位置:首页 > 蛋白库 > PSMD1_PONAB
PSMD1_PONAB
ID   PSMD1_PONAB             Reviewed;         953 AA.
AC   Q5R5S4;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 1;
DE   AltName: Full=26S proteasome regulatory subunit RPN2;
DE   AltName: Full=26S proteasome regulatory subunit S1;
GN   Name=PSMD1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250|UniProtKB:Q99460}.
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, a base containing 6 ATPases and few additional
CC       components including PSMD1. Interacts with ADRM1. Interacts with ZFAND1
CC       (By similarity). {ECO:0000250|UniProtKB:Q99460}.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR860782; CAH92892.1; -; mRNA.
DR   RefSeq; NP_001126695.1; NM_001133223.1.
DR   AlphaFoldDB; Q5R5S4; -.
DR   SMR; Q5R5S4; -.
DR   STRING; 9601.ENSPPYP00000014825; -.
DR   PRIDE; Q5R5S4; -.
DR   Ensembl; ENSPPYT00000015422; ENSPPYP00000014825; ENSPPYG00000013261.
DR   GeneID; 100173695; -.
DR   KEGG; pon:100173695; -.
DR   CTD; 5707; -.
DR   eggNOG; KOG2062; Eukaryota.
DR   GeneTree; ENSGT00940000153386; -.
DR   HOGENOM; CLU_002323_0_0_1; -.
DR   InParanoid; Q5R5S4; -.
DR   OMA; MIMVQQN; -.
DR   OrthoDB; 235012at2759; -.
DR   TreeFam; TF105742; -.
DR   Proteomes; UP000001595; Chromosome 2B.
DR   GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR016642; 26S_Psome_Rpn2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR   InterPro; IPR035266; PSMD1.
DR   InterPro; IPR040623; RPN2_C.
DR   PANTHER; PTHR10943:SF2; PTHR10943:SF2; 1.
DR   Pfam; PF01851; PC_rep; 3.
DR   Pfam; PF18004; RPN2_C; 1.
DR   PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Phosphoprotein; Proteasome; Reference proteome; Repeat.
FT   CHAIN           1..953
FT                   /note="26S proteasome non-ATPase regulatory subunit 1"
FT                   /id="PRO_0000312650"
FT   REPEAT          403..436
FT                   /note="PC 1"
FT   REPEAT          441..474
FT                   /note="PC 2"
FT   REPEAT          476..510
FT                   /note="PC 3"
FT   REPEAT          511..545
FT                   /note="PC 4"
FT   REPEAT          547..580
FT                   /note="PC 5"
FT   REPEAT          581..616
FT                   /note="PC 6"
FT   REPEAT          617..649
FT                   /note="PC 7"
FT   REPEAT          651..685
FT                   /note="PC 8"
FT   REPEAT          686..726
FT                   /note="PC 9"
FT   REPEAT          729..761
FT                   /note="PC 10"
FT   REGION          279..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          839..881
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          930..953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..874
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        939..953
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine; partial"
FT                   /evidence="ECO:0000250|UniProtKB:Q99460"
FT   MOD_RES         273
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99460"
FT   MOD_RES         290
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99460"
FT   MOD_RES         310
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99460"
FT   MOD_RES         311
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99460"
FT   MOD_RES         315
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99460"
FT   MOD_RES         720
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3TXS7"
FT   MOD_RES         830
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99460"
FT   MOD_RES         834
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99460"
SQ   SEQUENCE   953 AA;  105806 MW;  14613DCF6CA9E5FD CRC64;
     MITSAAGIIS LLDEDEPQLK EFALHKLNAV VNDFWAEISE SVDKIEVLYE DEGFRSRQFA
     ALVASKVFYH LGAFEESLNY ALGAGDLFNV NDNSEYVETI IAKCIDHYTK QCVENADLPE
     GEKKPIDQRL EGIVNKMFQR CLDDHKYKQA IGIALETRRL DVFEKTILES NDVPGMLAYS
     LKLCMSLMQN KQFRNKVLRV LVKIYMNLEK PDFINVCQCL IFLDDPQAVS DILEKLVKED
     NLLMAYQICF DLYESASQQF LSSVIQNLRT VGTPIASVPG STNTGTVPGS EKDSDSMETE
     EKTGSAFVGK TPEASPEPKD QTLKMIKILS GEMAIELHLQ FLIRNNNTDL MILKNTKDAV
     RNSVCHTATV IANSFMHCGT TSDQFLRDNL EWLARATNWA KFTATASLGV IHKGHEKEAL
     QLMATYLPKD TSPGSAYQEG GGLYALGLIH ANHGGDIIDY LLNQLKNASN DIVRHGGSLG
     LGLAAMGTAR QDVYDLLKTN LYQDDAVTGE AAGLALGLVM LGSKNAQAIE DMVGYAQETQ
     HEKILRGLAV GIALVMYGRM EEADALIESL CRDKDPILRR SGMYTVAMAY CGSGNNKAIR
     RLLHVAVSDV NDDVRRAAVE SLGFILFRTP EQCPSVVSLL SESYNPHVRY GAAMALGICC
     AGTGNKEAIN LLEPMTNDPV NYVRQGALIA SALIMIQQTE ITCPKVNQFR QLYSKVINDK
     HDDVMAKFGA ILAQGILDAG GHNVTISLQS RTGHTHMPSV VGVLVFTQFW FWFPLSHFLS
     LAYTPTCVIG LNKDLKMPKV QYKSNCKPST FAYPAPLEVP KEKEKEKVST AVLSITAKAK
     KKEKEKEKKE EEKMEVDEAE KKEEKEKKKE PEPNFQLLDN PARVMPAQLK VLTMPETCRY
     QPFKPLSIGG IIILKDTSED IEELVEPVAA HGPKIEEEEQ EPEPPEPFEY IDD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024