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Protein

Proteasomal ubiquitin receptor ADRM1

Gene

Adrm1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.2 Publications

GO - Molecular functioni

GO - Biological processi

  • adipose tissue development Source: BHF-UCL
  • follicle-stimulating hormone signaling pathway Source: BHF-UCL
  • oogenesis Source: BHF-UCL
  • ovarian follicle development Source: BHF-UCL
  • positive regulation of endopeptidase activity Source: MGI
  • positive regulation of growth hormone receptor signaling pathway Source: BHF-UCL
  • proteasome assembly Source: MGI
  • regulation of T cell differentiation in thymus Source: BHF-UCL
  • seminiferous tubule development Source: BHF-UCL
  • Sertoli cell development Source: BHF-UCL
  • spermatid development Source: BHF-UCL
  • thymus development Source: BHF-UCL
  • transcription elongation from RNA polymerase II promoter Source: MGI
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1929289. Adrm1.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus By similarity

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_0000020632Add
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 – 4051PhosphoserineBy similarity

Post-translational modificationi

Not N-glycosylated.
Not O-glycosylated.Curated

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9JKV1.
MaxQBiQ9JKV1.
PaxDbiQ9JKV1.
PRIDEiQ9JKV1.

PTM databases

iPTMnetiQ9JKV1.
PhosphoSiteiQ9JKV1.

Expressioni

Tissue specificityi

Present in all tissues examined (at protein level).2 Publications

Gene expression databases

BgeeiQ9JKV1.
CleanExiMM_ADRM1.
GenevisibleiQ9JKV1. MM.

Interactioni

Subunit structurei

Interacts with PSMD1, ubiquitin and UCHL5.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi207978. 8 interactions.
DIPiDIP-60625N.
IntActiQ9JKV1. 14 interactions.
STRINGi10090.ENSMUSP00000050076.

Structurei

Secondary structure

1
407
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 3411Combined sources
Beta strandi37 – 404Combined sources
Beta strandi45 – 517Combined sources
Beta strandi57 – 637Combined sources
Turni64 – 663Combined sources
Beta strandi69 – 746Combined sources
Beta strandi79 – 846Combined sources
Beta strandi93 – 986Combined sources
Turni99 – 1013Combined sources
Beta strandi104 – 1096Combined sources
Beta strandi111 – 1144Combined sources
Helixi117 – 12913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R2YX-ray1.70A2-150[»]
2Z59NMR-A22-130[»]
ProteinModelPortaliQ9JKV1.
SMRiQ9JKV1. Positions 1-407.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JKV1.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 132131Interaction with PSMD1Add
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.

Sequence similaritiesi

Belongs to the ADRM1 family.Curated
Contains 1 PH domain.Curated

Phylogenomic databases

eggNOGiKOG3037. Eukaryota.
ENOG410XSJJ. LUCA.
GeneTreeiENSGT00390000013839.
HOGENOMiHOG000005947.
HOVERGENiHBG073518.
InParanoidiQ9JKV1.
OMAiKRVDQCK.
OrthoDBiEOG70KGQZ.
PhylomeDBiQ9JKV1.
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.

Q9JKV1-1 [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 PPMPGSLGAS GSSGHELSAL
160 170 180 190 200
GGEGGLQSLL GNMSHSQLMQ LIGPAGLGGL GGLGALTGPG LASLLGSSGP
210 220 230 240 250
PASSSSSSSR SQSAAVTPSS STSSARATPA PSAPAAASAT SPSPAPSSGN
260 270 280 290 300
GTSTAASPTQ PIQLSDLQSI LATMNVPAGP GGSQQVDLAS VLTPEIMAPI
310 320 330 340 350
LANADVQERL LPYLPSGESL PQTADEIQNT LTSPQFQQAL GMFSAALASG
360 370 380 390 400
QLGPLMCQFG LPAEAVEAAN KGDVEAFAKA MQNNAKSDPK EGDTKDKKDE

EEDMSLD
Length:407
Mass (Da):42,060
Last modified:May 1, 2007 - v2
Checksum:i210AFDF7379C962D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091M → I in BAC35889 (PubMed:16141072).Curated
Sequence conflicti171 – 1711L → I in BAE26653 (PubMed:16141072).Curated
Sequence conflicti226 – 2261R → S in BAC35889 (PubMed:16141072).Curated
Sequence conflicti359 – 3591F → I in AAF33401 (PubMed:10919708).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF225959 mRNA. Translation: AAF33401.1.
AK075674 mRNA. Translation: BAC35889.1.
AK145474 mRNA. Translation: BAE26457.1.
AK145792 mRNA. Translation: BAE26653.1.
AK166878 mRNA. Translation: BAE39089.1.
AL663027 Genomic DNA. Translation: CAM16214.1.
BC008974 mRNA. Translation: AAH08974.1.
BC031517 mRNA. Translation: AAH31517.1.
CCDSiCCDS17171.1.
RefSeqiNP_062796.2. NM_019822.3.
UniGeneiMm.316654.
Mm.379082.

Genome annotation databases

EnsembliENSMUST00000061437; ENSMUSP00000050076; ENSMUSG00000039041.
GeneIDi56436.
KEGGimmu:56436.
UCSCiuc008oin.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF225959 mRNA. Translation: AAF33401.1.
AK075674 mRNA. Translation: BAC35889.1.
AK145474 mRNA. Translation: BAE26457.1.
AK145792 mRNA. Translation: BAE26653.1.
AK166878 mRNA. Translation: BAE39089.1.
AL663027 Genomic DNA. Translation: CAM16214.1.
BC008974 mRNA. Translation: AAH08974.1.
BC031517 mRNA. Translation: AAH31517.1.
CCDSiCCDS17171.1.
RefSeqiNP_062796.2. NM_019822.3.
UniGeneiMm.316654.
Mm.379082.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R2YX-ray1.70A2-150[»]
2Z59NMR-A22-130[»]
ProteinModelPortaliQ9JKV1.
SMRiQ9JKV1. Positions 1-407.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207978. 8 interactions.
DIPiDIP-60625N.
IntActiQ9JKV1. 14 interactions.
STRINGi10090.ENSMUSP00000050076.

PTM databases

iPTMnetiQ9JKV1.
PhosphoSiteiQ9JKV1.

Proteomic databases

EPDiQ9JKV1.
MaxQBiQ9JKV1.
PaxDbiQ9JKV1.
PRIDEiQ9JKV1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000061437; ENSMUSP00000050076; ENSMUSG00000039041.
GeneIDi56436.
KEGGimmu:56436.
UCSCiuc008oin.1. mouse.

Organism-specific databases

CTDi11047.
MGIiMGI:1929289. Adrm1.

Phylogenomic databases

eggNOGiKOG3037. Eukaryota.
ENOG410XSJJ. LUCA.
GeneTreeiENSGT00390000013839.
HOGENOMiHOG000005947.
HOVERGENiHBG073518.
InParanoidiQ9JKV1.
OMAiKRVDQCK.
OrthoDBiEOG70KGQZ.
PhylomeDBiQ9JKV1.
TreeFamiTF313410.

Miscellaneous databases

EvolutionaryTraceiQ9JKV1.
NextBioi312618.
PROiQ9JKV1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JKV1.
CleanExiMM_ADRM1.
GenevisibleiQ9JKV1. MM.

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. "Functional cloning of ARM-1, an adhesion-regulating molecule upregulated in metastatic tumor cells."
    Simins A.B., Weighardt H., Weidner K.M., Weidle U.H., Holzmann B.
    Clin. Exp. Metastasis 17:641-648(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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].
    Strain: Czech II.
    Tissue: Mammary tumor.
  5. "Adhesion properties of adhesion-regulating molecule 1 protein on endothelial cells."
    Lamerant N., Kieda C.
    FEBS J. 272:1833-1844(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, LACK OF GLYCOSYLATION.
  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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction."
    Schreiner P., Chen X., Husnjak K., Randles L., Zhang N., Elsasser S., Finley D., Dikic I., Walters K.J., Groll M.
    Nature 453:548-552(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 22-130, X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-150, FUNCTION, PH DOMAIN, INTERACTION WITH UBIQUITIN; UCHL5 AND PSMD1.

Entry informationi

Entry nameiADRM1_MOUSE
AccessioniPrimary (citable) accession number: Q9JKV1
Secondary accession number(s): Q3UKZ8, Q8BPH8, Q922A7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 1, 2007
Last modified: April 13, 2016
This is version 107 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.