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P62195

- PRS8_HUMAN

UniProt

P62195 - PRS8_HUMAN

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Protein
26S protease regulatory subunit 8
Gene
PSMC5, SUG1
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 – 1978ATP Reviewed prediction

GO - Molecular functioni

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

GO - Biological processi

  1. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  2. G1/S transition of mitotic cell cycle Source: Reactome
  3. RNA metabolic process Source: Reactome
  4. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  5. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  6. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  7. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  8. apoptotic process Source: Reactome
  9. cellular nitrogen compound metabolic process Source: Reactome
  10. gene expression Source: Reactome
  11. mRNA metabolic process Source: Reactome
  12. mitotic cell cycle Source: Reactome
  13. negative regulation of apoptotic process Source: Reactome
  14. negative regulation of programmed cell death Source: UniProtKB
  15. negative regulation of transcription, DNA-templated Source: Ensembl
  16. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  17. positive regulation of inclusion body assembly Source: Ensembl
  18. positive regulation of transcription, DNA-templated Source: UniProtKB
  19. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  20. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  21. protein polyubiquitination Source: Reactome
  22. regulation of apoptotic process Source: Reactome
  23. regulation of cellular amino acid metabolic process Source: Reactome
  24. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle 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 Reviewed prediction. Nucleus Reviewed prediction

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. nuclear proteasome complex Source: Ensembl
  9. nucleoplasm Source: Reactome
  10. nucleus Source: UniProtKB
  11. proteasome accessory complex Source: UniProtKB
  12. proteasome complex Source: UniProtKB
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 – 11Removed1 Publication
Chaini2 – 40640526S protease regulatory subunit 8
PRO_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

ArrayExpressiP62195.
BgeeiP62195.
CleanExiHS_PSMC5.
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 RUVBL1.5 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. 128 interactions.
IntActiP62195. 42 interactions.
MINTiMINT-5004394.
STRINGi9606.ENSP00000310572.

Structurei

Secondary structure

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

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.

Miscellaneous databases

EvolutionaryTraceiP62195.

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.

Phylogenomic databases

eggNOGiCOG1222.
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

MALDGPEQME LEEGKAGSGL RQYYLSKIEE LQLIVNDKSQ NLRRLQAQRN    50
ELNAKVRLLR EELQLLQEQG SYVGEVVRAM DKKKVLVKVH PEGKFVVDVD 100
KNIDINDVTP NCRVALRNDS YTLHKILPNK VDPLVSLMMV EKVPDSTYEM 150
IGGLDKQIKE IKEVIELPVK HPELFEALGI AQPKGVLLYG PPGTGKTLLA 200
RAVAHHTDCT FIRVSGSELV QKFIGEGARM VRELFVMARE HAPSIIFMDE 250
IDSIGSSRLE GGSGGDSEVQ RTMLELLNQL DGFEATKNIK VIMATNRIDI 300
LDSALLRPGR IDRKIEFPPP NEEARLDILK IHSRKMNLTR GINLRKIAEL 350
MPGASGAEVK GVCTEAGMYA LRERRVHVTQ EDFEMAVAKV MQKDSEKNMS 400
IKKLWK 406
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

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.
VSP_045441

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611E → R in BAA07919. 1 Publication
Sequence conflicti127 – 1282LP → ML in AAB88187. 1 Publication
Sequence conflicti266 – 2661D → S in AAC41735. 1 Publication
Sequence conflicti272 – 2721T → Q in AAC41735. 1 Publication
Sequence conflicti300 – 3001I → M in AAC41735. 1 Publication

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. 128 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.
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

ArrayExpressi P62195.
Bgeei P62195.
CleanExi HS_PSMC5.
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: September 3, 2014
This is version 112 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

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