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Protein

H/ACA ribonucleoprotein complex subunit 4

Gene

Nop60B

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

Functioni

Plays a central role in ribosomal RNA processing. Probable catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. Required for maintenance of the germline stem cell lineage during spermatogenesis.3 Publications

Catalytic activityi

RNA uridine = RNA pseudouridine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei123 – 1231NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

  • cellular response to starvation Source: FlyBase
  • germ cell development Source: FlyBase
  • neurogenesis Source: FlyBase
  • pseudouridine synthesis Source: FlyBase
  • ribosome biogenesis Source: FlyBase
  • rRNA processing Source: FlyBase
  • wing disc development Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Ribonucleoprotein

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
H/ACA ribonucleoprotein complex subunit 4 (EC:5.4.99.-)
Alternative name(s):
Nucleolar protein AT band 60B
Protein minifly
Gene namesi
Name:Nop60B
Synonyms:mfl
ORF Names:CG3333
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0259937. Nop60B.

Subcellular locationi

GO - Cellular componenti

  • intracellular ribonucleoprotein complex Source: UniProtKB-KW
  • nucleolus Source: FlyBase
  • nucleus Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 508508H/ACA ribonucleoprotein complex subunit 4PRO_0000121989Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei442 – 4421Phosphoserine1 Publication
Modified residuei443 – 4431Phosphothreonine1 Publication
Modified residuei444 – 4441Phosphoserine1 Publication
Modified residuei445 – 4451Phosphoserine1 Publication
Modified residuei449 – 4491Phosphothreonine1 Publication
Modified residuei455 – 4551Phosphoserine1 Publication
Modified residuei458 – 4581Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO44081.
PRIDEiO44081.

PTM databases

iPTMnetiO44081.

Expressioni

Developmental stagei

Isoform C is expressed both maternally and zygotically. Isoform A is expressed at the same level in adult females but at a much lower level in ovaries.1 Publication

Gene expression databases

BgeeiO44081.
ExpressionAtlasiO44081. differential.
GenevisibleiO44081. DM.

Interactioni

Subunit structurei

Component of the small nucleolar ribonucleoprotein particle containing H/ACA-type snoRNAs (H/ACA snoRNPs).By similarity

Protein-protein interaction databases

BioGridi63449. 4 interactions.
DIPiDIP-20128N.
IntActiO44081. 3 interactions.
MINTiMINT-1030866.
STRINGi7227.FBpp0099583.

Structurei

3D structure databases

ProteinModelPortaliO44081.
SMRiO44081. Positions 46-406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini294 – 36976PUAPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi8 – 169Poly-Lys
Compositional biasi461 – 47111Poly-LysAdd
BLAST
Compositional biasi489 – 49911Poly-LysAdd
BLAST

Sequence similaritiesi

Belongs to the pseudouridine synthase TruB family.Curated
Contains 1 PUA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2529. Eukaryota.
COG0130. LUCA.
GeneTreeiENSGT00510000047092.
InParanoidiO44081.
KOiK11131.
OMAiYVDYNAK.
OrthoDBiEOG7QC7W0.
PhylomeDBiO44081.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
InterProiIPR012960. Dyskerin-like.
IPR020103. PsdUridine_synth_cat_dom.
IPR002501. PsdUridine_synth_N.
IPR002478. PUA.
IPR015947. PUA-like_domain.
IPR004802. tRNA_PsdUridine_synth_B_fam.
IPR032819. TruB_C.
[Graphical view]
PANTHERiPTHR23127. PTHR23127. 1 hit.
PfamiPF08068. DKCLD. 1 hit.
PF01472. PUA. 1 hit.
PF16198. TruB_C_2. 1 hit.
PF01509. TruB_N. 1 hit.
[Graphical view]
SMARTiSM01136. DKCLD. 1 hit.
SM00359. PUA. 1 hit.
[Graphical view]
SUPFAMiSSF55120. SSF55120. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00425. CBF5. 1 hit.
PROSITEiPS50890. PUA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: O44081-1) [UniParc]FASTAAdd to basket

Also known as: B

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
MADVEVRKEK KKKKIKEEPL DGDDIGTLQK QGNFQIKPSS KIAELDTSQW
60 70 80 90 100
PLLLKNFDKL NIRSNHYTPL AHGSSPLNRD IKEYMKTGFI NLDKPSNPSS
110 120 130 140 150
HEVVAWIKKI LKVEKTGHSG TLDPKVTGCL IVCIDRATRL VKSQQSAGKE
160 170 180 190 200
YVAIFKLHGA VESVAKVRQG LEKLRGALFQ RPPLISAVKR QLRVRTVYDS
210 220 230 240 250
KLLDYDETRN MGVFWVSCEA GSYIRTMCVH LGLVLGVGGQ MLELRRVRSG
260 270 280 290 300
IQSERDGMVT MHDVLDAMWL YENHKDESML RRVIKPLEGL LVNHKRIIMK
310 320 330 340 350
DSSVNAVCYG AKITLPGVLR YEDGIEIDQE IVICTTKGEA ICLAIALMTT
360 370 380 390 400
ATMASCDHGV VAKIKRVIME RDTYPRKWGL GPKASAKKAL IAAGKLDKFG
410 420 430 440 450
RPNENTPKEW LTGYVDYNAK KPAAQEVSPT NGSSEPSKRK LSTSSVEETA
460 470 480 490 500
AAAVSEETPS KDKKKKKKKH KGDEEAPEAA EEEAEPVEKE KKKKKKKDKD

RDRDEAQE
Length:508
Mass (Da):56,831
Last modified:June 1, 1998 - v1
Checksum:i3CAE3F91C84E0A94
GO
Isoform C (identifier: O44081-2) [UniParc]FASTAAdd to basket

Also known as: alpha

The sequence of this isoform differs from the canonical sequence as follows:
     212-253: GVFWVSCEAG...LRRVRSGIQS → DLLIRSCNIW...LKSSHDTLLR
     254-508: Missing.

Show »
Length:253
Mass (Da):28,825
Checksum:i1CA160C68C4D6185
GO

Sequence cautioni

The sequence ABV82369.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691P → R in AAD19897 (PubMed:10087258).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei212 – 25342GVFWV…SGIQS → DLLIRSCNIWTITLIKEISS KIFLKIIECHRNLKSSHDTL LR in isoform C. 1 PublicationVSP_036583Add
BLAST
Alternative sequencei254 – 508255Missing in isoform C. 1 PublicationVSP_036584Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017230 mRNA. Translation: AAC97117.1.
AF089837 mRNA. Translation: AAD16092.1.
AF097634 Genomic DNA. Translation: AAD19897.1.
DQ841550 mRNA. Translation: ABH08965.1.
DQ857345 mRNA. Translation: ABI17547.1.
DQ857346 mRNA. Translation: ABI17548.1.
AE013599 Genomic DNA. Translation: AAF47178.1.
AE013599 Genomic DNA. Translation: AAX52682.1.
AY089408 mRNA. Translation: AAL90146.1.
BT030987 mRNA. Translation: ABV82369.1. Different initiation.
RefSeqiNP_001014547.1. NM_001014547.4. [O44081-1]
NP_001163286.1. NM_001169815.3. [O44081-1]
NP_001163289.1. NM_001169818.3. [O44081-1]
NP_525120.1. NM_080381.5. [O44081-1]
UniGeneiDm.1944.

Genome annotation databases

EnsemblMetazoaiFBtr0072258; FBpp0072166; FBgn0259937. [O44081-1]
FBtr0100213; FBpp0099583; FBgn0259937. [O44081-1]
FBtr0300227; FBpp0289464; FBgn0259937. [O44081-1]
FBtr0300861; FBpp0290083; FBgn0259937. [O44081-1]
GeneIDi37873.
KEGGidme:Dmel_CG3333.
UCSCiCG3333-RB. d. melanogaster.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017230 mRNA. Translation: AAC97117.1.
AF089837 mRNA. Translation: AAD16092.1.
AF097634 Genomic DNA. Translation: AAD19897.1.
DQ841550 mRNA. Translation: ABH08965.1.
DQ857345 mRNA. Translation: ABI17547.1.
DQ857346 mRNA. Translation: ABI17548.1.
AE013599 Genomic DNA. Translation: AAF47178.1.
AE013599 Genomic DNA. Translation: AAX52682.1.
AY089408 mRNA. Translation: AAL90146.1.
BT030987 mRNA. Translation: ABV82369.1. Different initiation.
RefSeqiNP_001014547.1. NM_001014547.4. [O44081-1]
NP_001163286.1. NM_001169815.3. [O44081-1]
NP_001163289.1. NM_001169818.3. [O44081-1]
NP_525120.1. NM_080381.5. [O44081-1]
UniGeneiDm.1944.

3D structure databases

ProteinModelPortaliO44081.
SMRiO44081. Positions 46-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63449. 4 interactions.
DIPiDIP-20128N.
IntActiO44081. 3 interactions.
MINTiMINT-1030866.
STRINGi7227.FBpp0099583.

PTM databases

iPTMnetiO44081.

Proteomic databases

PaxDbiO44081.
PRIDEiO44081.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0072258; FBpp0072166; FBgn0259937. [O44081-1]
FBtr0100213; FBpp0099583; FBgn0259937. [O44081-1]
FBtr0300227; FBpp0289464; FBgn0259937. [O44081-1]
FBtr0300861; FBpp0290083; FBgn0259937. [O44081-1]
GeneIDi37873.
KEGGidme:Dmel_CG3333.
UCSCiCG3333-RB. d. melanogaster.

Organism-specific databases

CTDi37873.
FlyBaseiFBgn0259937. Nop60B.

Phylogenomic databases

eggNOGiKOG2529. Eukaryota.
COG0130. LUCA.
GeneTreeiENSGT00510000047092.
InParanoidiO44081.
KOiK11131.
OMAiYVDYNAK.
OrthoDBiEOG7QC7W0.
PhylomeDBiO44081.

Miscellaneous databases

ChiTaRSiNop60B. fly.
GenomeRNAii37873.
PROiO44081.

Gene expression databases

BgeeiO44081.
ExpressionAtlasiO44081. differential.
GenevisibleiO44081. DM.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
InterProiIPR012960. Dyskerin-like.
IPR020103. PsdUridine_synth_cat_dom.
IPR002501. PsdUridine_synth_N.
IPR002478. PUA.
IPR015947. PUA-like_domain.
IPR004802. tRNA_PsdUridine_synth_B_fam.
IPR032819. TruB_C.
[Graphical view]
PANTHERiPTHR23127. PTHR23127. 1 hit.
PfamiPF08068. DKCLD. 1 hit.
PF01472. PUA. 1 hit.
PF16198. TruB_C_2. 1 hit.
PF01509. TruB_N. 1 hit.
[Graphical view]
SMARTiSM01136. DKCLD. 1 hit.
SM00359. PUA. 1 hit.
[Graphical view]
SUPFAMiSSF55120. SSF55120. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00425. CBF5. 1 hit.
PROSITEiPS50890. PUA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Nop60B gene of Drosophila encodes an essential nucleolar protein that functions in yeast."
    Phillips B., Billin A.N., Cadwell C., Buchholz R., Erickson C., Merriam J.R., Carbon J., Poole S.J.
    Mol. Gen. Genet. 260:20-29(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION.
  2. "minifly, a Drosophila gene required for ribosome biogenesis."
    Giordano E., Peluso I., Senger S., Furia M.
    J. Cell Biol. 144:1123-1133(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION.
  3. "The coding/non-coding overlapping architecture of the gene encoding the Drosophila pseudouridine synthase."
    Riccardo S., Tortoriello G., Giordano E., Turano M., Furia M.
    BMC Mol. Biol. 8:15-15(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND C), DEVELOPMENTAL STAGE.
  4. "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.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-468 (ISOFORM A).
    Strain: Berkeley.
    Tissue: Testis.
  7. Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-468 (ISOFORM A).
    Strain: Berkeley.
    Tissue: Embryo.
  8. "Mutations in Nop60B, the Drosophila homolog of human dyskeratosis congenita 1, affect the maintenance of the germ-line stem cell lineage during spermatogenesis."
    Kauffman T., Tran J., DiNardo S.
    Dev. Biol. 253:189-199(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "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-442; THR-443; SER-444; SER-445; THR-449; SER-455 AND THR-458, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiDKC1_DROME
AccessioniPrimary (citable) accession number: O44081
Secondary accession number(s): A8E745
, Q0GLB4, Q0MVP1, Q8T408, Q9UAN8, Q9V3Z5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 131 of the entry and version 1 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. 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.