13143Combined sources
Turni1319 – 13213Combined sources
Turni1322 – 13254Combined sources
Beta strandi1326 – 13327Combined sources
Beta strandi1340 – 13445Combined sources
Helixi1349 – 13513Combined sources
Helixi1352 – 136110Combined sources
Beta strandi1366 – 13694Combined sources
Beta strandi1373 – 13753Combined sources
Beta strandi1387 – 13904Combined sources
Beta strandi1392 – 13943Combined sources
Beta strandi1397 – 140610Combined sources
Beta strandi1408 – 141912Combined sources
Beta strandi1422 – 143110Combined sources
Beta strandi1436 – 14383Combined sources
Helixi1444 – 145714Combined sources
Beta strandi1464 – 14674Combined sources
Beta strandi1469 – 14724Combined sources
Helixi1473 – 148715Combined sources
Turni1488 – 14903Combined sources
Beta strandi1492 – 14943Combined sources
Helixi1496 – 150611Combined sources
Helixi1514 – 152815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S3EX-ray2.40A/B1250-1533[»]
3S3FX-ray2.70A/B1250-1533[»]
3S3HX-ray2.80A/B1250-1533[»]
3S3KX-ray3.20A/B1250-1533[»]
ProteinModelPortaliP35992.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini125 – 21894Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini219 – 31496Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini407 – 49892Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini499 – 58486Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini585 – 67490Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini675 – 77197Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST
Domaini775 – 86591Fibronectin type-III 7PROSITE-ProRule annotationAdd
BLAST
Domaini866 – 95691Fibronectin type-III 8PROSITE-ProRule annotationAdd
BLAST
Domaini957 – 1057101Fibronectin type-III 9PROSITE-ProRule annotationAdd
BLAST
Domaini1272 – 1527256Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1468 – 14747Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1673 – 168614Gln-richPROSITE-ProRule annotationAdd
BLAST
Compositional biasi1932 – 197241Gly-richPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 9 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00770000120452.
InParanoidiP35992.
KOiK05694.
OrthoDBiEOG7PCJFZ.

Family and domain databases

Gene3Di2.60.40.10. 12 hits.
3.90.190.10. 1 hit.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00041. fn3. 10 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 11 hits.
SM00194. PTPc. 1 hit.
SM00404. PTPc_motif. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 6 hits.
SSF52799. SSF52799. 1 hit.
PROSITEiPS50853. FN3. 9 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Isoform G is produced by readthrough of a stop codon between the codons for Arg-1631 and His-1633. This is likely to be a rare event with most transcripts using the stop codon following Arg-1631.Curated

Isoform GImported (identifier: P35992-5) [UniParc]FASTAAdd to basket

Also known as: FImported

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLYQLSKATT RIRLKRQKAV PQHRWLWSLA FLAAFTLKDV RCADLAISIP
60 70 80 90 100
NNPGLDDGAS YRLDYSPPFG YPEPNTTIAS REIGDEIQFS RALPGTKYNF
110 120 130 140 150
WLYYTNFTHH DWLTWTVTIT TAPDPPSNLS VQVRSGKNAI ILWSPPTQGS
160 170 180 190 200
YTAFKIKVLG LSEASSSYNR TFQVNDNTFQ HSVKELTPGA TYQVQAYTIY
210 220 230 240 250
DGKESVAYTS RNFTTKPNTP GKFIVWFRNE TTLLVLWQPP YPAGIYTHYK
260 270 280 290 300
VSIEPPDAND SVLYVEKEGE PPGPAQAAFK GLVPGRAYNI SVQTMSEDEI
310 320 330 340 350
SLPTTAQYRT VPLRPLNVTF DRDFITSNSF RVLWEAPKGI SEFDKYQVSV
360 370 380 390 400
ATTRRQSTVP RSNEPVAFFD FRDIAEPGKT FNVIVKTVSG KVTSWPATGD
410 420 430 440 450
VTLRPLPVRN LRSINDDKTN TMIITWEADP ASTQDEYRIV YHELETFNGD
460 470 480 490 500
TSTLTTDRTR FTLESLLPGR NYSLSVQAVS KKMESNETSI FVVTRPSSPI
510 520 530 540 550
IEDLKSIRMG LNISWKSDVN SKQEQYEVLY SRNGTSDLRT QKTKESRLVI
560 570 580 590 600
KNLQPGAGYE LKVFAVSHDL RSEPHAYFQA VYPNPPRNMT IETVRSNSVL
610 620 630 640 650
VHWSPPESGE FTEYSIRYRT DSEQQWVRLP SVRSTEADIT DMTKGEKYTI
660 670 680 690 700
QVNTVSFGVE SPVPQEVNTT VPPNPVSNII QLVDSRNITL EWPKPEGRVE
710 720 730 740 750
SYILKWWPSD NPGRVQTKNV SENKSADDLS TVRVLIGELM PGVQYKFDIQ
760 770 780 790 800
TTSYGILSGI TSLYPRTMPL IQSDVVVANG EKEDERDTIT LSYTPTPQSS
810 820 830 840 850
SKFDIYRFSL GDAEIRDKEK LANDTDRKVT FTGLVPGRLY NITVWTVSGG
860 870 880 890 900
VASLPIQRQD RLYPEPITQL HATNITDTEI SLRWDLPKGE YNDFDIAYLT
910 920 930 940 950
ADNLLAQNMT TRNEITISDL RPHRNYTFTV VVRSGTESSV LRSSSPLSAS
960 970 980 990 1000
FTTNEAVPGR VERFHPTDVQ PSEINFEWSL PSSEANGVIR QFSIAYTNIN
1010 1020 1030 1040 1050
NLTDAGMQDF ESEEAFGVIK NLKPGETYVF KIQAKTAIGF GPEREYRQTM
1060 1070 1080 1090 1100
PILAPPRPAT QVVPTEVYRS SSTIQIRFRK NYFSDQNGQV RMYTIIVAED
1110 1120 1130 1140 1150
DAKNASGLEM PSWLDVQSYS VWLPYQAIDP YYPFENRSVE DFTIGTENCD
1160 1170 1180 1190 1200
NHKIGYCNGP LKSGTTYRVK VRAFTGADKF TDTAYSFPIQ TDQDNTSLIV
1210 1220 1230 1240 1250
AITVPLTIIL VLLVTLLFYK RRRNNCRKTT KDSRANDNMS LPDSVIEQNR
1260 1270 1280 1290 1300
PILIKNFAEH YRLMSADSDF RFSEEFEELK HVGRDQPCTF ADLPCNRPKN
1310 1320 1330 1340 1350
RFTNILPYDH SRFKLQPVDD DEGSDYINAN YVPGHNSPRE FIVTQGPLHS
1360 1370 1380 1390 1400
TRDDFWRMCW ESNSRAIVML TRCFEKGREK CDQYWPNDTV PVFYGDIKVQ
1410 1420 1430 1440 1450
ILNDSHYADW VMTEFMLCRG SEQRILRHFH FTTWPDFGVP NPPQTLVRFV
1460 1470 1480 1490 1500
RAFRDRIGAE QRPIVVHCSA GVGRSGTFIT LDRILQQINT SDYVDIFGIV
1510 1520 1530 1540 1550
YAMRKERVWM VQTEQQYICI HQCLLAVLEG KENIVGPARE MHDNEGYEGQ
1560 1570 1580 1590 1600
QVQLDENGDV VATIEGHLSH HDLQQAEAEA IDDENAAILH DDQQPLTSSF
1610 1620 1630 1640 1650
TGHHTHMPPT TSMSSFGGGG GGHTNVDAPD RXHSVVNQSD NNNSVVIVLV
1660 1670 1680 1690 1700
DNKPSSMICK DSKGGNIDVL ESQQQQQQQQ QQQPNQGGHN ITTISAINGY
1710 1720 1730 1740 1750
NTLQHRRKSQ LITFSSSSCD IKNSLSHEYI NGSNGSAANG PPSSGSGSGS
1760 1770 1780 1790 1800
GPGSNRASRA NVRLSFAEED VMILPQNHSQ QSNHQDDEVF TRRRSLLEVE
1810 1820 1830 1840 1850
IGVEVGEDGE LAPHEMEEDL EEEDEDEELY MHDEFETHID TKSNNANDDS
1860 1870 1880 1890 1900
GGGSYEDSHA LHSSLGGSNR NSLEKDDDDI EVDVISTDVS CYDQLLGSSC
1910 1920 1930 1940 1950
NTRNGDDDDI ATLVGDGDYS TTKLSKASRL SGAGVGGLVV SGGGGGTAIG
1960 1970 1980 1990
GGIAVNGGGV LGNGVGSEAG GGIIYANPFM DDEGIAESGM

Note: No experimental confirmation available.Curated

Length:1,990
Mass (Da):222,740
Last modified:January 7, 2015 - v4
Checksum:i76FAAA08565AE8DA
GO
Isoform BImported (identifier: P35992-1) [UniParc]FASTAAdd to basket

Also known as: Long

The sequence of this isoform differs from the canonical sequence as follows:
     1632-1990: Missing.

Show »
Length:1,631
Mass (Da):185,081
Checksum:i22A59AB61665875D
GO
Isoform EImported (identifier: P35992-2) [UniParc]FASTAAdd to basket

Also known as: Short, IImported

The sequence of this isoform differs from the canonical sequence as follows:
     1549-1980: Missing.

Show »
Length:1,558
Mass (Da):177,366
Checksum:i716C60806FDAC9DD
GO
Isoform HImported (identifier: P35992-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     216-216: K → SRRTRHKELLDIKILRE
     1191-1191: T → TEMLSSP
     1632-1990: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:1,653
Mass (Da):187,743
Checksum:i2E58394F82C827DB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241D → I in AAA28484 (PubMed:1657401).Curated
Sequence conflicti127 – 1271S → L in AAA28484 (PubMed:1657401).Curated
Sequence conflicti188 – 1881P → L in AAO42638 (Ref. 5) Curated
Sequence conflicti369 – 3691F → S in AAA28484 (PubMed:1657401).Curated
Sequence conflicti369 – 3691F → S in AAA28952 (PubMed:1657402).Curated
Sequence conflicti558 – 5581G → A in AAA28484 (PubMed:1657401).Curated
Sequence conflicti558 – 5581G → A in AAA28952 (PubMed:1657402).Curated
Sequence conflicti810 – 8101L → S in AAA28484 (PubMed:1657401).Curated
Sequence conflicti810 – 8101L → S in AAA28952 (PubMed:1657402).Curated
Sequence conflicti1403 – 14031N → S in AAO42638 (Ref. 5) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei216 – 2161K → SRRTRHKELLDIKILRE in isoform H. CuratedVSP_057306
Alternative sequencei1191 – 11911T → TEMLSSP in isoform H. CuratedVSP_057307
Alternative sequencei1549 – 1980432Missing in isoform E. 2 PublicationsVSP_005143Add
BLAST
Alternative sequencei1632 – 1990359Missing in isoform B and isoform H. 1 PublicationCuratedVSP_057308Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80465 mRNA. Translation: AAA28484.1.
M80538 mRNA. Translation: AAA28952.1.
AE014298 Genomic DNA. Translation: AAF48072.3.
AE014298 Genomic DNA. Translation: AAS65319.2.
AE014298 Genomic DNA. Translation: AAS65320.2.
AE014298 Genomic DNA. Translation: ACL82919.1.
AE014298 Genomic DNA. Translation: AGB95296.1.
AE014298 Genomic DNA. Translation: AGB95297.1.
BT004474 mRNA. Translation: AAO42638.1.
BT126065 mRNA. Translation: ADY17764.1.
PIRiC41214.
D41214.
RefSeqiNP_001138187.1. NM_001144715.2. [P35992-2]
NP_001259453.1. NM_001272524.1. [P35992-6]
NP_001259454.1. NM_001272525.1. [P35992-2]
NP_727544.2. NM_167292.3. [P35992-1]
NP_996413.2. NM_206690.2. [P35992-5]
NP_996414.2. NM_206691.3. [P35992-5]
UniGeneiDm.7386.

Genome annotation databases

EnsemblMetazoaiFBtr0073522; FBpp0073369; FBgn0004370. [P35992-1]
FBtr0273235; FBpp0271743; FBgn0004370. [P35992-2]
FBtr0330394; FBpp0303420; FBgn0004370. [P35992-6]
FBtr0331406; FBpp0303823; FBgn0004370. [P35992-2]
GeneIDi32115.
KEGGidme:Dmel_CG1817.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80465 mRNA. Translation: AAA28484.1.
M80538 mRNA. Translation: AAA28952.1.
AE014298 Genomic DNA. Translation: AAF48072.3.
AE014298 Genomic DNA. Translation: AAS65319.2.
AE014298 Genomic DNA. Translation: AAS65320.2.
AE014298 Genomic DNA. Translation: ACL82919.1.
AE014298 Genomic DNA. Translation: AGB95296.1.
AE014298 Genomic DNA. Translation: AGB95297.1.
BT004474 mRNA. Translation: AAO42638.1.
BT126065 mRNA. Translation: ADY17764.1.
PIRiC41214.
D41214.
RefSeqiNP_001138187.1. NM_001144715.2. [P35992-2]
NP_001259453.1. NM_001272524.1. [P35992-6]
NP_001259454.1. NM_001272525.1. [P35992-2]
NP_727544.2. NM_167292.3. [P35992-1]
NP_996413.2. NM_206690.2. [P35992-5]
NP_996414.2. NM_206691.3. [P35992-5]
UniGeneiDm.7386.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S3EX-ray2.40A/B1250-1533[»]
3S3FX-ray2.70A/B1250-1533[»]
3S3HX-ray2.80A/B1250-1533[»]
3S3KX-ray3.20A/B1250-1533[»]
ProteinModelPortaliP35992.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58524. 4 interactions.
IntActiP35992. 5 interactions.

Proteomic databases

PaxDbiP35992.
PRIDEiP35992.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0073522; FBpp0073369; FBgn0004370. [P35992-1]
FBtr0273235; FBpp0271743; FBgn0004370. [P35992-2]
FBtr0330394; FBpp0303420; FBgn0004370. [P35992-6]
FBtr0331406; FBpp0303823; FBgn0004370. [P35992-2]
GeneIDi32115.
KEGGidme:Dmel_CG1817.

Organism-specific databases

CTDi32115.
FlyBaseiFBgn0004370. Ptp10D.

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00770000120452.
InParanoidiP35992.
KOiK05694.
OrthoDBiEOG7PCJFZ.

Miscellaneous databases

ChiTaRSiPtp10D. fly.
GenomeRNAii32115.
NextBioi776913.
PROiP35992.

Gene expression databases

BgeeiP35992.

Family and domain databases

Gene3Di2.60.40.10. 12 hits.
3.90.190.10. 1 hit.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00041. fn3. 10 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 11 hits.
SM00194. PTPc. 1 hit.
SM00404. PTPc_motif. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 6 hits.
SSF52799. SSF52799. 1 hit.
PROSITEiPS50853. FN3. 9 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two Drosophila receptor-like tyrosine phosphatase genes are expressed in a subset of developing axons and pioneer neurons in the embryonic CNS."
    Yang X., Seow K.T., Bahri S.M., Oon S.H., Chia W.
    Cell 67:661-673(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND E), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  2. "Three receptor-linked protein-tyrosine phosphatases are selectively expressed on central nervous system axons in the Drosophila embryo."
    Tian S.-S., Tsoulfas P., Zinn K.
    Cell 67:675-685(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E), TISSUE SPECIFICITY.
    Tissue: Embryo.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-1197 (ISOFORMS G/B/E).
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiPTP10_DROME
AccessioniPrimary (citable) accession number: P35992
Secondary accession number(s): A4V4B4
, B7Z142, F0JAM3, M9PEB6, M9PJI5, Q0KHT5, Q86NN9, Q8IR87, Q9VYW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 7, 2015
Last modified: April 1, 2015
This is version 138 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

This protein is translated by readthrough of a stop codon. Readthrough of the terminator codon TAG occurs between the codons for Arg-1631 and His-1633. There is currently no sequence that provides the identity of residue 1632.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.