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Protein

26S protease regulatory subunit 6B

Gene

PSMC4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi206 – 2138ATPSequence Analysis

GO - Molecular functioni

  • ATPase activity Source: ProtInc
  • ATP binding Source: UniProtKB-KW
  • proteasome-activating ATPase activity Source: GO_Central
  • TBP-class protein binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_188323. CLEC7A (Dectin-1) signaling.
REACT_188330. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_263873. degradation of AXIN.
REACT_263883. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
REACT_264438. degradation of DVL.
REACT_264478. Asymmetric localization of PCP proteins.
REACT_264605. Hedgehog ligand biogenesis.
REACT_267700. Degradation of GLI2 by the proteasome.
REACT_268156. Degradation of GLI1 by the proteasome.
REACT_268366. GLI3 is processed to GLI3R by the proteasome.
REACT_268718. Hedgehog 'on' state.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Names & Taxonomyi

Protein namesi
Recommended name:
26S protease regulatory subunit 6B
Alternative name(s):
26S proteasome AAA-ATPase subunit RPT3
MB67-interacting protein
MIP224
Proteasome 26S subunit ATPase 4
Tat-binding protein 7
Short name:
TBP-7
Gene namesi
Name:PSMC4
Synonyms:MIP224, TBP7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:9551. PSMC4.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • cytosolic proteasome complex Source: GO_Central
  • inclusion body Source: Ensembl
  • membrane Source: UniProtKB
  • nuclear proteasome complex Source: GO_Central
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • proteasome accessory complex Source: UniProtKB
  • proteasome complex Source: UniProtKB
  • proteasome regulatory particle, base subcomplex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33896.

Polymorphism and mutation databases

BioMutaiPSMC4.
DMDMi20532409.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 41841826S protease regulatory subunit 6BPRO_0000084686Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei21 – 211Phosphoserine1 Publication
Modified residuei25 – 251Phosphothreonine1 Publication
Modified residuei28 – 281Phosphoserine5 Publications
Modified residuei397 – 3971N6-acetyllysine1 Publication
Modified residuei401 – 4011N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP43686.
PaxDbiP43686.
PRIDEiP43686.

2D gel databases

OGPiP43686.

PTM databases

PhosphoSiteiP43686.

Expressioni

Gene expression databases

BgeeiP43686.
CleanExiHS_PSMC4.
ExpressionAtlasiP43686. baseline and differential.
GenevisibleiP43686. HS.

Organism-specific databases

HPAiHPA002044.
HPA005471.

Interactioni

Subunit structurei

Interacts with NR1I3. Interacts with PAAF1. Interacts with TRIM5.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PSMC5P6219511EBI-743997,EBI-357745
PSMC6P623333EBI-743997,EBI-357669
PSMD10O7583213EBI-743997,EBI-752185

Protein-protein interaction databases

BioGridi111677. 93 interactions.
DIPiDIP-29274N.
IntActiP43686. 23 interactions.
MINTiMINT-5004247.
STRINGi9606.ENSP00000157812.

Structurei

Secondary structure

1
418
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi338 – 34811Combined sources
Turni349 – 3513Combined sources
Helixi361 – 3644Combined sources
Helixi372 – 38817Combined sources
Beta strandi392 – 3943Combined sources
Helixi396 – 40611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DVWX-ray2.30B337-418[»]
ProteinModelPortaliP43686.
SMRiP43686. Positions 41-418.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43686.

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

eggNOGiCOG1222.
GeneTreeiENSGT00550000074962.
HOGENOMiHOG000225143.
HOVERGENiHBG000109.
InParanoidiP43686.
KOiK03063.
OMAiRTDETHE.
OrthoDBiEOG7F24ST.
PhylomeDBiP43686.
TreeFamiTF106227.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: P43686-1) [UniParc]FASTAAdd to basket

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
MEEIGILVEK AQDEIPALSV SRPQTGLSFL GPEPEDLEDL YSRYKKLQQE
60 70 80 90 100
LEFLEVQEEY IKDEQKNLKK EFLHAQEEVK RIQSIPLVIG QFLEAVDQNT
110 120 130 140 150
AIVGSTTGSN YYVRILSTID RELLKPNASV ALHKHSNALV DVLPPEADSS
160 170 180 190 200
IMMLTSDQKP DVMYADIGGM DIQKQEVREA VELPLTHFEL YKQIGIDPPR
210 220 230 240 250
GVLMYGPPGC GKTMLAKAVA HHTTAAFIRV VGSEFVQKYL GEGPRMVRDV
260 270 280 290 300
FRLAKENAPA IIFIDEIDAI ATKRFDAQTG ADREVQRILL ELLNQMDGFD
310 320 330 340 350
QNVNVKVIMA TNRADTLDPA LLRPGRLDRK IEFPLPDRRQ KRLIFSTITS
360 370 380 390 400
KMNLSEEVDL EDYVARPDKI SGADINSICQ ESGMLAVREN RYIVLAKDFE
410
KAYKTVIKKD EQEHEFYK
Length:418
Mass (Da):47,366
Last modified:May 10, 2002 - v2
Checksum:i80F9523C61B88F0C
GO
Isoform 2 (identifier: P43686-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     46-76: Missing.

Note: No experimental confirmation available.
Show »
Length:387
Mass (Da):43,508
Checksum:iFA64D44EE00E9A7B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731L → F in AAC32612 (Ref. 4) Curated
Sequence conflicti110 – 1101N → S in AAC32612 (Ref. 4) Curated
Sequence conflicti118 – 1181T → A no nucleotide entry (PubMed:8419915).Curated
Sequence conflicti157 – 1571D → G in AAC32612 (Ref. 4) Curated
Sequence conflicti185 – 1851L → V in AAC32612 (Ref. 4) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei46 – 7631Missing in isoform 2. 1 PublicationVSP_000022Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038965 mRNA. Translation: AAC26843.1.
U27515 mRNA. Translation: AAC99817.1.
AF020736 mRNA. Translation: AAC32612.1.
BT007232 mRNA. Translation: AAP35896.1.
AC007842 Genomic DNA. Translation: AAD39267.1.
BC000343 mRNA. Translation: AAH00343.1.
BC010396 mRNA. Translation: AAH10396.1.
BC014488 mRNA. Translation: AAH14488.1.
CCDSiCCDS12547.1. [P43686-1]
CCDS46076.1. [P43686-2]
RefSeqiNP_006494.1. NM_006503.3. [P43686-1]
NP_694546.1. NM_153001.2. [P43686-2]
UniGeneiHs.211594.

Genome annotation databases

EnsembliENST00000157812; ENSP00000157812; ENSG00000013275. [P43686-1]
ENST00000455878; ENSP00000413869; ENSG00000013275. [P43686-2]
ENST00000629691; ENSP00000487367; ENSG00000281221. [P43686-1]
ENST00000630857; ENSP00000485851; ENSG00000281221. [P43686-2]
GeneIDi5704.
KEGGihsa:5704.
UCSCiuc002omq.4. human. [P43686-1]
uc002omr.4. human. [P43686-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038965 mRNA. Translation: AAC26843.1.
U27515 mRNA. Translation: AAC99817.1.
AF020736 mRNA. Translation: AAC32612.1.
BT007232 mRNA. Translation: AAP35896.1.
AC007842 Genomic DNA. Translation: AAD39267.1.
BC000343 mRNA. Translation: AAH00343.1.
BC010396 mRNA. Translation: AAH10396.1.
BC014488 mRNA. Translation: AAH14488.1.
CCDSiCCDS12547.1. [P43686-1]
CCDS46076.1. [P43686-2]
RefSeqiNP_006494.1. NM_006503.3. [P43686-1]
NP_694546.1. NM_153001.2. [P43686-2]
UniGeneiHs.211594.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DVWX-ray2.30B337-418[»]
ProteinModelPortaliP43686.
SMRiP43686. Positions 41-418.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111677. 93 interactions.
DIPiDIP-29274N.
IntActiP43686. 23 interactions.
MINTiMINT-5004247.
STRINGi9606.ENSP00000157812.

PTM databases

PhosphoSiteiP43686.

Polymorphism and mutation databases

BioMutaiPSMC4.
DMDMi20532409.

2D gel databases

OGPiP43686.

Proteomic databases

MaxQBiP43686.
PaxDbiP43686.
PRIDEiP43686.

Protocols and materials databases

DNASUi5704.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000157812; ENSP00000157812; ENSG00000013275. [P43686-1]
ENST00000455878; ENSP00000413869; ENSG00000013275. [P43686-2]
ENST00000629691; ENSP00000487367; ENSG00000281221. [P43686-1]
ENST00000630857; ENSP00000485851; ENSG00000281221. [P43686-2]
GeneIDi5704.
KEGGihsa:5704.
UCSCiuc002omq.4. human. [P43686-1]
uc002omr.4. human. [P43686-2]

Organism-specific databases

CTDi5704.
GeneCardsiGC19P040477.
HGNCiHGNC:9551. PSMC4.
HPAiHPA002044.
HPA005471.
MIMi602707. gene.
neXtProtiNX_P43686.
PharmGKBiPA33896.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1222.
GeneTreeiENSGT00550000074962.
HOGENOMiHOG000225143.
HOVERGENiHBG000109.
InParanoidiP43686.
KOiK03063.
OMAiRTDETHE.
OrthoDBiEOG7F24ST.
PhylomeDBiP43686.
TreeFamiTF106227.

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_188323. CLEC7A (Dectin-1) signaling.
REACT_188330. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_263873. degradation of AXIN.
REACT_263883. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
REACT_264438. degradation of DVL.
REACT_264478. Asymmetric localization of PCP proteins.
REACT_264605. Hedgehog ligand biogenesis.
REACT_267700. Degradation of GLI2 by the proteasome.
REACT_268156. Degradation of GLI1 by the proteasome.
REACT_268366. GLI3 is processed to GLI3R by the proteasome.
REACT_268718. Hedgehog 'on' state.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

ChiTaRSiPSMC4. human.
EvolutionaryTraceiP43686.
GeneWikiiPSMC4.
GenomeRNAii5704.
NextBioi22160.
PROiP43686.
SOURCEiSearch...

Gene expression databases

BgeeiP43686.
CleanExiHS_PSMC4.
ExpressionAtlasiP43686. baseline and differential.
GenevisibleiP43686. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The type 1 human immunodeficiency virus Tat binding protein is a transcriptional activator belonging to an additional family of evolutionarily conserved genes."
    Ohana B., Moore P.A., Ruben S.M., Southgate C.D., Green M.R., Rosen C.A.
    Proc. Natl. Acad. Sci. U.S.A. 90:138-142(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Umbilical cord blood.
  3. "A component of the 26S proteasome binds on orphan member of the nuclear hormone receptor superfamily."
    Choi H.S., Seol W., Moore D.D.
    J. Steroid Biochem. Mol. Biol. 56:23-30(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH NR1I3.
  4. "Cloning and expression analysis of a novel human gene homologous to mouse proteasomal ATPase (Tat-binding protein 7)."
    Bi A., Yu L., Zheng L.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Lung, Pancreas and Skin.
  8. Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-10; 218-229; 307-313 AND 343-369, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hepatoma.
  9. "Tat-binding protein 7 is a subunit of the 26S protease."
    Dubiel W., Ferrell K., Rechsteiner M.
    Biol. Chem. Hoppe-Seyler 375:237-240(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION.
  10. "Proteasomal ATPase-associated factor 1 negatively regulates proteasome activity by interacting with proteasomal ATPases."
    Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.
    Mol. Cell. Biol. 25:3842-3853(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAAF1.
  11. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
    Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
    Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-397 AND LYS-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "TRIM5alpha associates with proteasomal subunits in cells while in complex with HIV-1 virions."
    Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L., Luban J., Campbell E.M.
    Retrovirology 8:93-93(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM5.
  20. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  23. "Structure of the oncoprotein gankyrin in complex with S6 ATPase of the 26S proteasome."
    Nakamura Y., Nakano K., Umehara T., Kimura M., Hayashizaki Y., Tanaka A., Horikoshi M., Padmanabhan B., Yokoyama S.
    Structure 15:179-189(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 337-418 IN COMPLEX WITH MOUSE PSMD10.

Entry informationi

Entry nameiPRS6B_HUMAN
AccessioniPrimary (citable) accession number: P43686
Secondary accession number(s): Q96FV5, Q9UBM3, Q9UEX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: May 10, 2002
Last modified: June 24, 2015
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.