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P16621

- LAR_DROME

UniProt

P16621 - LAR_DROME

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Protein

Tyrosine-protein phosphatase Lar

Gene

Lar

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

Functioni

Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase). It controls motor axon guidance.2 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 PublicationPROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1638 – 16381SubstrateBy similarity
Active sitei1670 – 16701Phosphocysteine intermediateBy similarity
Binding sitei1714 – 17141SubstrateBy similarity
Active sitei1961 – 19611Phosphocysteine intermediateBy similarity

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW
  2. protein tyrosine phosphatase activity Source: FlyBase
  3. SAM domain binding Source: FlyBase
  4. transmembrane receptor protein tyrosine phosphatase activity Source: FlyBase

GO - Biological processi

  1. axon extension Source: FlyBase
  2. axon guidance Source: FlyBase
  3. axon target recognition Source: FlyBase
  4. cell adhesion Source: FlyBase
  5. embryonic development via the syncytial blastoderm Source: FlyBase
  6. motor neuron axon guidance Source: FlyBase
  7. nervous system development Source: FlyBase
  8. oogenesis Source: FlyBase
  9. peptidyl-tyrosine dephosphorylation Source: GOC
  10. photoreceptor cell morphogenesis Source: FlyBase
  11. protein dephosphorylation Source: FlyBase
  12. R7 cell development Source: FlyBase
  13. regulation of axon extension involved in axon guidance Source: FlyBase
  14. regulation of cell shape Source: FlyBase
  15. retinal ganglion cell axon guidance Source: FlyBase
  16. synaptic growth at neuromuscular junction Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase, Receptor

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase Lar (EC:3.1.3.48)
Alternative name(s):
Protein-tyrosine-phosphate phosphohydrolase
dLAR
Gene namesi
Name:Lar
ORF Names:CG10443
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0000464. Lar.

Subcellular locationi

GO - Cellular componenti

  1. axon Source: FlyBase
  2. focal adhesion Source: FlyBase
  3. integral component of membrane Source: UniProtKB-KW
  4. microtubule associated complex Source: FlyBase
  5. plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Add
BLAST
Chaini33 – 20291997Tyrosine-protein phosphatase LarPRO_0000025431Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi57 ↔ 1111 PublicationPROSITE-ProRule annotation
Disulfide bondi161 ↔ 2091 PublicationPROSITE-ProRule annotation
Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi256 ↔ 301PROSITE-ProRule annotation
Glycosylationi298 – 2981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi553 – 5531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi616 – 6161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi666 – 6661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi721 – 7211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi774 – 7741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi915 – 9151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi962 – 9621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1183 – 11831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1304 – 13041N-linked (GlcNAc...)Sequence Analysis
Modified residuei1572 – 15721Phosphothreonine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP16621.
PRIDEiP16621.

Expressioni

Tissue specificityi

Selectively expressed in a subset of axons and pioneer neurons in the embryo.1 Publication

Gene expression databases

BgeeiP16621.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
AblP005224EBI-668630,EBI-534090
enaQ8T4F72EBI-668630,EBI-466810
Liprin-alphaQ9VM936EBI-668630,EBI-113116

Protein-protein interaction databases

BioGridi61235. 8 interactions.
DIPiDIP-38648N.
IntActiP16621. 3 interactions.
MINTiMINT-8310371.

Structurei

Secondary structure

1
2029
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 404
Beta strandi45 – 484
Beta strandi53 – 608
Beta strandi66 – 716
Beta strandi83 – 886
Turni89 – 913
Beta strandi92 – 998
Turni102 – 1043
Beta strandi107 – 1148
Beta strandi116 – 1183
Beta strandi120 – 13011
Beta strandi141 – 1444
Beta strandi149 – 1524
Beta strandi157 – 1593
Beta strandi162 – 1643
Beta strandi170 – 1756
Beta strandi187 – 1904
Beta strandi193 – 1964
Helixi201 – 2033
Beta strandi205 – 2139
Beta strandi216 – 2194
Beta strandi223 – 2286

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YD1X-ray1.80A33-232[»]
3PXJX-ray2.30A/B/C/D32-237[»]
ProteinModelPortaliP16621.
SMRiP16621. Positions 32-1102, 1168-1197, 1448-2024.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16621.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 13771345ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1403 – 2029627CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1378 – 140225HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 12893Ig-like C2-type 1Add
BLAST
Domaini140 – 22485Ig-like C2-type 2Add
BLAST
Domaini234 – 31683Ig-like C2-type 3Add
BLAST
Domaini324 – 41491Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini419 – 51395Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini517 – 60892Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini613 – 70795Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini711 – 810100Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini815 – 91197Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST
Domaini912 – 100594Fibronectin type-III 7PROSITE-ProRule annotationAdd
BLAST
Domaini1009 – 110294Fibronectin type-III 8PROSITE-ProRule annotationAdd
BLAST
Domaini1104 – 1206103Fibronectin type-III 9PROSITE-ProRule annotationAdd
BLAST
Domaini1474 – 1729256Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
BLAST
Domaini1761 – 2020260Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 8213Heparin-bindingAdd
BLAST
Regioni1670 – 16767Substrate bindingBy similarity

Sequence similaritiesi

Contains 9 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00760000118900.
InParanoidiP16621.
KOiK05695.
OrthoDBiEOG7M98FB.
PhylomeDBiP16621.

Family and domain databases

Gene3Di2.60.40.10. 12 hits.
3.90.190.10. 2 hits.
InterProiIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00041. fn3. 9 hits.
PF07679. I-set. 3 hits.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 9 hits.
SM00408. IGc2. 3 hits.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 6 hits.
SSF52799. SSF52799. 2 hits.
PROSITEiPS50853. FN3. 9 hits.
PS50835. IG_LIKE. 3 hits.
PS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P16621-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGLQMTAARP IAALSLLVLS LLTWTHPTIV DAAHPPEIIR KPQNQGVRVG
60 70 80 90 100
GVASFYCAAR GDPPPSIVWR KNGKKVSGTQ SRYTVLEQPG GISILRIEPV
110 120 130 140 150
RAGRDDAPYE CVAENGVGDA VSADATLTIY EGDKTPAGFP VITQGPGTRV
160 170 180 190 200
IEVGHTVLMT CKAIGNPTPN IYWIKNQTKV DMSNPRYSLK DGFLQIENSR
210 220 230 240 250
EEDQGKYECV AENSMGTEHS KATNLYVKVR RVPPTFSRPP ETISEVMLGS
260 270 280 290 300
NLNLSCIAVG SPMPHVKWMK GSEDLTPENE MPIGRNVLQL INIQESANYT
310 320 330 340 350
CIAASTLGQI DSVSVVKVQS LPTAPTDVQI SEVTATSVRL EWSYKGPEDL
360 370 380 390 400
QYYVIQYKPK NANQAFSEIS GIITMYYVVR ALSPYTEYEF YVIAVNNIGR
410 420 430 440 450
GPPSAPATCT TGETKMESAP RNVQVRTLSS STMVITWEPP ETPNGQVTGY
460 470 480 490 500
KVYYTTNSNQ PEASWNSQMV DNSELTTVSE LTPHAIYTVR VQAYTSMGAG
510 520 530 540 550
PMSTPVQVKA QQGVPSQPSN FRATDIGETA VTLQWTKPTH SSENIVHYEL
560 570 580 590 600
YWNDTYANQA HHKRISNSEA YTLDGLYPDT LYYIWLAARS QRGEGATTPP
610 620 630 640 650
IPVRTKQYVP GAPPRNITAI ATSSTTISLS WLPPPVERSN GRIIYYKVFF
660 670 680 690 700
VEVGREDDEA TTMTLNMTSI VLDELKRWTE YKIWVLAGTS VGDGPRSHPI
710 720 730 740 750
ILRTQEDVPG DPQDVKATPL NSTSIHVSWK PPLEKDRNGI IRGYHIHAQE
760 770 780 790 800
LRDEGKGFLN EPFKFDVVDT LEFNVTGLQP DTKYSIQVAA LTRKGDGDRS
810 820 830 840 850
AAIVVKTPGG VPVRPTVSLK IMEREPIVSI ELEWERPAQT YGELRGYRLR
860 870 880 890 900
WGVKDQALKE EMLSGPQMTK KRFDNLERGV EYEFRVAGSN HIGIGQETVK
910 920 930 940 950
IFQTPEGTPG GPPSNITIRF QTPDVLCVTW DPPTREHRNG IITRYDVQFH
960 970 980 990 1000
KKIDHGLGSE RNMTLRKAVF TNLEENTEYI FRVRAYTKQG AGPFSDKLIV
1010 1020 1030 1040 1050
ETERDMGRAP MSLQAEATSE QTAEIWWEPV TSRGKLLGYK IFYTMTAVED
1060 1070 1080 1090 1100
LDDWQTKTVG LTESADLVNL EKFAQYAVAI AARFKNGLGR LSEKVTVRIK
1110 1120 1130 1140 1150
PEDVPLNLRA HDVSTHSMTL SWSPPIRLTP VNYKISFDAM KVFVDSQGFS
1160 1170 1180 1190 1200
QTQIVPKREI ILKHYVKTHT INELSPFTTY NVNVSAIPSD YSYRPPTKIT
1210 1220 1230 1240 1250
VTTQMAAPQP MVKPDFYGVV NGEEILVILP QASEEYGPIS HYYLVVVPED
1260 1270 1280 1290 1300
KSNLHKIPDQ FLTDDLLPGR NKPERPNAPY IAAKFPQRSI PFTFHLGSGD
1310 1320 1330 1340 1350
DYHNFTNRKL EREKRYRIFV RAVVDTPQKH LYTSSPFSEF LSLDMREAPP
1360 1370 1380 1390 1400
GERPHRPDPN WPAEPEVSVN RNKDEPEILW VVLPLMVSTF IVSTALIVLC
1410 1420 1430 1440 1450
VVKRRRQPCK TPDQAAVTRP LMAADLGAGP TPSDPVDMRR LNFQTPGMIS
1460 1470 1480 1490 1500
HPPIPISEFA NHIERLKSND NQKFSQEYES IEPGQQFTWD NSNLEHNKSK
1510 1520 1530 1540 1550
NRYANVTAYD HSRVQLPAVE GVVGSDYINA NYCDGYRKHN AYVATQGPLQ
1560 1570 1580 1590 1600
ETFVDFWRMC WELKTATIVM MTRLEERTRI KCDQYWPTRG TETYGQIFVT
1610 1620 1630 1640 1650
ITETQELATY SIRTFQLCRQ GFNDRREIKQ LQFTAWPDHG VPDHPAPFLQ
1660 1670 1680 1690 1700
FLRRCRALTP PESGPVIVHC SAGVGRTGCY IVIDSMLERM KHEKIIDIYG
1710 1720 1730 1740 1750
HVTCLRAQRN YMVQTEDQYI FIHDAILEAI ICGVTEVPAR NLHTHLQKLL
1760 1770 1780 1790 1800
ITEPGETISG MEVEFKKLSN VKMDSSKFVT ANLPCNKHKN RLVHILPYES
1810 1820 1830 1840 1850
SRVYLTPIHG IEGSDYVNAS FIDGYRYRSA YIAAQGPVQD AAEDFWRMLW
1860 1870 1880 1890 1900
EHNSTIVVML TKLKEMGREK CFQYWPHERS VRYQYYVVDP IAEYNMPQYK
1910 1920 1930 1940 1950
LREFKVTDAR DGSSRTVRQF QFIDWPEQGV PKSGEGFIDF IGQVHKTKEQ
1960 1970 1980 1990 2000
FGQDGPITVH CSAGVGRSGV FITLSIVLER MQYEGVLDVF QTVRILRSQR
2010 2020
PAMVQTEDQY HFCYRAALEY LGSFDNYTN
Length:2,029
Mass (Da):229,056
Last modified:August 30, 2005 - v2
Checksum:iDF1F676A94050F2B
GO

Sequence cautioni

The sequence AAK93409.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti480 – 4812EL → DV(PubMed:2554325)Curated
Sequence conflicti480 – 4812EL → DV(PubMed:8598047)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M27700 mRNA. Translation: AAA28668.1.
U36857
, U36849, U36850, U36851, U36852, U36853, U36854, U36855, U36856 Genomic DNA. Translation: AAC47002.1.
AE014134 Genomic DNA. Translation: AAF53837.3.
AY051985 mRNA. Translation: AAK93409.1. Different initiation.
PIRiA36182. TDFFLK.
RefSeqiNP_523604.2. NM_078880.3.
UniGeneiDm.24416.

Genome annotation databases

EnsemblMetazoaiFBtr0081260; FBpp0080801; FBgn0000464.
GeneIDi35259.
KEGGidme:Dmel_CG10443.
UCSCiCG10443-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M27700 mRNA. Translation: AAA28668.1 .
U36857
, U36849 , U36850 , U36851 , U36852 , U36853 , U36854 , U36855 , U36856 Genomic DNA. Translation: AAC47002.1 .
AE014134 Genomic DNA. Translation: AAF53837.3 .
AY051985 mRNA. Translation: AAK93409.1 . Different initiation.
PIRi A36182. TDFFLK.
RefSeqi NP_523604.2. NM_078880.3.
UniGenei Dm.24416.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YD1 X-ray 1.80 A 33-232 [» ]
3PXJ X-ray 2.30 A/B/C/D 32-237 [» ]
ProteinModelPortali P16621.
SMRi P16621. Positions 32-1102, 1168-1197, 1448-2024.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 61235. 8 interactions.
DIPi DIP-38648N.
IntActi P16621. 3 interactions.
MINTi MINT-8310371.

Proteomic databases

PaxDbi P16621.
PRIDEi P16621.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0081260 ; FBpp0080801 ; FBgn0000464 .
GeneIDi 35259.
KEGGi dme:Dmel_CG10443.
UCSCi CG10443-RA. d. melanogaster.

Organism-specific databases

CTDi 104121.
FlyBasei FBgn0000464. Lar.

Phylogenomic databases

eggNOGi COG5599.
GeneTreei ENSGT00760000118900.
InParanoidi P16621.
KOi K05695.
OrthoDBi EOG7M98FB.
PhylomeDBi P16621.

Miscellaneous databases

EvolutionaryTracei P16621.
GenomeRNAii 35259.
NextBioi 792660.

Gene expression databases

Bgeei P16621.

Family and domain databases

Gene3Di 2.60.40.10. 12 hits.
3.90.190.10. 2 hits.
InterProi IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view ]
Pfami PF00041. fn3. 9 hits.
PF07679. I-set. 3 hits.
PF00102. Y_phosphatase. 2 hits.
[Graphical view ]
PRINTSi PR00700. PRTYPHPHTASE.
SMARTi SM00060. FN3. 9 hits.
SM00408. IGc2. 3 hits.
SM00194. PTPc. 2 hits.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 6 hits.
SSF52799. SSF52799. 2 hits.
PROSITEi PS50853. FN3. 9 hits.
PS50835. IG_LIKE. 3 hits.
PS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila."
    Streuli M., Krueger N.X., Tsai A.Y.M., Saito H.
    Proc. Natl. Acad. Sci. U.S.A. 86:8698-8702(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
  2. "The transmembrane tyrosine phosphatase DLAR controls motor axon guidance in Drosophila."
    Krueger N.X., van Vactor D., Wan H.I., Gelbart W.M., Goodman C.S., Saito H.
    Cell 84:611-622(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: Canton-S.
  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.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 428-2029.
    Strain: Berkeley.
    Tissue: Embryo.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1572, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  7. "The immunoglobulin-like domains 1 and 2 of the protein tyrosine phosphatase LAR adopt an unusual horseshoe-like conformation."
    Biersmith B.H., Hammel M., Geisbrecht E.R., Bouyain S.
    J. Mol. Biol. 408:616-627(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 32-237, HEPARIN-BINDING REGION, DISULFIDE BONDS.

Entry informationi

Entry nameiLAR_DROME
AccessioniPrimary (citable) accession number: P16621
Secondary accession number(s): Q960M3, Q9VIS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 30, 2005
Last modified: October 29, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

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