Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y5V3 (MAGD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Melanoma-associated antigen D1
Alternative name(s):
MAGE tumor antigen CCF
MAGE-D1 antigen
Neurotrophin receptor-interacting MAGE homolog
Gene names
Name:MAGED1
Synonyms:NRAGE
ORF Names:PP2250, PRO2292
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length778 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the apoptotic response after nerve growth factor (NGF) binding in neuronal cells. Inhibits cell cycle progression, and facilitates NGFR-mediated apoptosis. May act as a regulator of the function of DLX family members. May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. Plays a role in the circadian rythm regulation. May act as RORA co-regulator, modulating the expression of core clock genes such as ARNTL/BMAL1 and NFIL3, induced, or NR1D1, repressed. Ref.11

Subunit structure

Interacts with DLX5, DLX7 and MSX2 and forms homomultimers. Interacts with UNC5A. Interacts with TRIM28 and PJA1. Interacts with NGFR/p75NTR and RORA. Ref.11

Subcellular location

Cytoplasm By similarity. Cell membrane; Peripheral membrane protein By similarity. Nucleus By similarity. Note: Expression shifts from the cytoplasm to the plasma membrane upon stimulation with NGF By similarity.

Tissue specificity

Expressed in bone marrow stromal cells from both multiple myeloma patients and healthy donors. Seems to be ubiquitously expressed.

Sequence similarities

Contains 1 MAGE domain.

Sequence caution

The sequence AAD31421.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAG35551.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processBiological rhythms
Ubl conjugation pathway
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   Molecular functionTumor antigen
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Traceable author statement. Source: Reactome

apoptotic signaling pathway

Traceable author statement. Source: Reactome

circadian regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of epithelial cell proliferation

Inferred from direct assay PubMed 15930293. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

positive regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of branching involved in ureteric bud morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

regulation of apoptotic process

Traceable author statement PubMed 15930293. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Traceable author statement PubMed 15930293. Source: UniProtKB

   Cellular_componentchromatin

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from direct assay PubMed 15930293. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 15930293. Source: UniProtKB

transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PJA1Q8NG274EBI-716006,EBI-714606

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y5V3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9Y5V3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     15-15: Q → QNPDACRAVCHPLPQPPASTLPLSAFPTLCDPPYSQLRDPPAVLSCYCTPLGASPAP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 778778Melanoma-associated antigen D1
PRO_0000156723

Regions

Repeat296 – 30161
Repeat302 – 30762
Repeat308 – 31363
Repeat332 – 33764
Repeat338 – 34365
Repeat344 – 34966
Repeat350 – 35567
Repeat356 – 36168
Repeat362 – 36769
Repeat368 – 373610
Repeat374 – 379611
Repeat380 – 385612
Repeat386 – 391613
Repeat392 – 397614
Repeat398 – 403615
Repeat404 – 409616
Repeat410 – 415617
Repeat416 – 421618
Repeat422 – 427619
Repeat428 – 432520; approximate
Repeat433 – 438621
Repeat439 – 444622
Domain471 – 669199MAGE
Region296 – 44414922 X 6 AA tandem repeats of W-[PQ]-X-P-X-X
Compositional bias279 – 452174Pro-rich

Amino acid modifications

Modified residue921Phosphotyrosine Ref.10

Natural variations

Alternative sequence151Q → QNPDACRAVCHPLPQPPAST LPLSAFPTLCDPPYSQLRDP PAVLSCYCTPLGASPAP in isoform 2.
VSP_009286
Natural variant2381L → M.
Corresponds to variant rs12689461 [ dbSNP | Ensembl ].
VAR_060070

Experimental info

Sequence conflict1191P → S in AAG09704. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 26, 2005. Version 3.
Checksum: D818690052D166CE

FASTA77886,161
        10         20         30         40         50         60 
MAQKMDCGAG LLGFQAEASV EDSALLMQTL MEAIQISEAP PTNQATAAAS PQSSQPPTAN 

        70         80         90        100        110        120 
EMADIQVSAA AARPKSAFKV QNATTKGPNG VYDFSQAHNA KDVPNTQPKA AFKSQNATPK 

       130        140        150        160        170        180 
GPNAAYDFSQ AATTGELAAN KSEMAFKAQN ATTKVGPNAT YNFSQSLNAN DLANSRPKTP 

       190        200        210        220        230        240 
FKAWNDTTKA PTADTQTQNV NQAKMATSQA DIETDPGISE PDGATAQTSA DGSQAQNLES 

       250        260        270        280        290        300 
RTIIRGKRTR KINNLNVEEN SSGDQRRAPL AAGTWRSAPV PVTTQNPPGA PPNVLWQTPL 

       310        320        330        340        350        360 
AWQNPSGWQN QTARQTPPAR QSPPARQTPP AWQNPVAWQN PVIWPNPVIW QNPVIWPNPI 

       370        380        390        400        410        420 
VWPGPVVWPN PLAWQNPPGW QTPPGWQTPP GWQGPPDWQG PPDWPLPPDW PLPPDWPLPT 

       430        440        450        460        470        480 
DWPLPPDWIP ADWPIPPDWQ NLRPSPNLRP SPNSRASQNP GAAQPRDVAL LQERANKLVK 

       490        500        510        520        530        540 
YLMLKDYTKV PIKRSEMLRD IIREYTDVYP EIIERACFVL EKKFGIQLKE IDKEEHLYIL 

       550        560        570        580        590        600 
ISTPESLAGI LGTTKDTPKL GLLLVILGVI FMNGNRASEA VLWEALRKMG LRPGVRHPLL 

       610        620        630        640        650        660 
GDLRKLLTYE FVKQKYLDYR RVPNSNPPEY EFLWGLRSYH ETSKMKVLRF IAEVQKRDPR 

       670        680        690        700        710        720 
DWTAQFMEAA DEALDALDAA AAEAEARAEA RTRMGIGDEA VSGPWSWDDI EFELLTWDEE 

       730        740        750        760        770 
GDFGDPWSRI PFTFWARYHQ NARSRFPQTF AGPIIGPGGT ASANFAANFG AIGFFWVE 

« Hide

Isoform 2 [UniParc].

Checksum: CD8E13CE9B35EA7C
Show »

FASTA83491,959

References

« Hide 'large scale' references
[1]"NRAGE, a novel MAGE protein, interacts with the p75 neurotrophin receptor and facilitates nerve growth factor dependent apoptosis."
Salehi A.H., Roux P.P., Kubu C.J., Zeindler C., Bhakar A., Tannis L.-L., Verdi J.M., Barker P.A.
Neuron 27:279-288(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"hNRAGE, a human neurotrophin receptor interacting MAGE homologue, regulates p53 transcriptional activity and inhibits cell proliferation."
Wen C.-J., Xue B., Qin W.-X., Yu M., Zhang M.-Y., Zhao D.-H., Gao X., Gu J.-R., Li C.-J.
FEBS Lett. 564:171-176(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[3]"Identification and characterization of a new member of the MAGE gene family."
Chen Y.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS 1 AND 2).
Tissue: Blood and Skin.
[6]"Identification of a new, unorthodox member of the MAGE gene family."
Pold M., Zhou J., Chen G.L., Hall J.M., Vescio R.A., Berenson J.R.
Genomics 59:161-167(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 202-778 (ISOFORM 1).
Tissue: Bone marrow.
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 304-778.
Tissue: Testis.
[8]"A new melanoma antigen-encoding gene subfamily in human chromosome X."
Zhang C.G., Xing G.C., Wei H.D., Yu Y.T., He F.C.
Yi Chuan Xue Bao 28:197-203(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 396-778.
Tissue: Fetal liver.
[9]"Identification of the translational initiation codon in human MAGED1."
Kubu C.J., Goldhawk D.G., Barker P.A., Verdi J.M.
Genomics 70:150-152(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF THE TRANSLATIONAL INITIATION CODON.
[10]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases."
Doyle J.M., Gao J., Wang J., Yang M., Potts P.R.
Mol. Cell 39:963-974(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TRIM28 AND PJA1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF217963 mRNA. Translation: AAG09704.1.
AF258554 mRNA. Translation: AAG23757.1.
AF300328 mRNA. Translation: AAQ14483.1.
AL929410 Genomic DNA. Translation: CAH71560.1.
AL929410 Genomic DNA. Translation: CAH71561.1.
BC014070 mRNA. Translation: AAH14070.1.
BC032473 mRNA. Translation: AAH32473.1.
AF124440 mRNA. Translation: AAD31421.1. Different initiation.
AL133628 mRNA. Translation: CAB63752.1.
AF132205 mRNA. Translation: AAG35551.1. Different initiation.
CCDSCCDS14337.1. [Q9Y5V3-1]
CCDS35279.1. [Q9Y5V3-2]
PIRT43464.
RefSeqNP_001005332.1. NM_001005332.1. [Q9Y5V3-1]
NP_001005333.1. NM_001005333.1. [Q9Y5V3-2]
NP_008917.3. NM_006986.3. [Q9Y5V3-1]
UniGeneHs.5258.

3D structure databases

ProteinModelPortalQ9Y5V3.
SMRQ9Y5V3. Positions 465-672.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114879. 63 interactions.
IntActQ9Y5V3. 26 interactions.
MINTMINT-209401.
STRING9606.ENSP00000364847.

PTM databases

PhosphoSiteQ9Y5V3.

Polymorphism databases

DMDM62906893.

Proteomic databases

MaxQBQ9Y5V3.
PaxDbQ9Y5V3.
PRIDEQ9Y5V3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326587; ENSP00000325333; ENSG00000179222. [Q9Y5V3-1]
ENST00000375695; ENSP00000364847; ENSG00000179222. [Q9Y5V3-2]
ENST00000375722; ENSP00000364874; ENSG00000179222. [Q9Y5V3-1]
ENST00000375772; ENSP00000364927; ENSG00000179222. [Q9Y5V3-1]
ENST00000593373; ENSP00000472440; ENSG00000268018. [Q9Y5V3-2]
ENST00000597428; ENSP00000473070; ENSG00000268018. [Q9Y5V3-1]
ENST00000597768; ENSP00000471216; ENSG00000268018. [Q9Y5V3-1]
ENST00000599927; ENSP00000469692; ENSG00000268018. [Q9Y5V3-1]
GeneID9500.
KEGGhsa:9500.
UCSCuc004dpm.3. human. [Q9Y5V3-1]
uc004dpn.3. human. [Q9Y5V3-2]

Organism-specific databases

CTD9500.
GeneCardsGC0XP051562.
HGNCHGNC:6813. MAGED1.
HPACAB015165.
HPA043645.
MIM300224. gene.
neXtProtNX_Q9Y5V3.
PharmGKBPA30559.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG310785.
HOVERGENHBG003714.
KOK12464.
OMAWQNPVIW.
OrthoDBEOG75F4GM.
PhylomeDBQ9Y5V3.
TreeFamTF352132.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_578. Apoptosis.
SignaLinkQ9Y5V3.

Gene expression databases

BgeeQ9Y5V3.
CleanExHS_MAGED1.
GenevestigatorQ9Y5V3.

Family and domain databases

InterProIPR002190. MAGE.
[Graphical view]
PANTHERPTHR11736. PTHR11736. 1 hit.
PfamPF01454. MAGE. 1 hit.
[Graphical view]
PROSITEPS50838. MAGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAGED1. human.
GeneWikiMAGED1.
GenomeRNAi9500.
NextBio35594.
PROQ9Y5V3.
SOURCESearch...

Entry information

Entry nameMAGD1_HUMAN
AccessionPrimary (citable) accession number: Q9Y5V3
Secondary accession number(s): Q5VSH6 expand/collapse secondary AC list , Q8IZ84, Q8WY92, Q9H352, Q9HBT4, Q9UF36
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: April 26, 2005
Last modified: July 9, 2014
This is version 136 of the entry and version 3 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

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