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Q9UNF1 - MAGD2_HUMAN

UniProt

Q9UNF1 - MAGD2_HUMAN

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Protein

Melanoma-associated antigen D2

Gene

MAGED2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Keywords - Molecular functioni

Tumor antigen

Names & Taxonomyi

Protein namesi
Recommended name:
Melanoma-associated antigen D2
Alternative name(s):
11B6
Breast cancer-associated gene 1 protein
Short name:
BCG-1
Hepatocellular carcinoma-associated protein JCL-1
MAGE-D2 antigen
Gene namesi
Name:MAGED2
Synonyms:BCG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:16353. MAGED2.

Subcellular locationi

GO - Cellular componenti

  1. membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30560.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed6 Publications
Chaini2 – 606605Melanoma-associated antigen D2PRO_0000156727Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine6 Publications
Modified residuei5 – 51Phosphoserine1 Publication
Modified residuei72 – 721Phosphothreonine1 Publication
Modified residuei157 – 1571Phosphoserine1 Publication
Modified residuei190 – 1901Phosphoserine2 Publications
Modified residuei191 – 1911Phosphoserine3 Publications
Modified residuei194 – 1941Phosphoserine3 Publications
Modified residuei197 – 1971Phosphoserine1 Publication
Modified residuei244 – 2441Phosphoserine1 Publication
Modified residuei247 – 2471Phosphoserine7 Publications
Modified residuei265 – 2651Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UNF1.
PaxDbiQ9UNF1.
PRIDEiQ9UNF1.

PTM databases

PhosphoSiteiQ9UNF1.

Expressioni

Tissue specificityi

Widely expressed in normal tissues.

Gene expression databases

BgeeiQ9UNF1.
CleanExiHS_MAGED2.
ExpressionAtlasiQ9UNF1. baseline and differential.
GenevestigatoriQ9UNF1.

Organism-specific databases

HPAiHPA031572.
HPA031573.

Interactioni

Protein-protein interaction databases

BioGridi116121. 55 interactions.
IntActiQ9UNF1. 9 interactions.
MINTiMINT-1389350.
STRINGi9606.ENSP00000218439.

Structurei

3D structure databases

ProteinModelPortaliQ9UNF1.
SMRiQ9UNF1. Positions 273-479.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini279 – 478200MAGEPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi215 – 25844Arg-richAdd
BLAST

Sequence similaritiesi

Contains 1 MAGE domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG292115.
GeneTreeiENSGT00760000118824.
HOVERGENiHBG003714.
InParanoidiQ9UNF1.
OMAiEPTDAGI.
OrthoDBiEOG75F4GM.
PhylomeDBiQ9UNF1.
TreeFamiTF352132.

Family and domain databases

InterProiIPR028810. MAGED2.
IPR002190. MHD_dom.
[Graphical view]
PANTHERiPTHR11736. PTHR11736. 1 hit.
PTHR11736:SF11. PTHR11736:SF11. 1 hit.
PfamiPF01454. MAGE. 1 hit.
[Graphical view]
PROSITEiPS50838. MAGE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UNF1-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSDTSESGAG LTRFQAEASE KDSSSMMQTL LTVTQNVEVP ETPKASKALE 
        60         70         80         90        100
VSEDVKVSKA SGVSKATEVS KTPEAREAPA TQASSTTQLT DTQVLAAENK 
       110        120        130        140        150
SLAADTKKQN ADPQAVTMPA TETKKVSHVA DTKVNTKAQE TEAAPSQAPA 
       160        170        180        190        200
DEPEPESAAA QSQENQDTRP KVKAKKARKV KHLDGEEDGS SDQSQASGTT 
       210        220        230        240        250
GGRRVSKALM ASMARRASRG PIAFWARRAS RTRLAAWARR ALLSLRSPKA 
       260        270        280        290        300
RRGKARRRAA KLQSSQEPEA PPPRDVALLQ GRANDLVKYL LAKDQTKIPI 
       310        320        330        340        350
KRSDMLKDII KEYTDVYPEI IERAGYSLEK VFGIQLKEID KNDHLYILLS 
       360        370        380        390        400
TLEPTDAGIL GTTKDSPKLG LLMVLLSIIF MNGNRSSEAV IWEVLRKLGL 
       410        420        430        440        450
RPGIHHSLFG DVKKLITDEF VKQKYLDYAR VPNSNPPEYE FFWGLRSYYE 
       460        470        480        490        500
TSKMKVLKFA CKVQKKDPKE WAAQYREAME ADLKAAAEAA AEAKARAEIR 
       510        520        530        540        550
ARMGIGLGSE NAAGPCNWDE ADIGPWAKAR IQAGAEAKAK AQESGSASTG 
       560        570        580        590        600
ASTSTNNSAS ASASTSGGFS AGASLTATLT FGLFAGLGGA GASTSGSSGA 

CGFSYK
Length:606
Mass (Da):64,954
Last modified:September 26, 2001 - v2
Checksum:i352FD5BAF5088652
GO
Isoform 2 (identifier: Q9UNF1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     45-62: Missing.

Note: No experimental confirmation available.

Show »
Length:588
Mass (Da):63,167
Checksum:iAF568E2B27C5765B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731P → S in AAD00728. 1 PublicationCurated
Sequence conflicti377 – 3771S → C in BAC03896. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti187 – 1871E → D.
Corresponds to variant rs12014977 [ dbSNP | Ensembl ].		VAR_053508
Natural varianti266 – 2661Q → R.1 Publication
VAR_011639
Natural varianti458 – 4581K → Q in a breast cancer sample; somatic mutation. 1 Publication
VAR_036584

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei45 – 6218Missing in isoform 2. 1 PublicationVSP_008030Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF128527 mRNA. Translation: AAD33392.1.
AF128528 mRNA. Translation: AAD33393.1.
AF126181 mRNA. Translation: AAD28598.1.
AJ293618 mRNA. Translation: CAC19410.1.
U92544 mRNA. Translation: AAD00728.1.
AF320070 mRNA. Translation: AAG35066.2.
AK092463 mRNA. Translation: BAC03896.1.
Z98046 Genomic DNA. Translation: CAB10841.1.
CH471154 Genomic DNA. Translation: EAW93189.1.
BC000304 mRNA. Translation: AAH00304.1.
BC091503 mRNA. Translation: AAH91503.1.
AF148815 mRNA. Translation: AAF73137.1.
AF320907 mRNA. Translation: AAG38603.1.
CCDSiCCDS14362.1. [Q9UNF1-1]
RefSeqiNP_055414.2. NM_014599.5. [Q9UNF1-1]
NP_803182.1. NM_177433.2. [Q9UNF1-1]
NP_957516.1. NM_201222.2. [Q9UNF1-1]
UniGeneiHs.522665.

Genome annotation databases

EnsembliENST00000218439; ENSP00000218439; ENSG00000102316. [Q9UNF1-1]
ENST00000375053; ENSP00000364193; ENSG00000102316. [Q9UNF1-1]
ENST00000375058; ENSP00000364198; ENSG00000102316. [Q9UNF1-1]
ENST00000375068; ENSP00000364209; ENSG00000102316. [Q9UNF1-1]
ENST00000396224; ENSP00000379526; ENSG00000102316. [Q9UNF1-1]
GeneIDi10916.
KEGGihsa:10916.
UCSCiuc004dtk.1. human. [Q9UNF1-1]

Polymorphism databases

DMDMi17380153.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF128527 mRNA. Translation: AAD33392.1.
AF128528 mRNA. Translation: AAD33393.1.
AF126181 mRNA. Translation: AAD28598.1.
AJ293618 mRNA. Translation: CAC19410.1.
U92544 mRNA. Translation: AAD00728.1.
AF320070 mRNA. Translation: AAG35066.2.
AK092463 mRNA. Translation: BAC03896.1.
Z98046 Genomic DNA. Translation: CAB10841.1.
CH471154 Genomic DNA. Translation: EAW93189.1.
BC000304 mRNA. Translation: AAH00304.1.
BC091503 mRNA. Translation: AAH91503.1.
AF148815 mRNA. Translation: AAF73137.1.
AF320907 mRNA. Translation: AAG38603.1.
CCDSiCCDS14362.1. [Q9UNF1-1]
RefSeqiNP_055414.2. NM_014599.5. [Q9UNF1-1]
NP_803182.1. NM_177433.2. [Q9UNF1-1]
NP_957516.1. NM_201222.2. [Q9UNF1-1]
UniGeneiHs.522665.

3D structure databases

ProteinModelPortaliQ9UNF1.
SMRiQ9UNF1. Positions 273-479.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116121. 55 interactions.
IntActiQ9UNF1. 9 interactions.
MINTiMINT-1389350.
STRINGi9606.ENSP00000218439.

PTM databases

PhosphoSiteiQ9UNF1.

Polymorphism databases

DMDMi17380153.

Proteomic databases

MaxQBiQ9UNF1.
PaxDbiQ9UNF1.
PRIDEiQ9UNF1.

Protocols and materials databases

DNASUi10916.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000218439; ENSP00000218439; ENSG00000102316. [Q9UNF1-1]
ENST00000375053; ENSP00000364193; ENSG00000102316. [Q9UNF1-1]
ENST00000375058; ENSP00000364198; ENSG00000102316. [Q9UNF1-1]
ENST00000375068; ENSP00000364209; ENSG00000102316. [Q9UNF1-1]
ENST00000396224; ENSP00000379526; ENSG00000102316. [Q9UNF1-1]
GeneIDi10916.
KEGGihsa:10916.
UCSCiuc004dtk.1. human. [Q9UNF1-1]

Organism-specific databases

CTDi10916.
GeneCardsiGC0XP054834.
HGNCiHGNC:16353. MAGED2.
HPAiHPA031572.
HPA031573.
MIMi300470. gene.
neXtProtiNX_Q9UNF1.
PharmGKBiPA30560.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG292115.
GeneTreeiENSGT00760000118824.
HOVERGENiHBG003714.
InParanoidiQ9UNF1.
OMAiEPTDAGI.
OrthoDBiEOG75F4GM.
PhylomeDBiQ9UNF1.
TreeFamiTF352132.

Miscellaneous databases

ChiTaRSiMAGED2. human.
GeneWikiiMAGED2.
GenomeRNAii10916.
NextBioi41463.
PROiQ9UNF1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UNF1.
CleanExiHS_MAGED2.
ExpressionAtlasiQ9UNF1. baseline and differential.
GenevestigatoriQ9UNF1.

Family and domain databases

InterProiIPR028810. MAGED2.
IPR002190. MHD_dom.
[Graphical view]
PANTHERiPTHR11736. PTHR11736. 1 hit.
PTHR11736:SF11. PTHR11736:SF11. 1 hit.
PfamiPF01454. MAGE. 1 hit.
[Graphical view]
PROSITEiPS50838. MAGE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of genes overexpressed in freshly isolated breast cancer specimens."
    Kurt R.A., Urba W.J., Schoof D.D.
    Breast Cancer Res. Treat. 59:41-48(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-266.
    Tissue: Fetal lung, Mammary cancer and Mammary gland.
  2. "Expression pattern and further characterization of human MAGED2 and identification of rodent orthologues."
    Langnaese K., Kloos D.U., Wehnert M., Seidel B., Wieacker P.
    Cytogenet. Cell Genet. 94:233-240(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Hepatocellular carcinoma associated gene JCL-1."
    Jin C.L., Wang D.Y., Wan D.F., Gu J.R.
    Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Identification of genes which are differentially expressed in hepatocellular carcinoma by SSH method."
    Dong X.-Y., Chen W.-F.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  6. "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.
    , 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].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Lung and Skeletal muscle.
  9. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 77-100; 182-203; 220-227; 262-274; 312-323; 386-397 AND 431-446, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  10. "Isolation of genes which are differentially expressed in prostate cancer cells."
    Stubbs A.P., Abel P.D., Lalani E.-N., Stamp G.W.H.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE OF 346-424.
    Tissue: Prostatic carcinoma.
  11. "A new MAGE gene with ubiquitous expression does not code for known MAGE antigens recognized by T cells."
    Lucas S., Brasseur F., Boon T.
    Cancer Res. 59:4100-4103(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 369-503.
    Tissue: Testis.
  12. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-191 AND SER-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  16. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-190; SER-191; SER-194; SER-197; SER-247 AND SER-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; THR-72; SER-191; SER-244; SER-247 AND SER-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-458.
+Additional computationally mapped references.

Entry informationi

Entry nameiMAGD2_HUMAN
AccessioniPrimary (citable) accession number: Q9UNF1
Secondary accession number(s): A6NMX0
, O76058, Q5BJF3, Q8NAL6, Q9H218, Q9P0U9, Q9UM52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: January 7, 2015
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.