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)

Q13200

- PSMD2_HUMAN

UniProt

Q13200 - PSMD2_HUMAN

Protein

26S proteasome non-ATPase regulatory subunit 2

Gene

PSMD2

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 148 (01 Oct 2014)
      Sequence version 3 (15 Jul 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
    Binds to the intracellular domain of tumor necrosis factor type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside the death domain of TNFR1.

    GO - Molecular functioni

    1. enzyme regulator activity Source: InterPro
    2. protein 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 ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    14. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    15. protein polyubiquitination Source: Reactome
    16. regulation of apoptotic process Source: Reactome
    17. regulation of cellular amino acid metabolic process Source: Reactome
    18. regulation of protein catabolic process Source: InterPro
    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

    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 proteasome non-ATPase regulatory subunit 2
    Alternative name(s):
    26S proteasome regulatory subunit RPN1
    26S proteasome regulatory subunit S2
    26S proteasome subunit p97
    Protein 55.11
    Tumor necrosis factor type 1 receptor-associated protein 2
    Gene namesi
    Name:PSMD2
    Synonyms:TRAP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:9559. PSMD2.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Proteasome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33905.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 90890826S proteasome non-ATPase regulatory subunit 2PRO_0000173810Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei16 – 161Phosphoserine8 Publications
    Modified residuei24 – 241Phosphothreonine2 Publications
    Modified residuei29 – 291Phosphoserine1 Publication
    Modified residuei194 – 1941Phosphotyrosine1 Publication
    Modified residuei361 – 3611Phosphoserine3 Publications
    Modified residuei551 – 5511N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13200.
    PaxDbiQ13200.
    PeptideAtlasiQ13200.
    PRIDEiQ13200.

    PTM databases

    PhosphoSiteiQ13200.

    Expressioni

    Tissue specificityi

    Found in skeletal muscle, liver, heart, brain, kidney, pancreas, lung and placenta.

    Gene expression databases

    ArrayExpressiQ13200.
    BgeeiQ13200.
    CleanExiHS_PSMD2.
    GenevestigatoriQ13200.

    Organism-specific databases

    HPAiHPA045192.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q53HB32EBI-357648,EBI-9362707
    BAG1Q999332EBI-357648,EBI-1030678
    EBNA-LPQ8AZK72EBI-357648,EBI-1185167From a different organism.
    MLF1P583402EBI-357648,EBI-721328
    PSMC1P621916EBI-357648,EBI-357598
    PSMC5P621959EBI-357648,EBI-357745
    PSMD4P550363EBI-357648,EBI-359318
    ptplad1Q8K2C92EBI-357648,EBI-8329978From a different organism.
    UCHL5Q9Y5K55EBI-357648,EBI-1051183

    Protein-protein interaction databases

    BioGridi111681. 121 interactions.
    IntActiQ13200. 117 interactions.
    MINTiMINT-1142723.
    STRINGi9606.ENSP00000310129.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13200.
    SMRiQ13200. Positions 56-908.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati409 – 44234PC 1Add
    BLAST
    Repeati443 – 47937PC 2Add
    BLAST
    Repeati480 – 51435PC 3Add
    BLAST
    Repeati517 – 55135PC 4Add
    BLAST
    Repeati560 – 58930PC 5Add
    BLAST
    Repeati692 – 72332PC 6Add
    BLAST
    Repeati742 – 75716PC 7Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi623 – 64119Glu/Lys-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the proteasome subunit S2 family.Curated
    Contains 7 PC repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5110.
    HOVERGENiHBG001842.
    InParanoidiQ13200.
    KOiK03028.
    OMAiIAQGLTH.
    OrthoDBiEOG70KGNV.
    PhylomeDBiQ13200.
    TreeFamiTF105739.

    Family and domain databases

    InterProiIPR016643. 26S_Psome_Rpn1.
    IPR016024. ARM-type_fold.
    IPR002015. Proteasome/cyclosome_rpt.
    [Graphical view]
    PfamiPF01851. PC_rep. 2 hits.
    [Graphical view]
    PIRSFiPIRSF015965. 26S_Psome_Rpn1. 1 hit.
    SUPFAMiSSF48371. SSF48371. 4 hits.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13200-1) [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

    MEEGGRDKAP VQPQQSPAAA PGGTDEKPSG KERRDAGDKD KEQELSEEDK    50
    QLQDELEMLV ERLGEKDTSL YRPALEELRR QIRSSTTSMT SVPKPLKFLR 100
    PHYGKLKEIY ENMAPGENKR FAADIISVLA MTMSGERECL KYRLVGSQEE 150
    LASWGHEYVR HLAGEVAKEW QELDDAEKVQ REPLLTLVKE IVPYNMAHNA 200
    EHEACDLLME IEQVDMLEKD IDENAYAKVC LYLTSCVNYV PEPENSALLR 250
    CALGVFRKFS RFPEALRLAL MLNDMELVED IFTSCKDVVV QKQMAFMLGR 300
    HGVFLELSED VEEYEDLTEI MSNVQLNSNF LALARELDIM EPKVPDDIYK 350
    THLENNRFGG SGSQVDSARM NLASSFVNGF VNAAFGQDKL LTDDGNKWLY 400
    KNKDHGMLSA AASLGMILLW DVDGGLTQID KYLYSSEDYI KSGALLACGI 450
    VNSGVRNECD PALALLSDYV LHNSNTMRLG SIFGLGLAYA GSNREDVLTL 500
    LLPVMGDSKS SMEVAGVTAL ACGMIAVGSC NGDVTSTILQ TIMEKSETEL 550
    KDTYARWLPL GLGLNHLGKG EAIEAILAAL EVVSEPFRSF ANTLVDVCAY 600
    AGSGNVLKVQ QLLHICSEHF DSKEKEEDKD KKEKKDKDKK EAPADMGAHQ 650
    GVAVLGIALI AMGEEIGAEM ALRTFGHLLR YGEPTLRRAV PLALALISVS 700
    NPRLNILDTL SKFSHDADPE VSYNSIFAMG MVGSGTNNAR LAAMLRQLAQ 750
    YHAKDPNNLF MVRLAQGLTH LGKGTLTLCP YHSDRQLMSQ VAVAGLLTVL 800
    VSFLDVRNII LGKSHYVLYG LVAAMQPRML VTFDEELRPL PVSVRVGQAV 850
    DVVGQAGKPK TITGFQTHTT PVLLAHGERA ELATEEFLPV TPILEGFVIL 900
    RKNPNYDL 908
    Length:908
    Mass (Da):100,200
    Last modified:July 15, 1999 - v3
    Checksum:iFAD71E7B26101BE3
    GO
    Isoform 2 (identifier: Q13200-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-163: MEEGGRDKAP...WGHEYVRHLA → MSMS

    Note: No experimental confirmation available.

    Show »
    Length:749
    Mass (Da):82,193
    Checksum:i4007D2AAADF807A6
    GO
    Isoform 3 (identifier: Q13200-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-130: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:778
    Mass (Da):85,606
    Checksum:i5564271C57A5959D
    GO

    Sequence cautioni

    The sequence AAA87705.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101P → R in CAA60167. (PubMed:7601280)Curated
    Sequence conflicti21 – 211P → S(PubMed:9126987)Curated
    Sequence conflicti32 – 321E → G(PubMed:9126987)Curated
    Sequence conflicti43 – 431Q → L(PubMed:9126987)Curated
    Sequence conflicti57 – 571E → V(PubMed:9126987)Curated
    Sequence conflicti60 – 601V → A in BAA11226. (PubMed:8774743)Curated
    Sequence conflicti226 – 2261Y → S in AAA87705. (PubMed:9126987)Curated
    Sequence conflicti260 – 2601S → T in CAA60167. (PubMed:7601280)Curated
    Sequence conflicti281 – 2833IFT → SS in AAA87705. (PubMed:9126987)Curated
    Sequence conflicti415 – 4151G → A in BAA11226. (PubMed:8774743)Curated
    Sequence conflicti731 – 7311M → MGM(PubMed:9126987)Curated
    Sequence conflicti776 – 7761L → P in BAG63219. (PubMed:14702039)Curated
    Sequence conflicti900 – 9089LRKNPNYDL → FGRTPIMISK(PubMed:15489334)Curated
    Sequence conflicti900 – 9089LRKNPNYDL → FGRTPIMISK(PubMed:7601280)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti176 – 1761A → T.
    Corresponds to variant rs11545172 [ dbSNP | Ensembl ].
    VAR_051554
    Natural varianti313 – 3131E → D.1 Publication
    Corresponds to variant rs11545169 [ dbSNP | Ensembl ].
    VAR_051555
    Natural varianti724 – 7241N → Y.2 Publications
    Corresponds to variant rs17856236 [ dbSNP | Ensembl ].
    VAR_067451

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 163163MEEGG…VRHLA → MSMS in isoform 2. 1 PublicationVSP_055065Add
    BLAST
    Alternative sequencei1 – 130130Missing in isoform 3. 1 PublicationVSP_055066Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D78151 mRNA. Translation: BAA11226.1.
    BT009736 mRNA. Translation: AAP88738.1.
    AK301759 mRNA. Translation: BAG63219.1.
    AK302177 mRNA. Translation: BAG63543.1.
    AC078797 Genomic DNA. No translation available.
    BC002368 mRNA. Translation: AAH02368.1.
    BC002997 mRNA. Translation: AAH02997.1.
    BC007897 mRNA. Translation: AAH07897.1.
    U12596 mRNA. Translation: AAA87705.1. Different initiation.
    X86446 mRNA. Translation: CAA60167.1.
    CCDSiCCDS3258.1. [Q13200-1]
    CCDS63853.1. [Q13200-3]
    CCDS63854.1. [Q13200-2]
    RefSeqiNP_001265637.1. NM_001278708.1.
    NP_001265638.1. NM_001278709.1.
    NP_002799.3. NM_002808.4.
    UniGeneiHs.518464.

    Genome annotation databases

    EnsembliENST00000310118; ENSP00000310129; ENSG00000175166. [Q13200-1]
    ENST00000435761; ENSP00000402618; ENSG00000175166. [Q13200-2]
    ENST00000439383; ENSP00000416028; ENSG00000175166. [Q13200-3]
    GeneIDi5708.
    KEGGihsa:5708.
    UCSCiuc003fnn.1. human. [Q13200-1]

    Polymorphism databases

    DMDMi6174930.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D78151 mRNA. Translation: BAA11226.1 .
    BT009736 mRNA. Translation: AAP88738.1 .
    AK301759 mRNA. Translation: BAG63219.1 .
    AK302177 mRNA. Translation: BAG63543.1 .
    AC078797 Genomic DNA. No translation available.
    BC002368 mRNA. Translation: AAH02368.1 .
    BC002997 mRNA. Translation: AAH02997.1 .
    BC007897 mRNA. Translation: AAH07897.1 .
    U12596 mRNA. Translation: AAA87705.1 . Different initiation.
    X86446 mRNA. Translation: CAA60167.1 .
    CCDSi CCDS3258.1. [Q13200-1 ]
    CCDS63853.1. [Q13200-3 ]
    CCDS63854.1. [Q13200-2 ]
    RefSeqi NP_001265637.1. NM_001278708.1.
    NP_001265638.1. NM_001278709.1.
    NP_002799.3. NM_002808.4.
    UniGenei Hs.518464.

    3D structure databases

    ProteinModelPortali Q13200.
    SMRi Q13200. Positions 56-908.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111681. 121 interactions.
    IntActi Q13200. 117 interactions.
    MINTi MINT-1142723.
    STRINGi 9606.ENSP00000310129.

    Chemistry

    DrugBanki DB00188. Bortezomib.

    PTM databases

    PhosphoSitei Q13200.

    Polymorphism databases

    DMDMi 6174930.

    Proteomic databases

    MaxQBi Q13200.
    PaxDbi Q13200.
    PeptideAtlasi Q13200.
    PRIDEi Q13200.

    Protocols and materials databases

    DNASUi 5708.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000310118 ; ENSP00000310129 ; ENSG00000175166 . [Q13200-1 ]
    ENST00000435761 ; ENSP00000402618 ; ENSG00000175166 . [Q13200-2 ]
    ENST00000439383 ; ENSP00000416028 ; ENSG00000175166 . [Q13200-3 ]
    GeneIDi 5708.
    KEGGi hsa:5708.
    UCSCi uc003fnn.1. human. [Q13200-1 ]

    Organism-specific databases

    CTDi 5708.
    GeneCardsi GC03P184016.
    HGNCi HGNC:9559. PSMD2.
    HPAi HPA045192.
    MIMi 606223. gene.
    neXtProti NX_Q13200.
    PharmGKBi PA33905.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5110.
    HOVERGENi HBG001842.
    InParanoidi Q13200.
    KOi K03028.
    OMAi IAQGLTH.
    OrthoDBi EOG70KGNV.
    PhylomeDBi Q13200.
    TreeFami TF105739.

    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 PSMD2. human.
    GeneWikii PSMD2.
    GenomeRNAii 5708.
    NextBioi 22178.
    PROi Q13200.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13200.
    Bgeei Q13200.
    CleanExi HS_PSMD2.
    Genevestigatori Q13200.

    Family and domain databases

    InterProi IPR016643. 26S_Psome_Rpn1.
    IPR016024. ARM-type_fold.
    IPR002015. Proteasome/cyclosome_rpt.
    [Graphical view ]
    Pfami PF01851. PC_rep. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF015965. 26S_Psome_Rpn1. 1 hit.
    SUPFAMi SSF48371. SSF48371. 4 hits.
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning and functional analysis of the p97 subunit of the 26S proteasome, a polypeptide identical to the type-1 tumor-necrosis-factor-receptor-associated protein-2/55.11."
      Tsurumi C., Shimizu Y., Saeki M., Kato S., DeMartino G.N., Slaughter C.A., Fujimuro M., Yokosawa H., Yamasaki M., Hendil K.B., Toh-e A., Tanahashi N., Tanaka K.
      Eur. J. Biochem. 239:912-921(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 49-66; 81-85; 91-117; 138-145; 148-158; 182-193; 209-229; 438-441 AND 471-481.
      Tissue: Fibrosarcoma.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TYR-724.
    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 2 AND 3), VARIANT ASP-313.
      Tissue: Testis.
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [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], VARIANT TYR-724.
      Tissue: Lung, Muscle and Skin.
    6. "Two-hybrid cloning of a gene encoding TNF receptor-associated protein 2, a protein that interacts with the intracellular domain of the type 1 TNF receptor: identity with subunit 2 of the 26S protease."
      Dunbar J.D., Song H.Y., Guo D., Wu L.-W., Donner D.B.
      J. Immunol. 158:4252-4259(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-908.
    7. "A protein related to a proteasomal subunit binds to the intracellular domain of the p55 TNF receptor upstream to its 'death domain'."
      Boldin M.P., Mett I.L., Wallach D.
      FEBS Lett. 367:39-44(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-908.
      Tissue: Liver.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-24; SER-29 AND TYR-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-16 AND SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-24 AND SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPSMD2_HUMAN
    AccessioniPrimary (citable) accession number: Q13200
    Secondary accession number(s): B4DX07
    , B4DXY1, E7EW34, E9PCS3, Q12932, Q15321, Q53XQ4, Q96I12
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 148 of the entry and version 3 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 3
      Human chromosome 3: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3