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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
  • chemical synaptic transmission 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
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)DescriptionActionsGraphical viewLength
Mutagenesisi1127R → A: Disrupts RNA-binding. 1 Publication1
Mutagenesisi1167K → A: Disrupts RNA-binding. 1 Publication1
Mutagenesisi1199R → A: Disrupts RNA-binding. 1 Publication1
Mutagenesisi1235H → A: Disrupts RNA-binding. 1 Publication1
Mutagenesisi1330G → D in Pum680; abolishes interaction with brat and translational repression activity but not RNA-binding activity. 2 Publications1
Mutagenesisi1346E → K: Disrupts RNA-binding. 1 Publication1
Mutagenesisi1365C → R: Abolishes interaction with brat. 1 Publication1
Mutagenesisi1366T → D: Abolishes interaction with brat. 1 Publication1
Mutagenesisi1367F → S: Abolishes interaction with nos. 1 Publication1
Mutagenesisi1368N → S: Abolishes interaction with brat. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000759161 – 1533Maternal protein pumilioAdd BLAST1533

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei453Phosphoserine1 Publication1
Modified residuei468Phosphoserine1 Publication1
Modified residuei470Phosphoserine1 Publication1
Modified residuei477Phosphoserine1 Publication1
Modified residuei505Phosphoserine1 Publication1

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

BgeeiFBgn0003165.
ExpressionAtlasiP25822. baseline.
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 interactors.
IntActiP25822. 4 interactors.
MINTiMINT-822094.
STRINGi7227.FBpp0305823.

Structurei

Secondary structure

11533
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1094 – 1100Combined sources7
Helixi1109 – 1112Combined sources4
Helixi1116 – 1120Combined sources5
Helixi1123 – 1133Combined sources11
Helixi1138 – 1150Combined sources13
Helixi1152 – 1156Combined sources5
Turni1159 – 1161Combined sources3
Helixi1162 – 1171Combined sources10
Helixi1174 – 1184Combined sources11
Helixi1188 – 1192Combined sources5
Helixi1197 – 1207Combined sources11
Helixi1210 – 1218Combined sources9
Turni1219 – 1222Combined sources4
Helixi1224 – 1228Combined sources5
Helixi1233 – 1243Combined sources11
Helixi1246 – 1249Combined sources4
Helixi1250 – 1256Combined sources7
Turni1257 – 1259Combined sources3
Helixi1260 – 1264Combined sources5
Helixi1269 – 1279Combined sources11
Helixi1282 – 1292Combined sources11
Helixi1296 – 1300Combined sources5
Helixi1305 – 1315Combined sources11
Helixi1318 – 1326Combined sources9
Turni1327 – 1330Combined sources4
Helixi1332 – 1336Combined sources5
Helixi1341 – 1351Combined sources11
Helixi1354 – 1365Combined sources12
Beta strandi1366 – 1370Combined sources5
Helixi1371 – 1377Combined sources7
Helixi1381 – 1391Combined sources11
Helixi1394 – 1404Combined sources11
Helixi1405 – 1407Combined sources3
Helixi1408 – 1411Combined sources4
Turni1415 – 1417Combined sources3
Helixi1418 – 1425Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3H3DX-ray2.30X/Y1093-1411[»]
5KL1X-ray3.70A1091-1426[»]
5KL8X-ray4.00A1091-1426[»]
5KLAX-ray1.14A1091-1426[»]
ProteinModelPortaliP25822.
SMRiP25822.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25822.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1091 – 1428PUM-HDPROSITE-ProRule annotationAdd BLAST338
Repeati1111 – 1146Pumilio 1Add BLAST36
Repeati1147 – 1182Pumilio 2Add BLAST36
Repeati1183 – 1218Pumilio 3Add BLAST36
Repeati1219 – 1254Pumilio 4Add BLAST36
Repeati1255 – 1290Pumilio 5Add BLAST36
Repeati1291 – 1326Pumilio 6Add BLAST36
Repeati1327 – 1362Pumilio 7Add BLAST36
Repeati1366 – 1402Pumilio 8Add BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1126 – 1130Adenine-nucleotide binding in RNA targetBy similarity5
Regioni1162 – 1166Uracil-nucleotide binding in RNA targetBy similarity5
Regioni1198 – 1202Adenine-nucleotide binding in RNA targetBy similarity5
Regioni1234 – 1238Non-specific-nucleotide binding in RNA targetBy similarity5
Regioni1270 – 1274Adenine-nucleotide binding in RNA targetBy similarity5
Regioni1306 – 1310Uracil-nucleotide binding in RNA targetBy similarity5
Regioni1342 – 1346Guanine-nucleotide binding in RNA targetBy similarity5
Regioni1382 – 1386Uracil-nucleotide binding in RNA targetBy similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi34 – 45Ala-richAdd BLAST12
Compositional biasi57 – 77Gly/Val-richAdd BLAST21
Compositional biasi83 – 93Ala-richAdd BLAST11
Compositional biasi130 – 174Gly-richAdd BLAST45
Compositional biasi152 – 164Poly-GlyAdd BLAST13
Compositional biasi181 – 212Ala-richAdd BLAST32
Compositional biasi213 – 236Gln-richAdd BLAST24
Compositional biasi262 – 274Poly-GlnAdd BLAST13
Compositional biasi571 – 599Gly-richAdd BLAST29
Compositional biasi708 – 725Poly-GlnAdd BLAST18
Compositional biasi936 – 946Poly-AlaAdd BLAST11
Compositional biasi1050 – 1062Poly-AlaAdd BLAST13

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.
KOiK17943.
OMAiGQYNANL.
OrthoDBiEOG091G04QO.
PhylomeDBiP25822.

Family and domain databases

CDDicd07920. Pumilio. 1 hit.
Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR033133. PUM-HD.
IPR033712. Pumilio_RNA-bd.
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 differs from that shown. Reason: Frameshift at position 1293.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti362S → A in CAA44474 (PubMed:1576962).Curated1
Sequence conflicti1103R → P in AAB59189 (PubMed:1459455).Curated1
Sequence conflicti1165I → S in AAX33465 (Ref. 6) Curated1
Sequence conflicti1374V → M in AAQ22439 (PubMed:12537569).Curated1
Sequence conflicti1406 – 1407PH → KN in CAA44474 (PubMed:1576962).Curated2
Sequence conflicti1491N → S in AAQ22439 (PubMed:12537569).Curated1
Sequence conflicti1496V → I in AAB59189 (PubMed:1459455).Curated1
Sequence conflicti1519S → G in AAB59189 (PubMed:1459455).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0093131 – 598Missing in isoform E. 1 PublicationAdd BLAST598
Alternative sequenceiVSP_0082161 – 348Missing in isoform B. CuratedAdd BLAST348
Alternative sequenceiVSP_008217349 – 372AAMMP…NRNAA → MMKLLHDFILDARTAEDVAL TQEM in isoform B. CuratedAdd BLAST24
Alternative sequenceiVSP_009314599 – 659GAYAA…QNFDV → MVVLETASALLGGPYAQGAP ALKMVQKRYIGLHHWLGPIR SKELKEHIVSDDVLSLAFNH N in isoform E. 1 PublicationAdd BLAST61

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.
KEGGidme:Dmel_CG9755.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3H3DX-ray2.30X/Y1093-1411[»]
5KL1X-ray3.70A1091-1426[»]
5KL8X-ray4.00A1091-1426[»]
5KLAX-ray1.14A1091-1426[»]
ProteinModelPortaliP25822.
SMRiP25822.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66261. 5 interactors.
IntActiP25822. 4 interactors.
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.
KEGGidme:Dmel_CG9755.
UCSCiCG9755-RA. d. melanogaster. [P25822-1]

Organism-specific databases

CTDi41094.
FlyBaseiFBgn0003165. pum.

Phylogenomic databases

eggNOGiKOG1488. Eukaryota.
COG5099. LUCA.
GeneTreeiENSGT00390000017241.
InParanoidiP25822.
KOiK17943.
OMAiGQYNANL.
OrthoDBiEOG091G04QO.
PhylomeDBiP25822.

Miscellaneous databases

EvolutionaryTraceiP25822.
GenomeRNAii41094.
PROiP25822.

Gene expression databases

BgeeiFBgn0003165.
ExpressionAtlasiP25822. baseline.
GenevisibleiP25822. DM.

Family and domain databases

CDDicd07920. Pumilio. 1 hit.
Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR033133. PUM-HD.
IPR033712. Pumilio_RNA-bd.
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...

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: November 30, 2016
This is version 154 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.