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)

Q16186

- ADRM1_HUMAN

UniProt

Q16186 - ADRM1_HUMAN

Protein

Proteasomal ubiquitin receptor ADRM1

Gene

ADRM1

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 124 (01 Oct 2014)
      Sequence version 2 (23 Jan 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.5 Publications

    GO - Molecular functioni

    1. endopeptidase activator activity Source: UniProtKB
    2. protease binding Source: UniProtKB
    3. proteasome binding Source: UniProtKB
    4. protein binding Source: IntAct

    GO - Biological processi

    1. positive regulation of endopeptidase activity Source: GOC
    2. proteasome assembly Source: UniProtKB
    3. transcription elongation from RNA polymerase II promoter Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasomal ubiquitin receptor ADRM1
    Alternative name(s):
    110 kDa cell membrane glycoprotein
    Short name:
    Gp110
    Adhesion-regulating molecule 1
    Short name:
    ARM-1
    Proteasome regulatory particle non-ATPase 13
    Short name:
    hRpn13
    Rpn13 homolog
    Gene namesi
    Name:ADRM1
    Synonyms:GP110
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:15759. ADRM1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. integral component of plasma membrane Source: ProtInc
    3. membrane Source: ProtInc
    4. nucleus Source: HPA
    5. plasma membrane Source: HPA
    6. proteasome complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24599.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 407406Proteasomal ubiquitin receptor ADRM1PRO_0000020631Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine3 Publications
    Cross-linki34 – 34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
    Modified residuei211 – 2111Phosphoserine1 Publication
    Modified residuei217 – 2171Phosphothreonine2 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ16186.
    PaxDbiQ16186.
    PRIDEiQ16186.

    PTM databases

    PhosphoSiteiQ16186.

    Expressioni

    Gene expression databases

    BgeeiQ16186.
    CleanExiHS_ADRM1.
    GenevestigatoriQ16186.

    Organism-specific databases

    HPAiHPA042266.

    Interactioni

    Subunit structurei

    Interacts with PSMD1, ubiquitin and UCHL5.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DSK2P485104EBI-954387,EBI-6174From a different organism.
    Psmd14O355932EBI-954387,EBI-772796From a different organism.
    PSMD4P550362EBI-954387,EBI-359318
    RAD23BP547272EBI-954387,EBI-954531
    UBCP0CG4810EBI-954387,EBI-3390054
    UBQLN1Q9UMX04EBI-954387,EBI-741480
    UBQLN2Q9UHD93EBI-954387,EBI-947187
    UCHL5Q9Y5K517EBI-954387,EBI-1051183

    Protein-protein interaction databases

    BioGridi116235. 43 interactions.
    DIPiDIP-42668N.
    IntActiQ16186. 31 interactions.
    MINTiMINT-2869171.
    STRINGi9606.ENSP00000253003.

    Structurei

    Secondary structure

    1
    407
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 264
    Beta strandi28 – 4013
    Beta strandi45 – 517
    Beta strandi57 – 6610
    Beta strandi69 – 757
    Beta strandi79 – 846
    Beta strandi89 – 913
    Beta strandi93 – 986
    Turni99 – 1013
    Beta strandi104 – 1096
    Helixi114 – 1163
    Helixi117 – 12913
    Turni191 – 1955
    Beta strandi202 – 2043
    Beta strandi249 – 2535
    Turni254 – 2563
    Helixi266 – 2738
    Beta strandi276 – 2783
    Beta strandi282 – 2843
    Helixi285 – 2917
    Turni294 – 2963
    Helixi298 – 3025
    Helixi304 – 31310
    Helixi324 – 3285
    Helixi334 – 34815
    Beta strandi350 – 3523
    Helixi353 – 3586
    Helixi363 – 3719
    Helixi374 – 38411
    Beta strandi386 – 3883

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KQZNMR-A253-407[»]
    2KR0NMR-A1-407[»]
    2L5VNMR-A260-407[»]
    ProteinModelPortaliQ16186.
    SMRiQ16186. Positions 1-407.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16186.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 130109PHAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 132131Interaction with PSMD1Add
    BLAST
    Regioni362 – 40746Interaction with UCHL5Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi135 – 20268Gly-richAdd
    BLAST
    Compositional biasi193 – 25765Ser-richAdd
    BLAST
    Compositional biasi203 – 21311Poly-SerAdd
    BLAST

    Domaini

    The PH domain mediates interactions with PSMD1 and ubiquitin. Preferential binding to the proximal subunit of K48-linked diubiquitin allows UCHL5 access to the distal subunit By similarity.By similarity

    Sequence similaritiesi

    Belongs to the ADRM1 family.Curated
    Contains 1 PH domain.Curated

    Phylogenomic databases

    eggNOGiNOG288027.
    HOGENOMiHOG000005947.
    HOVERGENiHBG073518.
    InParanoidiQ16186.
    OMAiQNNAKPE.
    OrthoDBiEOG70KGQZ.
    PhylomeDBiQ16186.
    TreeFamiTF313410.

    Family and domain databases

    InterProiIPR006773. 26S_Psome_Ubiquitin-recp_Rpn13.
    [Graphical view]
    PANTHERiPTHR12225. PTHR12225. 1 hit.
    PfamiPF04683. Proteasom_Rpn13. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q16186-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTSGALFPS LVPGSRGASN KYLVEFRAGK MSLKGTTVTP DKRKGLVYIQ    50
    QTDDSLIHFC WKDRTSGNVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA 100
    GSKRLFFWMQ EPKTDQDEEH CRKVNEYLNN PPMPGALGAS GSSGHELSAL 150
    GGEGGLQSLL GNMSHSQLMQ LIGPAGLGGL GGLGALTGPG LASLLGSSGP 200
    PGSSSSSSSR SQSAAVTPSS TTSSTRATPA PSAPAAASAT SPSPAPSSGN 250
    GASTAASPTQ PIQLSDLQSI LATMNVPAGP AGGQQVDLAS VLTPEIMAPI 300
    LANADVQERL LPYLPSGESL PQTADEIQNT LTSPQFQQAL GMFSAALASG 350
    QLGPLMCQFG LPAEAVEAAN KGDVEAFAKA MQNNAKPEQK EGDTKDKKDE 400
    EEDMSLD 407
    Length:407
    Mass (Da):42,153
    Last modified:January 23, 2002 - v2
    Checksum:i2D38811DCA231864
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti142 – 1421S → T in BAA11023. (PubMed:8033103)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D64154 mRNA. Translation: BAA11023.1.
    AL354836 Genomic DNA. Translation: CAC22308.1.
    BR000321 mRNA. Translation: FAA00246.1.
    BC010733 mRNA. Translation: AAH10733.1.
    BC017245 mRNA. Translation: AAH17245.1.
    CCDSiCCDS13496.1.
    PIRiI52703.
    RefSeqiNP_001268366.1. NM_001281437.1.
    NP_001268367.1. NM_001281438.1.
    NP_008933.2. NM_007002.3.
    NP_783163.1. NM_175573.2.
    XP_005260314.1. XM_005260257.1.
    UniGeneiHs.90107.

    Genome annotation databases

    EnsembliENST00000253003; ENSP00000253003; ENSG00000130706.
    GeneIDi11047.
    KEGGihsa:11047.
    UCSCiuc002ycn.3. human.

    Polymorphism databases

    DMDMi20141265.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D64154 mRNA. Translation: BAA11023.1 .
    AL354836 Genomic DNA. Translation: CAC22308.1 .
    BR000321 mRNA. Translation: FAA00246.1 .
    BC010733 mRNA. Translation: AAH10733.1 .
    BC017245 mRNA. Translation: AAH17245.1 .
    CCDSi CCDS13496.1.
    PIRi I52703.
    RefSeqi NP_001268366.1. NM_001281437.1.
    NP_001268367.1. NM_001281438.1.
    NP_008933.2. NM_007002.3.
    NP_783163.1. NM_175573.2.
    XP_005260314.1. XM_005260257.1.
    UniGenei Hs.90107.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KQZ NMR - A 253-407 [» ]
    2KR0 NMR - A 1-407 [» ]
    2L5V NMR - A 260-407 [» ]
    ProteinModelPortali Q16186.
    SMRi Q16186. Positions 1-407.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116235. 43 interactions.
    DIPi DIP-42668N.
    IntActi Q16186. 31 interactions.
    MINTi MINT-2869171.
    STRINGi 9606.ENSP00000253003.

    PTM databases

    PhosphoSitei Q16186.

    Polymorphism databases

    DMDMi 20141265.

    Proteomic databases

    MaxQBi Q16186.
    PaxDbi Q16186.
    PRIDEi Q16186.

    Protocols and materials databases

    DNASUi 11047.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000253003 ; ENSP00000253003 ; ENSG00000130706 .
    GeneIDi 11047.
    KEGGi hsa:11047.
    UCSCi uc002ycn.3. human.

    Organism-specific databases

    CTDi 11047.
    GeneCardsi GC20P060877.
    HGNCi HGNC:15759. ADRM1.
    HPAi HPA042266.
    MIMi 610650. gene.
    neXtProti NX_Q16186.
    PharmGKBi PA24599.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG288027.
    HOGENOMi HOG000005947.
    HOVERGENi HBG073518.
    InParanoidi Q16186.
    OMAi QNNAKPE.
    OrthoDBi EOG70KGQZ.
    PhylomeDBi Q16186.
    TreeFami TF313410.

    Miscellaneous databases

    EvolutionaryTracei Q16186.
    GeneWikii ADRM1.
    GenomeRNAii 11047.
    NextBioi 41984.
    PROi Q16186.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q16186.
    CleanExi HS_ADRM1.
    Genevestigatori Q16186.

    Family and domain databases

    InterProi IPR006773. 26S_Psome_Ubiquitin-recp_Rpn13.
    [Graphical view ]
    PANTHERi PTHR12225. PTHR12225. 1 hit.
    Pfami PF04683. Proteasom_Rpn13. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of the complementary DNA of an M(r) 110,000 antigen expressed by human gastric carcinoma cells and upregulated by gamma-interferon."
      Shimada S., Ogawa M., Takahashi M., Schlom J., Greiner J.W.
      Cancer Res. 54:3831-3836(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "A novel proteasome-interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes."
      Hamazaki J., Iemura S., Natsume T., Yashiroda H., Tanaka K., Murata S.
      EMBO J. 25:4524-4536(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PSMD1 AND UCHL5, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    3. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
      Tissue: Brain and Pancreas.
    5. "hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37."
      Qiu X.-B., Ouyang S.-Y., Li C.-J., Miao S., Wang L., Goldberg A.L.
      EMBO J. 25:5742-5753(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH UCHL5, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    6. "Adrm1, a putative cell adhesion regulating protein, is a novel proteasome-associated factor."
      Joergensen J.P., Lauridsen A.-M., Kristensen P., Dissing K., Johnsen A.H., Hendil K.B., Hartmann-Petersen R.
      J. Mol. Biol. 360:1043-1052(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH 26S PROTEASOME, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1."
      Yao T., Song L., Xu W., DeMartino G.N., Florens L., Swanson S.K., Washburn M.P., Conaway R.C., Conaway J.W., Cohen R.E.
      Nat. Cell Biol. 8:994-1002(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PSMD1 AND UCHL5, IDENTIFICATION BY MASS SPECTROMETRY.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. Cited for: FUNCTION, INTERACTION WITH UBIQUITIN.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND THR-217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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 THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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 THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiADRM1_HUMAN
    AccessioniPrimary (citable) accession number: Q16186
    Secondary accession number(s): A0PKB1, Q96FJ7, Q9H1P2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2002
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 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

    Caution

    Although initially described as a cell membrane glycoprotein, ADRM1 is intracellular and non-glycosylated, and has probably no direct role in cell adhesion.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3