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Q16186

- ADRM1_HUMAN

UniProt

Q16186 - ADRM1_HUMAN

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Protein
Proteasomal ubiquitin receptor ADRM1
Gene
ADRM1, GP110
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

Cytoplasm. Nucleus 3 Publications

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24599.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 407406Proteasomal ubiquitin receptor ADRM1
PRO_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. 42 interactions.
DIPiDIP-42668N.
IntActiQ16186. 29 interactions.
MINTiMINT-2869171.
STRINGi9606.ENSP00000253003.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ16186.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 132131Interaction with PSMD1
Add
BLAST
Regioni362 – 40746Interaction with UCHL5
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Belongs to the ADRM1 family.
Contains 1 PH domain.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti142 – 1421S → T in BAA11023. 1 Publication

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. 42 interactions.
DIPi DIP-42668N.
IntActi Q16186. 29 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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 123 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.

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

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