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Reviewed, UniProtKB/Swiss-Prot Q9V3H2 (PSDE_DROME)

Last modified November 3, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    26S proteasome non-ATPase regulatory subunit 14
    EC=3.1.2.15
Alternative name(s):
    26S proteasome regulatory subunit rpn11
    26S proteasome regulatory complex subunit p37B
    Yippee-interacting protein 5
Gene names
Name: Rpn11
Synonyms: yip5
ORF Names: CG18174
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length308 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Metalloprotease component of the 26S proteasome that specifically cleaves 'Lys-63'-linked polyubiquitin chains. The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The function of the 'Lys-63'-specific deubiquitination of the proteasome is unclear By similarity.

Catalytic activity

Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol.

Subunit structure

Component of the 19S regulatory cap of the 26S proteasome.

Sequence similarities

Belongs to the peptidase M67A family. PSMD14 subfamily.

Contains 1 MPN (JAB/Mov34) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CG17337Q9V9H11EBI-178674,EBI-144341
Mov34P262701EBI-178674,EBI-253612

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 30830826S proteasome non-ATPase regulatory subunit 14
PRO_0000213955

Regions

Domain24 – 137114MPN
Motif111 – 12414JAMM motif

Sites

Metal binding1111Zinc; catalytic By similarity
Metal binding1131Zinc; catalytic By similarity
Metal binding1241Zinc; catalytic By similarity

Experimental info

Sequence conflict144 – 1452DP → YS in AAF27818. Ref.5
Sequence conflict2491L → F in AAF27818. Ref.5
Sequence conflict2681L → C AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9V3H2-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: CA43EEBD13B42A61

FASTA30834,401
        10         20         30         40         50         60 
MDRLLRLGGA MPQAAPPTDA PVVDTAEQVY ISSLALLKML KHGRAGVPME VMGLMLGEFV 

        70         80         90        100        110        120 
DDYTVQVIDV FAMPQTGTGV SVEAVDPVFQ AKMLDMLKQT GRPEMVVGWY HSHPGFGCWL 

       130        140        150        160        170        180 
SGVDINTQQS FEALSERAVA VVVDPIQSVK GKVVIDAFRL INPNMLVLGQ EPRQTTSNLG 

       190        200        210        220        230        240 
HLQKPSVQAL IHGLNRHYYS ISINYRKNEL EQKMLLNLHK KSWKDGLTLS DYNEHCSINE 

       250        260        270        280        290        300 
DTVAEMLDLA KNYNKSLEDE EKMTPEQLAI KNVGKQDPKR HLEEKVDKVM QNNIVQCLGA 


MLDTIVFK 

« Hide

References

« Hide 'large scale' references
[1]"The regulatory complex of Drosophila melanogaster 26S proteasomes. Subunit composition and localization of a deubiquitylating enzyme."
Hoelzl H., Kapelari B., Kellermann J., Seemueller E., Suemegi M., Udvardy A., Medalia O., Sperling J., Mueller S.A., Engel A., Baumeister W.
J. Cell Biol. 150:119-130(2000) [PubMed: 10893261] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 263-271, FUNCTION.
Tissue: Embryo.
[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. expand/collapse author list , 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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[4]"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: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]Roxstrom-Lindquist K., Faye I.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 80-308.
Tissue: Imaginal disk.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF145313 mRNA. Translation: AAF08394.1.
AE014134 Genomic DNA. Translation: AAF52215.1.
AY070977 mRNA. Translation: AAL48599.1.
AF195189 mRNA. Translation: AAF27818.1.
RefSeqNP_608905.1.
UniGeneDm.3343

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9V3H2. 7 interactions.
STRINGQ9V3H2.

Protein family/group databases

MEROPSM67.001.

Proteomic databases

PRIDEQ9V3H2.

Genome annotation databases

EnsemblFBtr0079027; FBpp0078664; FBgn0028694; Drosophila melanogaster. [Genome view]
GeneID33738.
KEGGdme:Dmel_CG18174.
NMPDRfig|7227.3.peg.837.

Organism-specific databases

CTD33738.
FlyBaseFBgn0028694. Rpn11.

Phylogenomic databases

HOGENOMQ9V3H2.
OMAQDPKKHL.

Gene expression databases

ArrayExpressQ9V3H2.
BgeeQ9V3H2.
GermOnlineCG18174. Drosophila melanogaster.

Family and domain databases

InterProIPR000555. Mov34_MPN_PAD1.
[Graphical view]
PfamPF01398. Mov34. 1 hit.
[Graphical view]
ProDomPD363422. Mov34-1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00232. JAB_MPN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio785010.

Entry information

Entry namePSDE_DROME
AccessionPrimary (citable) accession number: Q9V3H2
Secondary accession number(s): Q9NIU3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: May 1, 2000
Last modified: November 3, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents