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P98159

- NUDEL_DROME

UniProt

P98159 - NUDEL_DROME

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Protein
Serine protease nudel
Gene
ndl, CG10129
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Component of the extracellular signaling pathway that establishes the dorsal-ventral pathway of the embryo. Three proteases; ndl, gd and snk process easter to create active easter. Active easter defines cell identities along the dorsal-ventral continuum by activating the spz ligand for the Tl receptor in the ventral region of the embryo. Nudel, pipe and windbeutel together trigger the protease cascade within the extraembryonic perivitelline compartment which induces dorsoventral polarity of the Drosophila embryo.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1185 – 11851Charge relay system By similarity
Active sitei1233 – 12331Charge relay system By similarity
Active sitei1332 – 13321Charge relay system By similarity

GO - Molecular functioni

  1. peptidase activity Source: FlyBase
  2. serine-type endopeptidase activity Source: FlyBase
  3. serine-type peptidase activity Source: FlyBase

GO - Biological processi

  1. Toll signaling pathway Source: FlyBase
  2. dorsal/ventral axis specification Source: FlyBase
  3. egg activation Source: FlyBase
  4. eggshell chorion assembly Source: FlyBase
  5. maternal specification of dorsal/ventral axis, oocyte, soma encoded Source: FlyBase
  6. oocyte dorsal/ventral axis specification Source: FlyBase
  7. protein processing Source: FlyBase
  8. proteolysis Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.013.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine protease nudel (EC:3.4.21.-)
Gene namesi
Name:ndl
ORF Names:CG10129
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0002926. ndl.

Subcellular locationi

Secretedextracellular spaceextracellular matrix 1 Publication

GO - Cellular componenti

  1. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4343 Reviewed prediction
Add
BLAST
Chaini44 – 26162573Serine protease nudel
PRO_0000028136Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei215 – 2151Phosphoserine1 Publication
Modified residuei220 – 2201Phosphoserine1 Publication
Glycosylationi291 – 2911N-linked (GlcNAc...) Reviewed prediction
Glycosylationi347 – 3471N-linked (GlcNAc...) Reviewed prediction
Glycosylationi379 – 3791N-linked (GlcNAc...) Reviewed prediction
Glycosylationi417 – 4171N-linked (GlcNAc...) Reviewed prediction
Glycosylationi492 – 4921N-linked (GlcNAc...) Reviewed prediction
Glycosylationi515 – 5151N-linked (GlcNAc...) Reviewed prediction
Modified residuei574 – 5741Phosphoserine1 Publication
Modified residuei581 – 5811Phosphoserine1 Publication
Glycosylationi598 – 5981N-linked (GlcNAc...) Reviewed prediction
Glycosylationi794 – 7941O-linked (Xyl...) (glycosaminoglycan) Reviewed prediction
Glycosylationi827 – 8271N-linked (GlcNAc...) Reviewed prediction
Glycosylationi829 – 8291O-linked (Xyl...) (glycosaminoglycan) Reviewed prediction
Glycosylationi861 – 8611N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi891 ↔ 905 By similarity
Disulfide bondi899 ↔ 918 By similarity
Disulfide bondi912 ↔ 927 By similarity
Disulfide bondi957 ↔ 982 By similarity
Disulfide bondi964 ↔ 995 By similarity
Glycosylationi975 – 9751N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi989 ↔ 1004 By similarity
Glycosylationi1064 – 10641N-linked (GlcNAc...) Reviewed prediction
Modified residuei1134 – 11341Phosphoserine1 Publication
Modified residuei1136 – 11361Phosphoserine1 Publication
Disulfide bondi1170 ↔ 1186 By similarity
Disulfide bondi1276 ↔ 1338 Reviewed prediction
Disulfide bondi1305 ↔ 1317 By similarity
Disulfide bondi1328 ↔ 1359 By similarity
Disulfide bondi1396 ↔ 1408 By similarity
Disulfide bondi1401 ↔ 1421 By similarity
Disulfide bondi1415 ↔ 1430 By similarity
Glycosylationi1445 – 14451N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1728 ↔ 1745 By similarity
Disulfide bondi1734 ↔ 1764 By similarity
Disulfide bondi1758 ↔ 1773 By similarity
Disulfide bondi1776 ↔ 1789 By similarity
Disulfide bondi1783 ↔ 1802 By similarity
Disulfide bondi1796 ↔ 1811 By similarity
Glycosylationi1878 – 18781N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1956 – 19561N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2023 – 20231N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2055 ↔ 2071 By similarity
Glycosylationi2144 – 21441N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2173 – 21731N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2177 ↔ 2230 By similarity
Glycosylationi2197 – 21971N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2237 – 22371N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2269 – 22691N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2310 ↔ 2320 By similarity
Disulfide bondi2315 ↔ 2333 By similarity
Disulfide bondi2327 ↔ 2344 By similarity
Disulfide bondi2351 ↔ 2364 By similarity
Disulfide bondi2358 ↔ 2377 By similarity
Disulfide bondi2371 ↔ 2387 By similarity
Glycosylationi2420 – 24201N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2421 ↔ 2435 By similarity
Disulfide bondi2428 ↔ 2448 By similarity
Disulfide bondi2442 ↔ 2457 By similarity
Glycosylationi2556 – 25561N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2601 – 26011N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

Requires cleavage for activation (presumably).

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

PaxDbiP98159.

Expressioni

Tissue specificityi

Follicle.1 Publication

Gene expression databases

BgeeiP98159.

Interactioni

Protein-protein interaction databases

BioGridi64189. 1 interaction.
STRINGi7227.FBpp0076693.

Structurei

3D structure databases

ProteinModelPortaliP98159.
SMRiP98159. Positions 897-1053, 1100-1379, 1727-1811, 2037-2151, 2311-2461.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati261 – 2699WIID 1
Repeati320 – 3289WIID 2
Repeati399 – 4079WIID 3
Repeati446 – 4549WIID 4
Repeati477 – 4859WIID 5
Repeati528 – 5369WIID 6
Domaini889 – 92941LDL-receptor class A 1
Add
BLAST
Domaini929 – 95628LDL-receptor class A 2; truncated
Add
BLAST
Domaini955 – 100652LDL-receptor class A 3
Add
BLAST
Domaini1145 – 1383239Peptidase S1 1
Add
BLAST
Domaini1394 – 143239LDL-receptor class A 4
Add
BLAST
Domaini1713 – 174331LDL-receptor class A 5; truncated
Add
BLAST
Domaini1745 – 177531LDL-receptor class A 6; truncated
Add
BLAST
Domaini1774 – 181340LDL-receptor class A 7
Add
BLAST
Domaini2027 – 2301275Peptidase S1 2
Add
BLAST
Domaini2308 – 234639LDL-receptor class A 8
Add
BLAST
Domaini2349 – 238941LDL-receptor class A 9
Add
BLAST
Domaini2387 – 241933LDL-receptor class A 10; truncated
Add
BLAST
Domaini2419 – 245941LDL-receptor class A 11
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1031 – 10333Cell attachment site Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1489 – 1702214Ser/Thr-rich
Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.
Contains 2 peptidase S1 domains.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00740000115494.
InParanoidiP98159.
OMAiPNGEDER.
OrthoDBiEOG75B84T.
PhylomeDBiP98159.

Family and domain databases

Gene3Di4.10.400.10. 7 hits.
InterProiIPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR015420. Peptidase_S1A_nudel.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF09342. DUF1986. 1 hit.
PF00057. Ldl_recept_a. 4 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00192. LDLa. 9 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF57424. SSF57424. 7 hits.
PROSITEiPS01209. LDLRA_1. 6 hits.
PS50068. LDLRA_2. 8 hits.
PS50240. TRYPSIN_DOM. 2 hits.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P98159-1 [UniParc]FASTAAdd to Basket

« Hide

MNYNMDEMEA TRLLRHPRRW WSIGFGKRIV AISILVIIVL LFSLVYHGLV     50
VEKIDQVQQI AALNARHQVL FNQPFEEDQS ALIVSPQTLH FKLLDEDMNK 100
DMEDSKNRRR KHMRQMLVKF RLNKKHRMRR DLHGLDLLDP VRMEANMQHL 150
YTKLRSKRAR EALSQLEHEF VRCKKHTPQD CMSAFLRMYK MAKEVTEKME 200
KMKAIMREQQ PKLESSSMES HEQKGTFSPA DLIQVTTAEA TTVAVHATEK 250
PARTKIKPSR ISWIIDGHDH DESPVYTDGA PKKETTKAPW NTTQLVEITT 300
TKIDATATER TTVESTTEKI SWILDHFDKP QEILRTTEGP GQRIIRNVTT 350
TSASSEPIVD TENTNSDHVP TTENGLVFNI TTDGPVETTK STAQRKLSFD 400
WILDGEENVE PEVKSTNTTT TTAATTTTGA TSETIIVTTE LPKITFDWII 450
DGREVVEPQE TTTEVTGTTE RLRKMPFDWI IDGEEVVEPQ ENVTTTTIAT 500
TVAVSTTEIN ERIHNSTAYP TKPKPVKFDW IIDGGESSGE VSTSSTSQPK 550
LTTREAISNP ESPRSSHPLD NPTSIENMLE SFEQHEEQKP ILRVLNANES 600
SSETVTDGYE RQLWLKKFED QARPNQNELI DTFGTALDAK ALDKMGPKIN 650
PLNGHTWNAA DAQILSLCER VALRMRNKVA TMSDGETKEK GETFTASPSV 700
QFTSRAPGGF PVSGETMKAS AQFMFNPNFG MPSIPVCFYM TPANFRMPMW 750
SNTPTFMGMQ GAHFGGSSNP GAGIFFVPQQ FGPSGNFFGG SGGSGAGGQG 800
ANIFSKNASP QKPTNGQQQV YCSYMQNQSG QGAGQSQTSS QQQQGGQSAF 850
SNANFKMRHA NQTNTANQQG QIIYASYAGL PQQPIQERSR CPEPDQFSCF 900
GQQECIPAAR WCDNVVDCSD GSDESACTCA DRVDEERLCD GYEDCPMGED 950
ELGCFGCESL AYSCYENPQD FAKRNRSTIS MCYSRLERCD GFMNCLNGRD 1000
EEQCSMLVTD VADHMSHGAS ASEGYLYHNY RGDWHPVCNN GEKWAALACQ 1050
MDENSRMDHS ASLNVSFQTL TLPGPFIEPS LHAGVHFAQA CHGRNSHDSL 1100
VDHVAYVKCP PMQCGLPSKS SMLEHSKRVR RAVSDSKEIV GDGRIVGGSY 1150
TSALQWPFVV AIYRNGKFHC GGTIYSDRWI ISAAHCVINY GKYFYEVRAG 1200
LLRRSSYSPA TQIQPVSHVV VHQAYERRSM RNDLSLLRLL NPLQFNRWVK 1250
PICLPDKGRT TVGDDWIWGP VEHTLCTVVG WGAIREKGPS SDPMRQVIVP 1300
IRKKCTDPED QASEDICAGD PDGGRDACQG DSGGPLFCRS VSNPDEFYLA 1350
GVVSHGNGCA RPQEFGVYTR VTLYLDWLEM ATTPRLLPKL QPLQLCPGFI 1400
CVWGGKRCIA KRQRCDRNVD CLGGEDEVGC TYNFLPDMVG GVRQNISTTT 1450
ESDYHPVKES EEKSKMREVI PIDDEDLKAE QDEEDLLKST TSLGQTETTQ 1500
GPMDLSFAEQ ITSTTSDDLS ITDETTSTDF TVSDSATSPS TLLPTTTNPS 1550
TWLPSTNIET STFSFTTTES EASTKQETLP TTVAQTTTIP TSTEDLKKLT 1600
DLVTEFIEST TFETTMEVET TTLSLTSTDA PKLVTTEGVK ETTTTEDTTT 1650
ISSIVTLTTT PLATISTTIL TTEKHVAVTT LAPTTTTESA KTTTTHSSST 1700
HSEKDQIQIP NKFVCKKMSQ IVDIMMRCDR KVDCEDGTDE LDCTCKDYLK 1750
GSLKGLICDG KADCEDLTDE QNCVECQSNE FRCPLSKTCL PLSSRCDNKV 1800
DCKFKEDEKD CFALTNGHDV HFDVHQQPKF SSTGIFSRNG HGVWRVVCAH 1850
ETGYHEHQAK TADAVCALLG FNGAHYFNSS EFVTQHEMQP ITPELKGGRN 1900
RMSAQIHSMV GDNVQFTENE VIIPELGHPS ASRPEKDRLL PRKCVGIYVE 1950
CNPYSNKTTP LKTFSAGQVV KEKPIEQVPV LSPTIETHNT PNVHFKPQIP 2000
AMVVNKKDEI LDRLDKLIKS KKNKTILVNE QLHEAIEELH WPWLADVYMN 2050
GDLWCIGVLI DKHWVMVHES CLSGIDLETH YVSVLLGGGK TKRSAHRSNH 2100
EQIRRVDCFE GVPKSNVLLL HLERPVRFTH HVLPTFLPDS SHQNQSHARQ 2150
CISVLHDDAT GRIKTVAITR IHNATNCDSC YKLQEKQPPA NLMRLLNVSA 2200
EDMASISEEV ELINGVAPTE LPAITKFTTC NQFGLKNVSD AHHNPSDQGV 2250
LVCRDSHTGW FPTALFNYNN SDCQSFKQPF GIRTLELVYK SLQDIIDKPS 2300
CKMLLPAPDC STHRCPLGTC LPQAAMCNGR SDCHDGSDEE ETKCRQQKQQ 2350
CAPGEMKCRT SFKCVPKSKF CDHVPDCEDM TDEPTICSCF TYLQATDPSK 2400
ICDGKRNCWD KSDESSVLCN CTADHFQCSS SPEDCIPRDF VCDKEKDCPN 2450
GEDERYCFGI EHPLHLQKKD FWTNSQHTQP EIAPQYGQVI EQTYGIWHTK 2500
CFPKSKPPQV DEVREICKKL GYNPYRQPSY RLIDDEENKP VHTYELADRQ 2550
GRSFSNESLM GKYRDSTKAL IISKFSPLQL NERLTLFLKS SRPIAELVRW 2600
NATDSSMCYR LEIRCA 2616
Length:2,616
Mass (Da):292,492
Last modified:May 10, 2004 - v2
Checksum:i052F92CBAE9EB163
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831I → T in AAA83086. 1 Publication
Sequence conflicti120 – 1201F → L in AAA83086. 1 Publication
Sequence conflicti363 – 3631N → T in AAA83086. 1 Publication
Sequence conflicti831 – 8311Q → R in AAA83086. 1 Publication
Sequence conflicti864 – 8641N → S in AAA83086. 1 Publication
Sequence conflicti1150 – 11501Y → H in AAA83086. 1 Publication
Sequence conflicti1344 – 13441P → A in AAA83086. 1 Publication
Sequence conflicti1410 – 14101A → S in AAA83086. 1 Publication
Sequence conflicti1607 – 16071I → M in AAA83086. 1 Publication
Sequence conflicti1632 – 16321K → I in AAA83086. 1 Publication
Sequence conflicti1670 – 16701L → P in AAA83086. 1 Publication
Sequence conflicti1794 – 17941S → K in AAA83086. 1 Publication
Sequence conflicti1863 – 18631D → N in AAA83086. 1 Publication
Sequence conflicti1886 – 18883HEM → QEK in AAA83086. 1 Publication
Sequence conflicti1903 – 19031S → A in AAA83086. 1 Publication
Sequence conflicti2147 – 21471H → N in AAA83086. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U29153 mRNA. Translation: AAA83086.1.
AE014296 Genomic DNA. Translation: AAF50656.1.
PIRiA57096.
RefSeqiNP_523947.2. NM_079223.2.
UniGeneiDm.2737.

Genome annotation databases

EnsemblMetazoaiFBtr0076984; FBpp0076693; FBgn0002926.
GeneIDi38738.
KEGGidme:Dmel_CG10129.
UCSCiCG10129-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U29153 mRNA. Translation: AAA83086.1 .
AE014296 Genomic DNA. Translation: AAF50656.1 .
PIRi A57096.
RefSeqi NP_523947.2. NM_079223.2.
UniGenei Dm.2737.

3D structure databases

ProteinModelPortali P98159.
SMRi P98159. Positions 897-1053, 1100-1379, 1727-1811, 2037-2151, 2311-2461.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 64189. 1 interaction.
STRINGi 7227.FBpp0076693.

Protein family/group databases

MEROPSi S01.013.

Proteomic databases

PaxDbi P98159.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0076984 ; FBpp0076693 ; FBgn0002926 .
GeneIDi 38738.
KEGGi dme:Dmel_CG10129.
UCSCi CG10129-RA. d. melanogaster.

Organism-specific databases

CTDi 38738.
FlyBasei FBgn0002926. ndl.

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00740000115494.
InParanoidi P98159.
OMAi PNGEDER.
OrthoDBi EOG75B84T.
PhylomeDBi P98159.

Miscellaneous databases

GenomeRNAii 38738.
NextBioi 810123.

Gene expression databases

Bgeei P98159.

Family and domain databases

Gene3Di 4.10.400.10. 7 hits.
InterProi IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR015420. Peptidase_S1A_nudel.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF09342. DUF1986. 1 hit.
PF00057. Ldl_recept_a. 4 hits.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00261. LDLRECEPTOR.
SMARTi SM00192. LDLa. 9 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 2 hits.
SSF57424. SSF57424. 7 hits.
PROSITEi PS01209. LDLRA_1. 6 hits.
PS50068. LDLRA_2. 8 hits.
PS50240. TRYPSIN_DOM. 2 hits.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "An unusual mosaic protein with a protease domain, encoded by the nudel gene, is involved in defining embryonic dorsoventral polarity in Drosophila."
    Hong C.C., Hashimoto C.
    Cell 82:785-794(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Oregon-R.
    Tissue: Ovary.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "Positive and negative regulation of Easter, a member of the serine protease family that controls dorsal-ventral patterning in the Drosophila embryo."
    Misra S., Hecht P., Maeda R., Anderson K.V.
    Development 125:1261-1267(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF EASTER.
  5. "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 SER-215; SER-220; SER-574; SER-581; SER-1134 AND SER-1136, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiNUDEL_DROME
AccessioniPrimary (citable) accession number: P98159
Secondary accession number(s): Q9VRX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 10, 2004
Last modified: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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