SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P60900

- PSA6_HUMAN

UniProt

P60900 - PSA6_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Proteasome subunit alpha type-6
Gene
PSMA6, PROS27
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.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

GO - Molecular functioni

  1. NF-kappaB binding Source: BHF-UCL
  2. RNA binding Source: UniProtKB
  3. endopeptidase activity Source: UniProtKB
  4. protein binding Source: IntAct
  5. purine ribonucleoside triphosphate binding Source: BHF-UCL
  6. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

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

Hydrolase, Protease, Threonine protease

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

MEROPSiT01.971.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-6 (EC:3.4.25.1)
Alternative name(s):
27 kDa prosomal protein
Short name:
PROS-27
Short name:
p27K
Macropain iota chain
Multicatalytic endopeptidase complex iota chain
Proteasome iota chain
Gene namesi
Name:PSMA6
Synonyms:PROS27
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:9535. PSMA6.

Subcellular locationi

Cytoplasm. Nucleus. CytoplasmP-body By similarity
Note: Colocalizes with TRIM5 in the cytoplasmic bodies By similarity.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytoplasmic mRNA processing body Source: UniProtKB
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. myofibril Source: BHF-UCL
  6. nuclear matrix Source: BHF-UCL
  7. nucleoplasm Source: Reactome
  8. nucleus Source: BHF-UCL
  9. polysome Source: BHF-UCL
  10. proteasome core complex Source: UniProtKB
  11. proteasome core complex, alpha-subunit complex Source: BHF-UCL
  12. sarcomere Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33880.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 246246Proteasome subunit alpha type-6
PRO_0000124130Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi5 – 51O-linked (GlcNAc) By similarity
Cross-linki59 – 59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei102 – 1021N6-acetyllysine1 Publication
Modified residuei104 – 1041N6-acetyllysine1 Publication
Modified residuei159 – 1591Phosphotyrosine By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP60900.
PaxDbiP60900.
PeptideAtlasiP60900.
PRIDEiP60900.

2D gel databases

REPRODUCTION-2DPAGEIPI00029623.
SWISS-2DPAGEP60900.
UCD-2DPAGEP60900.

PTM databases

PhosphoSiteiP60900.

Expressioni

Gene expression databases

BgeeiP60900.
CleanExiHS_PSMA6.
GenevestigatoriP60900.

Organism-specific databases

HPAiHPA003049.

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 ALKBH4.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PSMA2P257875EBI-357793,EBI-603262
PSMA3P257884EBI-357793,EBI-348380
PSMA4P257894EBI-357793,EBI-359310
PSMA7O1481811EBI-357793,EBI-603272
UCHL5Q9Y5K54EBI-357793,EBI-1051183

Protein-protein interaction databases

BioGridi111660. 101 interactions.
DIPiDIP-29367N.
IntActiP60900. 29 interactions.
MINTiMINT-5001118.
STRINGi9606.ENSP00000261479.

Structurei

3D structure databases

ProteinModelPortaliP60900.
SMRiP60900. Positions 2-245.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091084.
HOVERGENiHBG107363.
InParanoidiP60900.
KOiK02730.
PhylomeDBiP60900.
TreeFamiTF106210.

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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P60900-1) [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

MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI    50
VTQKKVPDKL LDSSTVTHLF KITENIGCVM TGMTADSRSQ VQRARYEAAN 100
WKYKYGYEIP VDMLCKRIAD ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ 150
VYKCDPAGYY CGFKATAAGV KQTESTSFLE KKVKKKFDWT FEQTVETAIT 200
CLSTVLSIDF KPSEIEVGVV TVENPKFRIL TEAEIDAHLV ALAERD 246
Length:246
Mass (Da):27,399
Last modified:April 13, 2004 - v1
Checksum:i94D1FD3C0A7CC72A
GO
Isoform 2 (identifier: P60900-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MSRGSSAGFDRHITIFSPEGRLYQV → MAGLRR

Note: No experimental confirmation available.

Show »
Length:227
Mass (Da):25,290
Checksum:i436E2FE91E1BCDE8
GO
Isoform 3 (identifier: P60900-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.

Note: No experimental confirmation available.

Show »
Length:167
Mass (Da):18,816
Checksum:iF46774830B65E327
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti233 – 2331A → S.
Corresponds to variant rs15434 [ dbSNP | Ensembl ].
VAR_051546

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7979Missing in isoform 3.
VSP_054586Add
BLAST
Alternative sequencei1 – 2525MSRGS…RLYQV → MAGLRR in isoform 2.
VSP_054587Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591K → C in CAA43964. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59417 mRNA. Translation: CAA42052.1.
CR456944 mRNA. Translation: CAG33225.1.
AK298920 mRNA. Translation: BAG61026.1.
AK302008 mRNA. Translation: BAG63411.1.
AK313011 mRNA. Translation: BAG35846.1.
AK316223 mRNA. Translation: BAH14594.1.
AL121594 Genomic DNA. No translation available.
AL133163 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65876.1.
CH471078 Genomic DNA. Translation: EAW65877.1.
BC002979 mRNA. Translation: AAH02979.1.
BC017882 mRNA. Translation: AAH17882.1.
BC022354 mRNA. Translation: AAH22354.1.
BC023659 mRNA. Translation: AAH23659.1.
BC070137 mRNA. Translation: AAH70137.1.
X61972 mRNA. Translation: CAA43964.1.
CCDSiCCDS61437.1. [P60900-2]
CCDS61438.1. [P60900-3]
CCDS9655.1. [P60900-1]
PIRiS30274.
RefSeqiNP_001269161.1. NM_001282232.1. [P60900-3]
NP_001269162.1. NM_001282233.1. [P60900-3]
NP_001269163.1. NM_001282234.1. [P60900-2]
NP_002782.1. NM_002791.2. [P60900-1]
UniGeneiHs.446260.

Genome annotation databases

EnsembliENST00000261479; ENSP00000261479; ENSG00000100902.
ENST00000540871; ENSP00000444844; ENSG00000100902.
ENST00000555764; ENSP00000452566; ENSG00000100902.
GeneIDi5687.
KEGGihsa:5687.
UCSCiuc001wtd.3. human. [P60900-1]

Polymorphism databases

DMDMi46397659.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59417 mRNA. Translation: CAA42052.1 .
CR456944 mRNA. Translation: CAG33225.1 .
AK298920 mRNA. Translation: BAG61026.1 .
AK302008 mRNA. Translation: BAG63411.1 .
AK313011 mRNA. Translation: BAG35846.1 .
AK316223 mRNA. Translation: BAH14594.1 .
AL121594 Genomic DNA. No translation available.
AL133163 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65876.1 .
CH471078 Genomic DNA. Translation: EAW65877.1 .
BC002979 mRNA. Translation: AAH02979.1 .
BC017882 mRNA. Translation: AAH17882.1 .
BC022354 mRNA. Translation: AAH22354.1 .
BC023659 mRNA. Translation: AAH23659.1 .
BC070137 mRNA. Translation: AAH70137.1 .
X61972 mRNA. Translation: CAA43964.1 .
CCDSi CCDS61437.1. [P60900-2 ]
CCDS61438.1. [P60900-3 ]
CCDS9655.1. [P60900-1 ]
PIRi S30274.
RefSeqi NP_001269161.1. NM_001282232.1. [P60900-3 ]
NP_001269162.1. NM_001282233.1. [P60900-3 ]
NP_001269163.1. NM_001282234.1. [P60900-2 ]
NP_002782.1. NM_002791.2. [P60900-1 ]
UniGenei Hs.446260.

3D structure databases

ProteinModelPortali P60900.
SMRi P60900. Positions 2-245.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111660. 101 interactions.
DIPi DIP-29367N.
IntActi P60900. 29 interactions.
MINTi MINT-5001118.
STRINGi 9606.ENSP00000261479.

Chemistry

ChEMBLi CHEMBL2364701.

Protein family/group databases

MEROPSi T01.971.

PTM databases

PhosphoSitei P60900.

Polymorphism databases

DMDMi 46397659.

2D gel databases

REPRODUCTION-2DPAGE IPI00029623.
SWISS-2DPAGE P60900.
UCD-2DPAGE P60900.

Proteomic databases

MaxQBi P60900.
PaxDbi P60900.
PeptideAtlasi P60900.
PRIDEi P60900.

Protocols and materials databases

DNASUi 5687.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261479 ; ENSP00000261479 ; ENSG00000100902 .
ENST00000540871 ; ENSP00000444844 ; ENSG00000100902 .
ENST00000555764 ; ENSP00000452566 ; ENSG00000100902 .
GeneIDi 5687.
KEGGi hsa:5687.
UCSCi uc001wtd.3. human. [P60900-1 ]

Organism-specific databases

CTDi 5687.
GeneCardsi GC14P035747.
HGNCi HGNC:9535. PSMA6.
HPAi HPA003049.
MIMi 602855. gene.
neXtProti NX_P60900.
PharmGKBi PA33880.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0638.
HOGENOMi HOG000091084.
HOVERGENi HBG107363.
InParanoidi P60900.
KOi K02730.
PhylomeDBi P60900.
TreeFami TF106210.

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 PSMA6.
GenomeRNAii 5687.
NextBioi 22090.
PROi P60900.
SOURCEi Search...

Gene expression databases

Bgeei P60900.
CleanExi HS_PSMA6.
Genevestigatori P60900.

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. "The prosomal RNA-binding protein p27K is a member of the alpha-type human prosomal gene family."
    Bey F., Pereira I.S., Coux O., Viegas-Pequignot E., Targa F.R., Nothwang H.G., Dutrillaux B., Scherrer K.
    Mol. Gen. Genet. 237:193-205(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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).
  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] (ISOFORMS 1; 2 AND 3).
    Tissue: Cerebellum and Testis.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Brain, Lymph, Skeletal muscle and Skin.
  7. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 12-43; 60-88; 105-116; 154-164; 172-181 AND 229-246, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  8. "The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous."
    DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z., Moomaw C.R., Dawson P.A., Slaughter C.A.
    Biochim. Biophys. Acta 1079:29-38(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-246 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  9. "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: PARTIAL PROTEIN SEQUENCE.
  10. "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.
  11. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
    Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
    Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-59.
    Tissue: Mammary cancer.
  12. "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-102 AND LYS-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Human ALKBH4 interacts with proteins associated with transcription."
    Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A., Falnes P.O.
    PLoS ONE 7:E49045-E49045(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ALKBH4.

Entry informationi

Entry nameiPSA6_HUMAN
AccessioniPrimary (citable) accession number: P60900
Secondary accession number(s): B2R7J9
, B4DQR4, B4DXJ9, P34062, Q6IB60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: September 3, 2014
This is version 124 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

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. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi