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Protein

Proteasomal ubiquitin receptor ADRM1

Gene

Adrm1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a proteasomal ubiquitin receptor. Recruits and activates the deubiquitinating enzyme UCHL5 at the 26S proteasome (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

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
Rpn13 homolog
Gene namesi
Name:Adrm1
Synonyms:Gp110
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi69248. Adrm1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 407406Proteasomal ubiquitin receptor ADRM1PRO_0000020633Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Cross-linki34 – 34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei140 – 1401PhosphoserineBy similarity
Modified residuei211 – 2111PhosphoserineBy similarity
Modified residuei217 – 2171PhosphothreonineBy similarity
Modified residuei405 – 4051PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9JMB5.
PRIDEiQ9JMB5.

PTM databases

iPTMnetiQ9JMB5.
PhosphoSiteiQ9JMB5.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

GenevisibleiQ9JMB5. RN.

Interactioni

Subunit structurei

Interacts with PSMD1, ubiquitin and UCHL5.By similarity

Protein-protein interaction databases

BioGridi249259. 2 interactions.
IntActiQ9JMB5. 1 interaction.
STRINGi10116.ENSRNOP00000010087.

Structurei

3D structure databases

ProteinModelPortaliQ9JMB5.
SMRiQ9JMB5. Positions 22-130.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 132131Interaction with PSMD1By similarityAdd
BLAST
Regioni362 – 40746Interaction with UCHL5By similarityAdd
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

eggNOGiKOG3037. Eukaryota.
ENOG410XSJJ. LUCA.
GeneTreeiENSGT00390000013839.
HOGENOMiHOG000005947.
HOVERGENiHBG073518.
InParanoidiQ9JMB5.
OMAiKRVDQCK.
OrthoDBiEOG70KGQZ.
PhylomeDBiQ9JMB5.
TreeFamiTF313410.

Family and domain databases

InterProiIPR006773. 26S_Psome_Ubiquitin-recp_Rpn13.
IPR032368. RPN13_C.
[Graphical view]
PANTHERiPTHR12225. PTHR12225. 2 hits.
PfamiPF04683. Proteasom_Rpn13. 1 hit.
PF16550. RPN13_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9JMB5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTSGALFPS LVPGSRGSST KYLVEFRAGK MSLKGTTVTP DKRKGLVYIQ
60 70 80 90 100
QTDDSLIHFC WKDRTSGTVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA
110 120 130 140 150
GSKRLFFWMQ EPKTDQDEEH CRKVNECLNN PPMPGTLGAS GSSGHELSAL
160 170 180 190 200
GGEGGLQSLL GNMSHSQLMQ LIGPAGLGGL GGLGALTGPG LASLLGSSGP
210 220 230 240 250
PASSSSSSSR SQSAAVTPSS TTSSARATPA PSAPAAASAT SPSPAPSSGN
260 270 280 290 300
GTSTAASPTQ PIQLSDLQSI LATMNVPAGP GGSQQVDLAS VLTPEIMAPI
310 320 330 340 350
LANADVQERL LPYLPSGESL PQTAEEIQNT LTSPQFQQAL GMFSAALASG
360 370 380 390 400
QLGPLMCQFG LPAEAVEAAN KGDVEAFAKA MQNNAKSDPK EGDTKDKKDE

EEDMSLD
Length:407
Mass (Da):42,102
Last modified:May 1, 2007 - v2
Checksum:i811BFF38EFDE5F90
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201T → I in BAA92929 (PubMed:11018266).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032742 mRNA. Translation: BAA92929.1.
BC061773 mRNA. Translation: AAH61773.1.
RefSeqiNP_113896.1. NM_031708.1.
UniGeneiRn.9320.

Genome annotation databases

EnsembliENSRNOT00000091941; ENSRNOP00000074216; ENSRNOG00000055984.
GeneIDi65138.
KEGGirno:65138.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032742 mRNA. Translation: BAA92929.1.
BC061773 mRNA. Translation: AAH61773.1.
RefSeqiNP_113896.1. NM_031708.1.
UniGeneiRn.9320.

3D structure databases

ProteinModelPortaliQ9JMB5.
SMRiQ9JMB5. Positions 22-130.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249259. 2 interactions.
IntActiQ9JMB5. 1 interaction.
STRINGi10116.ENSRNOP00000010087.

PTM databases

iPTMnetiQ9JMB5.
PhosphoSiteiQ9JMB5.

Proteomic databases

PaxDbiQ9JMB5.
PRIDEiQ9JMB5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000091941; ENSRNOP00000074216; ENSRNOG00000055984.
GeneIDi65138.
KEGGirno:65138.

Organism-specific databases

CTDi11047.
RGDi69248. Adrm1.

Phylogenomic databases

eggNOGiKOG3037. Eukaryota.
ENOG410XSJJ. LUCA.
GeneTreeiENSGT00390000013839.
HOGENOMiHOG000005947.
HOVERGENiHBG073518.
InParanoidiQ9JMB5.
OMAiKRVDQCK.
OrthoDBiEOG70KGQZ.
PhylomeDBiQ9JMB5.
TreeFamiTF313410.

Miscellaneous databases

NextBioi613959.
PROiQ9JMB5.

Gene expression databases

GenevisibleiQ9JMB5. RN.

Family and domain databases

InterProiIPR006773. 26S_Psome_Ubiquitin-recp_Rpn13.
IPR032368. RPN13_C.
[Graphical view]
PANTHERiPTHR12225. PTHR12225. 2 hits.
PfamiPF04683. Proteasom_Rpn13. 1 hit.
PF16550. RPN13_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rat homologue of the human Mr 110000 antigen is the protein that expresses widely in various tissues."
    Nakane T., Inada Y., Itoh F., Chiba S.
    Biochim. Biophys. Acta 1493:378-382(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  2. "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: Prostate.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiADRM1_RAT
AccessioniPrimary (citable) accession number: Q9JMB5
Secondary accession number(s): Q6P795
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 1, 2007
Last modified: January 20, 2016
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.