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P62195

- PRS8_HUMAN

UniProt

P62195 - PRS8_HUMAN

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Protein

26S protease regulatory subunit 8

Gene

PSMC5

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

Functioni

The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi190 – 1978ATPSequence Analysis

GO - Molecular functioni

  1. ATPase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. thyrotropin-releasing hormone receptor binding Source: UniProtKB
  4. transcription cofactor activity Source: ProtInc
  5. transcription factor binding Source: UniProtKB

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 programmed cell death Source: UniProtKB
  14. negative regulation of transcription, DNA-templated Source: Ensembl
  15. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  16. positive regulation of inclusion body assembly Source: Ensembl
  17. positive regulation of transcription, DNA-templated Source: UniProtKB
  18. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  19. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  20. protein polyubiquitination Source: Reactome
  21. regulation of apoptotic process Source: Reactome
  22. regulation of cellular amino acid metabolic process Source: Reactome
  23. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  24. RNA metabolic process Source: Reactome
  25. small molecule metabolic process Source: Reactome
  26. transcription from RNA polymerase II promoter Source: ProtInc
  27. viral process Source: Reactome
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_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_25325. AUF1 (hnRNP D0) destabilizes mRNA.
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 protease regulatory subunit 8
Alternative name(s):
26S proteasome AAA-ATPase subunit RPT6
Proteasome 26S subunit ATPase 5
Proteasome subunit p45
Thyroid hormone receptor-interacting protein 1
Short name:
TRIP1
p45/SUG
Gene namesi
Name:PSMC5
Synonyms:SUG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:9552. PSMC5.

Subcellular locationi

Cytoplasm Curated. Nucleus Curated

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. cytoplasm Source: UniProtKB
  3. cytoplasmic vesicle Source: UniProtKB
  4. cytosol Source: Reactome
  5. cytosolic proteasome complex Source: Ensembl
  6. extracellular vesicular exosome Source: UniProt
  7. inclusion body Source: Ensembl
  8. membrane Source: UniProtKB
  9. nuclear proteasome complex Source: Ensembl
  10. nucleoplasm Source: Reactome
  11. nucleus Source: UniProtKB
  12. proteasome accessory complex Source: UniProtKB
  13. proteasome complex Source: UniProtKB
  14. proteasome regulatory particle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33897.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 40640526S protease regulatory subunit 8PRO_0000084721Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei222 – 2221N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP62195.
PaxDbiP62195.
PRIDEiP62195.

PTM databases

PhosphoSiteiP62195.

Expressioni

Gene expression databases

BgeeiP62195.
CleanExiHS_PSMC5.
ExpressionAtlasiP62195. baseline and differential.
GenevestigatoriP62195.

Organism-specific databases

HPAiHPA017871.

Interactioni

Subunit structurei

Interacts, in vitro, with the thyroid hormone receptor (in a thyroid hormone T3-dependent manner) and with retinoid X receptor (RXR) (By similarity). Interacts with NDC80. Interacts with PAAF1. Interacts with TRIM5. Component of a complex with USP49 and RUVBL1.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P03255-12EBI-357745,EBI-6692439From a different organism.
Camk2aP112754EBI-357745,EBI-2640645From a different organism.
Camk2bP084133EBI-357745,EBI-916155From a different organism.
ERCC3P194474EBI-357745,EBI-1183307
PAAF1Q9BRP42EBI-357745,EBI-1056358
PLEKHO1Q53GL09EBI-357745,EBI-949945
PSMC2P3599810EBI-357745,EBI-359710
PSMC4P4368611EBI-357745,EBI-743997
PSMC6P623338EBI-357745,EBI-357669
PSMD2Q132009EBI-357745,EBI-357648

Protein-protein interaction databases

BioGridi111678. 134 interactions.
IntActiP62195. 42 interactions.
MINTiMINT-5004394.
STRINGi9606.ENSP00000310572.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi322 – 33312Combined sources
Beta strandi336 – 3383Combined sources
Helixi344 – 3496Combined sources
Helixi356 – 37217Combined sources
Beta strandi376 – 3783Combined sources
Helixi380 – 39112Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KRKNMR-A320-395[»]
3KW6X-ray2.10A318-395[»]
ProteinModelPortaliP62195.
SMRiP62195. Positions 27-396.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62195.

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

eggNOGiCOG1222.
GeneTreeiENSGT00550000074947.
HOVERGENiHBG000109.
InParanoidiP62195.
KOiK03066.
OMAiVMGTKKV.
PhylomeDBiP62195.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

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. Align

Isoform 1 (identifier: P62195-1) [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
MALDGPEQME LEEGKAGSGL RQYYLSKIEE LQLIVNDKSQ NLRRLQAQRN
60 70 80 90 100
ELNAKVRLLR EELQLLQEQG SYVGEVVRAM DKKKVLVKVH PEGKFVVDVD
110 120 130 140 150
KNIDINDVTP NCRVALRNDS YTLHKILPNK VDPLVSLMMV EKVPDSTYEM
160 170 180 190 200
IGGLDKQIKE IKEVIELPVK HPELFEALGI AQPKGVLLYG PPGTGKTLLA
210 220 230 240 250
RAVAHHTDCT FIRVSGSELV QKFIGEGARM VRELFVMARE HAPSIIFMDE
260 270 280 290 300
IDSIGSSRLE GGSGGDSEVQ RTMLELLNQL DGFEATKNIK VIMATNRIDI
310 320 330 340 350
LDSALLRPGR IDRKIEFPPP NEEARLDILK IHSRKMNLTR GINLRKIAEL
360 370 380 390 400
MPGASGAEVK GVCTEAGMYA LRERRVHVTQ EDFEMAVAKV MQKDSEKNMS

IKKLWK
Length:406
Mass (Da):45,626
Last modified:June 21, 2004 - v1
Checksum:i29C6410C4A85A7F7
GO
Isoform 2 (identifier: P62195-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: Missing.

Show »
Length:398
Mass (Da):44,784
Checksum:i450BB51DA8C9381D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611E → R in BAA07919. (PubMed:7729537)Curated
Sequence conflicti127 – 1282LP → ML in AAB88187. (PubMed:9110174)Curated
Sequence conflicti266 – 2661D → S in AAC41735. (PubMed:7776974)Curated
Sequence conflicti272 – 2721T → Q in AAC41735. (PubMed:7776974)Curated
Sequence conflicti300 – 3001I → M in AAC41735. (PubMed:7776974)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035901
Natural varianti258 – 2581R → W.
Corresponds to variant rs11543211 [ dbSNP | Ensembl ].
VAR_048119

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 88Missing in isoform 2. 1 PublicationVSP_045441

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D44467 mRNA. Translation: BAA07919.1.
L38810 mRNA. Translation: AAC41735.1.
AK290758 mRNA. Translation: BAF83447.1.
AK291878 mRNA. Translation: BAF84567.1.
AC015651 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94270.1.
CH471109 Genomic DNA. Translation: EAW94271.1.
CH471109 Genomic DNA. Translation: EAW94272.1.
BC001932 mRNA. Translation: AAH01932.1.
BC002367 mRNA. Translation: AAH02367.3.
AF035309 mRNA. Translation: AAB88187.1.
CCDSiCCDS11645.1. [P62195-1]
CCDS56043.1. [P62195-2]
PIRiS60343.
S65536.
RefSeqiNP_001186092.1. NM_001199163.1. [P62195-2]
NP_002796.4. NM_002805.5. [P62195-1]
UniGeneiHs.79387.

Genome annotation databases

EnsembliENST00000310144; ENSP00000310572; ENSG00000087191. [P62195-1]
ENST00000375812; ENSP00000364970; ENSG00000087191. [P62195-2]
ENST00000580864; ENSP00000462495; ENSG00000087191. [P62195-2]
ENST00000581882; ENSP00000463938; ENSG00000087191. [P62195-2]
GeneIDi5705.
KEGGihsa:5705.
UCSCiuc002jcb.3. human. [P62195-1]

Polymorphism databases

DMDMi49065819.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D44467 mRNA. Translation: BAA07919.1 .
L38810 mRNA. Translation: AAC41735.1 .
AK290758 mRNA. Translation: BAF83447.1 .
AK291878 mRNA. Translation: BAF84567.1 .
AC015651 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94270.1 .
CH471109 Genomic DNA. Translation: EAW94271.1 .
CH471109 Genomic DNA. Translation: EAW94272.1 .
BC001932 mRNA. Translation: AAH01932.1 .
BC002367 mRNA. Translation: AAH02367.3 .
AF035309 mRNA. Translation: AAB88187.1 .
CCDSi CCDS11645.1. [P62195-1 ]
CCDS56043.1. [P62195-2 ]
PIRi S60343.
S65536.
RefSeqi NP_001186092.1. NM_001199163.1. [P62195-2 ]
NP_002796.4. NM_002805.5. [P62195-1 ]
UniGenei Hs.79387.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KRK NMR - A 320-395 [» ]
3KW6 X-ray 2.10 A 318-395 [» ]
ProteinModelPortali P62195.
SMRi P62195. Positions 27-396.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111678. 134 interactions.
IntActi P62195. 42 interactions.
MINTi MINT-5004394.
STRINGi 9606.ENSP00000310572.

PTM databases

PhosphoSitei P62195.

Polymorphism databases

DMDMi 49065819.

Proteomic databases

MaxQBi P62195.
PaxDbi P62195.
PRIDEi P62195.

Protocols and materials databases

DNASUi 5705.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000310144 ; ENSP00000310572 ; ENSG00000087191 . [P62195-1 ]
ENST00000375812 ; ENSP00000364970 ; ENSG00000087191 . [P62195-2 ]
ENST00000580864 ; ENSP00000462495 ; ENSG00000087191 . [P62195-2 ]
ENST00000581882 ; ENSP00000463938 ; ENSG00000087191 . [P62195-2 ]
GeneIDi 5705.
KEGGi hsa:5705.
UCSCi uc002jcb.3. human. [P62195-1 ]

Organism-specific databases

CTDi 5705.
GeneCardsi GC17P061904.
HGNCi HGNC:9552. PSMC5.
HPAi HPA017871.
MIMi 601681. gene.
neXtProti NX_P62195.
PharmGKBi PA33897.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1222.
GeneTreei ENSGT00550000074947.
HOVERGENi HBG000109.
InParanoidi P62195.
KOi K03066.
OMAi VMGTKKV.
PhylomeDBi P62195.

Enzyme and pathway databases

Reactomei 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_25325. AUF1 (hnRNP D0) destabilizes mRNA.
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 PSMC5. human.
EvolutionaryTracei P62195.
GeneWikii PSMC5.
GenomeRNAii 5705.
NextBioi 22166.
PROi P62195.
SOURCEi Search...

Gene expression databases

Bgeei P62195.
CleanExi HS_PSMC5.
ExpressionAtlasi P62195. baseline and differential.
Genevestigatori P62195.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00004. AAA. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01242. 26Sp45. 1 hit.
PROSITEi PS00674. AAA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning of a new putative ATPase subunit p45 of the human 26S proteasome, a homolog of yeast transcriptional factor Sug1p."
    Akiyama K., Yokota K., Kagawa S., Shimbara N., Demartino G.N., Slaughter C.A., Noda C., Tanaka K.
    FEBS Lett. 363:151-156(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Hepatoma.
  2. "Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor."
    Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.
    Mol. Endocrinol. 9:243-254(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORMS 1 AND 2).
    Tissue: Skeletal muscle.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Lung carcinoma.
  6. "Large-scale concatenation cDNA sequencing."
    Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
    Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-406.
    Tissue: Brain.
  7. "HEC binds to the seventh regulatory subunit of the 26 S proteasome and modulates the proteolysis of mitotic cyclins."
    Chen Y., Sharp Z.D., Lee W.-H.
    J. Biol. Chem. 272:24081-24087(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NDC80.
  8. "Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins."
    Zheng L., Chen Y., Lee W.-H.
    Mol. Cell. Biol. 19:5417-5428(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NDC80.
  9. "Proteasomal ATPase-associated factor 1 negatively regulates proteasome activity by interacting with proteasomal ATPases."
    Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.
    Mol. Cell. Biol. 25:3842-3853(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAAF1.
  10. "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.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-222, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "TRIM5alpha associates with proteasomal subunits in cells while in complex with HIV-1 virions."
    Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L., Luban J., Campbell E.M.
    Retrovirology 8:93-93(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM5.
  15. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "USP49 deubiquitinates histone H2B and regulates cotranscriptional pre-mRNA splicing."
    Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S., Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M., Giles K.E., Ma L., Wang H.
    Genes Dev. 27:1581-1595(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH USP49 AND RUVBL1.
  18. "Crystal structure of a domain of 26s proteasome regulatory subunit 8 from Homo sapiens. Northeast structural genomics consortium target ID HR3102A."
    Northeast structural genomics consortium (NESG)
    Submitted (JAN-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 318-395, STRUCTURE BY NMR OF 320-395.
  19. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-60.

Entry informationi

Entry nameiPRS8_HUMAN
AccessioniPrimary (citable) accession number: P62195
Secondary accession number(s): A8K3Z3
, A8K763, O35051, O43208, P47210, P52915, P52916
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 21, 2004
Last modified: October 29, 2014
This is version 114 of the entry and version 1 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3