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Q99436

- PSB7_HUMAN

UniProt

Q99436 - PSB7_HUMAN

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Protein

Proteasome subunit beta type-7

Gene

PSMB7

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. This unit is responsible of the trypsin-like activity.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei44 – 441NucleophileBy similarity

GO - Molecular functioni

  1. 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

MEROPSiT01.017.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-7 (EC:3.4.25.1)
Alternative name(s):
Macropain chain Z
Multicatalytic endopeptidase complex chain Z
Proteasome subunit Z
Gene namesi
Name:PSMB7
Synonyms:Z
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:9544. PSMB7.

Subcellular locationi

Cytoplasm 1 PublicationPROSITE-ProRule annotation. Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. microtubule cytoskeleton Source: HPA
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProt
  6. proteasome complex Source: UniProtKB
  7. proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33889.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 4343Removed in mature formPRO_0000026645Add
BLAST
Chaini44 – 277234Proteasome subunit beta type-7PRO_0000026646Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

MaxQBiQ99436.
PaxDbiQ99436.
PeptideAtlasiQ99436.
PRIDEiQ99436.

PTM databases

PhosphoSiteiQ99436.

Expressioni

Tissue specificityi

Expressed at a low level in colonic mucosa. Up-regulated in colorectal cancer tissues.1 Publication

Gene expression databases

BgeeiQ99436.
CleanExiHS_PSMB7.
ExpressionAtlasiQ99436. baseline and differential.
GenevestigatoriQ99436.

Organism-specific databases

HPAiHPA052408.

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. This subunit can be displaced by the equivalent immune-specific subunit PSMB10. Interacts with HIV-1 TAT protein.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PSMB1P206188EBI-603319,EBI-372273
PSMB5P280747EBI-603319,EBI-357828
PSMB9P280655EBI-603319,EBI-603300

Protein-protein interaction databases

BioGridi111668. 72 interactions.
IntActiQ99436. 25 interactions.
MINTiMINT-1351242.
STRINGi9606.ENSP00000259457.

Structurei

3D structure databases

ProteinModelPortaliQ99436.
SMRiQ99436. Positions 44-263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00510000046533.
HOGENOMiHOG000182856.
HOVERGENiHBG093416.
InParanoidiQ99436.
KOiK02739.
OMAiQIWCAGA.
OrthoDBiEOG7CRTQJ.
PhylomeDBiQ99436.
TreeFamiTF106222.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR024689. Proteasome_bsu_C.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF12465. Pr_beta_C. 1 hit.
PF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_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: Q99436-1) [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
MAAVSVYAPP VGGFSFDNCR RNAVLEADFA KRGYKLPKVR KTGTTIAGVV
60 70 80 90 100
YKDGIVLGAD TRATEGMVVA DKNCSKIHFI SPNIYCCGAG TAADTDMTTQ
110 120 130 140 150
LISSNLELHS LSTGRLPRVV TANRMLKQML FRYQGYIGAA LVLGGVDVTG
160 170 180 190 200
PHLYSIYPHG STDKLPYVTM GSGSLAAMAV FEDKFRPDME EEEAKNLVSE
210 220 230 240 250
AIAAGIFNDL GSGSNIDLCV ISKNKLDFLR PYTVPNKKGT RLGRYRCEKG
260 270
TTAVLTEKIT PLEIEVLEET VQTMDTS
Length:277
Mass (Da):29,965
Last modified:May 1, 1997 - v1
Checksum:iA610C949A0ACF1CE
GO
Isoform 2 (identifier: Q99436-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     133-142: YQGYIGAALV → FWLLGSNGCI
     143-277: Missing.

Note: No experimental confirmation available.

Show »
Length:142
Mass (Da):15,323
Checksum:i2B639D6E1A7C144F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391V → A.1 Publication
Corresponds to variant rs4574 [ dbSNP | Ensembl ].
VAR_013292

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei133 – 14210YQGYIGAALV → FWLLGSNGCI in isoform 2. 1 PublicationVSP_056573
Alternative sequencei143 – 277135Missing in isoform 2. 1 PublicationVSP_056574Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D38048 mRNA. Translation: BAA07238.1.
AK303460 mRNA. Translation: BAG64503.1.
AL137846 Genomic DNA. Translation: CAI10873.1.
CH471090 Genomic DNA. Translation: EAW87582.1.
CH471090 Genomic DNA. Translation: EAW87583.1.
BC000509 mRNA. Translation: AAH00509.1.
BC008414 mRNA. No translation available.
BC017116 mRNA. Translation: AAH17116.2.
CCDSiCCDS6855.1. [Q99436-1]
RefSeqiNP_002790.1. NM_002799.3.
UniGeneiHs.213470.

Genome annotation databases

EnsembliENST00000259457; ENSP00000259457; ENSG00000136930. [Q99436-1]
GeneIDi5695.
KEGGihsa:5695.
UCSCiuc004boj.4. human. [Q99436-1]

Polymorphism databases

DMDMi17380263.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D38048 mRNA. Translation: BAA07238.1 .
AK303460 mRNA. Translation: BAG64503.1 .
AL137846 Genomic DNA. Translation: CAI10873.1 .
CH471090 Genomic DNA. Translation: EAW87582.1 .
CH471090 Genomic DNA. Translation: EAW87583.1 .
BC000509 mRNA. Translation: AAH00509.1 .
BC008414 mRNA. No translation available.
BC017116 mRNA. Translation: AAH17116.2 .
CCDSi CCDS6855.1. [Q99436-1 ]
RefSeqi NP_002790.1. NM_002799.3.
UniGenei Hs.213470.

3D structure databases

ProteinModelPortali Q99436.
SMRi Q99436. Positions 44-263.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111668. 72 interactions.
IntActi Q99436. 25 interactions.
MINTi MINT-1351242.
STRINGi 9606.ENSP00000259457.

Chemistry

ChEMBLi CHEMBL2364701.

Protein family/group databases

MEROPSi T01.017.

PTM databases

PhosphoSitei Q99436.

Polymorphism databases

DMDMi 17380263.

Proteomic databases

MaxQBi Q99436.
PaxDbi Q99436.
PeptideAtlasi Q99436.
PRIDEi Q99436.

Protocols and materials databases

DNASUi 5695.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000259457 ; ENSP00000259457 ; ENSG00000136930 . [Q99436-1 ]
GeneIDi 5695.
KEGGi hsa:5695.
UCSCi uc004boj.4. human. [Q99436-1 ]

Organism-specific databases

CTDi 5695.
GeneCardsi GC09M127115.
HGNCi HGNC:9544. PSMB7.
HPAi HPA052408.
MIMi 604030. gene.
neXtProti NX_Q99436.
PharmGKBi PA33889.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00510000046533.
HOGENOMi HOG000182856.
HOVERGENi HBG093416.
InParanoidi Q99436.
KOi K02739.
OMAi QIWCAGA.
OrthoDBi EOG7CRTQJ.
PhylomeDBi Q99436.
TreeFami TF106222.

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 PSMB7. human.
GeneWikii PSMB7.
GenomeRNAii 5695.
NextBioi 22122.
PROi Q99436.
SOURCEi Search...

Gene expression databases

Bgeei Q99436.
CleanExi HS_PSMB7.
ExpressionAtlasi Q99436. baseline and differential.
Genevestigatori Q99436.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR024689. Proteasome_bsu_C.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF12465. Pr_beta_C. 1 hit.
PF00227. Proteasome. 1 hit.
[Graphical view ]
PRINTSi PR00141. PROTEASOME.
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Newly identified pair of proteasomal subunits regulated reciprocally by interferon gamma."
    Hisamatsu H., Shimbara N., Saito Y., Kristensen P., Hendil K.B., Fujiwara T., Takahashi E., Tanahashi N., Tamura T., Ichihara A., Tanaka K.
    J. Exp. Med. 183:1807-1816(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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 2).
    Tissue: Thymus.
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1), VARIANT ALA-39.
    Tissue: Lung, Urinary bladder and Uterus.
  6. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 165-184 AND 259-277, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  7. "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.
  8. "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.
  9. "Proteomic expression analysis of surgical human colorectal cancer tissues: up-regulation of PSB7, PRDX1, and SRP9 and hypoxic adaptation in cancer."
    Rho J.H., Qin S., Wang J.Y., Roehrl M.H.
    J. Proteome Res. 7:2959-2972(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPSB7_HUMAN
AccessioniPrimary (citable) accession number: Q99436
Secondary accession number(s): B4E0P1
, Q5TBG6, Q96AG8, Q9BWA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 1997
Last modified: October 29, 2014
This is version 149 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 9
    Human chromosome 9: 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