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Database: UniProt
Entry: PSD10_RAT
LinkDB: PSD10_RAT
Original site: PSD10_RAT 
ID   PSD10_RAT               Reviewed;         231 AA.
AC   Q9Z2X3;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 10;
DE   AltName: Full=26S proteasome regulatory subunit p28;
DE   AltName: Full=Gankyrin;
GN   Name=Psmd10;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Placenta;
RA   Higashitsuji H., Fujita J.;
RT   "Cloning of rat gankyrin homologue containing ankyrin repeats.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a chaperone during the assembly of the 26S
CC       proteasome, specifically of the PA700/19S regulatory complex (RC). In
CC       the initial step of the base subcomplex assembly is part of an
CC       intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles
CC       with a PSMD5:PSMC2:PSMC1:PSMD2 module (By similarity). Independently of
CC       the proteasome, regulates EGF-induced AKT activation through inhibition
CC       of the RHOA/ROCK/PTEN pathway, leading to prolonged AKT activation.
CC       Plays an important role in RAS-induced tumorigenesis (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: Acts as an oncoprotein by being involved in negative
CC       regulation of tumor suppressors RB1 and p53/TP53. Overexpression is
CC       leading to phosphorylation of RB1 and proteasomal degradation of RB1.
CC       Regulates CDK4-mediated phosphorylation of RB1 by competing with CDKN2A
CC       for binding with CDK4. Facilitates binding of MDM2 to p53/TP53 and the
CC       mono- and polyubiquitination of p53/TP53 by MDM2 suggesting a function
CC       in targeting the TP53:MDM2 complex to the 26S proteasome. Involved in
CC       p53-independent apoptosis. Involved in regulation of NF-kappa-B by
CC       retaining it in the cytoplasm. Binds to the NF-kappa-B component RELA
CC       and accelerates its XPO1/CRM1-mediated nuclear export (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Part of transient complex containing PSMD10, PSMC4, PSMC5 and
CC       PAAF1 formed during the assembly of the 26S proteasome. Stays
CC       associated throughout the assembly of the PA700/19S RC and is released
CC       upon association with the 20S core. Interacts with PSMC4. Interacts
CC       with RB1. Interacts with CDK4. Interacts with MDM2. Interacts with
CC       RELA. Associates with a CDK4:CCND2 serine/threonine kinase complex (By
CC       similarity). Interacts with ARHGDIA and increases the interaction
CC       between ARHGDIA and RHOA, hence promotes ARHGDIA inactivation of RHOA
CC       and ROCK (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
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DR   EMBL; AB022014; BAA36954.1; -; mRNA.
DR   RefSeq; NP_446377.1; NM_053925.1.
DR   AlphaFoldDB; Q9Z2X3; -.
DR   SMR; Q9Z2X3; -.
DR   BioGRID; 250589; 1.
DR   STRING; 10116.ENSRNOP00000071060; -.
DR   PhosphoSitePlus; Q9Z2X3; -.
DR   jPOST; Q9Z2X3; -.
DR   GeneID; 116722; -.
DR   KEGG; rno:116722; -.
DR   AGR; RGD:620350; -.
DR   CTD; 5716; -.
DR   RGD; 620350; Psmd10.
DR   InParanoid; Q9Z2X3; -.
DR   OrthoDB; 2543462at2759; -.
DR   PhylomeDB; Q9Z2X3; -.
DR   Reactome; R-RNO-1169091; Activation of NF-kappaB in B cells.
DR   Reactome; R-RNO-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-RNO-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-RNO-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-RNO-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; R-RNO-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-RNO-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-RNO-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-RNO-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-RNO-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR   Reactome; R-RNO-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-RNO-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR   Reactome; R-RNO-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-RNO-4608870; Asymmetric localization of PCP proteins.
DR   Reactome; R-RNO-4641257; Degradation of AXIN.
DR   Reactome; R-RNO-4641258; Degradation of DVL.
DR   Reactome; R-RNO-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-RNO-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR   Reactome; R-RNO-5610780; Degradation of GLI1 by the proteasome.
DR   Reactome; R-RNO-5610785; GLI3 is processed to GLI3R by the proteasome.
DR   Reactome; R-RNO-5632684; Hedgehog 'on' state.
DR   Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
DR   Reactome; R-RNO-5668541; TNFR2 non-canonical NF-kB pathway.
DR   Reactome; R-RNO-5676590; NIK-->noncanonical NF-kB signaling.
DR   Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-RNO-5689603; UCH proteinases.
DR   Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR   Reactome; R-RNO-68867; Assembly of the pre-replicative complex.
DR   Reactome; R-RNO-68949; Orc1 removal from chromatin.
DR   Reactome; R-RNO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-RNO-69481; G2/M Checkpoints.
DR   Reactome; R-RNO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-RNO-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR   Reactome; R-RNO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-RNO-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-RNO-8941858; Regulation of RUNX3 expression and activity.
DR   Reactome; R-RNO-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-RNO-8951664; Neddylation.
DR   Reactome; R-RNO-9755511; KEAP1-NFE2L2 pathway.
DR   Reactome; R-RNO-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR   Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:Q9Z2X3; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0000502; C:proteasome complex; ISO:RGD.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; ISO:RGD.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IBA:GO_Central.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IBA:GO_Central.
DR   GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0043409; P:negative regulation of MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0070682; P:proteasome regulatory particle assembly; ISS:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   PANTHER; PTHR24171; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 1.
DR   PANTHER; PTHR24171:SF9; L-ASPARAGINASE; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 5.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
PE   2: Evidence at transcript level;
KW   ANK repeat; Apoptosis; Chaperone; Cytoplasm; Nucleus; Reference proteome;
KW   Repeat.
FT   CHAIN           1..231
FT                   /note="26S proteasome non-ATPase regulatory subunit 10"
FT                   /id="PRO_0000067047"
FT   REPEAT          3..36
FT                   /note="ANK 1"
FT   REPEAT          37..69
FT                   /note="ANK 2"
FT   REPEAT          70..102
FT                   /note="ANK 3"
FT   REPEAT          103..135
FT                   /note="ANK 4"
FT   REPEAT          136..168
FT                   /note="ANK 5"
FT   REPEAT          169..201
FT                   /note="ANK 6"
FT   REPEAT          202..226
FT                   /note="ANK 7"
SQ   SEQUENCE   231 AA;  24985 MW;  F5241DC9A816066E CRC64;
     MEGCVSNLMV CNLAYNGKLD ELKESILADK SLATRTDQDS RTALHWACSA GHTEIVEFLL
     QLGVPVNEKD DAGWSPLHIA ASAGRDEIVK ALLIKGAQVN AVNQNGCTAL HYAASKNRHE
     IAVMLLEGGA NPDAKNHYDA TAMHRAAAKG NLKMVHILLF YKASTNIQDT EGNTPLHLAC
     DEERVEEAKL LVTQGASIYI ENKEEKTPLQ VAKGGLGLIL KRIAESEEAS M
//
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