SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P16621

- LAR_DROME

UniProt

P16621 - LAR_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Tyrosine-protein phosphatase Lar

Gene
Lar, CG10443
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 Publication

Sites

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

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW
  2. protein binding Source: IntAct
  3. protein tyrosine phosphatase activity Source: FlyBase
  4. SAM domain binding Source: FlyBase
  5. 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 13771345Extracellular Reviewed predictionAdd
BLAST
Transmembranei1378 – 140225Helical; Reviewed predictionAdd
BLAST
Topological domaini1403 – 2029627Cytoplasmic Reviewed predictionAdd
BLAST

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 Publication
Disulfide bondi161 ↔ 2091 Publication
Glycosylationi176 – 1761N-linked (GlcNAc...) Reviewed prediction
Glycosylationi253 – 2531N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi256 ↔ 301 Reviewed prediction
Glycosylationi298 – 2981N-linked (GlcNAc...) Reviewed prediction
Glycosylationi553 – 5531N-linked (GlcNAc...) Reviewed prediction
Glycosylationi616 – 6161N-linked (GlcNAc...) Reviewed prediction
Glycosylationi666 – 6661N-linked (GlcNAc...) Reviewed prediction
Glycosylationi721 – 7211N-linked (GlcNAc...) Reviewed prediction
Glycosylationi774 – 7741N-linked (GlcNAc...) Reviewed prediction
Glycosylationi915 – 9151N-linked (GlcNAc...) Reviewed prediction
Glycosylationi962 – 9621N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1183 – 11831N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1304 – 13041N-linked (GlcNAc...) Reviewed prediction
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 32-1003, 1063-1099, 1448-2024.

Miscellaneous databases

EvolutionaryTraceiP16621.

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 1Add
BLAST
Domaini419 – 51395Fibronectin type-III 2Add
BLAST
Domaini517 – 60892Fibronectin type-III 3Add
BLAST
Domaini613 – 70795Fibronectin type-III 4Add
BLAST
Domaini711 – 810100Fibronectin type-III 5Add
BLAST
Domaini815 – 91197Fibronectin type-III 6Add
BLAST
Domaini912 – 100594Fibronectin type-III 7Add
BLAST
Domaini1009 – 110294Fibronectin type-III 8Add
BLAST
Domaini1104 – 1206103Fibronectin type-III 9Add
BLAST
Domaini1474 – 1729256Tyrosine-protein phosphatase 1Add
BLAST
Domaini1761 – 2020260Tyrosine-protein phosphatase 2Add
BLAST

Region

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

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00590000082937.
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

MGLQMTAARP IAALSLLVLS LLTWTHPTIV DAAHPPEIIR KPQNQGVRVG     50
GVASFYCAAR GDPPPSIVWR KNGKKVSGTQ SRYTVLEQPG GISILRIEPV 100
RAGRDDAPYE CVAENGVGDA VSADATLTIY EGDKTPAGFP VITQGPGTRV 150
IEVGHTVLMT CKAIGNPTPN IYWIKNQTKV DMSNPRYSLK DGFLQIENSR 200
EEDQGKYECV AENSMGTEHS KATNLYVKVR RVPPTFSRPP ETISEVMLGS 250
NLNLSCIAVG SPMPHVKWMK GSEDLTPENE MPIGRNVLQL INIQESANYT 300
CIAASTLGQI DSVSVVKVQS LPTAPTDVQI SEVTATSVRL EWSYKGPEDL 350
QYYVIQYKPK NANQAFSEIS GIITMYYVVR ALSPYTEYEF YVIAVNNIGR 400
GPPSAPATCT TGETKMESAP RNVQVRTLSS STMVITWEPP ETPNGQVTGY 450
KVYYTTNSNQ PEASWNSQMV DNSELTTVSE LTPHAIYTVR VQAYTSMGAG 500
PMSTPVQVKA QQGVPSQPSN FRATDIGETA VTLQWTKPTH SSENIVHYEL 550
YWNDTYANQA HHKRISNSEA YTLDGLYPDT LYYIWLAARS QRGEGATTPP 600
IPVRTKQYVP GAPPRNITAI ATSSTTISLS WLPPPVERSN GRIIYYKVFF 650
VEVGREDDEA TTMTLNMTSI VLDELKRWTE YKIWVLAGTS VGDGPRSHPI 700
ILRTQEDVPG DPQDVKATPL NSTSIHVSWK PPLEKDRNGI IRGYHIHAQE 750
LRDEGKGFLN EPFKFDVVDT LEFNVTGLQP DTKYSIQVAA LTRKGDGDRS 800
AAIVVKTPGG VPVRPTVSLK IMEREPIVSI ELEWERPAQT YGELRGYRLR 850
WGVKDQALKE EMLSGPQMTK KRFDNLERGV EYEFRVAGSN HIGIGQETVK 900
IFQTPEGTPG GPPSNITIRF QTPDVLCVTW DPPTREHRNG IITRYDVQFH 950
KKIDHGLGSE RNMTLRKAVF TNLEENTEYI FRVRAYTKQG AGPFSDKLIV 1000
ETERDMGRAP MSLQAEATSE QTAEIWWEPV TSRGKLLGYK IFYTMTAVED 1050
LDDWQTKTVG LTESADLVNL EKFAQYAVAI AARFKNGLGR LSEKVTVRIK 1100
PEDVPLNLRA HDVSTHSMTL SWSPPIRLTP VNYKISFDAM KVFVDSQGFS 1150
QTQIVPKREI ILKHYVKTHT INELSPFTTY NVNVSAIPSD YSYRPPTKIT 1200
VTTQMAAPQP MVKPDFYGVV NGEEILVILP QASEEYGPIS HYYLVVVPED 1250
KSNLHKIPDQ FLTDDLLPGR NKPERPNAPY IAAKFPQRSI PFTFHLGSGD 1300
DYHNFTNRKL EREKRYRIFV RAVVDTPQKH LYTSSPFSEF LSLDMREAPP 1350
GERPHRPDPN WPAEPEVSVN RNKDEPEILW VVLPLMVSTF IVSTALIVLC 1400
VVKRRRQPCK TPDQAAVTRP LMAADLGAGP TPSDPVDMRR LNFQTPGMIS 1450
HPPIPISEFA NHIERLKSND NQKFSQEYES IEPGQQFTWD NSNLEHNKSK 1500
NRYANVTAYD HSRVQLPAVE GVVGSDYINA NYCDGYRKHN AYVATQGPLQ 1550
ETFVDFWRMC WELKTATIVM MTRLEERTRI KCDQYWPTRG TETYGQIFVT 1600
ITETQELATY SIRTFQLCRQ GFNDRREIKQ LQFTAWPDHG VPDHPAPFLQ 1650
FLRRCRALTP PESGPVIVHC SAGVGRTGCY IVIDSMLERM KHEKIIDIYG 1700
HVTCLRAQRN YMVQTEDQYI FIHDAILEAI ICGVTEVPAR NLHTHLQKLL 1750
ITEPGETISG MEVEFKKLSN VKMDSSKFVT ANLPCNKHKN RLVHILPYES 1800
SRVYLTPIHG IEGSDYVNAS FIDGYRYRSA YIAAQGPVQD AAEDFWRMLW 1850
EHNSTIVVML TKLKEMGREK CFQYWPHERS VRYQYYVVDP IAEYNMPQYK 1900
LREFKVTDAR DGSSRTVRQF QFIDWPEQGV PKSGEGFIDF IGQVHKTKEQ 1950
FGQDGPITVH CSAGVGRSGV FITLSIVLER MQYEGVLDVF QTVRILRSQR 2000
PAMVQTEDQY HFCYRAALEY LGSFDNYTN 2029
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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti480 – 4812EL → DV1 Publication
Sequence conflicti480 – 4812EL → DV1 Publication

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 32-1003, 1063-1099, 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 ENSGT00590000082937.
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: July 9, 2014
This is version 158 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

Similar proteinsi