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P62191

- PRS4_HUMAN

UniProt

P62191 - PRS4_HUMAN

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Protein

26S protease regulatory subunit 4

Gene

PSMC1

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 bindingi226 – 2338ATPSequence Analysis

GO - Molecular functioni

  1. ATPase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. poly(A) RNA 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. ATP catabolic process Source: GOC
  7. cellular nitrogen compound metabolic process Source: Reactome
  8. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  9. G1/S transition of mitotic cell cycle Source: Reactome
  10. gene expression Source: Reactome
  11. mitotic cell cycle Source: Reactome
  12. mRNA metabolic process Source: Reactome
  13. negative regulation of apoptotic process Source: Reactome
  14. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  15. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  16. protein polyubiquitination Source: Reactome
  17. regulation of apoptotic process Source: Reactome
  18. regulation of cellular amino acid metabolic process Source: Reactome
  19. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  20. RNA metabolic process Source: Reactome
  21. small molecule metabolic process Source: Reactome
  22. viral process Source: Reactome
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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 protease regulatory subunit 4
Short name:
P26s4
Alternative name(s):
26S proteasome AAA-ATPase subunit RPT2
Proteasome 26S subunit ATPase 1
Gene namesi
Name:PSMC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:9547. PSMC1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. membrane Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProt
  6. proteasome accessory complex Source: UniProtKB
  7. proteasome complex Source: UniProtKB
  8. proteasome regulatory particle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33892.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 44043926S protease regulatory subunit 4PRO_0000084677Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei4 – 41Phosphoserine1 Publication
Cross-linki237 – 237Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei258 – 2581N6-acetyllysine1 Publication
Modified residuei439 – 4391Phosphotyrosine1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP62191.
PaxDbiP62191.
PeptideAtlasiP62191.
PRIDEiP62191.

PTM databases

PhosphoSiteiP62191.

Expressioni

Gene expression databases

BgeeiP62191.
CleanExiHS_PSMC1.
ExpressionAtlasiP62191. baseline.
GenevestigatoriP62191.

Organism-specific databases

HPAiHPA000872.

Interactioni

Subunit structurei

Interacts with SCA7. Interacts with NGLY1. Interacts with PAAF1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KDM1AO603412EBI-357598,EBI-710124
PSMC2P359984EBI-357598,EBI-359710
PSMC6P623333EBI-357598,EBI-357669
PSMD2Q132006EBI-357598,EBI-357648
SUV39H1O434632EBI-357598,EBI-349968

Protein-protein interaction databases

BioGridi111673. 85 interactions.
IntActiP62191. 30 interactions.
MINTiMINT-1141832.
STRINGi9606.ENSP00000261303.

Structurei

3D structure databases

ProteinModelPortaliP62191.
SMRiP62191. Positions 78-439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

eggNOGiCOG1222.
GeneTreeiENSGT00550000074818.
HOGENOMiHOG000225143.
HOVERGENiHBG000109.
InParanoidiP62191.
KOiK03062.
OMAiMCTEAGL.
OrthoDBiEOG7F24ST.
PhylomeDBiP62191.
TreeFamiTF106226.

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: P62191-1) [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
MGQSQSGGHG PGGGKKDDKD KKKKYEPPVP TRVGKKKKKT KGPDAASKLP
60 70 80 90 100
LVTPHTQCRL KLLKLERIKD YLLMEEEFIR NQEQMKPLEE KQEEERSKVD
110 120 130 140 150
DLRGTPMSVG TLEEIIDDNH AIVSTSVGSE HYVSILSFVD KDLLEPGCSV
160 170 180 190 200
LLNHKVHAVI GVLMDDTDPL VTVMKVEKAP QETYADIGGL DNQIQEIKES
210 220 230 240 250
VELPLTHPEY YEEMGIKPPK GVILYGPPGT GKTLLAKAVA NQTSATFLRV
260 270 280 290 300
VGSELIQKYL GDGPKLVREL FRVAEEHAPS IVFIDEIDAI GTKRYDSNSG
310 320 330 340 350
GEREIQRTML ELLNQLDGFD SRGDVKVIMA TNRIETLDPA LIRPGRIDRK
360 370 380 390 400
IEFPLPDEKT KKRIFQIHTS RMTLADDVTL DDLIMAKDDL SGADIKAICT
410 420 430 440
EAGLMALRER RMKVTNEDFK KSKENVLYKK QEGTPEGLYL
Length:440
Mass (Da):49,185
Last modified:June 21, 2004 - v1
Checksum:iACA80782F4F96F49
GO
Isoform 2 (identifier: P62191-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.

Note: No experimental confirmation available.

Show »
Length:367
Mass (Da):41,167
Checksum:iF96ACDAF2907971C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191K → E in AAA35484. (PubMed:1429620)Curated
Sequence conflicti70 – 701D → G in AAH67741. (PubMed:15489334)Curated
Sequence conflicti120 – 1201H → R in AAH16368. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7373Missing in isoform 2. 1 PublicationVSP_055768Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02426 mRNA. Translation: AAA35484.1.
AK299121 mRNA. Translation: BAG61175.1.
CR457044 mRNA. Translation: CAG33325.1.
AL161662 Genomic DNA. No translation available.
AL355074 Genomic DNA. No translation available.
BC000512 mRNA. Translation: AAH00512.1.
BC016368 mRNA. Translation: AAH16368.1.
BC067741 mRNA. Translation: AAH67741.1.
BC073818 mRNA. Translation: AAH73818.1.
CCDSiCCDS32139.1. [P62191-1]
PIRiA44468.
RefSeqiNP_002793.2. NM_002802.2. [P62191-1]
UniGeneiHs.356654.

Genome annotation databases

EnsembliENST00000261303; ENSP00000261303; ENSG00000100764. [P62191-1]
ENST00000543772; ENSP00000445147; ENSG00000100764. [P62191-2]
GeneIDi5700.
KEGGihsa:5700.
UCSCiuc001xyf.3. human. [P62191-1]

Polymorphism databases

DMDMi49065817.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02426 mRNA. Translation: AAA35484.1 .
AK299121 mRNA. Translation: BAG61175.1 .
CR457044 mRNA. Translation: CAG33325.1 .
AL161662 Genomic DNA. No translation available.
AL355074 Genomic DNA. No translation available.
BC000512 mRNA. Translation: AAH00512.1 .
BC016368 mRNA. Translation: AAH16368.1 .
BC067741 mRNA. Translation: AAH67741.1 .
BC073818 mRNA. Translation: AAH73818.1 .
CCDSi CCDS32139.1. [P62191-1 ]
PIRi A44468.
RefSeqi NP_002793.2. NM_002802.2. [P62191-1 ]
UniGenei Hs.356654.

3D structure databases

ProteinModelPortali P62191.
SMRi P62191. Positions 78-439.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111673. 85 interactions.
IntActi P62191. 30 interactions.
MINTi MINT-1141832.
STRINGi 9606.ENSP00000261303.

PTM databases

PhosphoSitei P62191.

Polymorphism databases

DMDMi 49065817.

Proteomic databases

MaxQBi P62191.
PaxDbi P62191.
PeptideAtlasi P62191.
PRIDEi P62191.

Protocols and materials databases

DNASUi 5700.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261303 ; ENSP00000261303 ; ENSG00000100764 . [P62191-1 ]
ENST00000543772 ; ENSP00000445147 ; ENSG00000100764 . [P62191-2 ]
GeneIDi 5700.
KEGGi hsa:5700.
UCSCi uc001xyf.3. human. [P62191-1 ]

Organism-specific databases

CTDi 5700.
GeneCardsi GC14P090722.
H-InvDB HIX0030744.
HGNCi HGNC:9547. PSMC1.
HPAi HPA000872.
MIMi 602706. gene.
neXtProti NX_P62191.
PharmGKBi PA33892.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1222.
GeneTreei ENSGT00550000074818.
HOGENOMi HOG000225143.
HOVERGENi HBG000109.
InParanoidi P62191.
KOi K03062.
OMAi MCTEAGL.
OrthoDBi EOG7F24ST.
PhylomeDBi P62191.
TreeFami TF106226.

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 PSMC1. human.
GeneWikii PSMC1.
GenomeRNAii 5700.
NextBioi 22146.
PROi P62191.
SOURCEi Search...

Gene expression databases

Bgeei P62191.
CleanExi HS_PSMC1.
ExpressionAtlasi P62191. baseline.
Genevestigatori P62191.

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. "Subunit 4 of the 26 S protease is a member of a novel eukaryotic ATPase family."
    Dubiel W., Ferrell K., Pratt G., Rechsteiner M.C.
    J. Biol. Chem. 267:22699-22702(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  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 2).
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    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: Bone marrow, Brain, Lung and Prostate.
  6. "Association of ataxin-7 with the proteasome subunit S4 of the 19S regulatory complex."
    Matilla A., Gorbea C., Einum D.D., Townsend J., Michalik A., van Broeckhoven C., Jensen C.C., Murphy K.J., Ptacek L.J., Fu Y.H.
    Hum. Mol. Genet. 10:2821-2831(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCA7.
  7. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "A complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins."
    Katiyar S., Li G., Lennarz W.J.
    Proc. Natl. Acad. Sci. U.S.A. 101:13774-13779(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NGLY1.
  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. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
    Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
    Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-237.
    Tissue: Mammary cancer.
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPRS4_HUMAN
AccessioniPrimary (citable) accession number: P62191
Secondary accession number(s): B4DR63
, P49014, Q03527, Q6IAW0, Q6NW36, Q96AZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 21, 2004
Last modified: November 26, 2014
This is version 117 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3