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Protein

26S proteasome non-ATPase regulatory subunit 9

Gene

PSMD9

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). During the base subcomplex assembly is part of an intermediate PSMD9:PSMC6:PSMC3 module, also known as modulator trimer complex; PSMD9 is released during the further base assembly process.1 Publication

GO - Molecular functioni

  • bHLH transcription factor binding Source: BHF-UCL
  • transcription coactivator activity Source: BHF-UCL

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-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome non-ATPase regulatory subunit 9
Alternative name(s):
26S proteasome regulatory subunit p27
Gene namesi
Name:PSMD9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:9567. PSMD9.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • nucleus Source: BHF-UCL
  • proteasome regulatory particle Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33913.

Polymorphism and mutation databases

BioMutaiPSMD9.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22322326S proteasome non-ATPase regulatory subunit 9PRO_0000173852Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei129 – 1291PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO00233.
MaxQBiO00233.
PaxDbiO00233.
PRIDEiO00233.
TopDownProteomicsiO00233-1. [O00233-1]

2D gel databases

OGPiO00233.

PTM databases

iPTMnetiO00233.
PhosphoSiteiO00233.

Expressioni

Tissue specificityi

Expressed in all tissues tested, highly expressed in liver and kidney.

Gene expression databases

BgeeiO00233.
CleanExiHS_PSMD9.
ExpressionAtlasiO00233. baseline and differential.
GenevisibleiO00233. HS.

Organism-specific databases

HPAiHPA040512.
HPA044220.

Interactioni

Subunit structurei

Interacts with PSMC3. Part of a transient complex (modulator) containing PSMD9, PSMC6 and PSMC3 formed during the assembly of the 26S proteasome.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AHCYL1O438653EBI-750973,EBI-2371423
BANPQ8N9N53EBI-750973,EBI-744695
CCDC136Q96JN2-23EBI-750973,EBI-10171416
NCKIPSDQ9NZQ33EBI-750973,EBI-745080
PSMC3P179809EBI-750973,EBI-359720
PSMC6P623338EBI-750973,EBI-357669
TRIM39Q9HCM94EBI-750973,EBI-739510
TRIM42A1L4B63EBI-750973,EBI-10172216

GO - Molecular functioni

  • bHLH transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi111687. 67 interactions.
IntActiO00233. 15 interactions.
MINTiMINT-1435362.
STRINGi9606.ENSP00000440485.

Structurei

3D structure databases

ProteinModelPortaliO00233.
SMRiO00233. Positions 23-99, 136-218.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini108 – 19588PDZAdd
BLAST

Sequence similaritiesi

Belongs to the proteasome subunit p27 family.Curated
Contains 1 PDZ (DHR) domain.Curated

Phylogenomic databases

eggNOGiKOG3129. Eukaryota.
COG0265. LUCA.
GeneTreeiENSGT00390000004147.
HOGENOMiHOG000216665.
HOVERGENiHBG001851.
InParanoidiO00233.
KOiK06693.
OMAiLGCNIVP.
PhylomeDBiO00233.
TreeFamiTF105995.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
[Graphical view]
PfamiPF13180. PDZ_2. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform p27-L (identifier: O00233-1) [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
MSDEEARQSG GSSQAGVVTV SDVQELMRRK EEIEAQIKAN YDVLESQKGI
60 70 80 90 100
GMNEPLVDCE GYPRSDVDLY QVRTARHNII CLQNDHKAVM KQVEEALHQL
110 120 130 140 150
HARDKEKQAR DMAEAHKEAM SRKLGQSESQ GPPRAFAKVN SISPGSPASI
160 170 180 190 200
AGLQVDDEIV EFGSVNTQNF QSLHNIGSVV QHSEGKPLNV TVIRRGEKHQ
210 220
LRLVPTRWAG KGLLGCNIIP LQR
Length:223
Mass (Da):24,682
Last modified:January 11, 2011 - v3
Checksum:i98B3A623323A8F37
GO
Isoform p27-S (identifier: O00233-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     186-223: KPLNVTVIRRGEKHQLRLVPTRWAGKGLLGCNIIPLQR → ALAPTILLSVSMNLTTPGTSSRSP

Show »
Length:209
Mass (Da):22,764
Checksum:i0DA575AA7A0C5005
GO
Isoform 3 (identifier: O00233-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     47-151: Missing.

Note: No experimental confirmation available.
Show »
Length:118
Mass (Da):13,053
Checksum:i69E5EA1033F547B9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171V → A.Combined sources2 Publications
Corresponds to variant rs2230681 [ dbSNP | Ensembl ].
VAR_009953
Natural varianti74 – 741T → I.
Corresponds to variant rs2291116 [ dbSNP | Ensembl ].
VAR_057047
Natural varianti134 – 1341R → W.
Corresponds to variant rs1177573 [ dbSNP | Ensembl ].
VAR_057048
Natural varianti197 – 1971E → G.
Corresponds to variant rs14259 [ dbSNP | Ensembl ].
VAR_057049

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei47 – 151105Missing in isoform 3. 1 PublicationVSP_046004Add
BLAST
Alternative sequencei186 – 22338KPLNV…IPLQR → ALAPTILLSVSMNLTTPGTS SRSP in isoform p27-S. 1 PublicationVSP_005300Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB003177 mRNA. Translation: BAA19790.1.
AK315389 mRNA. Translation: BAG37782.1.
CB111716 mRNA. No translation available.
AC069503 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98296.1.
BC002383 mRNA. Translation: AAH02383.1.
BC004184 mRNA. Translation: AAH04184.1.
BC004213 mRNA. Translation: AAH04213.1.
CCDSiCCDS58284.1. [O00233-3]
CCDS9225.1. [O00233-1]
RefSeqiNP_001248329.1. NM_001261400.2. [O00233-3]
NP_002804.2. NM_002813.6. [O00233-1]
UniGeneiHs.131151.

Genome annotation databases

EnsembliENST00000537407; ENSP00000445058; ENSG00000110801. [O00233-2]
ENST00000541212; ENSP00000440485; ENSG00000110801. [O00233-1]
ENST00000542602; ENSP00000443772; ENSG00000110801. [O00233-3]
GeneIDi5715.
KEGGihsa:5715.
UCSCiuc001ubl.5. human. [O00233-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB003177 mRNA. Translation: BAA19790.1.
AK315389 mRNA. Translation: BAG37782.1.
CB111716 mRNA. No translation available.
AC069503 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98296.1.
BC002383 mRNA. Translation: AAH02383.1.
BC004184 mRNA. Translation: AAH04184.1.
BC004213 mRNA. Translation: AAH04213.1.
CCDSiCCDS58284.1. [O00233-3]
CCDS9225.1. [O00233-1]
RefSeqiNP_001248329.1. NM_001261400.2. [O00233-3]
NP_002804.2. NM_002813.6. [O00233-1]
UniGeneiHs.131151.

3D structure databases

ProteinModelPortaliO00233.
SMRiO00233. Positions 23-99, 136-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111687. 67 interactions.
IntActiO00233. 15 interactions.
MINTiMINT-1435362.
STRINGi9606.ENSP00000440485.

PTM databases

iPTMnetiO00233.
PhosphoSiteiO00233.

Polymorphism and mutation databases

BioMutaiPSMD9.

2D gel databases

OGPiO00233.

Proteomic databases

EPDiO00233.
MaxQBiO00233.
PaxDbiO00233.
PRIDEiO00233.
TopDownProteomicsiO00233-1. [O00233-1]

Protocols and materials databases

DNASUi5715.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000537407; ENSP00000445058; ENSG00000110801. [O00233-2]
ENST00000541212; ENSP00000440485; ENSG00000110801. [O00233-1]
ENST00000542602; ENSP00000443772; ENSG00000110801. [O00233-3]
GeneIDi5715.
KEGGihsa:5715.
UCSCiuc001ubl.5. human. [O00233-1]

Organism-specific databases

CTDi5715.
GeneCardsiPSMD9.
HGNCiHGNC:9567. PSMD9.
HPAiHPA040512.
HPA044220.
MIMi603146. gene.
neXtProtiNX_O00233.
PharmGKBiPA33913.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3129. Eukaryota.
COG0265. LUCA.
GeneTreeiENSGT00390000004147.
HOGENOMiHOG000216665.
HOVERGENiHBG001851.
InParanoidiO00233.
KOiK06693.
OMAiLGCNIVP.
PhylomeDBiO00233.
TreeFamiTF105995.

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-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

GeneWikiiPSMD9.
GenomeRNAii5715.
NextBioi22202.
PROiO00233.
SOURCEiSearch...

Gene expression databases

BgeeiO00233.
CleanExiHS_PSMD9.
ExpressionAtlasiO00233. baseline and differential.
GenevisibleiO00233. HS.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
[Graphical view]
PfamiPF13180. PDZ_2. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and characterization of a human proteasomal modulator subunit, p27 (PSMD9)."
    Watanabe T.K., Saito A., Suzuki M., Fujiwara T., Takahashi E., Slaughter C.A., DeMartino G.N., Hendil K.B., Chung C.H., Tanahashi N., Tanaka K.
    Genomics 50:241-250(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P27-S AND P27-L).
  2. "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 P27-L), VARIANT ALA-17.
    Tissue: Hippocampus.
  3. "Identification of intrahepatic cholangiocarcinoma related genes by comparison with normal liver tissues using expressed sequence tags."
    Wang A.G., Yoon S.Y., Oh J.H., Jeon Y.J., Kim M., Kim J.M., Byun S.S., Yang J.O., Kim J.H., Kim D.G., Yeom Y.I., Yoo H.S., Kim Y.S., Kim N.S.
    Biochem. Biophys. Res. Commun. 345:1022-1032(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT ALA-17.
    Tissue: Liver.
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [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].
    Tissue: Muscle.
  7. "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, INTERACTION WITH PSMC3, SUBUNIT.
  8. "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.
  9. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPSMD9_HUMAN
AccessioniPrimary (citable) accession number: O00233
Secondary accession number(s): B2RD35, G3V1Q6, Q9BQ42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 11, 2011
Last modified: April 13, 2016
This is version 156 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 component of the 26S proteasome.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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.