Q96MG7 (MAGG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Melanoma-associated antigen G1

Alternative name(s):
Hepatocellular carcinoma-associated protein 4
MAGE-G1 antigen
Necdin-like protein 2

Gene names

Name:	NDNL2
Synonyms:	HCA4, MAGEG1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	304 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). In vitro enhances ubiquitin ligase activity of NSMCE1. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May be a growth suppressor that facilitates the entry of the cell into cell cycle arrest. Ref.12
Subunit structure	Component of the SMC5-SMC6 complex which consists at least of SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NDNL2. NSMCE1, NSMCE4A or EID3 and NDNL2 probably form a subcomplex that bridges the head domains of the SMC5:SMC6 heterodimer. Interacts with PJA1. Binds the C-terminus of E2F1 and NGFR By similarity. Ref.7 Ref.10 Ref.12
Subcellular location	Cytoplasm By similarity. Nucleus. Chromosome › telomere Probable Ref.7.
Tissue specificity	Ubiquitous. Ref.6
Sequence similarities	Contains 1 MAGE domain.
Sequence caution	The sequence BAB84964.1 differs from that shown. Reason: Frameshift at position 290.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair Growth regulation Ubl conjugation pathway
Cellular component	Chromosome Cytoplasm Nucleus Telomere
Molecular function	Tumor antigen
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW DNA repair Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of protein ubiquitination Inferred from direct assay Ref.12. Source: UniProtKB regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara
Cellular_component	Smc5-Smc6 complex Inferred from direct assay Ref.7. Source: UniProtKB chromosome, telomeric region Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EID3	Q8N140	4	EBI-2557356,EBI-744483
NSMCE1	Q8WV22	15	EBI-2557356,EBI-2557372
NSMCE4A	Q9NXX6	3	EBI-2557356,EBI-2557393
PJA1	Q8NG27	2	EBI-2557356,EBI-714606

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 304

304

Melanoma-associated antigen G1

PRO_0000156733

Regions

Domain

85 – 285

201

MAGE

Region

78 – 304

227

Interaction with NSMCE1

Amino acid modifications

Modified residue

57

1

Phosphoserine Ref.8

Modified residue

64

1

Phosphoserine Ref.8

Experimental info

Mutagenesis

96 – 97

2

LL → AA: Decreases interaction with NSMCE1, no effect on interaction with NSMCE4A, abolishes in vitro promotion of NSMCE1 ubiquitin ligase activity. Ref.12

Mutagenesis

180

1

M → A: Abolishes interaction with EID3. Ref.10 Ref.12

Mutagenesis

181

1

I → A: Abolishes interaction with EID3. Ref.10 Ref.12

Mutagenesis

185

1

L → A: Abolishes interaction with EID3. Ref.10 Ref.12

Mutagenesis

266

1

F → A: Abolishes interaction with EID3. Ref.10 Ref.12

Mutagenesis

270

1

V → A: Abolishes interaction with EID3. Ref.10 Ref.12

Secondary structure

1

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304

Helix Strand Turn

Details...

Helix

82 – 102

21

Helix

108 – 114

7

Helix

117 – 122

6

Helix

123 – 138

16

Beta strand

140 – 146

7

Beta strand

150 – 156

7

Helix

174 – 188

15

Turn

189 – 191

3

Helix

195 – 204

10

Helix

220 – 230

11

Helix

252 – 255

4

Helix

260 – 271

12

Beta strand

275 – 277

3

Helix

278 – 293

16

Sequences

	Sequence		Length	Mass (Da)
	Q96MG7 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: C00E2FB2D2CCED7B	FASTA	304	34,308
	10 20 30 40 50 60 MLQKPRNRGR SGGQAERDRD WSHSGNPGAS RAGEDARVLR DGFAEEAPST SRGPGGSQGS 70 80 90 100 110 120 QGPSPQGARR AQAAPAVGPR SQKQLELKVS ELVQFLLIKD QKKIPIKRAD ILKHVIGDYK 130 140 150 160 170 180 DIFPDLFKRA AERLQYVFGY KLVELEPKSN TYILINTLEP VEEDAEMRGD QGTPTTGLLM 190 200 210 220 230 240 IVLGLIFMKG NTIKETEAWD FLRRLGVYPT KKHLIFGDPK KLITEDFVRQ RYLEYRRIPH 250 260 270 280 290 300 TDPVDYEFQW GPRTNLETSK MKVLKFVAKV HNQDPKDWPA QYCEALADEE NRARPQPSGP APSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of genes in the chromosome X that are differentially expressed in hepatocellular carcinoma." Dong X.-Y., Chen W.-F. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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]. Tissue: Skeletal muscle.
[3]	"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: Brain, Lung, Spleen and Testis.
[4]	"The nucleotide sequence of a long cDNA clone isolated from human spleen." Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-304. Tissue: Spleen.
[5]	"Identification of new genes of the MAGE family." Lucas S., Boon T. Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 189-288. Tissue: Testis.
[6]	"A necdin/MAGE-like gene in the chromosome 15 autism susceptibility region: expression, imprinting, and mapping of the human and mouse orthologues." Chibuk T.K., Bischof J.M., Wevrick R. BMC Genet. 2:22-22(2001) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[7]	"Identification of the proteins, including MAGEG1, that make up the human SMC5-6 protein complex." Taylor E.M., Copsey A.C., Hudson J.J., Vidot S., Lehmann A.R. Mol. Cell. Biol. 28:1197-1206(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NSMCE1 AND SMC6, IDENTIFICATION IN THE SMC5-SMC6 COMPLEX.
[8]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-64, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Interactions between the Nse3 and Nse4 components of the SMC5-6 complex identify evolutionarily conserved interactions between MAGE and EID Families." Hudson J.J., Bednarova K., Kozakova L., Liao C., Guerineau M., Colnaghi R., Vidot S., Marek J., Bathula S.R., Lehmann A.R., Palecek J. PLoS ONE 6:E17270-E17270(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EID3 AND NSMCE1, MUTAGENESIS OF MET-180; ILE-181; LEU-185; PHE-266 AND VAL-270.
[11]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"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: X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 78-294 IN COMPLEX WITH NSMCE1, FUNCTION, INTERACTION WITH NSMCE1; NSMCE4A AND PJA1, MUTAGENESIS OF 96-LEU-LEU-97.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF490510 mRNA. Translation: AAM08357.1.
AK056957 mRNA. Translation: BAB71325.1.
BC041166 mRNA. Translation: AAH41166.2.
BC053999 mRNA. Translation: AAH53999.1.
AK074138 mRNA. Translation: BAB84964.1. Frameshift.
AF320911 Genomic DNA. Translation: AAG38607.1.

IPI

IPI00217104.

RefSeq

NP_619649.1. NM_138704.3.

UniGene

Hs.94011.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3NW0	X-ray	2.92	B	78-294	[»]

ProteinModelPortal

Q96MG7.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96MG7. 8 interactions.

STRING

9606.ENSP00000330694.

PTM databases

PhosphoSite

Q96MG7.

Polymorphism databases

DMDM

46396494.

Proteomic databases

PaxDb

Q96MG7.

PRIDE

Q96MG7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000332303; ENSP00000330694; ENSG00000185115.

GeneID

56160.

KEGG

hsa:56160.

UCSC

uc001zco.3. human.

Organism-specific databases

CTD

56160.

GeneCards

GC15M029560.

HGNC

HGNC:7677. NDNL2.

MIM

608243. gene.

neXtProt

NX_Q96MG7.

PharmGKB

PA31480.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG292115.

HOGENOM

HOG000231161.

HOVERGEN

HBG006315.

InParanoid

Q96MG7.

OMA

IKETEVW.

OrthoDB

EOG44J2JT.

PhylomeDB

Q96MG7.

Enzyme and pathway databases

Pathway_Interaction_DB

p75ntrpathway. p75(NTR)-mediated signaling.

Gene expression databases

Bgee

Q96MG7.

CleanEx

HS_NDNL2.

Genevestigator

Q96MG7.

GermOnline

ENSG00000185115. Homo sapiens.

Family and domain databases

InterPro

IPR002190. MAGE.
[Graphical view]

PANTHER

PTHR11736. PTHR11736. 1 hit.

Pfam

PF01454. MAGE. 1 hit.
[Graphical view]

PROSITE

PS50838. MAGE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q96MG7.

GenomeRNAi

56160.

NextBio

61786.

PMAP-CutDB

Q96MG7.

SOURCE

Search...

Entry information

Entry name

MAGG1_HUMAN

Accession

Primary (citable) accession number: Q96MG7
Secondary accession number(s): Q8IW16, Q8TEI6, Q9H214

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.