Reviewed, UniProtKB/Swiss-Prot Q16186 (ADRM1_HUMAN)

Names and origin

Protein names

Recommended name:
    Protein ADRM1
Alternative name(s):
    Adhesion-regulating molecule 1
    110 kDa cell membrane glycoprotein
    Gp110
    Proteasome regulatory particle non-ATPase 13
      Short name=hRpn13

Gene names

Name:	ADRM1
Synonyms:	GP110

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	407 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.
Subunit structure	Interacts with PSMD1 and UCHL5.
Subcellular location	Cytoplasm. Nucleus.
Sequence similarities	Belongs to the ADRM1 family.
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	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	RNA elongation from RNA polymerase II promoter Inferred from mutant phenotype. Source: UniProtKB proteasome assembly Ref.2 Inferred from direct assay. Source: UniProtKB
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-KW integral to plasma membrane Ref.1 Traceable author statement. Source: ProtInc membrane fraction Ref.1 Traceable author statement. Source: ProtInc nucleus Inferred from electronic annotation. Source: InterPro proteasome complex Ref.2 Inferred from direct assay. Source: UniProtKB
Molecular function	proteasome activator activity Ref.2 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 407	406	Protein ADRM1		PRO_0000020631
Regions
	Region	2 – 132	131	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	2	1	N-acetylthreonine
	Modified residue	211	1	Phosphoserine
	Modified residue	213	1	Phosphoserine By similarity
	Modified residue	217	1	Phosphothreonine
	Modified residue	220	1	Phosphoserine
	Modified residue	405	1	Phosphoserine
Experimental info
	Sequence conflict	142	1	S → T in BAA11023. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q16186-1 [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: 8033103] [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: 16990800] [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: 11780052] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Pancreas.
[5]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, MASS SPECTROMETRY. Tissue: Epithelium.
[6]	"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: 17139257] [Abstract] Cited for: FUNCTION, INTERACTION WITH UCHL5, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[7]	"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: 16815440] [Abstract] Cited for: FUNCTION, INTERACTION WITH 26S PROTEASOME, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[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: 16906146] [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: 17323924] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, MASS SPECTROMETRY.
[10]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; THR-217; SER-220 AND SER-405, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
PIR	I52703.
RefSeq	NP_008933.2. NP_783163.1.
UniGene	Hs.90107
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q16186.
PTM databases
PhosphoSite	Q16186.
Genome annotation databases
Ensembl	ENSG00000130706. Homo sapiens. [Contig view]
GeneID	11047.
KEGG	hsa:11047.
Organism-specific databases
H-InvDB	HIX0015977.
HGNC	HGNC:15759. ADRM1.
MIM	610650. gene.
PharmGKB	PA24599.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	Q16186.
HOVERGEN	Q16186.
Gene expression databases
CleanEx	HS_ADRM1.
GermOnline	ENSG00000130706. Homo sapiens.
Family and domain databases
InterPro	IPR006773. ARM_1. [Graphical view]
PANTHER	PTHR12225. ARM_1. 1 hit.
Pfam	PF04683. ARM_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
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:	November 25, 2008
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)