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Q16186 (ADRM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ADRM1
Synonyms:GP110
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity. Ref.2 Ref.5 Ref.6 Ref.8 Ref.10

Subunit structure

Interacts with PSMD1, ubiquitin and UCHL5. Ref.2 Ref.5 Ref.6 Ref.8 Ref.10

Subcellular location

Cytoplasm. Nucleus Ref.2 Ref.5 Ref.6.

Domain

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 similarities

Belongs to the ADRM1 family.

Contains 1 PH domain.

Caution

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

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 407406Proteasomal ubiquitin receptor ADRM1
PRO_0000020631

Regions

Domain22 – 130109PH
Region2 – 132131Interaction with PSMD1
Region362 – 40746Interaction with UCHL5
Compositional bias135 – 20268Gly-rich
Compositional bias193 – 25765Ser-rich
Compositional bias203 – 21311Poly-Ser

Amino acid modifications

Modified residue21N-acetylthreonine Ref.12 Ref.14 Ref.15
Modified residue2111Phosphoserine Ref.11
Modified residue2171Phosphothreonine Ref.7 Ref.11
Cross-link34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Experimental info

Sequence conflict1421S → T in BAA11023. Ref.1

Secondary structure

........................................................ 407
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16186 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 2D38811DCA231864

FASTA40742,153
        10         20         30         40         50         60 
MTTSGALFPS LVPGSRGASN KYLVEFRAGK MSLKGTTVTP DKRKGLVYIQ QTDDSLIHFC 

        70         80         90        100        110        120 
WKDRTSGNVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA GSKRLFFWMQ EPKTDQDEEH 

       130        140        150        160        170        180 
CRKVNEYLNN PPMPGALGAS GSSGHELSAL GGEGGLQSLL GNMSHSQLMQ LIGPAGLGGL 

       190        200        210        220        230        240 
GGLGALTGPG LASLLGSSGP PGSSSSSSSR SQSAAVTPSS TTSSTRATPA PSAPAAASAT 

       250        260        270        280        290        300 
SPSPAPSSGN GASTAASPTQ PIQLSDLQSI LATMNVPAGP AGGQQVDLAS VLTPEIMAPI 

       310        320        330        340        350        360 
LANADVQERL LPYLPSGESL PQTADEIQNT LTSPQFQQAL GMFSAALASG QLGPLMCQFG 

       370        380        390        400 
LPAEAVEAAN KGDVEAFAKA MQNNAKPEQK EGDTKDKKDE EEDMSLD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Proteasome subunit Rpn13 is a novel ubiquitin receptor."
Husnjak K., Elsasser S., Zhang N., Chen X., Randles L., Shi Y., Hofmann K., Walters K.J., Finley D., Dikic I.
Nature 453:481-488(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH UBIQUITIN.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI52703.
RefSeqNP_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.
UniGeneHs.90107.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KQZNMR-A253-407[»]
2KR0NMR-A1-407[»]
2L5VNMR-A260-407[»]
ProteinModelPortalQ16186.
SMRQ16186. Positions 1-407.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116235. 40 interactions.
DIPDIP-42668N.
IntActQ16186. 29 interactions.
MINTMINT-2869171.
STRING9606.ENSP00000253003.

PTM databases

PhosphoSiteQ16186.

Polymorphism databases

DMDM20141265.

Proteomic databases

PaxDbQ16186.
PRIDEQ16186.

Protocols and materials databases

DNASU11047.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253003; ENSP00000253003; ENSG00000130706.
GeneID11047.
KEGGhsa:11047.
UCSCuc002ycn.3. human.

Organism-specific databases

CTD11047.
GeneCardsGC20P060877.
HGNCHGNC:15759. ADRM1.
HPAHPA042266.
MIM610650. gene.
neXtProtNX_Q16186.
PharmGKBPA24599.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG288027.
HOGENOMHOG000005947.
HOVERGENHBG073518.
InParanoidQ16186.
OMAQNNAKPE.
OrthoDBEOG70KGQZ.
PhylomeDBQ16186.
TreeFamTF313410.

Gene expression databases

BgeeQ16186.
CleanExHS_ADRM1.
GenevestigatorQ16186.

Family and domain databases

InterProIPR006773. 26S_Psome_Ubiquitin-recp_Rpn13.
[Graphical view]
PANTHERPTHR12225. PTHR12225. 1 hit.
PfamPF04683. Proteasom_Rpn13. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ16186.
GeneWikiADRM1.
GenomeRNAi11047.
NextBio41984.
PROQ16186.
SOURCESearch...

Entry information

Entry nameADRM1_HUMAN
AccessionPrimary (citable) accession number: Q16186
Secondary accession number(s): A0PKB1, Q96FJ7, Q9H1P2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2002
Last modified: April 16, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM