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Protein

Maternal protein pumilio

Gene

pum

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

Functioni

Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE) (PubMed:1459455, PubMed:1576962, PubMed:9404893, PubMed:9660969, PubMed:22345517). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of deadenylase complexes leading to translational inhibition and mRNA degradation (By similarity). Also mediates deadenylation-independent repression by promoting accessibility of miRNAs (PubMed:22345517). Mediates post-transcriptional silencing of E2f mRNA by binding to its 3'-UTR and promoting miRNA regulation (PubMed:22345517). Required for abdominal development and to support proliferation and self-renewal of germ cells. Pum is the only gene required for nos activity that is not also required for posterior localization of germline determinants. Pum is required during embryogenesis when nos activity apparently moves anteriorly from the posterior pole (PubMed:1459455, PubMed:1576962, PubMed:9404893, PubMed:9660969).By similarity5 Publications

GO - Molecular functioni

  • mRNA 3'-UTR binding Source: UniProtKB
  • RNA binding Source: FlyBase
  • translation repressor activity, nucleic acid binding Source: FlyBase

GO - Biological processi

  • anterior/posterior axis specification, embryo Source: FlyBase
  • behavioral response to ethanol Source: FlyBase
  • cell fate determination Source: FlyBase
  • cell migration Source: FlyBase
  • dendrite morphogenesis Source: FlyBase
  • germ cell development Source: FlyBase
  • germ-line stem cell division Source: FlyBase
  • head involution Source: FlyBase
  • long-term memory Source: FlyBase
  • mitotic nuclear division Source: FlyBase
  • modulation of synaptic transmission Source: FlyBase
  • negative regulation of cell cycle Source: FlyBase
  • negative regulation of epidermal growth factor receptor signaling pathway Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: FlyBase
  • negative regulation of translation Source: FlyBase
  • nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: FlyBase
  • oogenesis Source: FlyBase
  • pole cell migration Source: FlyBase
  • positive regulation of nuclear-transcribed mRNA poly(A) tail shortening Source: FlyBase
  • positive regulation of translation Source: FlyBase
  • posttranscriptional gene silencing Source: UniProtKB
  • regulation of synaptic growth at neuromuscular junction Source: FlyBase
  • synaptic transmission Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Repressor

Keywords - Biological processi

Translation regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Maternal protein pumilio
Gene namesi
Name:pum
ORF Names:CG9755
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003165. pum.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: It is concentrated in the cortical region of the embryo beneath the nuclei.1 Publication

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • muscle cell postsynaptic density Source: FlyBase
  • neuromuscular junction Source: FlyBase
  • nuclear envelope Source: FlyBase
  • type Ib terminal bouton Source: FlyBase
  • type Is terminal bouton Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Flies display defective abdomen pattern formation and are embryonic lethal.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1127 – 11271R → A: Disrupts RNA-binding. 1 Publication
Mutagenesisi1167 – 11671K → A: Disrupts RNA-binding. 1 Publication
Mutagenesisi1199 – 11991R → A: Disrupts RNA-binding. 1 Publication
Mutagenesisi1235 – 12351H → A: Disrupts RNA-binding. 1 Publication
Mutagenesisi1330 – 13301G → D in Pum680; abolishes interaction with brat and translational repression activity but not RNA-binding activity. 2 Publications
Mutagenesisi1346 – 13461E → K: Disrupts RNA-binding. 1 Publication
Mutagenesisi1365 – 13651C → R: Abolishes interaction with brat. 1 Publication
Mutagenesisi1366 – 13661T → D: Abolishes interaction with brat. 1 Publication
Mutagenesisi1367 – 13671F → S: Abolishes interaction with nos. 1 Publication
Mutagenesisi1368 – 13681N → S: Abolishes interaction with brat. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15331533Maternal protein pumilioPRO_0000075916Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei453 – 4531Phosphoserine1 Publication
Modified residuei468 – 4681Phosphoserine1 Publication
Modified residuei470 – 4701Phosphoserine1 Publication
Modified residuei477 – 4771Phosphoserine1 Publication
Modified residuei505 – 5051Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP25822.
PRIDEiP25822.

PTM databases

iPTMnetiP25822.

Expressioni

Developmental stagei

Expressed both maternally and zygotically in embryos.2 Publications

Gene expression databases

BgeeiP25822.
GenevisibleiP25822. DM.

Interactioni

Subunit structurei

Interacts with nos and brat. Acts via the formation of a quaternary complex composed of pum, nos, brat and the 3'-UTR mRNA of hb.2 Publications

Protein-protein interaction databases

BioGridi66261. 5 interactions.
IntActiP25822. 4 interactions.
MINTiMINT-822094.
STRINGi7227.FBpp0305823.

Structurei

Secondary structure

1
1533
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1094 – 11007Combined sources
Helixi1109 – 11124Combined sources
Helixi1116 – 11205Combined sources
Helixi1123 – 113311Combined sources
Helixi1138 – 115013Combined sources
Helixi1152 – 11565Combined sources
Helixi1161 – 117111Combined sources
Helixi1174 – 118613Combined sources
Helixi1189 – 11924Combined sources
Helixi1195 – 120511Combined sources
Helixi1210 – 12178Combined sources
Helixi1218 – 12203Combined sources
Helixi1224 – 12285Combined sources
Helixi1233 – 124210Combined sources
Helixi1246 – 12494Combined sources
Helixi1250 – 12567Combined sources
Turni1257 – 12593Combined sources
Helixi1260 – 12645Combined sources
Helixi1269 – 127911Combined sources
Turni1282 – 12843Combined sources
Helixi1286 – 12949Combined sources
Turni1295 – 13017Combined sources
Turni1303 – 13053Combined sources
Helixi1306 – 131510Combined sources
Helixi1318 – 132811Combined sources
Helixi1332 – 13365Combined sources
Helixi1341 – 135111Combined sources
Helixi1354 – 136411Combined sources
Turni1369 – 13724Combined sources
Helixi1373 – 13775Combined sources
Helixi1381 – 139010Combined sources
Helixi1394 – 13996Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H3DX-ray2.30X/Y1093-1411[»]
ProteinModelPortaliP25822.
SMRiP25822. Positions 1093-1404.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25822.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1091 – 1428338PUM-HDPROSITE-ProRule annotationAdd
BLAST
Repeati1111 – 114636Pumilio 1Add
BLAST
Repeati1147 – 118236Pumilio 2Add
BLAST
Repeati1183 – 121836Pumilio 3Add
BLAST
Repeati1219 – 125436Pumilio 4Add
BLAST
Repeati1255 – 129036Pumilio 5Add
BLAST
Repeati1291 – 132636Pumilio 6Add
BLAST
Repeati1327 – 136236Pumilio 7Add
BLAST
Repeati1366 – 140237Pumilio 8Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1126 – 11305Adenine-nucleotide binding in RNA targetBy similarity
Regioni1162 – 11665Uracil-nucleotide binding in RNA targetBy similarity
Regioni1198 – 12025Adenine-nucleotide binding in RNA targetBy similarity
Regioni1234 – 12385Non-specific-nucleotide binding in RNA targetBy similarity
Regioni1270 – 12745Adenine-nucleotide binding in RNA targetBy similarity
Regioni1306 – 13105Uracil-nucleotide binding in RNA targetBy similarity
Regioni1342 – 13465Guanine-nucleotide binding in RNA targetBy similarity
Regioni1382 – 13865Uracil-nucleotide binding in RNA targetBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi34 – 4512Ala-richAdd
BLAST
Compositional biasi57 – 7721Gly/Val-richAdd
BLAST
Compositional biasi83 – 9311Ala-richAdd
BLAST
Compositional biasi130 – 17445Gly-richAdd
BLAST
Compositional biasi152 – 16413Poly-GlyAdd
BLAST
Compositional biasi181 – 21232Ala-richAdd
BLAST
Compositional biasi213 – 23624Gln-richAdd
BLAST
Compositional biasi262 – 27413Poly-GlnAdd
BLAST
Compositional biasi571 – 59929Gly-richAdd
BLAST
Compositional biasi708 – 72518Poly-GlnAdd
BLAST
Compositional biasi936 – 94611Poly-AlaAdd
BLAST
Compositional biasi1050 – 106213Poly-AlaAdd
BLAST

Domaini

The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. RNA-binding occurs on the concave side of the surface. Pum is composed of 8 pumilio repeats of 36 residues; each repeat binds a single nucleotide in its RNA target. Residues at positions 12 and 16 of the pumilio repeat bind each RNA base via hydrogen bonding or van der Waals contacts with the Watson-Crick edge, while the amino acid at position 13 makes a stacking interaction. The recognition of RNA by pumilio repeats is base specific: cysteine and glutamine at position 12 and 16, respectively, bind adenine; asparagine and glutamine bind uracil; and serine and glutamate bind guanine.By similarity

Sequence similaritiesi

Contains 1 PUM-HD domain.PROSITE-ProRule annotation
Contains 8 pumilio repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1488. Eukaryota.
COG5099. LUCA.
GeneTreeiENSGT00390000017241.
InParanoidiP25822.
OMAiGQYNANL.
OrthoDBiEOG7T7GT5.
PhylomeDBiP25822.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR033133. PUM-HD.
IPR001313. Pumilio_RNA-bd_rpt.
[Graphical view]
PfamiPF00806. PUF. 8 hits.
[Graphical view]
SMARTiSM00025. Pumilio. 8 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50302. PUM. 8 hits.
PS50303. PUM_HD. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P25822-1) [UniParc]FASTAAdd to basket

Also known as: C, D

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
MKFLGGNDDR NGRGGVGVGT DAIVGSRGGV SQDAADAAGA AAAAAVGYVF
60 70 80 90 100
QQRPSPGGVG VGVGGVGGGV PGVGAVGSTL HEAAAAEYAA HFAQKQQQTR
110 120 130 140 150
WACGDDGHGI DNPDKWKYNP PMNPANAAPG GPPGNGSNGG PGAIGTIGMG
160 170 180 190 200
SGLGGGGGGG AGGGNNGGSG TNGGLHHQSM AAAAANMAAM QQAAALAKHN
210 220 230 240 250
HMISQAAAAV AAQQQHQHPH QQHPQQQQQQ QQAQNQGHPH HLMGGGNGLG
260 270 280 290 300
NGNGLGIQHP GQQQQQQQQQ QQQQHPGQYN ANLLNHAAAL GHMSSYAQSG
310 320 330 340 350
GSMYDHHGGA MHPGMNGGMP KQQPLGPPGA GGPQDYVYMG GQTTVPMGAA
360 370 380 390 400
MMPPQNQYMN SSAVAAANRN AAITTSTAKK LWEKSDGKGV SSSTPGGPLH
410 420 430 440 450
PLQIPGIGDP SSVWKDHTWS TQGENILVPP PSRAYAHGGA SDTSNSGNAG
460 470 480 490 500
ILSPRDSTCA KVVEYVFSGS PTNKDSSLSG LEPHLRNLKF DDNDKSRDDK
510 520 530 540 550
EKANSPFDTN GLKKDDQVTN SNGVVNGIDD DKGFNRTPGS RQPSPAEESQ
560 570 580 590 600
PRPPNLLFPP LPFNHMLMDH GQGMGGGLGG VVGSGNGVGG GSGGGGAGGA
610 620 630 640 650
YAAHQQMAAQ MSQLQPPMMN GVGGGMPMAA QSPMLNHQAA GPNHMESPGN
660 670 680 690 700
LLQQQNFDVQ QLFRSQNPGL AAVATNAAAA AAAAAAATSA ASAAAAVGAP
710 720 730 740 750
PVPNGSLQQS QQQQQQQQQQ QQQQQMHMAA ASQQFLAAQQ QAQNAAYAAQ
760 770 780 790 800
QATSYVINPG QEAAPYMGMI AAAQMPYYGV APWGMYPGNL IPQQGTQPRR
810 820 830 840 850
PLTPSQQGAE NQPYQVIPAF LDHTGSLLMG GPRTGTPMRL VSPAPVLVPP
860 870 880 890 900
GATRAGPPPP QGPQLYQPQP QTAQQNLYSQ QNGSSVGGLA LNTSSLTGRR
910 920 930 940 950
DSFDRSTSAF SPSTMDYTSS GVAAAANAVN STVAQAAAAA AAAAAARGKW
960 970 980 990 1000
PGAMSGAASG AYGALGAGNA SASPLGAPIT PPPSAQSCLL GSRAPGAESR
1010 1020 1030 1040 1050
QRQQQQQQLA AVGLPATAAA AQAAVAAAAN NMFGSNSSIF SNPLAIPGTA
1060 1070 1080 1090 1100
AVAAAAAAAA AANSRQVAAT AAAAAAVAAA AGGVGGAPQP GRSRLLEDFR
1110 1120 1130 1140 1150
NQRYPNLQLR DLANHIVEFS QDQHGSRFIQ QKLERATAAE KQMVFSEILA
1160 1170 1180 1190 1200
AAYSLMTDVF GNYVIQKFFE FGTPEQKNTL GMQVKGHVLQ LALQMYGCRV
1210 1220 1230 1240 1250
IQKALESISP EQQQEIVHEL DGHVLKCVKD QNGNHVVQKC IECVDPVALQ
1260 1270 1280 1290 1300
FIINAFKGQV YSLSTHPYGC RVIQRILEHC TAEQTTPILD ELHEHTEQLI
1310 1320 1330 1340 1350
QDQYGNYVIQ HVLEHGKQED KSILINSVRG KVLVLSQHKF ASNVVEKCVT
1360 1370 1380 1390 1400
HATRGERTGL IDEVCTFNDN ALHVMMKDQY ANYVVQKMID VSEPTQLKKL
1410 1420 1430 1440 1450
MTKIRPHMAA LRKYTYGKHI NAKLEKYYMK ITNPITVGTG AGGVPAASSA
1460 1470 1480 1490 1500
AAVSSGATSA SVTACTSGSS TTTTSTTNSL ASPTICSVQE NGSAMVVEPS
1510 1520 1530
SPDASESSSS VVSGAVNSSL GPIGPPTNGN VVL
Length:1,533
Mass (Da):157,528
Last modified:September 19, 2003 - v2
Checksum:i0A343220BB1F0B27
GO
Isoform B (identifier: P25822-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-348: Missing.
     349-372: AAMMPPQNQYMNSSAVAAANRNAA → MMKLLHDFILDARTAEDVALTQEM

Note: No experimental confirmation available.
Show »
Length:1,185
Mass (Da):123,520
Checksum:i850A3AEDEC837AD0
GO
Isoform E (identifier: P25822-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-598: Missing.
     599-659: GAYAAHQQMA...NLLQQQNFDV → MVVLETASAL...DVLSLAFNHN

Note: No experimental confirmation available.
Show »
Length:935
Mass (Da):97,754
Checksum:i22ECEC73646072EF
GO

Sequence cautioni

The sequence AAX33465.1 differs from that shown. Reason: Frameshift at position 1293. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti362 – 3621S → A in CAA44474 (PubMed:1576962).Curated
Sequence conflicti1103 – 11031R → P in AAB59189 (PubMed:1459455).Curated
Sequence conflicti1165 – 11651I → S in AAX33465 (Ref. 6) Curated
Sequence conflicti1374 – 13741V → M in AAQ22439 (PubMed:12537569).Curated
Sequence conflicti1406 – 14072PH → KN in CAA44474 (PubMed:1576962).Curated
Sequence conflicti1491 – 14911N → S in AAQ22439 (PubMed:12537569).Curated
Sequence conflicti1496 – 14961V → I in AAB59189 (PubMed:1459455).Curated
Sequence conflicti1519 – 15191S → G in AAB59189 (PubMed:1459455).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 598598Missing in isoform E. 1 PublicationVSP_009313Add
BLAST
Alternative sequencei1 – 348348Missing in isoform B. CuratedVSP_008216Add
BLAST
Alternative sequencei349 – 37224AAMMP…NRNAA → MMKLLHDFILDARTAEDVAL TQEM in isoform B. CuratedVSP_008217Add
BLAST
Alternative sequencei599 – 65961GAYAA…QNFDV → MVVLETASALLGGPYAQGAP ALKMVQKRYIGLHHWLGPIR SKELKEHIVSDDVLSLAFNH N in isoform E. 1 PublicationVSP_009314Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62589 mRNA. Translation: CAA44474.1.
L07943 mRNA. Translation: AAB59189.1.
AE014297 Genomic DNA. Translation: AAF54340.2.
AE014297 Genomic DNA. Translation: AAF54338.2.
AE014297 Genomic DNA. Translation: AAN13409.1.
AE014297 Genomic DNA. Translation: AAN13410.1.
AE014297 Genomic DNA. Translation: AAO41523.1.
BT001872 mRNA. Translation: AAN71644.1.
BT009970 mRNA. Translation: AAQ22439.1.
BT021317 mRNA. Translation: AAX33465.1. Frameshift.
PIRiA46221.
RefSeqiNP_001262403.1. NM_001275474.1. [P25822-1]
NP_524285.2. NM_079561.4. [P25822-1]
NP_731314.1. NM_169258.3. [P25822-1]
NP_731315.1. NM_169259.3. [P25822-1]
NP_731316.2. NM_169260.4. [P25822-2]
NP_788604.1. NM_176427.3. [P25822-3]
UniGeneiDm.1115.

Genome annotation databases

EnsemblMetazoaiFBtr0081990; FBpp0081470; FBgn0003165. [P25822-1]
FBtr0081991; FBpp0081471; FBgn0003165. [P25822-1]
FBtr0081992; FBpp0081472; FBgn0003165. [P25822-1]
FBtr0333667; FBpp0305823; FBgn0003165. [P25822-1]
GeneIDi41094.
UCSCiCG9755-RA. d. melanogaster. [P25822-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62589 mRNA. Translation: CAA44474.1.
L07943 mRNA. Translation: AAB59189.1.
AE014297 Genomic DNA. Translation: AAF54340.2.
AE014297 Genomic DNA. Translation: AAF54338.2.
AE014297 Genomic DNA. Translation: AAN13409.1.
AE014297 Genomic DNA. Translation: AAN13410.1.
AE014297 Genomic DNA. Translation: AAO41523.1.
BT001872 mRNA. Translation: AAN71644.1.
BT009970 mRNA. Translation: AAQ22439.1.
BT021317 mRNA. Translation: AAX33465.1. Frameshift.
PIRiA46221.
RefSeqiNP_001262403.1. NM_001275474.1. [P25822-1]
NP_524285.2. NM_079561.4. [P25822-1]
NP_731314.1. NM_169258.3. [P25822-1]
NP_731315.1. NM_169259.3. [P25822-1]
NP_731316.2. NM_169260.4. [P25822-2]
NP_788604.1. NM_176427.3. [P25822-3]
UniGeneiDm.1115.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H3DX-ray2.30X/Y1093-1411[»]
ProteinModelPortaliP25822.
SMRiP25822. Positions 1093-1404.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66261. 5 interactions.
IntActiP25822. 4 interactions.
MINTiMINT-822094.
STRINGi7227.FBpp0305823.

PTM databases

iPTMnetiP25822.

Proteomic databases

PaxDbiP25822.
PRIDEiP25822.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081990; FBpp0081470; FBgn0003165. [P25822-1]
FBtr0081991; FBpp0081471; FBgn0003165. [P25822-1]
FBtr0081992; FBpp0081472; FBgn0003165. [P25822-1]
FBtr0333667; FBpp0305823; FBgn0003165. [P25822-1]
GeneIDi41094.
UCSCiCG9755-RA. d. melanogaster. [P25822-1]

Organism-specific databases

CTDi41094.
FlyBaseiFBgn0003165. pum.

Phylogenomic databases

eggNOGiKOG1488. Eukaryota.
COG5099. LUCA.
GeneTreeiENSGT00390000017241.
InParanoidiP25822.
OMAiGQYNANL.
OrthoDBiEOG7T7GT5.
PhylomeDBiP25822.

Miscellaneous databases

EvolutionaryTraceiP25822.
GenomeRNAii41094.
NextBioi822132.
PROiP25822.

Gene expression databases

BgeeiP25822.
GenevisibleiP25822. DM.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR033133. PUM-HD.
IPR001313. Pumilio_RNA-bd_rpt.
[Graphical view]
PfamiPF00806. PUF. 8 hits.
[Graphical view]
SMARTiSM00025. Pumilio. 8 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50302. PUM. 8 hits.
PS50303. PUM_HD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila pumilio gene: an unusually long transcription unit and an unusual protein."
    Macdonald P.M.
    Development 114:221-232(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  2. "Pumilio is essential for function but not for distribution of the Drosophila abdominal determinant Nanos."
    Barker D.D., Wang C., Moore J., Dickinson L.K., Lehmann R.
    Genes Dev. 6:2312-2326(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    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] (ISOFORMS A AND E).
    Strain: Berkeley.
    Tissue: Embryo.
  6. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Embryo.
  7. "The Pumilio protein binds RNA through a conserved domain that defines a new class of RNA-binding proteins."
    Zamore P.D., Williamson J.R., Lehmann R.
    RNA 3:1421-1433(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING, FUNCTION.
  8. "The Pumilio RNA-binding domain is also a translational regulator."
    Wharton R.P., Sonoda J., Lee T., Patterson M., Murata Y.
    Mol. Cell 1:863-872(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-1330.
  9. "Recruitment of Nanos to hunchback mRNA by Pumilio."
    Sonoda J., Wharton R.P.
    Genes Dev. 13:2704-2712(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOS, RNA-BINDING.
  10. "Drosophila Brain tumor is a translational repressor."
    Sonoda J., Wharton R.P.
    Genes Dev. 15:762-773(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRAT AND NOS.
  11. "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-453; SER-468; SER-470; SER-477 AND SER-505, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  12. "Pumilio facilitates miRNA regulation of the E2F3 oncogene."
    Miles W.O., Tschop K., Herr A., Ji J.Y., Dyson N.J.
    Genes Dev. 26:356-368(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING.
  13. "Structure of Pumilio reveals similarity between RNA and peptide binding motifs."
    Edwards T.A., Pyle S.E., Wharton R.P., Aggarwal A.K.
    Cell 105:281-289(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1092-1411, MUTAGENESIS OF ARG-1127; LYS-1167; ARG-1199; HIS-1235; GLY-1330; GLU-1346; CYS-1365; THR-1366; PHE-1367 AND ASN-1368.

Entry informationi

Entry nameiPUM_DROME
AccessioniPrimary (citable) accession number: P25822
Secondary accession number(s): A4V2K5
, Q5BIA7, Q7YU65, Q8IGA8, Q9VHH4, Q9VHH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: September 19, 2003
Last modified: May 11, 2016
This is version 148 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

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 one 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.