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Q05195

- MAD1_HUMAN

UniProt

Q05195 - MAD1_HUMAN

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Protein

Max dimerization protein 1

Gene

MXD1

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

Functioni

Transcriptional repressor. MAD binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. MAD thus antagonizes MYC transcriptional activity by competing for MAX.

GO - Molecular functioni

  1. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  2. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: NTNU_SB
  3. sequence-specific DNA binding transcription factor activity Source: ProtInc
  4. transcription cofactor activity Source: ProtInc
  5. transcription corepressor activity Source: ProtInc

GO - Biological processi

  1. cell proliferation Source: ProtInc
  2. multicellular organismal development Source: ProtInc
  3. negative regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Max dimerization protein 1
Short name:
Max dimerizer 1
Alternative name(s):
Protein MAD
Gene namesi
Name:MXD1
Synonyms:MAD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:6761. MXD1.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30520.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 221221Max dimerization protein 1PRO_0000127264Add
BLAST

Post-translational modificationi

Ubiquitinated by BIRC2/c-IAP1, leading to its subsequent degradation by the proteasome.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ05195.
PRIDEiQ05195.

PTM databases

PhosphoSiteiQ05195.

Expressioni

Gene expression databases

BgeeiQ05195.
CleanExiHS_MXD1.
ExpressionAtlasiQ05195. baseline and differential.
GenevestigatoriQ05195.

Organism-specific databases

HPAiHPA001599.

Interactioni

Subunit structurei

Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX. Interacts with RNF17 (By similarity).By similarity

Protein-protein interaction databases

BioGridi110259. 23 interactions.
DIPiDIP-204N.
IntActiQ05195. 1 interaction.
MINTiMINT-1510489.
STRINGi9606.ENSP00000264444.

Structurei

Secondary structure

1
221
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1911Combined sources
Helixi58 – 8124Combined sources
Beta strandi87 – 893Combined sources
Helixi95 – 13440Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E91NMR-B8-20[»]
1G1ENMR-A6-21[»]
1NLWX-ray2.00A/D57-136[»]
1PD7NMR-B5-28[»]
1S5QNMR-A6-21[»]
ProteinModelPortaliQ05195.
SMRiQ05195. Positions 57-135.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05195.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 10853bHLHPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi21 – 4929Nuclear localization signalSequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG238408.
GeneTreeiENSGT00510000046360.
HOGENOMiHOG000247060.
HOVERGENiHBG006314.
InParanoidiQ05195.
KOiK09114.
OMAiDCDRKAI.
PhylomeDBiQ05195.
TreeFamiTF315654.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q05195-1) [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
MAAAVRMNIQ MLLEAADYLE RREREAEHGY ASMLPYNNKD RDALKRRNKS
60 70 80 90 100
KKNNSSSRST HNEMEKNRRA HLRLCLEKLK GLVPLGPESS RHTTLSLLTK
110 120 130 140 150
AKLHIKKLED CDRKAVHQID QLQREQRHLK RQLEKLGIER IRMDSIGSTV
160 170 180 190 200
SSERSDSDRE EIDVDVESTD YLTGDLDWSS SSVSDSDERG SMQSLGSDEG
210 220
YSSTSIKRIK LQDSHKACLG L
Length:221
Mass (Da):25,254
Last modified:February 1, 1995 - v1
Checksum:iB39FAEBFD708B6AB
GO
Isoform 2 (identifier: Q05195-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     58-67: Missing.

Note: No experimental confirmation available.

Show »
Length:211
Mass (Da):24,027
Checksum:i0C30C9CD1A02730B
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei58 – 6710Missing in isoform 2. 1 PublicationVSP_043074

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06895 mRNA. Translation: AAA36194.1.
CR536495 mRNA. Translation: CAG38734.1.
CR541692 mRNA. Translation: CAG46493.1.
AK312734 mRNA. Translation: BAG35605.1.
AC019206 Genomic DNA. Translation: AAY14867.1.
CH471053 Genomic DNA. Translation: EAW99839.1.
BC069377 mRNA. Translation: AAH69377.1.
BC069433 mRNA. Translation: AAH69433.1.
BC098396 mRNA. Translation: AAH98396.1.
BC113531 mRNA. Translation: AAI13532.1.
BC117260 mRNA. Translation: AAI17261.1.
BC143831 mRNA. Translation: AAI43832.1.
CCDSiCCDS1896.1. [Q05195-1]
CCDS56123.1. [Q05195-2]
PIRiA45181.
RefSeqiNP_001189442.1. NM_001202513.1.
NP_001189443.1. NM_001202514.1. [Q05195-2]
NP_002348.1. NM_002357.3. [Q05195-1]
UniGeneiHs.468908.

Genome annotation databases

EnsembliENST00000264444; ENSP00000264444; ENSG00000059728. [Q05195-1]
ENST00000540449; ENSP00000443935; ENSG00000059728. [Q05195-2]
GeneIDi4084.
KEGGihsa:4084.
UCSCiuc002sfy.3. human. [Q05195-1]
uc010yqs.2. human. [Q05195-2]

Polymorphism databases

DMDMi729978.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06895 mRNA. Translation: AAA36194.1 .
CR536495 mRNA. Translation: CAG38734.1 .
CR541692 mRNA. Translation: CAG46493.1 .
AK312734 mRNA. Translation: BAG35605.1 .
AC019206 Genomic DNA. Translation: AAY14867.1 .
CH471053 Genomic DNA. Translation: EAW99839.1 .
BC069377 mRNA. Translation: AAH69377.1 .
BC069433 mRNA. Translation: AAH69433.1 .
BC098396 mRNA. Translation: AAH98396.1 .
BC113531 mRNA. Translation: AAI13532.1 .
BC117260 mRNA. Translation: AAI17261.1 .
BC143831 mRNA. Translation: AAI43832.1 .
CCDSi CCDS1896.1. [Q05195-1 ]
CCDS56123.1. [Q05195-2 ]
PIRi A45181.
RefSeqi NP_001189442.1. NM_001202513.1.
NP_001189443.1. NM_001202514.1. [Q05195-2 ]
NP_002348.1. NM_002357.3. [Q05195-1 ]
UniGenei Hs.468908.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E91 NMR - B 8-20 [» ]
1G1E NMR - A 6-21 [» ]
1NLW X-ray 2.00 A/D 57-136 [» ]
1PD7 NMR - B 5-28 [» ]
1S5Q NMR - A 6-21 [» ]
ProteinModelPortali Q05195.
SMRi Q05195. Positions 57-135.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110259. 23 interactions.
DIPi DIP-204N.
IntActi Q05195. 1 interaction.
MINTi MINT-1510489.
STRINGi 9606.ENSP00000264444.

PTM databases

PhosphoSitei Q05195.

Polymorphism databases

DMDMi 729978.

Proteomic databases

PaxDbi Q05195.
PRIDEi Q05195.

Protocols and materials databases

DNASUi 4084.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264444 ; ENSP00000264444 ; ENSG00000059728 . [Q05195-1 ]
ENST00000540449 ; ENSP00000443935 ; ENSG00000059728 . [Q05195-2 ]
GeneIDi 4084.
KEGGi hsa:4084.
UCSCi uc002sfy.3. human. [Q05195-1 ]
uc010yqs.2. human. [Q05195-2 ]

Organism-specific databases

CTDi 4084.
GeneCardsi GC02P070124.
HGNCi HGNC:6761. MXD1.
HPAi HPA001599.
MIMi 600021. gene.
neXtProti NX_Q05195.
PharmGKBi PA30520.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG238408.
GeneTreei ENSGT00510000046360.
HOGENOMi HOG000247060.
HOVERGENi HBG006314.
InParanoidi Q05195.
KOi K09114.
OMAi DCDRKAI.
PhylomeDBi Q05195.
TreeFami TF315654.

Miscellaneous databases

ChiTaRSi MXD1. human.
EvolutionaryTracei Q05195.
GeneWikii MXD1.
GenomeRNAii 4084.
NextBioi 16006.
PROi Q05195.
SOURCEi Search...

Gene expression databases

Bgeei Q05195.
CleanExi HS_MXD1.
ExpressionAtlasi Q05195. baseline and differential.
Genevestigatori Q05195.

Family and domain databases

Gene3Di 4.10.280.10. 1 hit.
InterProi IPR011598. bHLH_dom.
[Graphical view ]
Pfami PF00010. HLH. 1 hit.
[Graphical view ]
SMARTi SM00353. HLH. 1 hit.
[Graphical view ]
SUPFAMi SSF47459. SSF47459. 1 hit.
PROSITEi PS50888. BHLH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity."
    Ayer D.E., Kretzner L., Eisenman R.N.
    Cell 72:211-222(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Lung.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "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 1).
    Tissue: Placenta.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Brain and Placenta.
  7. "c-IAP1 cooperates with Myc by acting as a ubiquitin ligase for Mad1."
    Xu L., Zhu J., Hu X., Zhu H., Kim H.T., LaBaer J., Goldberg A., Yuan J.
    Mol. Cell 28:914-922(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY BIRC2/C-IAP1.

Entry informationi

Entry nameiMAD1_HUMAN
AccessioniPrimary (citable) accession number: Q05195
Secondary accession number(s): B2R6V8
, B7ZLI6, D6W5G2, Q6FI41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 26, 2014
This is version 138 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3