Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P48556

- PSMD8_HUMAN

UniProt

P48556 - PSMD8_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

26S proteasome non-ATPase regulatory subunit 8

Gene

PSMD8

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

Functioni

Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Necessary for activation of the CDC28 kinase.

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  4. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  5. apoptotic process Source: Reactome
  6. cellular nitrogen compound metabolic process Source: Reactome
  7. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  8. G1/S transition of mitotic cell cycle Source: Reactome
  9. gene expression Source: Reactome
  10. mitotic cell cycle Source: Reactome
  11. mRNA metabolic process Source: Reactome
  12. negative regulation of apoptotic process Source: Reactome
  13. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  14. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  15. protein polyubiquitination Source: Reactome
  16. regulation of apoptotic process Source: Reactome
  17. regulation of cellular amino acid metabolic process Source: Reactome
  18. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  19. RNA metabolic process Source: Reactome
  20. small molecule metabolic process Source: Reactome
  21. viral process Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_206597. Degradation of GLI2 by the proteasome.
REACT_228111. Hedgehog ligand biogenesis.
REACT_228209. Hh ligand biogenesis disease.
REACT_231645. GLI3 is processed to GLI3R by the proteasome.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_267605. Degradation of GLI1 by the proteasome.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome non-ATPase regulatory subunit 8
Alternative name(s):
26S proteasome regulatory subunit RPN12
26S proteasome regulatory subunit S14
p31
Gene namesi
Name:PSMD8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:9566. PSMD8.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProt
  5. proteasome accessory complex Source: UniProtKB
  6. proteasome complex Source: UniProtKB
  7. proteasome regulatory particle Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33912.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 35035026S proteasome non-ATPase regulatory subunit 8PRO_0000173846Add
BLAST

Proteomic databases

MaxQBiP48556.
PaxDbiP48556.
PRIDEiP48556.

PTM databases

PhosphoSiteiP48556.

Expressioni

Gene expression databases

BgeeiP48556.
CleanExiHS_PSMD8.
ExpressionAtlasiP48556. baseline and differential.
GenevestigatoriP48556.

Organism-specific databases

HPAiCAB021101.
HPA006702.

Interactioni

Protein-protein interaction databases

BioGridi111686. 71 interactions.
IntActiP48556. 9 interactions.
MINTiMINT-1136185.
STRINGi9606.ENSP00000215071.

Structurei

3D structure databases

ProteinModelPortaliP48556.
SMRiP48556. Positions 102-343.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the proteasome subunit S14 family.Curated

Phylogenomic databases

eggNOGiNOG285042.
HOGENOMiHOG000196008.
HOVERGENiHBG024389.
InParanoidiP48556.
KOiK03031.
OMAiNVYIRHP.
OrthoDBiEOG7T7GTQ.
PhylomeDBiP48556.
TreeFamiTF106233.

Family and domain databases

InterProiIPR006746. 26S_Psome_Rpn12.
[Graphical view]
PANTHERiPTHR12387. PTHR12387. 1 hit.

Sequencei

Sequence statusi: Complete.

P48556-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFIKGRAPRA PPRERRRATR GGLRQVVAPP RALGSTSRPH FRRASVCRRR
60 70 80 90 100
CRKSGGLLAA SRKMAAAAVN GAAGFSSSGP AATSGAVLQA ATGMYEQLKG
110 120 130 140 150
EWNRKSPNLS KCGEELGRLK LVLLELNFLP TTGTKLTKQQ LILARDILEI
160 170 180 190 200
GAQWSILRKD IPSFERYMAQ LKCYYFDYKE QLPESAYMHQ LLGLNLLFLL
210 220 230 240 250
SQNRVAEFHT ELERLPAKDI QTNVYIKHPV SLEQYLMEGS YNKVFLAKGN
260 270 280 290 300
IPAESYTFFI DILLDTIRDE IAGCIEKAYE KILFTEATRI LFFNTPKKMT
310 320 330 340 350
DYAKKRGWVL GPNNYYSFAS QQQKPEDTTI PSTELAKQVI EYARQLEMIV
Length:350
Mass (Da):39,612
Last modified:October 5, 2010 - v2
Checksum:iFF20203213333CB3
GO

Sequence cautioni

The sequence AAC62833.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAH01164.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH65006.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA07237.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK301771 mRNA. Translation: BAG63230.1.
AC005789 Genomic DNA. Translation: AAC62833.1. Sequence problems.
CH471126 Genomic DNA. Translation: EAW56785.1.
BC001164 mRNA. Translation: AAH01164.3. Different initiation.
BC065006 mRNA. Translation: AAH65006.2. Different initiation.
D38047 mRNA. Translation: BAA07237.1. Different initiation.
CCDSiCCDS12515.2.
PIRiS56108.
RefSeqiNP_002803.2. NM_002812.4.
UniGeneiHs.78466.

Genome annotation databases

EnsembliENST00000215071; ENSP00000215071; ENSG00000099341.
ENST00000620216; ENSP00000481136; ENSG00000099341.
GeneIDi5714.
KEGGihsa:5714.
UCSCiuc002oii.4. human.

Polymorphism databases

DMDMi308153477.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK301771 mRNA. Translation: BAG63230.1 .
AC005789 Genomic DNA. Translation: AAC62833.1 . Sequence problems.
CH471126 Genomic DNA. Translation: EAW56785.1 .
BC001164 mRNA. Translation: AAH01164.3 . Different initiation.
BC065006 mRNA. Translation: AAH65006.2 . Different initiation.
D38047 mRNA. Translation: BAA07237.1 . Different initiation.
CCDSi CCDS12515.2.
PIRi S56108.
RefSeqi NP_002803.2. NM_002812.4.
UniGenei Hs.78466.

3D structure databases

ProteinModelPortali P48556.
SMRi P48556. Positions 102-343.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111686. 71 interactions.
IntActi P48556. 9 interactions.
MINTi MINT-1136185.
STRINGi 9606.ENSP00000215071.

PTM databases

PhosphoSitei P48556.

Polymorphism databases

DMDMi 308153477.

Proteomic databases

MaxQBi P48556.
PaxDbi P48556.
PRIDEi P48556.

Protocols and materials databases

DNASUi 5714.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000215071 ; ENSP00000215071 ; ENSG00000099341 .
ENST00000620216 ; ENSP00000481136 ; ENSG00000099341 .
GeneIDi 5714.
KEGGi hsa:5714.
UCSCi uc002oii.4. human.

Organism-specific databases

CTDi 5714.
GeneCardsi GC19P038865.
H-InvDB HIX0040074.
HGNCi HGNC:9566. PSMD8.
HPAi CAB021101.
HPA006702.
neXtProti NX_P48556.
PharmGKBi PA33912.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG285042.
HOGENOMi HOG000196008.
HOVERGENi HBG024389.
InParanoidi P48556.
KOi K03031.
OMAi NVYIRHP.
OrthoDBi EOG7T7GTQ.
PhylomeDBi P48556.
TreeFami TF106233.

Enzyme and pathway databases

Reactomei REACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_206597. Degradation of GLI2 by the proteasome.
REACT_228111. Hedgehog ligand biogenesis.
REACT_228209. Hh ligand biogenesis disease.
REACT_231645. GLI3 is processed to GLI3R by the proteasome.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_267605. Degradation of GLI1 by the proteasome.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

ChiTaRSi PSMD8. human.
GeneWikii PSMD8.
GenomeRNAii 5714.
NextBioi 22198.
PROi P48556.

Gene expression databases

Bgeei P48556.
CleanExi HS_PSMD8.
ExpressionAtlasi P48556. baseline and differential.
Genevestigatori P48556.

Family and domain databases

InterProi IPR006746. 26S_Psome_Rpn12.
[Graphical view ]
PANTHERi PTHR12387. PTHR12387. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Testis.
  2. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] OF 67-350.
    Tissue: Muscle and Skin.
  5. "Nin1p, a regulatory subunit of the 26S proteasome, is necessary for activation of Cdc28p kinase of Saccharomyces cerevisiae."
    Kominami K., DeMartino G.N., Moomaw C., Slaughter C.A., Shimbara N., Fujimuro M., Yokosawa H., Hisamatsu H., Tanahashi N., Shimizu Y., Tanaka K., Toh-e A.
    EMBO J. 14:3105-3115(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 71-350.
  6. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
    Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
    Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPSMD8_HUMAN
AccessioniPrimary (citable) accession number: P48556
Secondary accession number(s): B4DX18, Q6P1L7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 5, 2010
Last modified: November 26, 2014
This is version 136 of the entry and version 2 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

It is uncertain whether Met-1 or Met-64 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3