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P43686

- PRS6B_HUMAN

UniProt

P43686 - PRS6B_HUMAN

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Protein
26S protease regulatory subunit 6B
Gene
PSMC4, MIP224, TBP7
Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 2138ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATPase activity Source: ProtInc
  3. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  3. G1/S transition of mitotic cell cycle Source: Reactome
  4. RNA metabolic process Source: Reactome
  5. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  6. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  7. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  8. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  9. apoptotic process Source: Reactome
  10. blastocyst development Source: Ensembl
  11. cellular nitrogen compound metabolic process Source: Reactome
  12. gene expression Source: Reactome
  13. mRNA metabolic process Source: Reactome
  14. mitotic cell cycle Source: Reactome
  15. negative regulation of apoptotic process Source: Reactome
  16. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  17. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  18. protein polyubiquitination Source: Reactome
  19. proteolysis Source: ProtInc
  20. regulation of apoptotic process Source: Reactome
  21. regulation of cellular amino acid metabolic process Source: Reactome
  22. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  23. small molecule metabolic process Source: Reactome
  24. viral process Source: Reactome
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_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_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
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_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: Chromosome 19

Organism-specific databases

HGNCiHGNC:9551. PSMC4.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. cytosolic proteasome complex Source: Ensembl
  4. inclusion body Source: Ensembl
  5. nucleoplasm Source: Reactome
  6. nucleus Source: UniProt
  7. proteasome accessory complex Source: UniProtKB
  8. proteasome complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33896.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 41841826S protease regulatory subunit 6B
PRO_0000084686Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei21 – 211Phosphoserine1 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

ArrayExpressiP43686.
BgeeiP43686.
CleanExiHS_PSMC4.
GenevestigatoriP43686.

Organism-specific databases

HPAiHPA002044.
HPA005471.

Interactioni

Subunit structurei

Interacts with NR1I3. Interacts with PAAF1. Interacts with TRIM5.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PSMC5P6219511EBI-743997,EBI-357745
PSMC6P623333EBI-743997,EBI-357669
PSMD10O758328EBI-743997,EBI-752185

Protein-protein interaction databases

BioGridi111677. 83 interactions.
DIPiDIP-29274N.
IntActiP43686. 20 interactions.
MINTiMINT-5004247.
STRINGi9606.ENSP00000157812.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DVWX-ray2.30B337-418[»]
ProteinModelPortaliP43686.
SMRiP43686. Positions 41-418.

Miscellaneous databases

EvolutionaryTraceiP43686.

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.

Phylogenomic databases

eggNOGiCOG1222.
HOGENOMiHOG000225143.
HOVERGENiHBG000109.
InParanoidiP43686.
KOiK03063.
OMAiLYIKYKK.
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. Align

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

MEEIGILVEK AQDEIPALSV SRPQTGLSFL GPEPEDLEDL YSRYKKLQQE    50
LEFLEVQEEY IKDEQKNLKK EFLHAQEEVK RIQSIPLVIG QFLEAVDQNT 100
AIVGSTTGSN YYVRILSTID RELLKPNASV ALHKHSNALV DVLPPEADSS 150
IMMLTSDQKP DVMYADIGGM DIQKQEVREA VELPLTHFEL YKQIGIDPPR 200
GVLMYGPPGC GKTMLAKAVA HHTTAAFIRV VGSEFVQKYL GEGPRMVRDV 250
FRLAKENAPA IIFIDEIDAI ATKRFDAQTG ADREVQRILL ELLNQMDGFD 300
QNVNVKVIMA TNRADTLDPA LLRPGRLDRK IEFPLPDRRQ KRLIFSTITS 350
KMNLSEEVDL EDYVARPDKI SGADINSICQ ESGMLAVREN RYIVLAKDFE 400
KAYKTVIKKD EQEHEFYK 418
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei46 – 7631Missing in isoform 2.
VSP_000022Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731L → F in AAC32612. 1 Publication
Sequence conflicti110 – 1101N → S in AAC32612. 1 Publication
Sequence conflicti118 – 1181T → A no nucleotide entry 1 Publication
Sequence conflicti157 – 1571D → G in AAC32612. 1 Publication
Sequence conflicti185 – 1851L → V in AAC32612. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
GeneIDi5704.
KEGGihsa:5704.
UCSCiuc002omq.4. human. [P43686-1]
uc002omr.4. human. [P43686-2]

Polymorphism databases

DMDMi20532409.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS12547.1. [P43686-1 ]
CCDS46076.1. [P43686-2 ]
RefSeqi NP_006494.1. NM_006503.3. [P43686-1 ]
NP_694546.1. NM_153001.2. [P43686-2 ]
UniGenei Hs.211594.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DVW X-ray 2.30 B 337-418 [» ]
ProteinModelPortali P43686.
SMRi P43686. Positions 41-418.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111677. 83 interactions.
DIPi DIP-29274N.
IntActi P43686. 20 interactions.
MINTi MINT-5004247.
STRINGi 9606.ENSP00000157812.

PTM databases

PhosphoSitei P43686.

Polymorphism databases

DMDMi 20532409.

2D gel databases

OGPi P43686.

Proteomic databases

MaxQBi P43686.
PaxDbi P43686.
PRIDEi P43686.

Protocols and materials databases

DNASUi 5704.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000157812 ; ENSP00000157812 ; ENSG00000013275 . [P43686-1 ]
ENST00000455878 ; ENSP00000413869 ; ENSG00000013275 . [P43686-2 ]
GeneIDi 5704.
KEGGi hsa:5704.
UCSCi uc002omq.4. human. [P43686-1 ]
uc002omr.4. human. [P43686-2 ]

Organism-specific databases

CTDi 5704.
GeneCardsi GC19P040477.
HGNCi HGNC:9551. PSMC4.
HPAi HPA002044.
HPA005471.
MIMi 602707. gene.
neXtProti NX_P43686.
PharmGKBi PA33896.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1222.
HOGENOMi HOG000225143.
HOVERGENi HBG000109.
InParanoidi P43686.
KOi K03063.
OMAi LYIKYKK.
OrthoDBi EOG7F24ST.
PhylomeDBi P43686.
TreeFami TF106227.

Enzyme and pathway databases

Reactomei 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_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
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_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

ChiTaRSi PSMC4. human.
EvolutionaryTracei P43686.
GeneWikii PSMC4.
GenomeRNAii 5704.
NextBioi 22160.
PROi P43686.
SOURCEi Search...

Gene expression databases

ArrayExpressi P43686.
Bgeei P43686.
CleanExi HS_PSMC4.
Genevestigatori P43686.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00004. AAA. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01242. 26Sp45. 1 hit.
PROSITEi PS00674. AAA. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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: September 3, 2014
This is version 149 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

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