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Protein

Proteasome activator complex subunit 1

Gene

PSME1

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

Functioni

Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

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:
Proteasome activator complex subunit 1
Alternative name(s):
11S regulator complex subunit alpha
Short name:
REG-alpha
Activator of multicatalytic protease subunit 1
Interferon gamma up-regulated I-5111 protein
Short name:
IGUP I-5111
Proteasome activator 28 subunit alpha
Short name:
PA28a
Short name:
PA28alpha
Gene namesi
Name:PSME1
Synonyms:IFI5111
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:9568. PSME1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: Reactome
  • proteasome activator complex Source: InterPro
  • proteasome complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33914.

Polymorphism and mutation databases

DMDMi1170519.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249Proteasome activator complex subunit 1PRO_0000161779Add
BLAST

Proteomic databases

MaxQBiQ06323.
PaxDbiQ06323.
PRIDEiQ06323.

2D gel databases

DOSAC-COBS-2DPAGEQ06323.
OGPiQ06323.
SWISS-2DPAGEQ06323.

PTM databases

PhosphoSiteiQ06323.

Expressioni

Inductioni

By IFNG/IFN-gamma.

Gene expression databases

BgeeiQ06323.
CleanExiHS_PSME1.
ExpressionAtlasiQ06323. baseline and differential.
GenevisibleiQ06323. HS.

Organism-specific databases

HPAiHPA006632.

Interactioni

Subunit structurei

Heterodimer of PSME1 and PSME2, which forms a hexameric ring. PSME1 can form homoheptamers.1 Publication

Protein-protein interaction databases

BioGridi111692. 71 interactions.
IntActiQ06323. 21 interactions.
MINTiMINT-5002728.
STRINGi9606.ENSP00000372155.

Structurei

Secondary structure

1
249
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 3023Combined sources
Helixi32 – 4514Combined sources
Helixi47 – 493Combined sources
Helixi108 – 13730Combined sources
Helixi148 – 19043Combined sources
Helixi196 – 23237Combined sources
Helixi234 – 2385Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AVOX-ray2.80A/C/E/G/I/K/M4-63[»]
B/D/F/H/J/L/N104-242[»]
ProteinModelPortaliQ06323.
SMRiQ06323. Positions 4-63, 104-242.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06323.

Family & Domainsi

Sequence similaritiesi

Belongs to the PA28 family.Curated

Phylogenomic databases

eggNOGiNOG265006.
GeneTreeiENSGT00510000046374.
HOGENOMiHOG000282822.
HOVERGENiHBG053745.
InParanoidiQ06323.
KOiK06696.
OMAiTQISKYY.
OrthoDBiEOG7GTT4C.
PhylomeDBiQ06323.
TreeFamiTF106236.

Family and domain databases

Gene3Di1.20.120.180. 1 hit.
1.20.5.120. 1 hit.
InterProiIPR009077. Proteasome_activ_pa28.
IPR003186. Proteasome_activ_pa28_C.
IPR003185. Proteasome_activ_pa28_N.
[Graphical view]
PANTHERiPTHR10660. PTHR10660. 1 hit.
PfamiPF02251. PA28_alpha. 1 hit.
PF02252. PA28_beta. 1 hit.
[Graphical view]
SUPFAMiSSF47216. SSF47216. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q06323-1) [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
MAMLRVQPEA QAKVDVFRED LCTKTENLLG SYFPKKISEL DAFLKEPALN
60 70 80 90 100
EANLSNLKAP LDIPVPDPVK EKEKEERKKQ QEKEDKDEKK KGEDEDKGPP
110 120 130 140 150
CGPVNCNEKI VVLLQRLKPE IKDVIEQLNL VTTWLQLQIP RIEDGNNFGV
160 170 180 190 200
AVQEKVFELM TSLHTKLEGF HTQISKYFSE RGDAVTKAAK QPHVGDYRQL
210 220 230 240
VHELDEAEYR DIRLMVMEIR NAYAVLYDII LKNFEKLKKP RGETKGMIY
Length:249
Mass (Da):28,723
Last modified:November 1, 1995 - v1
Checksum:i5E27727E5A0B0AAB
GO
Isoform 2 (identifier: Q06323-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     224-249: AVLYDIILKNFEKLKKPRGETKGMIY → VRRQGQGRGGQRQLSQATHSLTLQARG

Note: Gene prediction based on EST data.
Show »
Length:250
Mass (Da):28,602
Checksum:iD860008F47D35F97
GO
Isoform 3 (identifier: Q06323-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     224-233: AVLYDIILKN → VRRLCYMTSS
     234-249: Missing.

Note: Gene prediction based on EST data.
Show »
Length:233
Mass (Da):26,870
Checksum:i4B9A7BFE858CC6D9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti55 – 551S → N.
Corresponds to variant rs1803830 [ dbSNP | Ensembl ].
VAR_011993
Natural varianti244 – 2441T → K.
Corresponds to variant rs14930 [ dbSNP | Ensembl ].
VAR_011994

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei224 – 24926AVLYD…KGMIY → VRRQGQGRGGQRQLSQATHS LTLQARG in isoform 2. CuratedVSP_046880Add
BLAST
Alternative sequencei224 – 23310AVLYDIILKN → VRRLCYMTSS in isoform 3. CuratedVSP_055166
Alternative sequencei234 – 24916Missing in isoform 3. CuratedVSP_055167Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07633 mRNA. Translation: AAA16521.1.
U10360 Genomic DNA. Translation: AAA53230.1.
AF078829 Genomic DNA. Translation: AAF02217.1.
BT019337 mRNA. Translation: AAV38144.1.
AK312211 mRNA. Translation: BAG35144.1.
CR456780 mRNA. Translation: CAG33061.1.
AL136295 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66105.1.
BC000352 mRNA. Translation: AAH00352.1.
BC007503 mRNA. Translation: AAH07503.1.
AB007137 Genomic DNA. Translation: BAA28836.1.
CCDSiCCDS41930.1. [Q06323-2]
CCDS61415.1. [Q06323-3]
CCDS9612.1. [Q06323-1]
PIRiA54859.
RefSeqiNP_001268457.1. NM_001281528.1. [Q06323-3]
NP_006254.1. NM_006263.3. [Q06323-1]
UniGeneiHs.75348.

Genome annotation databases

EnsembliENST00000206451; ENSP00000206451; ENSG00000092010. [Q06323-1]
ENST00000382708; ENSP00000372155; ENSG00000092010. [Q06323-2]
ENST00000561435; ENSP00000453976; ENSG00000092010. [Q06323-3]
GeneIDi5720.
KEGGihsa:5720.
UCSCiuc001wmg.3. human. [Q06323-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07633 mRNA. Translation: AAA16521.1.
U10360 Genomic DNA. Translation: AAA53230.1.
AF078829 Genomic DNA. Translation: AAF02217.1.
BT019337 mRNA. Translation: AAV38144.1.
AK312211 mRNA. Translation: BAG35144.1.
CR456780 mRNA. Translation: CAG33061.1.
AL136295 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66105.1.
BC000352 mRNA. Translation: AAH00352.1.
BC007503 mRNA. Translation: AAH07503.1.
AB007137 Genomic DNA. Translation: BAA28836.1.
CCDSiCCDS41930.1. [Q06323-2]
CCDS61415.1. [Q06323-3]
CCDS9612.1. [Q06323-1]
PIRiA54859.
RefSeqiNP_001268457.1. NM_001281528.1. [Q06323-3]
NP_006254.1. NM_006263.3. [Q06323-1]
UniGeneiHs.75348.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AVOX-ray2.80A/C/E/G/I/K/M4-63[»]
B/D/F/H/J/L/N104-242[»]
ProteinModelPortaliQ06323.
SMRiQ06323. Positions 4-63, 104-242.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111692. 71 interactions.
IntActiQ06323. 21 interactions.
MINTiMINT-5002728.
STRINGi9606.ENSP00000372155.

PTM databases

PhosphoSiteiQ06323.

Polymorphism and mutation databases

DMDMi1170519.

2D gel databases

DOSAC-COBS-2DPAGEQ06323.
OGPiQ06323.
SWISS-2DPAGEQ06323.

Proteomic databases

MaxQBiQ06323.
PaxDbiQ06323.
PRIDEiQ06323.

Protocols and materials databases

DNASUi5720.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000206451; ENSP00000206451; ENSG00000092010. [Q06323-1]
ENST00000382708; ENSP00000372155; ENSG00000092010. [Q06323-2]
ENST00000561435; ENSP00000453976; ENSG00000092010. [Q06323-3]
GeneIDi5720.
KEGGihsa:5720.
UCSCiuc001wmg.3. human. [Q06323-1]

Organism-specific databases

CTDi5720.
GeneCardsiGC14P024605.
HGNCiHGNC:9568. PSME1.
HPAiHPA006632.
MIMi600654. gene.
neXtProtiNX_Q06323.
PharmGKBiPA33914.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG265006.
GeneTreeiENSGT00510000046374.
HOGENOMiHOG000282822.
HOVERGENiHBG053745.
InParanoidiQ06323.
KOiK06696.
OMAiTQISKYY.
OrthoDBiEOG7GTT4C.
PhylomeDBiQ06323.
TreeFamiTF106236.

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

ChiTaRSiPSME1. human.
EvolutionaryTraceiQ06323.
GeneWikiiPSME1.
GenomeRNAii5720.
NextBioi22232.
PROiQ06323.
SOURCEiSearch...

Gene expression databases

BgeeiQ06323.
CleanExiHS_PSME1.
ExpressionAtlasiQ06323. baseline and differential.
GenevisibleiQ06323. HS.

Family and domain databases

Gene3Di1.20.120.180. 1 hit.
1.20.5.120. 1 hit.
InterProiIPR009077. Proteasome_activ_pa28.
IPR003186. Proteasome_activ_pa28_C.
IPR003185. Proteasome_activ_pa28_N.
[Graphical view]
PANTHERiPTHR10660. PTHR10660. 1 hit.
PfamiPF02251. PA28_alpha. 1 hit.
PF02252. PA28_beta. 1 hit.
[Graphical view]
SUPFAMiSSF47216. SSF47216. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Interferon-gamma up-regulates a unique set of proteins in human keratinocytes. Molecular cloning and expression of the cDNA encoding the RGD-sequence-containing protein IGUP I-5111."
    Honore B., Leffers H., Madsen P., Celis J.E.
    Eur. J. Biochem. 218:421-430(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Lung fibroblast.
  2. "Molecular cloning and expression of a gamma-interferon-inducible activator of the multicatalytic protease."
    Realini C., Dubiel W., Pratt G., Ferrell K., Rechsteiner M.
    J. Biol. Chem. 269:20727-20732(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    Tissue: Blood.
  3. "Organization of the genes encoding the human proteasome activators PA28alpha and beta."
    McCusker D., Wilson M., Trowsdale J.
    Immunogenetics 49:438-445(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  4. "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).
  5. "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: Spleen.
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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].
    Tissue: Muscle.
  10. "Characterization of the mouse PA28 activator complex gene family: complete organizations of the three member genes and a physical map of the approximately 150-kb region containing the alpha- and beta-subunit genes."
    Kohda K., Ishibashi T., Shimbara N., Tanaka K., Matsuda Y., Kasahara M.
    J. Immunol. 160:4923-4935(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-118.
  11. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
    Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
    Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-35; 191-197 AND 199-209.
    Tissue: Keratinocyte.
  12. "The proteasome 11S regulator subunit REG alpha (PA28 alpha) is a heptamer."
    Johnston S.C., Whitby F.G., Realini C., Rechsteiner M., Hill C.P.
    Protein Sci. 6:2469-2473(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Entry informationi

Entry nameiPSME1_HUMAN
AccessioniPrimary (citable) accession number: Q06323
Secondary accession number(s): A6NJG9
, H0YNE3, Q6IBM2, Q9UEF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 24, 2015
This is version 150 of the entry and version 1 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 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.