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Protein

MAX gene-associated protein

Gene

MGA

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

Functioni

Functions as a dual-specificity transcription factor, regulating the expression of both MAX-network and T-box family target genes. Functions as a repressor or an activator. Binds to 5'-AATTTCACACCTAGGTGTGAAATT-3' core sequence and seems to regulate MYC-MAX target genes. Suppresses transcriptional activation by MYC and inhibits MYC-dependent cell transformation. Function activated by heterodimerization with MAX. This heterodimerization serves the dual function of both generating an E-box-binding heterodimer and simultaneously blocking interaction of a corepressor (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi84 – 260177T-boxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

SIGNORiQ8IWI9.

Names & Taxonomyi

Protein namesi
Recommended name:
MAX gene-associated protein
Alternative name(s):
MAX dimerization protein 5
Gene namesi
Name:MGA
Synonyms:KIAA0518, MAD5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:14010. MGA.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • MLL1 complex Source: UniProtKB
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134976336.

Polymorphism and mutation databases

BioMutaiMGA.
DMDMi527504082.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 30263026MAX gene-associated proteinPRO_0000342692Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki329 – 329Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki460 – 460Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei534 – 5341PhosphoserineCombined sources
Cross-linki570 – 570Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei607 – 6071PhosphoserineCombined sources
Modified residuei645 – 6451PhosphoserineCombined sources
Modified residuei851 – 8511PhosphoserineCombined sources
Modified residuei924 – 9241PhosphoserineCombined sources
Cross-linki1207 – 1207Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1208 – 12081PhosphoserineCombined sources
Modified residuei1430 – 14301PhosphoserineCombined sources
Modified residuei1457 – 14571PhosphoserineCombined sources
Cross-linki1946 – 1946Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki2074 – 2074Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki2096 – 2096Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki2155 – 2155Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki2199 – 2199Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki2245 – 2245Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki2374 – 2374Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei2502 – 25021PhosphoserineCombined sources
Modified residuei2871 – 28711PhosphoserineCombined sources
Modified residuei2882 – 28821PhosphoserineCombined sources
Modified residuei2939 – 29391PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8IWI9.
MaxQBiQ8IWI9.
PaxDbiQ8IWI9.
PeptideAtlasiQ8IWI9.
PRIDEiQ8IWI9.

PTM databases

iPTMnetiQ8IWI9.

Expressioni

Gene expression databases

BgeeiQ8IWI9.
CleanExiHS_MGA.
ExpressionAtlasiQ8IWI9. baseline and differential.
GenevisibleiQ8IWI9. HS.

Organism-specific databases

HPAiHPA042278.
HPA058183.

Interactioni

Subunit structurei

Interacts with MAX. Requires dimerization with MAX for E-box binding (By similarity). Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with ZMYND11.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAXP612443EBI-2815196,EBI-751711

Protein-protein interaction databases

BioGridi116870. 50 interactions.
DIPiDIP-57615N.
IntActiQ8IWI9. 22 interactions.
MINTiMINT-1183008.
STRINGi9606.ENSP00000219905.

Structurei

3D structure databases

ProteinModelPortaliQ8IWI9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2384 – 243552bHLHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1111 – 114737Sequence analysisAdd
BLAST
Coiled coili2778 – 280225Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi967 – 98115Gln-richAdd
BLAST
Compositional biasi1255 – 12639Poly-Ser
Compositional biasi1594 – 1714121Thr-richAdd
BLAST

Domaini

Transcription repression is enhanced or dependent on the presence of the T-box DNA-binding domain.By similarity

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation
Contains 1 T-box DNA-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3585. Eukaryota.
ENOG410XSTS. LUCA.
GeneTreeiENSGT00740000115029.
HOGENOMiHOG000113578.
HOVERGENiHBG108131.
InParanoidiQ8IWI9.
OMAiHRDPVFY.
TreeFamiTF106341.

Family and domain databases

Gene3Di2.60.40.820. 1 hit.
4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR032060. DUF4801.
IPR008967. p53-like_TF_DNA-bd.
IPR001699. TF_T-box.
IPR018186. TF_T-box_CS.
[Graphical view]
PANTHERiPTHR11267. PTHR11267. 1 hit.
PfamiPF16059. DUF4801. 1 hit.
PF00010. HLH. 1 hit.
PF00907. T-box. 1 hit.
[Graphical view]
PRINTSiPR00937. TBOX.
SMARTiSM00353. HLH. 1 hit.
SM00425. TBOX. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
SSF49417. SSF49417. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
PS01264. TBOX_2. 1 hit.
PS50252. TBOX_3. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8IWI9-1) [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
MEEKQQIILA NQDGGTVAGA APTFFVILKQ PGNGKTDQGI LVTNQDACAL
60 70 80 90 100
ASSVSSPVKS KGKICLPADC TVGGITVTLD NNSMWNEFYH RSTEMILTKQ
110 120 130 140 150
GRRMFPYCRY WITGLDSNLK YILVMDISPV DNHRYKWNGR WWEPSGKAEP
160 170 180 190 200
HVLGRVFIHP ESPSTGHYWM HQPVSFYKLK LTNNTLDQEG HIILHSMHRY
210 220 230 240 250
LPRLHLVPAE KAVEVIQLNG PGVHTFTFPQ TEFFAVTAYQ NIQITQLKID
260 270 280 290 300
YNPFAKGFRD DGLNNKPQRD GKQKNSSDQE GNNISSSSGH RVRLTEGQGS
310 320 330 340 350
EIQPGDLDPL SRGHETSGKG LEKTSLNIKR DFLGFMDTDS ALSEVPQLKQ
360 370 380 390 400
EISECLIASS FEDDSRVASP LDQNGSFNVV IKEEPLDDYD YELGECPEGV
410 420 430 440 450
TVKQEETDEE TDVYSNSDDD PILEKQLKRH NKVDNPEADH LSSKWLPSSP
460 470 480 490 500
SGVAKAKMFK LDTGKMPVVY LEPCAVTRST VKISELPDNM LSTSRKDKSS
510 520 530 540 550
MLAELEYLPT YIENSNETAF CLGKESENGL RKHSPDLRVV QKYPLLKEPQ
560 570 580 590 600
WKYPDISDSI STERILDDSK DSVGDSLSGK EDLGRKRTTM LKIATAAKVV
610 620 630 640 650
NANQNASPNV PGKRGRPRKL KLCKAGRPPK NTGKSLISTK NTPVSPGSTF
660 670 680 690 700
PDVKPDLEDV DGVLFVSFES KEALDIHAVD GTTEESSSLQ ASTTNDSGYR
710 720 730 740 750
ARISQLEKEL IEDLKTLRHK QVIHPGLQEV GLKLNSVDPT MSIDLKYLGV
760 770 780 790 800
QLPLAPATSF PFWNLTGTNP ASPDAGFPFV SRTGKTNDFT KIKGWRGKFH
810 820 830 840 850
SASASRNEGG NSESSLKNRS AFCSDKLDEY LENEGKLMET SMGFSSNAPT
860 870 880 890 900
SPVVYQLPTK STSYVRTLDS VLKKQSTISP STSYSLKPHS VPPVSRKAKS
910 920 930 940 950
QNRQATFSGR TKSSYKSILP YPVSPKQKYS HVILGDKVTK NSSGIISENQ
960 970 980 990 1000
ANNFVVPTLD ENIFPKQISL RQAQQQQQQQ QGSRPPGLSK SQVKLMDLED
1010 1020 1030 1040 1050
CALWEGKPRT YITEERADVS LTTLLTAQAS LKTKPIHTII RKRAPPCNND
1060 1070 1080 1090 1100
FCRLGCVCSS LALEKRQPAH CRRPDCMFGC TCLKRKVVLV KGGSKTKHFQ
1110 1120 1130 1140 1150
RKAAHRDPVF YDTLGEEARE EEEGIREEEE QLKEKKKRKK LEYTICETEP
1160 1170 1180 1190 1200
EQPVRHYPLW VKVEGEVDPE PVYIPTPSVI EPMKPLLLPQ PEVLSPTVKG
1210 1220 1230 1240 1250
KLLTGIKSPR SYTPKPNPVI REEDKDPVYL YFESMMTCAR VRVYERKKED
1260 1270 1280 1290 1300
QRQPSSSSSP SPSFQQQTSC HSSPENHNNA KEPDSEQQPL KQLTCDLEDD
1310 1320 1330 1340 1350
SDKLQEKSWK SSCNEGESSS TSYMHQRSPG GPTKLIEIIS DCNWEEDRNK
1360 1370 1380 1390 1400
ILSILSQHIN SNMPQSLKVG SFIIELASQR KSRGEKNPPV YSSRVKISMP
1410 1420 1430 1440 1450
SCQDQDDMAE KSGSETPDGP LSPGKMEDIS PVQTDALDSV RERLHGGKGL
1460 1470 1480 1490 1500
PFYAGLSPAG KLVAYKRKPS SSTSGLIQVA SNAKVAASRK PRTLLPSTSN
1510 1520 1530 1540 1550
SKMASSSGTA TNRPGKNLKA FVPAKRPIAA RPSPGGVFTQ FVMSKVGALQ
1560 1570 1580 1590 1600
QKIPGVSTPQ TLAGTQKFSI RPSPVMVVTP VVSSEPVQVC SPVTAAVTTT
1610 1620 1630 1640 1650
TPQVFLENTT AVTPMTAISD VETKETTYSS GATTTGVVEV SETNTSTSVT
1660 1670 1680 1690 1700
STQSTATVNL TKTTGITTPV ASVAFPKSLV ASPSTITLPV ASTASTSLVV
1710 1720 1730 1740 1750
VTAAASSSMV TTPTSSLGSV PIILSGINGS PPVSQRPENA AQIPVATPQV
1760 1770 1780 1790 1800
SPNTVKRAGP RLLHPNGQIV QLLPLHQLRG SNTQPNLQPV MFRNPGSVMG
1810 1820 1830 1840 1850
IRLPAPSKPS ETPPSSTSSS AFSVMNPVIQ AVGSSSAVNV ITQAPSLLSS
1860 1870 1880 1890 1900
GASFVSQAGT LTLRISPPEP QSFASKTGSE TKITYSSGGQ PVGTASLIPL
1910 1920 1930 1940 1950
QSGSFALLQL PGQKPVPSSI LQHVASLQMK RESQNPDQKD ETNSIKREQE
1960 1970 1980 1990 2000
TKKVLQSEGE AVDPEANVIK QNSGAATSEE TLNDSLEDRG DHLDEECLPE
2010 2020 2030 2040 2050
EGCATVKPSE HSCITGSHTD QDYKDVNEEY GARNRKSSKE KVAVLEVRTI
2060 2070 2080 2090 2100
SEKASNKTVQ NLSKVQHQKL GDVKVEQQKG FDNPEENSSE FPVTFKEESK
2110 2120 2130 2140 2150
FELSGSKVME QQSNLQPEAK EKECGDSLEK DRERWRKHLK GPLTRKCVGA
2160 2170 2180 2190 2200
SQECKKEADE QLIKETKTCQ ENSDVFQQEQ GISDLLGKSG ITEDARVLKT
2210 2220 2230 2240 2250
ECDSWSRISN PSAFSIVPRR AAKSSRGNGH FQGHLLLPGE QIQPKQEKKG
2260 2270 2280 2290 2300
GRSSADFTVL DLEEDDEDDN EKTDDSIDEI VDVVSDYQSE EVDDVEKNNC
2310 2320 2330 2340 2350
VEYIEDDEEH VDIETVEELS EEINVAHLKT TAAHTQSFKQ PSCTHISADE
2360 2370 2380 2390 2400
KAAERSRKAP PIPLKLKPDY WSDKLQKEAE AFAYYRRTHT ANERRRRGEM
2410 2420 2430 2440 2450
RDLFEKLKIT LGLLHSSKVS KSLILTRAFS EIQGLTDQAD KLIGQKNLLT
2460 2470 2480 2490 2500
RKRNILIRKV SSLSGKTEEV VLKKLEYIYA KQQALEAQKR KKKMGSDEFD
2510 2520 2530 2540 2550
ISPRISKQQE GSSASSVDLG QMFINNRRGK PLILSRKKDQ ATENTSPLNT
2560 2570 2580 2590 2600
PHTSANLVMT PQGQLLTLKG PLFSGPVVAV SPDLLESDLK PQVAGSAVAL
2610 2620 2630 2640 2650
PENDDLFMMP RIVNVTSLAT EGGLVDMGGS KYPHEVPDSK PSDHLKDTVR
2660 2670 2680 2690 2700
NEDNSLEDKG RISSRGNRDG RVTLGPTQVF LANKDSGYPQ IVDVSNMQKA
2710 2720 2730 2740 2750
QEFLPKKISG DMRGIQYKWK ESESRGERVK SKDSSFHKLK MKDLKDSSIE
2760 2770 2780 2790 2800
MELRKVTSAI EEAALDSSEL LTNMEDEDDT DETLTSLLNE IAFLNQQLND
2810 2820 2830 2840 2850
DSVGLAELPS SMDTEFPGDA RRAFISKVPP GSRATFQVEH LGTGLKELPD
2860 2870 2880 2890 2900
VQGESDSISP LLLHLEDDDF SENEKQLAEP ASEPDVLKIV IDSEIKDSLL
2910 2920 2930 2940 2950
SNKKAIDGGK NTSGLPAEPE SVSSPPTLHM KTGLENSNST DTLWRPMPKL
2960 2970 2980 2990 3000
APLGLKVANP SSDADGQSLK VMPCLAPIAA KVGSVGHKMN LTGNDQEGRE
3010 3020
SKVMPTLAPV VAKLGNSGAS PSSAGK
Length:3,026
Mass (Da):331,836
Last modified:July 24, 2013 - v3
Checksum:i33D363321F6E40CD
GO
Isoform 2 (identifier: Q8IWI9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1790: Missing.
     2488-3026: Missing.

Note: No experimental confirmation available.
Show »
Length:697
Mass (Da):77,234
Checksum:i6F8E87B777DD16BE
GO
Isoform 3 (identifier: Q8IWI9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1529-1763: AARPSPGGVF...TVKRAGPRLL → ENAAQIPVAT...RSPSGMNLFR

Note: No experimental confirmation available.
Show »
Length:2,856
Mass (Da):315,219
Checksum:iE79165E8AF0C9FE6
GO
Isoform 4 (identifier: Q8IWI9-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1763-1763: L → LLIPVQQGSPTLRPVSNTQLQGHRMVLQPVRSPSGMNLFR

Note: No experimental confirmation available.
Show »
Length:3,065
Mass (Da):336,159
Checksum:i430B04B7ED92B4A8
GO

Sequence cautioni

The sequence BAB14186.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti266 – 2661K → N in BAB14186 (PubMed:14702039).Curated
Sequence conflicti742 – 7421S → R in BAB14186 (PubMed:14702039).Curated
Sequence conflicti1138 – 11381R → K in AAH38449 (PubMed:15489334).Curated
Sequence conflicti2191 – 21911Missing in BAB14543 (PubMed:14702039).Curated
Sequence conflicti2326 – 23261A → T in BAB14543 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti338 – 3381T → A.
Corresponds to variant rs3803348 [ dbSNP | Ensembl ].
VAR_044341
Natural varianti716 – 7161T → S.
Corresponds to variant rs2178004 [ dbSNP | Ensembl ].
VAR_044342
Natural varianti1270 – 12701C → R.
Corresponds to variant rs17677811 [ dbSNP | Ensembl ].
VAR_044343
Natural varianti1523 – 15231P → A.
Corresponds to variant rs17677991 [ dbSNP | Ensembl ].
VAR_057268

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 17901790Missing in isoform 2. 1 PublicationVSP_034534Add
BLAST
Alternative sequencei1529 – 1763235AARPS…GPRLL → ENAAQIPVATPQVSPNTVKR AGPRLLLIPVQQGSPTLRPV SNTQLQGHRMVLQPVRSPSG MNLFR in isoform 3. CuratedVSP_047669Add
BLAST
Alternative sequencei1763 – 17631L → LLIPVQQGSPTLRPVSNTQL QGHRMVLQPVRSPSGMNLFR in isoform 4. CuratedVSP_047670
Alternative sequencei2488 – 3026539Missing in isoform 2. 1 PublicationVSP_034535Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK022696 mRNA. Translation: BAB14186.1. Different initiation.
AK023360 mRNA. Translation: BAB14543.1.
AC016134 Genomic DNA. No translation available.
AC073657 Genomic DNA. No translation available.
BC038449 mRNA. Translation: AAH38449.1.
AB011090 mRNA. Translation: BAA25444.1.
AL050181 mRNA. Translation: CAB43310.1.
CCDSiCCDS55959.1. [Q8IWI9-4]
CCDS55960.1. [Q8IWI9-3]
PIRiT00081.
RefSeqiNP_001074010.2. NM_001080541.2. [Q8IWI9-3]
NP_001157745.1. NM_001164273.1. [Q8IWI9-4]
UniGeneiHs.187569.

Genome annotation databases

EnsembliENST00000219905; ENSP00000219905; ENSG00000174197. [Q8IWI9-4]
ENST00000545763; ENSP00000442467; ENSG00000174197. [Q8IWI9-3]
ENST00000566586; ENSP00000456141; ENSG00000174197. [Q8IWI9-3]
ENST00000570161; ENSP00000457035; ENSG00000174197. [Q8IWI9-4]
GeneIDi23269.
KEGGihsa:23269.
UCSCiuc010ucy.2. human. [Q8IWI9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK022696 mRNA. Translation: BAB14186.1. Different initiation.
AK023360 mRNA. Translation: BAB14543.1.
AC016134 Genomic DNA. No translation available.
AC073657 Genomic DNA. No translation available.
BC038449 mRNA. Translation: AAH38449.1.
AB011090 mRNA. Translation: BAA25444.1.
AL050181 mRNA. Translation: CAB43310.1.
CCDSiCCDS55959.1. [Q8IWI9-4]
CCDS55960.1. [Q8IWI9-3]
PIRiT00081.
RefSeqiNP_001074010.2. NM_001080541.2. [Q8IWI9-3]
NP_001157745.1. NM_001164273.1. [Q8IWI9-4]
UniGeneiHs.187569.

3D structure databases

ProteinModelPortaliQ8IWI9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116870. 50 interactions.
DIPiDIP-57615N.
IntActiQ8IWI9. 22 interactions.
MINTiMINT-1183008.
STRINGi9606.ENSP00000219905.

PTM databases

iPTMnetiQ8IWI9.

Polymorphism and mutation databases

BioMutaiMGA.
DMDMi527504082.

Proteomic databases

EPDiQ8IWI9.
MaxQBiQ8IWI9.
PaxDbiQ8IWI9.
PeptideAtlasiQ8IWI9.
PRIDEiQ8IWI9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219905; ENSP00000219905; ENSG00000174197. [Q8IWI9-4]
ENST00000545763; ENSP00000442467; ENSG00000174197. [Q8IWI9-3]
ENST00000566586; ENSP00000456141; ENSG00000174197. [Q8IWI9-3]
ENST00000570161; ENSP00000457035; ENSG00000174197. [Q8IWI9-4]
GeneIDi23269.
KEGGihsa:23269.
UCSCiuc010ucy.2. human. [Q8IWI9-1]

Organism-specific databases

CTDi23269.
GeneCardsiMGA.
H-InvDBHIX0012158.
HGNCiHGNC:14010. MGA.
HPAiHPA042278.
HPA058183.
MIMi616061. gene.
neXtProtiNX_Q8IWI9.
PharmGKBiPA134976336.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3585. Eukaryota.
ENOG410XSTS. LUCA.
GeneTreeiENSGT00740000115029.
HOGENOMiHOG000113578.
HOVERGENiHBG108131.
InParanoidiQ8IWI9.
OMAiHRDPVFY.
TreeFamiTF106341.

Enzyme and pathway databases

SIGNORiQ8IWI9.

Miscellaneous databases

ChiTaRSiMGA. human.
GenomeRNAii23269.
PROiQ8IWI9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IWI9.
CleanExiHS_MGA.
ExpressionAtlasiQ8IWI9. baseline and differential.
GenevisibleiQ8IWI9. HS.

Family and domain databases

Gene3Di2.60.40.820. 1 hit.
4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR032060. DUF4801.
IPR008967. p53-like_TF_DNA-bd.
IPR001699. TF_T-box.
IPR018186. TF_T-box_CS.
[Graphical view]
PANTHERiPTHR11267. PTHR11267. 1 hit.
PfamiPF16059. DUF4801. 1 hit.
PF00010. HLH. 1 hit.
PF00907. T-box. 1 hit.
[Graphical view]
PRINTSiPR00937. TBOX.
SMARTiSM00353. HLH. 1 hit.
SM00425. TBOX. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
SSF49417. SSF49417. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
PS01264. TBOX_2. 1 hit.
PS50252. TBOX_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 183-1134 (ISOFORM 1).
    Tissue: Ovary and Teratocarcinoma.
  2. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] OF 1-1139 (ISOFORM 1).
    Tissue: Duodenum.
  4. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2377-3026 (ISOFORM 1).
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2778-3026 (ISOFORM 1).
    Tissue: Uterus.
  6. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
    Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
    Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-924; SER-1208 AND SER-1457, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645 AND SER-2871, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-534; SER-1208; SER-1430; SER-1457 AND SER-2502, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2882, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-607; SER-851; SER-924; SER-1208; SER-1457; SER-2502; SER-2882 AND SER-2939, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  14. Cited for: INTERACTION WITH ZMYND11.
  15. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-460; LYS-570; LYS-1946; LYS-2074; LYS-2096 AND LYS-2199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2074; LYS-2096 AND LYS-2199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-329; LYS-1207; LYS-1946; LYS-2074; LYS-2096; LYS-2155; LYS-2199; LYS-2245 AND LYS-2374, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMGAP_HUMAN
AccessioniPrimary (citable) accession number: Q8IWI9
Secondary accession number(s): E7ENI0
, F5H7K2, Q9H8R3, Q9H9N7, Q9UG69, Q9Y4E9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 24, 2013
Last modified: July 6, 2016
This is version 118 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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

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.