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Protein Page:
PSMD14 (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PSMD14 a component of the 26S proteasome. 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. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. Note: This description may include information from UniProtKB.
Protein type: Protease; Proteasome complex; EC 3.4.19.-
Chromosomal Location of Human Ortholog: 2q24.2
Cellular Component: cytosol; nucleoplasm; nucleus; proteasome complex
Molecular Function: metal ion binding; metallopeptidase activity; protein binding
Biological Process: 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; apoptosis; axon guidance; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; double-strand break repair via homologous recombination; double-strand break repair via nonhomologous end joining; epidermal growth factor 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; MAPKKK cascade; mitotic cell cycle; negative regulation of apoptosis; negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle; nerve growth factor receptor signaling pathway; polyamine metabolic process; positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle; programmed cell death; protein polyubiquitination; Ras protein signal transduction; regulation of amino acid metabolic process; regulation of apoptosis; regulation of mRNA stability; regulation of ubiquitin-protein ligase activity during mitotic cell cycle; response to ethanol; small GTPase mediated signal transduction; stimulatory C-type lectin receptor signaling pathway; T cell receptor signaling pathway; tumor necrosis factor-mediated signaling pathway; ubiquitin-dependent protein catabolic process; vascular endothelial growth factor receptor signaling pathway; viral reproduction
Reference #:  O00487 (UniProtKB)
Alt. Names/Synonyms: 26S proteasome non-ATPase regulatory subunit 14; 26S proteasome regulatory subunit rpn11; 26S proteasome-associated PAD1 homolog 1; PAD1; POH1; proteasome (prosome, macropain) 26S subunit, non-ATPase, 14; PSDE; PSMD14; RPN11
Gene Symbols: PSMD14
Molecular weight: 34,577 Da
Basal Isoelectric point: 6.06  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PSMD14

Protein Structure Not Found.


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Modification Sites and Domains  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 58 Y32‑p VDTAEQVyIsSLALL
0 1 S34‑p TAEQVyIsSLALLKM
0 4 K43‑ub LALLKMLkHGRAGVP
0 1 K94‑ub VDPVFQAkMLDMLKQ
0 1 S150‑p VVVDPIQsVkGkVVI
0 24 K152‑ub VDPIQsVkGkVVIDA
0 21 K154‑ub PIQsVkGkVVIDAFR
0 5 K186‑ub SNLGHLNkPSIQALI
0 2 K209‑ub SITINYRkNELEQkM
0 1 K215‑ub RkNELEQkMLLNLHk
0 3 K222‑ub kMLLNLHkksWMEGL
0 1 K223‑ub MLLNLHkksWMEGLT
0 3 S224‑p LLNLHkksWMEGLTL
0 1 Y234‑p EGLTLQDySEHCKHN
0 4 K246‑ub KHNESVVkEMLELAk
0 5 K253‑ub kEMLELAkNYNkAVE
0 11 K257‑ub ELAkNYNkAVEEEDk
0 2 K264 kAVEEEDKMtPEQLA
0 2 K264‑ub kAVEEEDkMtPEQLA
0 12 T266‑p VEEEDkMtPEQLAIk
0 3 K273‑ub tPEQLAIkNVGkQDP
0 2 K277‑ub LAIkNVGkQDPKRHL
  mouse

 
Y32‑p VDTAEQVyISSLALL
S34 TAEQVyISSLALLKM
K43 LALLKMLKHGRAGVP
K94 VDPVFQAKMLDMLKQ
S150 VVVDPIQSVkGKVVI
K152‑ub VDPIQSVkGKVVIDA
K154 PIQSVkGKVVIDAFR
K186 SNLGHLNKPSIQALI
K209 SITINYRKNELEQKM
K215 RKNELEQKMLLNLHK
K222 KMLLNLHKKSWMEGL
K223 MLLNLHKKSWMEGLT
S224 LLNLHKKSWMEGLTL
Y234 EGLTLQDYSEHCKHN
K246‑ub KHNESVVkEMLELAK
K253 kEMLELAKNYNkAVE
K257‑ub ELAKNYNkAVEEEDk
K264‑ac kAVEEEDkMTPEQLA
K264 kAVEEEDKMTPEQLA
T266 VEEEDkMTPEQLAIk
K273‑ub TPEQLAIkNVGKQDP
K277 LAIkNVGKQDPKRHL
  rat

 
Y32‑p VDTAEQVyISSLALL
S34 TAEQVyISSLALLKM
K43 LALLKMLKHGRAGVP
K94 VDPVFQAKMLDMLKQ
S150 VVVDPIQSVKGKVVI
K152 VDPIQSVKGKVVIDA
K154 PIQSVKGKVVIDAFR
K186 SNLGHLNKPSIQALI
K209 SITINYRKNELEQKM
K215 RKNELEQKMLLNLHK
K222 KMLLNLHKKSWMEGL
K223 MLLNLHKKSWMEGLT
S224 LLNLHKKSWMEGLTL
Y234 EGLTLQDYSEHCKHN
K246 KHNESVVKEMLELAK
K253 KEMLELAKNYNKAVE
K257 ELAKNYNKAVEEEDk
K264‑ac KAVEEEDkMTPEQLA
K264 KAVEEEDKMTPEQLA
T266 VEEEDkMTPEQLAIK
K273 TPEQLAIKNVGKQDP
K277 LAIKNVGKQDPKRHL
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