Q16186 (ADRM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ADRM1
Synonyms:	GP110

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	407 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11
Subunit structure	Interacts with PSMD1, ubiquitin and UCHL5. Ref.2 Ref.5 Ref.6 Ref.8 Ref.11
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.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteasome assembly Inferred from direct assay Ref.2. Source: UniProtKB transcription elongation from RNA polymerase II promoter Inferred from mutant phenotype PubMed 11818576. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc nucleus Inferred from direct assay. Source: HPA proteasome complex Inferred from direct assay Ref.2. Source: UniProtKB
Molecular_function	endopeptidase activator activity Inferred from direct assay Ref.2. Source: UniProtKB proteasome binding Inferred from direct assay PubMed 18162577. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
UCHL5	Q9Y5K5	7	EBI-954387,EBI-1051183

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 407

407

Proteasomal ubiquitin receptor ADRM1

PRO_0000020631

Regions

Domain

22 – 130

109

PH

Region

1 – 132

132

Interaction with PSMD1

Region

362 – 407

46

Interaction with UCHL5

Compositional bias

135 – 202

68

Gly-rich

Compositional bias

193 – 257

65

Ser-rich

Compositional bias

203 – 213

11

Poly-Ser

Amino acid modifications

Modified residue

211

1

Phosphoserine Ref.12

Modified residue

213

1

Phosphoserine By similarity

Modified residue

217

1

Phosphothreonine Ref.7 Ref.12

Cross-link

34

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.10

Experimental info

Sequence conflict

142

1

S → T in BAA11023. Ref.1

Secondary structure

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407

Helix Strand Turn

Details...

Beta strand

23 – 26

4

Beta strand

28 – 40

13

Beta strand

45 – 51

7

Beta strand

57 – 66

10

Beta strand

69 – 75

7

Beta strand

79 – 84

6

Beta strand

89 – 91

3

Beta strand

93 – 98

6

Turn

99 – 101

3

Beta strand

104 – 109

6

Helix

114 – 116

3

Helix

117 – 129

13

Turn

191 – 195

5

Beta strand

202 – 204

3

Beta strand

249 – 253

5

Turn

254 – 256

3

Helix

266 – 273

8

Beta strand

276 – 278

3

Beta strand

282 – 284

3

Helix

285 – 291

7

Turn

294 – 296

3

Helix

298 – 302

5

Helix

304 – 313

10

Helix

324 – 328

5

Helix

334 – 348

15

Beta strand

350 – 352

3

Helix

353 – 358

6

Helix

363 – 371

9

Helix

374 – 384

11

Beta strand

386 – 388

3

Sequences

	Sequence		Length	Mass (Da)
	Q16186 [UniParc]. Last modified January 23, 2002. Version 2. Checksum: 2D38811DCA231864	FASTA	407	42,153
	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

References

	« Hide 'large scale' referencesShow '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, 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, 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, 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, MASS SPECTROMETRY. 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, 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]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-34, MASS SPECTROMETRY.
[11]	"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.
[12]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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].
+	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.

IPI

IPI00033030.

PIR

I52703.

RefSeq

NP_008933.2. NM_007002.2.
NP_783163.1. NM_175573.1.

UniGene

Hs.90107.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KQZ	NMR	-	A	253-407	[»]
2KR0	NMR	-	A	1-407	[»]
2L5V	NMR	-	A	260-407	[»]

ProteinModelPortal

Q16186.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-42668N.

IntAct

Q16186. 10 interactions.

MINT

MINT-2869171.

STRING

9606.ENSP00000253003.

PTM databases

PhosphoSite

Q16186.

Polymorphism databases

DMDM

20141265.

Proteomic databases

PaxDb

Q16186.

PRIDE

Q16186.

Protocols and materials databases

DNASU

11047.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000253003; ENSP00000253003; ENSG00000130706.

GeneID

11047.

KEGG

hsa:11047.

UCSC

uc002ycn.3. human.

Organism-specific databases

CTD

11047.

GeneCards

GC20P060877.

HGNC

HGNC:15759. ADRM1.

HPA

HPA042266.

MIM

610650. gene.

neXtProt

NX_Q16186.

PharmGKB

PA24599.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG288027.

HOGENOM

HOG000005947.

HOVERGEN

HBG073518.

InParanoid

Q16186.

OMA

MNVPAGP.

OrthoDB

EOG4QZ7MN.

Gene expression databases

Bgee

Q16186.

CleanEx

HS_ADRM1.

Genevestigator

Q16186.

GermOnline

ENSG00000130706. Homo sapiens.

Family and domain databases

InterPro

IPR006773. 26S_Psome_Ubiquitin-recp_Rpn13.
[Graphical view]

PANTHER

PTHR12225. PTHR12225. 1 hit.

Pfam

PF04683. Proteasom_Rpn13. 1 hit.
[Graphical view]

PROSITE

PS50003. PH_DOMAIN. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q16186.

GenomeRNAi

11047.

NextBio

41984.

SOURCE

Search...

Entry information

Entry name

ADRM1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.