Full text data of PSMD5
PSMD5
(KIAA0072)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
26S proteasome non-ATPase regulatory subunit 5 (26S protease subunit S5 basic; 26S proteasome subunit S5B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
26S proteasome non-ATPase regulatory subunit 5 (26S protease subunit S5 basic; 26S proteasome subunit S5B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00002134
IPI00002134 Proteasome 26S non-ATPase subunit 5 Cleavage of peptide bonds with very broad specificity, proteasome: 15 subunits, C3 regulatory effect through tyrosine phosphorilation soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00002134 Proteasome 26S non-ATPase subunit 5 Cleavage of peptide bonds with very broad specificity, proteasome: 15 subunits, C3 regulatory effect through tyrosine phosphorilation soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q16401
ID PSMD5_HUMAN Reviewed; 504 AA.
AC Q16401; B4DZM8; Q15045; Q4VXG8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 5;
DE AltName: Full=26S protease subunit S5 basic;
DE AltName: Full=26S proteasome subunit S5B;
GN Name=PSMD5; Synonyms=KIAA0072;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 75-96;
RP 311-337 AND 431-449.
RC TISSUE=Mammary cancer;
RX PubMed=7559544; DOI=10.1074/jbc.270.40.23726;
RA Deveraux Q., Jensen C., Rechsteiner M.;
RT "Molecular cloning and expression of a 26 S protease subunit enriched
RT in dileucine repeats.";
RL J. Biol. Chem. 270:23726-23729(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S.,
RA Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II.
RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 2-10, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [9]
RP FUNCTION AS PROTEASOME CHAPERONE, SUBUNIT, AND INTERACTION WITH PSMC2.
RX PubMed=19490896; DOI=10.1016/j.cell.2009.05.008;
RA Kaneko T., Hamazaki J., Iemura S., Sasaki K., Furuyama K., Natsume T.,
RA Tanaka K., Murata S.;
RT "Assembly pathway of the Mammalian proteasome base subcomplex is
RT mediated by multiple specific chaperones.";
RL Cell 137:914-925(2009).
RN [10]
RP INTERACTION WITH PSMC1; PSMC2; PSMD1 AND PSMD6.
RX PubMed=19217412; DOI=10.1016/j.molcel.2009.01.010;
RA Le Tallec B., Barrault M.B., Guerois R., Carre T., Peyroche A.;
RT "Hsm3/S5b participates in the assembly pathway of the 19S regulatory
RT particle of the proteasome.";
RL Mol. Cell 33:389-399(2009).
RN [11]
RP FUNCTION AS PROTEASOME CHAPERONE, AND INTERACTION WITH PSMC2.
RX PubMed=19412159; DOI=10.1038/nature08063;
RA Roelofs J., Park S., Haas W., Tian G., McAllister F.E., Huo Y.,
RA Lee B.H., Zhang F., Shi Y., Gygi S.P., Finley D.;
RT "Chaperone-mediated pathway of proteasome regulatory particle
RT assembly.";
RL Nature 459:861-865(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Acts as a chaperone during the assembly of the 26S
CC proteasome, specifically of the base subcomplex of the PA700/19S
CC regulatory complex (RC). In the initial step of the base
CC subcomplex assembly is part of an intermediate
CC PSMD5:PSMC2:PSMC1:PSMD2 module which probably assembles with a
CC PSMD10:PSMC4:PSMC5:PAAF1 module followed by dissociation of PSMD5.
CC -!- SUBUNIT: Interacts with PSMC1, PSMC2, PSMD1 and PSMD6. Part of
CC transient complex containing PSMD5, PSMC2, PSMC1 and PSMD2 formed
CC during the assembly of the 26S proteasome.
CC -!- INTERACTION:
CC P35998:PSMC2; NbExp=5; IntAct=EBI-752143, EBI-359710;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16401-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16401-2; Sequence=VSP_045176;
CC -!- DOMAIN: Rich in dileucine repeats, which have been implicated in
CC trafficking of a variety of transmembrane proteins.
CC -!- SIMILARITY: Belongs to the proteasome subunit S5B/HSM3 family.
CC -!- CAUTION: Was initially identified as a genuine component of the
CC 26S proteasome.
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DR EMBL; S79862; AAB35397.1; -; mRNA.
DR EMBL; D31889; BAA06687.1; -; mRNA.
DR EMBL; AK303007; BAG64140.1; -; mRNA.
DR EMBL; AL161911; CAI95118.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87471.1; -; Genomic_DNA.
DR EMBL; BC014478; AAH14478.1; -; mRNA.
DR RefSeq; NP_001257356.1; NM_001270427.1.
DR RefSeq; NP_005038.1; NM_005047.3.
DR UniGene; Hs.193725; -.
DR ProteinModelPortal; Q16401; -.
DR IntAct; Q16401; 20.
DR MINT; MINT-5004744; -.
DR STRING; 9606.ENSP00000210313; -.
DR PhosphoSite; Q16401; -.
DR DMDM; 3122657; -.
DR PaxDb; Q16401; -.
DR PRIDE; Q16401; -.
DR DNASU; 5711; -.
DR Ensembl; ENST00000210313; ENSP00000210313; ENSG00000095261.
DR Ensembl; ENST00000373904; ENSP00000363011; ENSG00000095261.
DR GeneID; 5711; -.
DR KEGG; hsa:5711; -.
DR UCSC; uc011lye.3; human.
DR CTD; 5711; -.
DR GeneCards; GC09M123577; -.
DR HGNC; HGNC:9563; PSMD5.
DR HPA; HPA003216; -.
DR MIM; 604452; gene.
DR neXtProt; NX_Q16401; -.
DR PharmGKB; PA33909; -.
DR eggNOG; NOG245712; -.
DR HOGENOM; HOG000231963; -.
DR HOVERGEN; HBG053741; -.
DR InParanoid; Q16401; -.
DR KO; K06692; -.
DR OMA; FVEYVVD; -.
DR PhylomeDB; Q16401; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; PSMD5; -.
DR GenomeRNAi; 5711; -.
DR NextBio; 22190; -.
DR PRO; PR:Q16401; -.
DR ArrayExpress; Q16401; -.
DR Bgee; Q16401; -.
DR CleanEx; HS_PSMD5; -.
DR Genevestigator; Q16401; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0070682; P:proteasome regulatory particle assembly; TAS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IEA:GOC.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR019538; 26S_Psome_nonATP_su5.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR Pfam; PF10508; Proteasom_PSMB; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Complete proteome;
KW Direct protein sequencing; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 504 26S proteasome non-ATPase regulatory
FT subunit 5.
FT /FTId=PRO_0000173835.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 145 187 Missing (in isoform 2).
FT /FTId=VSP_045176.
FT VARIANT 21 21 E -> G (in dbSNP:rs2297575).
FT /FTId=VAR_051556.
FT VARIANT 72 72 L -> H (in dbSNP:rs17282618).
FT /FTId=VAR_051557.
SQ SEQUENCE 504 AA; 56196 MW; 30F31602DDF4EF89 CRC64;
MAAQALALLR EVARLEAPLE ELRALHSVLQ AVPLNELRQQ AAELRLGPLF SLLNENHREK
TTLCVSILER LLQAMEPVHV ARNLRVDLQR GLIHPDDSVK ILTLSQIGRI VENSDAVTEI
LNNAELLKQI VYCIGGENLS VAKAAIKSLS RISLTQAGLE ALFESNLLDD LKSVMKTNDI
VRYRVYELII EISSVSPESL NYCTTSGLVT QLLRELTGED VLVRATCIEM VTSLAYTHHG
RQYLAQEGVI DQISNIIVGA DSDPFSSFYL PGFVKFFGNL AVMDSPQQIC ERYPIFVEKV
FEMIESQDPT MIGVAVDTVG ILGSNVEGKQ VLQKTGTRFE RLLMRIGHQS KNAPVELKIR
CLDAISSLLY LPPEQQTDDL LRMTESWFSS LSRDPLELFR GISSQPFPEL HCAALKVFTA
IANQPWAQKL MFNSPGFVEY VVDRSVEHDK ASKDAKYELV KALANSKTIA EIFGNPNYLR
LRTYLSEGPY YVKPVSTTAV EGAE
//
ID PSMD5_HUMAN Reviewed; 504 AA.
AC Q16401; B4DZM8; Q15045; Q4VXG8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 5;
DE AltName: Full=26S protease subunit S5 basic;
DE AltName: Full=26S proteasome subunit S5B;
GN Name=PSMD5; Synonyms=KIAA0072;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 75-96;
RP 311-337 AND 431-449.
RC TISSUE=Mammary cancer;
RX PubMed=7559544; DOI=10.1074/jbc.270.40.23726;
RA Deveraux Q., Jensen C., Rechsteiner M.;
RT "Molecular cloning and expression of a 26 S protease subunit enriched
RT in dileucine repeats.";
RL J. Biol. Chem. 270:23726-23729(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S.,
RA Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II.
RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 2-10, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [9]
RP FUNCTION AS PROTEASOME CHAPERONE, SUBUNIT, AND INTERACTION WITH PSMC2.
RX PubMed=19490896; DOI=10.1016/j.cell.2009.05.008;
RA Kaneko T., Hamazaki J., Iemura S., Sasaki K., Furuyama K., Natsume T.,
RA Tanaka K., Murata S.;
RT "Assembly pathway of the Mammalian proteasome base subcomplex is
RT mediated by multiple specific chaperones.";
RL Cell 137:914-925(2009).
RN [10]
RP INTERACTION WITH PSMC1; PSMC2; PSMD1 AND PSMD6.
RX PubMed=19217412; DOI=10.1016/j.molcel.2009.01.010;
RA Le Tallec B., Barrault M.B., Guerois R., Carre T., Peyroche A.;
RT "Hsm3/S5b participates in the assembly pathway of the 19S regulatory
RT particle of the proteasome.";
RL Mol. Cell 33:389-399(2009).
RN [11]
RP FUNCTION AS PROTEASOME CHAPERONE, AND INTERACTION WITH PSMC2.
RX PubMed=19412159; DOI=10.1038/nature08063;
RA Roelofs J., Park S., Haas W., Tian G., McAllister F.E., Huo Y.,
RA Lee B.H., Zhang F., Shi Y., Gygi S.P., Finley D.;
RT "Chaperone-mediated pathway of proteasome regulatory particle
RT assembly.";
RL Nature 459:861-865(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Acts as a chaperone during the assembly of the 26S
CC proteasome, specifically of the base subcomplex of the PA700/19S
CC regulatory complex (RC). In the initial step of the base
CC subcomplex assembly is part of an intermediate
CC PSMD5:PSMC2:PSMC1:PSMD2 module which probably assembles with a
CC PSMD10:PSMC4:PSMC5:PAAF1 module followed by dissociation of PSMD5.
CC -!- SUBUNIT: Interacts with PSMC1, PSMC2, PSMD1 and PSMD6. Part of
CC transient complex containing PSMD5, PSMC2, PSMC1 and PSMD2 formed
CC during the assembly of the 26S proteasome.
CC -!- INTERACTION:
CC P35998:PSMC2; NbExp=5; IntAct=EBI-752143, EBI-359710;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16401-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16401-2; Sequence=VSP_045176;
CC -!- DOMAIN: Rich in dileucine repeats, which have been implicated in
CC trafficking of a variety of transmembrane proteins.
CC -!- SIMILARITY: Belongs to the proteasome subunit S5B/HSM3 family.
CC -!- CAUTION: Was initially identified as a genuine component of the
CC 26S proteasome.
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DR EMBL; S79862; AAB35397.1; -; mRNA.
DR EMBL; D31889; BAA06687.1; -; mRNA.
DR EMBL; AK303007; BAG64140.1; -; mRNA.
DR EMBL; AL161911; CAI95118.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87471.1; -; Genomic_DNA.
DR EMBL; BC014478; AAH14478.1; -; mRNA.
DR RefSeq; NP_001257356.1; NM_001270427.1.
DR RefSeq; NP_005038.1; NM_005047.3.
DR UniGene; Hs.193725; -.
DR ProteinModelPortal; Q16401; -.
DR IntAct; Q16401; 20.
DR MINT; MINT-5004744; -.
DR STRING; 9606.ENSP00000210313; -.
DR PhosphoSite; Q16401; -.
DR DMDM; 3122657; -.
DR PaxDb; Q16401; -.
DR PRIDE; Q16401; -.
DR DNASU; 5711; -.
DR Ensembl; ENST00000210313; ENSP00000210313; ENSG00000095261.
DR Ensembl; ENST00000373904; ENSP00000363011; ENSG00000095261.
DR GeneID; 5711; -.
DR KEGG; hsa:5711; -.
DR UCSC; uc011lye.3; human.
DR CTD; 5711; -.
DR GeneCards; GC09M123577; -.
DR HGNC; HGNC:9563; PSMD5.
DR HPA; HPA003216; -.
DR MIM; 604452; gene.
DR neXtProt; NX_Q16401; -.
DR PharmGKB; PA33909; -.
DR eggNOG; NOG245712; -.
DR HOGENOM; HOG000231963; -.
DR HOVERGEN; HBG053741; -.
DR InParanoid; Q16401; -.
DR KO; K06692; -.
DR OMA; FVEYVVD; -.
DR PhylomeDB; Q16401; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; PSMD5; -.
DR GenomeRNAi; 5711; -.
DR NextBio; 22190; -.
DR PRO; PR:Q16401; -.
DR ArrayExpress; Q16401; -.
DR Bgee; Q16401; -.
DR CleanEx; HS_PSMD5; -.
DR Genevestigator; Q16401; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0070682; P:proteasome regulatory particle assembly; TAS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IEA:GOC.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR019538; 26S_Psome_nonATP_su5.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR Pfam; PF10508; Proteasom_PSMB; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Complete proteome;
KW Direct protein sequencing; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 504 26S proteasome non-ATPase regulatory
FT subunit 5.
FT /FTId=PRO_0000173835.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 145 187 Missing (in isoform 2).
FT /FTId=VSP_045176.
FT VARIANT 21 21 E -> G (in dbSNP:rs2297575).
FT /FTId=VAR_051556.
FT VARIANT 72 72 L -> H (in dbSNP:rs17282618).
FT /FTId=VAR_051557.
SQ SEQUENCE 504 AA; 56196 MW; 30F31602DDF4EF89 CRC64;
MAAQALALLR EVARLEAPLE ELRALHSVLQ AVPLNELRQQ AAELRLGPLF SLLNENHREK
TTLCVSILER LLQAMEPVHV ARNLRVDLQR GLIHPDDSVK ILTLSQIGRI VENSDAVTEI
LNNAELLKQI VYCIGGENLS VAKAAIKSLS RISLTQAGLE ALFESNLLDD LKSVMKTNDI
VRYRVYELII EISSVSPESL NYCTTSGLVT QLLRELTGED VLVRATCIEM VTSLAYTHHG
RQYLAQEGVI DQISNIIVGA DSDPFSSFYL PGFVKFFGNL AVMDSPQQIC ERYPIFVEKV
FEMIESQDPT MIGVAVDTVG ILGSNVEGKQ VLQKTGTRFE RLLMRIGHQS KNAPVELKIR
CLDAISSLLY LPPEQQTDDL LRMTESWFSS LSRDPLELFR GISSQPFPEL HCAALKVFTA
IANQPWAQKL MFNSPGFVEY VVDRSVEHDK ASKDAKYELV KALANSKTIA EIFGNPNYLR
LRTYLSEGPY YVKPVSTTAV EGAE
//
MIM
604452
*RECORD*
*FIELD* NO
604452
*FIELD* TI
*604452 PROTEASOME 26S SUBUNIT, NON-ATPase, 5; PSMD5
;;PROTEASE 26S, SUBUNIT 5B; S5B
read more*FIELD* TX
The covalent attachment of ubiquitin to proteins produces substrates for
the 26S ATP-dependent protease. This enzyme is composed of the
multicatalytic protease, or proteasome, and a regulatory ATPase complex.
Both the multicatalytic protease and the regulatory complex are
multisubunit structures that associate in the presence of ATP to form
the 26S enzyme. Deveraux et al. (1994) identified a 50-kD subunit of the
regulatory complex, which they called subunit 5 (S5) based upon its
relative mobility on SDS-polyacrylamide gels. Deveraux et al. (1995)
demonstrated that 2 distinct subunits of the 26S protease migrate as
50-kD proteins, and thus, S5 represents 2 proteins, which the authors
termed S5A (PSMD4; 601648) and S5B, also called PSMD5. Deveraux et al.
(1995) sequenced peptides from the PSMD5 subunit of the human red blood
cell 26S protease. Using the amino acid sequence, they isolated human
cDNAs comprising a full-length PSMD5 cDNA. The deduced 505-amino acid
PSMD5 protein is enriched in leucine residues, particularly in the
N-terminal region. PSMD5 contains 9 dileucine repeats and a sequence,
NPNY, similar to the tyrosine-based motifs. Dileucine repeats and
tyrosine-based motifs are thought to contribute to internalization
and/or targeting. PSMD5 has a calculated molecular mass of 56 kD and
focuses at pH 5.3 on 2-dimensional gels. Recombinant PSMD5 did not bind
to ubiquitin polymers.
By sequencing cDNAs randomly selected from a cDNA library derived from a
human immature myeloid cell line, Nomura et al. (1994) isolated a
partial cDNA encoding PSMD5, which they called KIAA0072. Northern blot
analysis detected PSMD5 expression in a wide variety of human tissues,
with the highest expression in lung and skeletal muscle. Deveraux et al.
(1995) noted that the nucleotide sequence of the KIAA0072 cDNA is
identical to the corresponding nucleotide sequence of the S5B cDNA.
Using somatic cell hybrid analysis, Nomura et al. (1994) mapped the
PSMD5 gene to chromosome 9.
*FIELD* RF
1. Deveraux, Q.; Jensen, C.; Rechsteiner, M.: Molecular cloning and
expression of a 26 S protease subunit enriched in dileucine repeats. J.
Biol. Chem. 270: 23726-23729, 1995.
2. Deveraux, Q.; Ustrell, V.; Pickart, C.; Rechsteiner, M.: A 26
S protease subunit that binds ubiquitin conjugates. J. Biol. Chem. 269:
7059-7061, 1994.
3. Nomura, N.; Nagase, T.; Miyajima, N.; Sazuka, T.; Tanaka, A.; Sato,
S.; Seki, N.; Kawarabayasi, Y.; Ishikawa, K.; Tabata, S.: Prediction
of the coding sequences of unidentified human genes. II. The coding
sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis
of cDNA clones from human cell line KG-1. DNA Res. 1: 223-229, 1994.
*FIELD* CD
Patti M. Sherman: 1/20/2000
*FIELD* ED
mgross: 01/24/2000
psherman: 1/21/2000
*RECORD*
*FIELD* NO
604452
*FIELD* TI
*604452 PROTEASOME 26S SUBUNIT, NON-ATPase, 5; PSMD5
;;PROTEASE 26S, SUBUNIT 5B; S5B
read more*FIELD* TX
The covalent attachment of ubiquitin to proteins produces substrates for
the 26S ATP-dependent protease. This enzyme is composed of the
multicatalytic protease, or proteasome, and a regulatory ATPase complex.
Both the multicatalytic protease and the regulatory complex are
multisubunit structures that associate in the presence of ATP to form
the 26S enzyme. Deveraux et al. (1994) identified a 50-kD subunit of the
regulatory complex, which they called subunit 5 (S5) based upon its
relative mobility on SDS-polyacrylamide gels. Deveraux et al. (1995)
demonstrated that 2 distinct subunits of the 26S protease migrate as
50-kD proteins, and thus, S5 represents 2 proteins, which the authors
termed S5A (PSMD4; 601648) and S5B, also called PSMD5. Deveraux et al.
(1995) sequenced peptides from the PSMD5 subunit of the human red blood
cell 26S protease. Using the amino acid sequence, they isolated human
cDNAs comprising a full-length PSMD5 cDNA. The deduced 505-amino acid
PSMD5 protein is enriched in leucine residues, particularly in the
N-terminal region. PSMD5 contains 9 dileucine repeats and a sequence,
NPNY, similar to the tyrosine-based motifs. Dileucine repeats and
tyrosine-based motifs are thought to contribute to internalization
and/or targeting. PSMD5 has a calculated molecular mass of 56 kD and
focuses at pH 5.3 on 2-dimensional gels. Recombinant PSMD5 did not bind
to ubiquitin polymers.
By sequencing cDNAs randomly selected from a cDNA library derived from a
human immature myeloid cell line, Nomura et al. (1994) isolated a
partial cDNA encoding PSMD5, which they called KIAA0072. Northern blot
analysis detected PSMD5 expression in a wide variety of human tissues,
with the highest expression in lung and skeletal muscle. Deveraux et al.
(1995) noted that the nucleotide sequence of the KIAA0072 cDNA is
identical to the corresponding nucleotide sequence of the S5B cDNA.
Using somatic cell hybrid analysis, Nomura et al. (1994) mapped the
PSMD5 gene to chromosome 9.
*FIELD* RF
1. Deveraux, Q.; Jensen, C.; Rechsteiner, M.: Molecular cloning and
expression of a 26 S protease subunit enriched in dileucine repeats. J.
Biol. Chem. 270: 23726-23729, 1995.
2. Deveraux, Q.; Ustrell, V.; Pickart, C.; Rechsteiner, M.: A 26
S protease subunit that binds ubiquitin conjugates. J. Biol. Chem. 269:
7059-7061, 1994.
3. Nomura, N.; Nagase, T.; Miyajima, N.; Sazuka, T.; Tanaka, A.; Sato,
S.; Seki, N.; Kawarabayasi, Y.; Ishikawa, K.; Tabata, S.: Prediction
of the coding sequences of unidentified human genes. II. The coding
sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis
of cDNA clones from human cell line KG-1. DNA Res. 1: 223-229, 1994.
*FIELD* CD
Patti M. Sherman: 1/20/2000
*FIELD* ED
mgross: 01/24/2000
psherman: 1/21/2000