Proteasome subunit beta type-2

Details

Name
Proteasome subunit beta type-2
Synonyms
  • 3.4.25.1
  • Macropain subunit C7-I
  • Multicatalytic endopeptidase complex subunit C7-I
  • Proteasome component C7-I
Gene Name
PSMB2
Organism
Humans
Amino acid sequence
>lcl|BSEQ0016762|Proteasome subunit beta type-2
MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYI
QKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDY
LAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSV
RIIDKNGIHDLDNISFPKQGS
Number of residues
201
Molecular Weight
22836.02
Theoretical pI
7.04
GO Classification
Functions
endopeptidase activity / threonine-type endopeptidase activity
Processes
activation of MAPKK activity / anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process / antigen processing and presentation of exogenous peptide antigen via MHC class I / antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent / antigen processing and presentation of peptide antigen via MHC class I / apoptotic process / axon guidance / cellular nitrogen compound metabolic process / DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest / epidermal growth factor receptor signaling pathway / Fc-epsilon receptor signaling pathway / fibroblast growth factor receptor signaling pathway / G1/S transition of mitotic cell cycle / gene expression / innate immune response / insulin receptor signaling pathway / MAPK cascade / mitotic cell cycle / negative regulation of apoptotic process / negative regulation of canonical Wnt signaling pathway / negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle / neurotrophin TRK receptor signaling pathway / NIK/NF-kappaB signaling / polyamine metabolic process / positive regulation of canonical Wnt signaling pathway / positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition / programmed cell death / proteasomal ubiquitin-independent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / protein polyubiquitination / Ras protein signal transduction / regulation of apoptotic process / regulation of cellular amino acid metabolic process / regulation of mRNA stability / regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle / response to organic cyclic compound / small GTPase mediated signal transduction / small molecule metabolic process / stimulatory C-type lectin receptor signaling pathway / T cell receptor signaling pathway / tumor necrosis factor-mediated signaling pathway / vascular endothelial growth factor receptor signaling pathway / viral process
Components
cytoplasm / cytosol / extracellular exosome / membrane / nucleoplasm / nucleus / proteasome complex / proteasome core complex
General Function
Threonine-type endopeptidase activity
Specific Function
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 subunit has a trypsin-like activity.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0004612|606 bp
ATGGAGTACCTCATCGGTATCCAAGGCCCCGACTATGTTCTTGTCGCCTCCGACCGGGTG
GCCGCCAGCAATATTGTCCAGATGAAGGACGATCATGACAAGATGTTTAAGATGAGTGAA
AAGATATTACTCCTGTGTGTTGGAGAGGCTGGAGACACTGTACAGTTTGCAGAATATATT
CAGAAAAACGTGCAACTTTATAAGATGCGAAATGGATATGAATTGTCTCCCACGGCAGCA
GCTAACTTCACACGCCGAAACCTGGCTGACTGTCTTCGGAGTCGGACCCCATATCATGTG
AACCTCCTCCTGGCTGGCTATGATGAGCATGAAGGGCCAGCGCTGTATTACATGGACTAC
CTGGCAGCCTTGGCCAAGGCCCCTTTTGCAGCCCACGGCTATGGTGCCTTCCTGACTCTC
AGTATCCTCGACCGATACTACACACCGACTATCTCACGTGAGAGGGCAGTGGAACTCCTT
AGGAAATGTCTGGAGGAGCTCCAGAAACGCTTCATCCTGAATCTGCCAACCTTCAGTGTT
CGAATCATTGACAAAAATGGCATCCATGACCTGGATAACATTTCCTTCCCCAAACAGGGC
TCCTAA
Chromosome Location
Not Available
Locus
1p34.2
External Identifiers
ResourceLink
UniProtKB IDP49721
UniProtKB Entry NamePSB2_HUMAN
GenBank Protein ID565649
GenBank Gene IDD26599
GenAtlas IDPSMB2
HGNC IDHGNC:9539
General References
  1. Nothwang HG, Tamura T, Tanaka K, Ichihara A: Sequence analyses and inter-species comparisons of three novel human proteasomal subunits, HsN3, HsC7-I and HsC10-II, confine potential proteolytic active-site residues. Biochim Biophys Acta. 1994 Oct 18;1219(2):361-8. [Article]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [Article]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  4. Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. Electrophoresis. 1992 Dec;13(12):960-9. [Article]
  5. Kristensen P, Johnsen AH, Uerkvitz W, Tanaka K, Hendil KB: Human proteasome subunits from 2-dimensional gels identified by partial sequencing. Biochem Biophys Res Commun. 1994 Dec 30;205(3):1785-9. [Article]
  6. Apcher GS, Heink S, Zantopf D, Kloetzel PM, Schmid HP, Mayer RJ, Kruger E: Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits. FEBS Lett. 2003 Oct 9;553(1-2):200-4. [Article]
  7. Wang X, Chen CF, Baker PR, Chen PL, Kaiser P, Huang L: Mass spectrometric characterization of the affinity-purified human 26S proteasome complex. Biochemistry. 2007 Mar 20;46(11):3553-65. Epub 2007 Feb 27. [Article]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [Article]
  9. Wada T, Yamashita Y, Saga Y, Takahashi K, Koinuma K, Choi YL, Kaneda R, Fujiwara S, Soda M, Watanabe H, Kurashina K, Hatanaka H, Enomoto M, Takada S, Mano H, Suzuki M: Screening for genetic abnormalities involved in ovarian carcinogenesis using retroviral expression libraries. Int J Oncol. 2009 Nov;35(5):973-6. [Article]
  10. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [Article]
  11. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  12. Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, De Juan-Pardo E, Demeyer K, Hole K, Larrea E, Timmerman E, Prieto J, Arnesen T, Sherman F, Gevaert K, Aldabe R: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. Proc Natl Acad Sci U S A. 2012 Jul 31;109(31):12449-54. doi: 10.1073/pnas.1210303109. Epub 2012 Jul 18. [Article]
  13. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB08515(3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDEexperimentalunknownDetails
DB08889Carfilzomibapproved, investigationalyesinhibitorDetails