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Protein

26S proteasome non-ATPase regulatory subunit 5

Gene

PSMD5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD5:PSMC2:PSMC1:PSMD2 module which probably assembles with a PSMD10:PSMC4:PSMC5:PAAF1 module followed by dissociation of PSMD5.2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-350562. Regulation of ornithine decarboxylase (ODC).
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641257. Degradation of AXIN.
R-HSA-4641258. Degradation of DVL.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-5362768. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-HSA-69481. G2/M Checkpoints.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome non-ATPase regulatory subunit 5
Alternative name(s):
26S protease subunit S5 basic
26S proteasome subunit S5B
Gene namesi
Name:PSMD5
Synonyms:KIAA0072
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:9563. PSMD5.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • proteasome accessory complex Source: UniProtKB
  • proteasome complex Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33909.

Polymorphism and mutation databases

BioMutaiPSMD5.
DMDMi3122657.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources2 Publications
Chaini2 – 50450326S proteasome non-ATPase regulatory subunit 5PRO_0000173835Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ16401.
MaxQBiQ16401.
PaxDbiQ16401.
PeptideAtlasiQ16401.
PRIDEiQ16401.
TopDownProteomicsiQ16401-1. [Q16401-1]

PTM databases

iPTMnetiQ16401.
PhosphoSiteiQ16401.

Expressioni

Gene expression databases

BgeeiQ16401.
CleanExiHS_PSMD5.
ExpressionAtlasiQ16401. baseline and differential.
GenevisibleiQ16401. HS.

Organism-specific databases

HPAiHPA003216.

Interactioni

Subunit structurei

Interacts with PSMC1, PSMC2, PSMD1 and PSMD6. Part of transient complex containing PSMD5, PSMC2, PSMC1 and PSMD2 formed during the assembly of the 26S proteasome.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PSMC1P621917EBI-752143,EBI-357598
PSMC2P3599810EBI-752143,EBI-359710
TFCP2Q128003EBI-752143,EBI-717422

Protein-protein interaction databases

BioGridi111684. 85 interactions.
IntActiQ16401. 37 interactions.
MINTiMINT-5004744.
STRINGi9606.ENSP00000210313.

Structurei

3D structure databases

ProteinModelPortaliQ16401.
SMRiQ16401. Positions 209-234, 295-323.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Rich in dileucine repeats, which have been implicated in trafficking of a variety of transmembrane proteins.

Sequence similaritiesi

Belongs to the proteasome subunit S5B/HSM3 family.Curated

Phylogenomic databases

eggNOGiKOG4413. Eukaryota.
ENOG410XTFA. LUCA.
GeneTreeiENSGT00390000013040.
HOGENOMiHOG000231963.
HOVERGENiHBG053741.
InParanoidiQ16401.
KOiK06692.
OMAiFVEYVVD.
PhylomeDBiQ16401.
TreeFamiTF106231.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR019538. 26S_Psome_nonATP_su5.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
[Graphical view]
PfamiPF10508. Proteasom_PSMB. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q16401-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAQALALLR EVARLEAPLE ELRALHSVLQ AVPLNELRQQ AAELRLGPLF
60 70 80 90 100
SLLNENHREK TTLCVSILER LLQAMEPVHV ARNLRVDLQR GLIHPDDSVK
110 120 130 140 150
ILTLSQIGRI VENSDAVTEI LNNAELLKQI VYCIGGENLS VAKAAIKSLS
160 170 180 190 200
RISLTQAGLE ALFESNLLDD LKSVMKTNDI VRYRVYELII EISSVSPESL
210 220 230 240 250
NYCTTSGLVT QLLRELTGED VLVRATCIEM VTSLAYTHHG RQYLAQEGVI
260 270 280 290 300
DQISNIIVGA DSDPFSSFYL PGFVKFFGNL AVMDSPQQIC ERYPIFVEKV
310 320 330 340 350
FEMIESQDPT MIGVAVDTVG ILGSNVEGKQ VLQKTGTRFE RLLMRIGHQS
360 370 380 390 400
KNAPVELKIR CLDAISSLLY LPPEQQTDDL LRMTESWFSS LSRDPLELFR
410 420 430 440 450
GISSQPFPEL HCAALKVFTA IANQPWAQKL MFNSPGFVEY VVDRSVEHDK
460 470 480 490 500
ASKDAKYELV KALANSKTIA EIFGNPNYLR LRTYLSEGPY YVKPVSTTAV

EGAE
Length:504
Mass (Da):56,196
Last modified:January 23, 2007 - v3
Checksum:i30F31602DDF4EF89
GO
Isoform 2 (identifier: Q16401-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     145-187: Missing.

Show »
Length:461
Mass (Da):51,312
Checksum:i4D817EA22EC9DA9E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211E → G.
Corresponds to variant rs2297575 [ dbSNP | Ensembl ].
VAR_051556
Natural varianti72 – 721L → H.
Corresponds to variant rs17282618 [ dbSNP | Ensembl ].
VAR_051557

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei145 – 18743Missing in isoform 2. 1 PublicationVSP_045176Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S79862 mRNA. Translation: AAB35397.1.
D31889 mRNA. Translation: BAA06687.1.
AK303007 mRNA. Translation: BAG64140.1.
AL161911 Genomic DNA. Translation: CAI95118.1.
CH471090 Genomic DNA. Translation: EAW87471.1.
BC014478 mRNA. Translation: AAH14478.1.
CCDSiCCDS59143.1. [Q16401-2]
CCDS6824.1. [Q16401-1]
RefSeqiNP_001257356.1. NM_001270427.1. [Q16401-2]
NP_005038.1. NM_005047.3. [Q16401-1]
UniGeneiHs.193725.

Genome annotation databases

EnsembliENST00000210313; ENSP00000210313; ENSG00000095261. [Q16401-1]
ENST00000373904; ENSP00000363011; ENSG00000095261. [Q16401-2]
GeneIDi5711.
KEGGihsa:5711.
UCSCiuc004bko.5. human. [Q16401-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S79862 mRNA. Translation: AAB35397.1.
D31889 mRNA. Translation: BAA06687.1.
AK303007 mRNA. Translation: BAG64140.1.
AL161911 Genomic DNA. Translation: CAI95118.1.
CH471090 Genomic DNA. Translation: EAW87471.1.
BC014478 mRNA. Translation: AAH14478.1.
CCDSiCCDS59143.1. [Q16401-2]
CCDS6824.1. [Q16401-1]
RefSeqiNP_001257356.1. NM_001270427.1. [Q16401-2]
NP_005038.1. NM_005047.3. [Q16401-1]
UniGeneiHs.193725.

3D structure databases

ProteinModelPortaliQ16401.
SMRiQ16401. Positions 209-234, 295-323.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111684. 85 interactions.
IntActiQ16401. 37 interactions.
MINTiMINT-5004744.
STRINGi9606.ENSP00000210313.

PTM databases

iPTMnetiQ16401.
PhosphoSiteiQ16401.

Polymorphism and mutation databases

BioMutaiPSMD5.
DMDMi3122657.

Proteomic databases

EPDiQ16401.
MaxQBiQ16401.
PaxDbiQ16401.
PeptideAtlasiQ16401.
PRIDEiQ16401.
TopDownProteomicsiQ16401-1. [Q16401-1]

Protocols and materials databases

DNASUi5711.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000210313; ENSP00000210313; ENSG00000095261. [Q16401-1]
ENST00000373904; ENSP00000363011; ENSG00000095261. [Q16401-2]
GeneIDi5711.
KEGGihsa:5711.
UCSCiuc004bko.5. human. [Q16401-1]

Organism-specific databases

CTDi5711.
GeneCardsiPSMD5.
HGNCiHGNC:9563. PSMD5.
HPAiHPA003216.
MIMi604452. gene.
neXtProtiNX_Q16401.
PharmGKBiPA33909.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4413. Eukaryota.
ENOG410XTFA. LUCA.
GeneTreeiENSGT00390000013040.
HOGENOMiHOG000231963.
HOVERGENiHBG053741.
InParanoidiQ16401.
KOiK06692.
OMAiFVEYVVD.
PhylomeDBiQ16401.
TreeFamiTF106231.

Enzyme and pathway databases

ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-350562. Regulation of ornithine decarboxylase (ODC).
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641257. Degradation of AXIN.
R-HSA-4641258. Degradation of DVL.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-5362768. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-HSA-69481. G2/M Checkpoints.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiPSMD5. human.
GeneWikiiPSMD5.
GenomeRNAii5711.
PROiQ16401.
SOURCEiSearch...

Gene expression databases

BgeeiQ16401.
CleanExiHS_PSMD5.
ExpressionAtlasiQ16401. baseline and differential.
GenevisibleiQ16401. HS.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR019538. 26S_Psome_nonATP_su5.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
[Graphical view]
PfamiPF10508. Proteasom_PSMB. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression of a 26 S protease subunit enriched in dileucine repeats."
    Deveraux Q., Jensen C., Rechsteiner M.
    J. Biol. Chem. 270:23726-23729(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 75-96; 311-337 AND 431-449.
    Tissue: Mammary cancer.
  2. "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."
    Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
    DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Skin.
  7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-10, ACETYLATION AT ALA-2.
    Tissue: Platelet.
  8. Bienvenut W.V.
    Submitted (OCT-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-10, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  9. "Assembly pathway of the Mammalian proteasome base subcomplex is mediated by multiple specific chaperones."
    Kaneko T., Hamazaki J., Iemura S., Sasaki K., Furuyama K., Natsume T., Tanaka K., Murata S.
    Cell 137:914-925(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS PROTEASOME CHAPERONE, SUBUNIT, INTERACTION WITH PSMC2.
  10. "Hsm3/S5b participates in the assembly pathway of the 19S regulatory particle of the proteasome."
    Le Tallec B., Barrault M.B., Guerois R., Carre T., Peyroche A.
    Mol. Cell 33:389-399(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSMC1; PSMC2; PSMD1 AND PSMD6.
  11. "Chaperone-mediated pathway of proteasome regulatory particle assembly."
    Roelofs J., Park S., Haas W., Tian G., McAllister F.E., Huo Y., Lee B.H., Zhang F., Shi Y., Gygi S.P., Finley D.
    Nature 459:861-865(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS PROTEASOME CHAPERONE, INTERACTION WITH PSMC2.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPSMD5_HUMAN
AccessioniPrimary (citable) accession number: Q16401
Secondary accession number(s): B4DZM8, Q15045, Q4VXG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Was initially identified as a genuine component of the 26S proteasome.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.