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PSD11_RAT
ID   PSD11_RAT               Reviewed;         422 AA.
AC   F1LMZ8;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 11;
DE   AltName: Full=26S proteasome regulatory subunit RPN6;
GN   Name=Psmd11;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC       involved in the ATP-dependent degradation of ubiquitinated proteins.
CC       This complex plays a key role in the maintenance of protein homeostasis
CC       by removing misfolded or damaged proteins, which could impair cellular
CC       functions, and by removing proteins whose functions are no longer
CC       required. Therefore, the proteasome participates in numerous cellular
CC       processes, including cell cycle progression, apoptosis, or DNA damage
CC       repair. In the complex, PSMD11 is required for proteasome assembly.
CC       Plays a key role in increased proteasome activity in embryonic stem
CC       cells (ESCs): its high expression in ESCs promotes enhanced assembly of
CC       the 26S proteasome, followed by higher proteasome activity.
CC       {ECO:0000250|UniProtKB:O00231}.
CC   -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC       The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC       regulatory subunits (RP). The regulatory particle is made of a lid
CC       composed of 9 subunits including PSMD11, a base containing 6 ATPases
CC       and few additional components. {ECO:0000250|UniProtKB:O00231}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated by AMPK. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S9 family. {ECO:0000305}.
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DR   PDB; 6EPC; EM; 12.30 A; Q=1-422.
DR   PDB; 6EPD; EM; 15.40 A; Q=1-422.
DR   PDB; 6EPE; EM; 12.80 A; Q=1-422.
DR   PDB; 6EPF; EM; 11.80 A; Q=1-422.
DR   PDBsum; 6EPC; -.
DR   PDBsum; 6EPD; -.
DR   PDBsum; 6EPE; -.
DR   PDBsum; 6EPF; -.
DR   AlphaFoldDB; F1LMZ8; -.
DR   SMR; F1LMZ8; -.
DR   IntAct; F1LMZ8; 3.
DR   STRING; 10116.ENSRNOP00000062146; -.
DR   iPTMnet; F1LMZ8; -.
DR   jPOST; F1LMZ8; -.
DR   PaxDb; F1LMZ8; -.
DR   PRIDE; F1LMZ8; -.
DR   RGD; 1306450; Psmd11.
DR   eggNOG; KOG1463; Eukaryota.
DR   InParanoid; F1LMZ8; -.
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-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-6798695; Neutrophil degranulation.
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:F1LMZ8; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR   GO; GO:0000502; C:proteasome complex; ISO:RGD.
DR   GO; GO:0005838; C:proteasome regulatory particle; ISO:RGD.
DR   GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR   GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR   GO; GO:0043248; P:proteasome assembly; ISS:UniProtKB.
DR   GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR035295; PSMD11.
DR   InterPro; IPR040780; Rpn6_C_helix.
DR   InterPro; IPR040773; Rpn6_N.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10678:SF6; PTHR10678:SF6; 1.
DR   Pfam; PF01399; PCI; 1.
DR   Pfam; PF18503; RPN6_C_helix; 1.
DR   Pfam; PF18055; RPN6_N; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Proteasome; Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O00231"
FT   CHAIN           2..422
FT                   /note="26S proteasome non-ATPase regulatory subunit 11"
FT                   /id="PRO_0000419978"
FT   DOMAIN          224..392
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O00231"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00231"
FT   CROSSLNK        274
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O00231"
SQ   SEQUENCE   422 AA;  47464 MW;  CE113054CBEBDB05 CRC64;
     MAAAAVVEFQ RAQSLLSTDR EASIDILHSI VKRDIQENDE EAVQVKEQSI LELGSLLAKT
     GQAAELGGLL KYVRPFLNSI SKAKAARLVR SLLDLFLDME AATGQEVELC LECIEWAKSE
     KRTFLRQALE ARLVSLYFDT KRYQEALHLG SQLLRELKKM DDKALLVEVQ LLESKTYHAL
     SNLPKARAAL TSARTTANAI YCPPKLQATL DMQSGIIHAA EEKDWKTAYS YFYEAFEGYD
     SIDSPKAITS LKYMLLCKIM LNTPEDVQAL VSGKLALRYA GRQTEALKCV AQASKNRSLA
     DFEKALTDYR AELRDDPIIS THLAKLYDNL LEQNLIRVIE PFSRVQIEHI SSLIKLSKAD
     VERKLSQMIL DKKFHGILDQ GEGVLIIFDE PPVDKTYEAA LETIQNMSKV VDSLYNKAKK
     LT
 
 
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