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P25788

- PSA3_HUMAN

UniProt

P25788 - PSA3_HUMAN

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Protein

Proteasome subunit alpha type-3

Gene
PSMA3, HC8, PSC8
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2.2 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Host-virus interaction

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.

Protein family/group databases

MEROPSiT01.977.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-3 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit C8
Multicatalytic endopeptidase complex subunit C8
Proteasome component C8
Gene namesi
Name:PSMA3
Synonyms:HC8, PSC8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:9532. PSMA3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
  6. proteasome complex Source: ProtInc
  7. proteasome core complex Source: BHF-UCL
  8. proteasome core complex, alpha-subunit complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33877.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 255254Proteasome subunit alpha type-3PRO_0000124091Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine4 Publications
Modified residuei57 – 571N6-acetyllysine1 Publication
Modified residuei206 – 2061N6-acetyllysine1 Publication
Modified residuei230 – 2301N6-acetyllysine1 Publication
Modified residuei243 – 2431Phosphoserine1 Publication
Modified residuei250 – 2501Phosphoserine11 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP25788.
PaxDbiP25788.
PRIDEiP25788.

2D gel databases

OGPiP25788.
REPRODUCTION-2DPAGEIPI00171199.

PTM databases

PhosphoSiteiP25788.

Expressioni

Inductioni

Down-regulated by antioxidants BO-653 and probucol. Up-regulated by bacterial lipopolysaccharides (LPS) and TNF.3 Publications

Gene expression databases

ArrayExpressiP25788.
BgeeiP25788.
CleanExiHS_PSMA3.
GenevestigatoriP25788.

Organism-specific databases

HPAiHPA000905.

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with AURKB. Interacts with CDKN1A. Interacts with HIV-1 TAT protein. Interacts with hepatitis C virus (HCV) F protein. Interacts with Epstein-Barr virus EBNA3 proteins. Interacts with MDM2 and RB1. Interacts with the C-terminus of TBXA2R isoform 2.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MDM2Q009872EBI-348380,EBI-389668
PMLP295902EBI-348380,EBI-295890
PSMA1P257863EBI-348380,EBI-359352
PSMA4P257894EBI-348380,EBI-359310
PSMA6P609004EBI-348380,EBI-357793
PSMA7O148186EBI-348380,EBI-603272

Protein-protein interaction databases

BioGridi111657. 182 interactions.
IntActiP25788. 43 interactions.
MINTiMINT-1035201.
STRINGi9606.ENSP00000216455.

Structurei

3D structure databases

ProteinModelPortaliP25788.
SMRiP25788. Positions 2-246.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091086.
HOVERGENiHBG105566.
InParanoidiP25788.
KOiK02727.
OMAiVPDGRHF.
OrthoDBiEOG73JKW6.
PhylomeDBiP25788.
TreeFamiTF106208.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P25788-1) [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

MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV    50
EKLVLSKLYE EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR 100
SNFGYNIPLK HLADRVAMYV HAYTLYSAVR PFGCSFMLGS YSVNDGAQLY 150
MIDPSGVSYG YWGCAIGKAR QAAKTEIEKL QMKEMTCRDI VKEVAKIIYI 200
VHDEVKDKAF ELELSWVGEL TNGRHEIVPK DIREEAEKYA KESLKEEDES 250
DDDNM 255
Length:255
Mass (Da):28,433
Last modified:January 23, 2007 - v2
Checksum:iA1854ED3C0650FB1
GO
Isoform 2 (identifier: P25788-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     136-142: Missing.

Show »
Length:248
Mass (Da):27,647
Checksum:iE1C4F1C97EC83DAD
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei136 – 1427Missing in isoform 2. VSP_005280

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911I → M in AAH29402. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D00762 mRNA. Translation: BAA00659.1.
BT006711 mRNA. Translation: AAP35357.1.
BT019715 mRNA. Translation: AAV38520.1.
AK315158 mRNA. Translation: BAG37603.1.
CH471061 Genomic DNA. Translation: EAW80719.1.
BC005265 mRNA. Translation: AAH05265.1.
BC029402 mRNA. Translation: AAH29402.1.
BC038990 mRNA. Translation: AAH38990.1.
CCDSiCCDS45113.1. [P25788-2]
CCDS9731.1. [P25788-1]
PIRiS15971. SNHUC8.
RefSeqiNP_002779.1. NM_002788.3. [P25788-1]
NP_687033.1. NM_152132.2. [P25788-2]
UniGeneiHs.558799.

Genome annotation databases

EnsembliENST00000216455; ENSP00000216455; ENSG00000100567. [P25788-1]
ENST00000412908; ENSP00000390491; ENSG00000100567. [P25788-2]
GeneIDi5684.
KEGGihsa:5684.
UCSCiuc001xdj.2. human. [P25788-1]
uc001xdk.2. human. [P25788-2]

Polymorphism databases

DMDMi130859.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D00762 mRNA. Translation: BAA00659.1 .
BT006711 mRNA. Translation: AAP35357.1 .
BT019715 mRNA. Translation: AAV38520.1 .
AK315158 mRNA. Translation: BAG37603.1 .
CH471061 Genomic DNA. Translation: EAW80719.1 .
BC005265 mRNA. Translation: AAH05265.1 .
BC029402 mRNA. Translation: AAH29402.1 .
BC038990 mRNA. Translation: AAH38990.1 .
CCDSi CCDS45113.1. [P25788-2 ]
CCDS9731.1. [P25788-1 ]
PIRi S15971. SNHUC8.
RefSeqi NP_002779.1. NM_002788.3. [P25788-1 ]
NP_687033.1. NM_152132.2. [P25788-2 ]
UniGenei Hs.558799.

3D structure databases

ProteinModelPortali P25788.
SMRi P25788. Positions 2-246.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111657. 182 interactions.
IntActi P25788. 43 interactions.
MINTi MINT-1035201.
STRINGi 9606.ENSP00000216455.

Chemistry

ChEMBLi CHEMBL2364701.

Protein family/group databases

MEROPSi T01.977.

PTM databases

PhosphoSitei P25788.

Polymorphism databases

DMDMi 130859.

2D gel databases

OGPi P25788.
REPRODUCTION-2DPAGE IPI00171199.

Proteomic databases

MaxQBi P25788.
PaxDbi P25788.
PRIDEi P25788.

Protocols and materials databases

DNASUi 5684.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216455 ; ENSP00000216455 ; ENSG00000100567 . [P25788-1 ]
ENST00000412908 ; ENSP00000390491 ; ENSG00000100567 . [P25788-2 ]
GeneIDi 5684.
KEGGi hsa:5684.
UCSCi uc001xdj.2. human. [P25788-1 ]
uc001xdk.2. human. [P25788-2 ]

Organism-specific databases

CTDi 5684.
GeneCardsi GC14P058711.
H-InvDB HIX0155215.
HGNCi HGNC:9532. PSMA3.
HPAi HPA000905.
MIMi 176843. gene.
176845. gene.
neXtProti NX_P25788.
PharmGKBi PA33877.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0638.
HOGENOMi HOG000091086.
HOVERGENi HBG105566.
InParanoidi P25788.
KOi K02727.
OMAi VPDGRHF.
OrthoDBi EOG73JKW6.
PhylomeDBi P25788.
TreeFami TF106208.

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

GeneWikii PSMA3.
GenomeRNAii 5684.
NextBioi 22072.
PROi P25788.
SOURCEi Search...

Gene expression databases

ArrayExpressi P25788.
Bgeei P25788.
CleanExi HS_PSMA3.
Genevestigatori P25788.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view ]
SMARTi SM00948. Proteasome_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequence analysis of cDNAs for five major subunits of human proteasomes (multi-catalytic proteinase complexes)."
    Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H., Tanaka K., Ichihara A.
    Biochim. Biophys. Acta 1089:95-102(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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 (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Bone marrow, Pancreas and Urinary bladder.
  6. "Human proteasome subunits from 2-dimensional gels identified by partial sequencing."
    Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.
    Biochem. Biophys. Res. Commun. 205:1785-1789(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 116-130.
  7. "Gene expression induced by BO-653, probucol and BHQ in human endothelial cells."
    Takabe W., Mataki C., Wada Y., Ishii M., Izumi A., Aburatani H., Hamakubo T., Niki E., Kodama T., Noguchi N.
    J. Atheroscler. Thromb. 7:223-230(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY BO-653 AND PROBUCOL.
  8. "A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome."
    Touitou R., Richardson J., Bose S., Nakanishi M., Rivett J., Allday M.J.
    EMBO J. 20:2367-2375(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDKN1A.
  9. "Mapping and structural dissection of human 20 s proteasome using proteomic approaches."
    Claverol S., Burlet-Schiltz O., Girbal-Neuhauser E., Gairin J.E., Monsarrat B.
    Mol. Cell. Proteomics 1:567-578(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT SER-2, PHOSPHORYLATION AT SER-250.
  10. "Analysis of gene expression during maturation of immature dendritic cells derived from peripheral blood monocytes."
    Matsunaga T., Ishida T., Takekawa M., Nishimura S., Adachi M., Imai K.
    Scand. J. Immunol. 56:593-601(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  11. "Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits."
    Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P., Mayer R.J., Krueger E.
    FEBS Lett. 553:200-204(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 TAT.
  12. "Human Aurora-B binds to a proteasome alpha-subunit HC8 and undergoes degradation in a proteasome-dependent manner."
    Shu F., Guo S., Dang Y., Qi M., Zhou G., Guo Z., Zhang Y., Wu C., Zhao S., Yu L.
    Mol. Cell. Biochem. 254:157-162(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AURKB.
  13. "Epstein-Barr virus EBNA3 proteins bind to the C8/alpha7 subunit of the 20S proteasome and are degraded by 20S proteasomes in vitro, but are very stable in latently infected B cells."
    Touitou R., O'Nions J., Heaney J., Allday M.J.
    J. Gen. Virol. 86:1269-1277(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EBNA3.
  14. "MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein."
    Sdek P., Ying H., Chang D.L., Qiu W., Zheng H., Touitou R., Allday M.J., Xiao Z.X.
    Mol. Cell 20:699-708(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MDM2 AND RB1.
  15. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Chemical structure-dependent gene expression of proteasome subunits via regulation of the antioxidant response element."
    Takabe W., Matsukawa N., Kodama T., Tanaka K., Noguchi N.
    Free Radic. Res. 40:21-30(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY BO-653.
  18. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "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-243 AND SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  20. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  21. "Low expression of cell-surface thromboxane A2 receptor beta-isoform through the negative regulation of its membrane traffic by proteasomes."
    Sasaki M., Sukegawa J., Miyosawa K., Yanagisawa T., Ohkubo S., Nakahata N.
    Prostaglandins Other Lipid Mediat. 83:237-249(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TBXA2R.
  22. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  25. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Ubiquitin-independent degradation of hepatitis C virus F protein."
    Yuksek K., Chen W.-L., Chien D., Ou J.-H.
    J. Virol. 83:612-621(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCV F PROTEIN.
  27. "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-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  28. "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-57; LYS-206 AND LYS-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "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-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPSA3_HUMAN
AccessioniPrimary (citable) accession number: P25788
Secondary accession number(s): B2RCK6
, Q86U83, Q8N1D8, Q9BS70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 168 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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