Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P62191

- PRS4_HUMAN

UniProt

P62191 - PRS4_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (21 Jun 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. nucleoside-triphosphatase activity Source: InterPro
    4. peptidase activity Source: UniProtKB-KW
    5. poly(A) RNA binding Source: UniProtKB
    6. protein binding Source: IntAct

    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 catabolic process Source: InterPro
    17. protein polyubiquitination Source: Reactome
    18. regulation of apoptotic process Source: Reactome
    19. regulation of cellular amino acid metabolic process Source: Reactome
    20. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    21. RNA metabolic process Source: Reactome
    22. small molecule metabolic process Source: Reactome
    23. viral process Source: Reactome

    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 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: ProtInc

    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.
    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. 81 interactions.
    IntActiP62191. 29 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.
    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

    MGQSQSGGHG PGGGKKDDKD KKKKYEPPVP TRVGKKKKKT KGPDAASKLP    50
    LVTPHTQCRL KLLKLERIKD YLLMEEEFIR NQEQMKPLEE KQEEERSKVD 100
    DLRGTPMSVG TLEEIIDDNH AIVSTSVGSE HYVSILSFVD KDLLEPGCSV 150
    LLNHKVHAVI GVLMDDTDPL VTVMKVEKAP QETYADIGGL DNQIQEIKES 200
    VELPLTHPEY YEEMGIKPPK GVILYGPPGT GKTLLAKAVA NQTSATFLRV 250
    VGSELIQKYL GDGPKLVREL FRVAEEHAPS IVFIDEIDAI GTKRYDSNSG 300
    GEREIQRTML ELLNQLDGFD SRGDVKVIMA TNRIETLDPA LIRPGRIDRK 350
    IEFPLPDEKT KKRIFQIHTS RMTLADDVTL DDLIMAKDDL SGADIKAICT 400
    EAGLMALRER RMKVTNEDFK KSKENVLYKK QEGTPEGLYL 440
    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:
    EMBL
    GenBank
    DDBJ
    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.
    PIRiA44468.
    RefSeqiNP_002793.2. NM_002802.2.
    UniGeneiHs.356654.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi49065817.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    PIRi A44468.
    RefSeqi NP_002793.2. NM_002802.2.
    UniGenei Hs.356654.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi 111673. 81 interactions.
    IntActi P62191. 29 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.

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

    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

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

    Gene expression databases

    Bgeei P62191.
    CleanExi HS_PSMC1.
    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

    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: October 1, 2014
    This is version 115 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