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Protein

Max dimerization protein 1

Gene

MXD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: NTNU_SB
  • sequence-specific DNA binding transcription factor activity Source: ProtInc
  • transcription cofactor activity Source: ProtInc
  • transcription corepressor activity Source: ProtInc

GO - Biological processi

  • cell proliferation Source: ProtInc
  • multicellular organismal development Source: ProtInc
  • 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 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:6761. MXD1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30520.

Polymorphism and mutation databases

BioMutaiMXD1.
DMDMi729978.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
MAXP612442EBI-8833637,EBI-751711

Protein-protein interaction databases

BioGridi110259. 22 interactions.
DIPiDIP-204N.
IntActiQ05195. 3 interactions.
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.
OMAiLQDNHKT.
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. AlignAdd to basket

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]

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.
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.

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...

Protein-protein interaction databases

BioGridi110259. 22 interactions.
DIPiDIP-204N.
IntActiQ05195. 3 interactions.
MINTiMINT-1510489.
STRINGi9606.ENSP00000264444.

PTM databases

PhosphoSiteiQ05195.

Polymorphism and mutation databases

BioMutaiMXD1.
DMDMi729978.

Proteomic databases

PaxDbiQ05195.
PRIDEiQ05195.

Protocols and materials databases

DNASUi4084.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi4084.
GeneCardsiGC02P070124.
HGNCiHGNC:6761. MXD1.
HPAiHPA001599.
MIMi600021. gene.
neXtProtiNX_Q05195.
PharmGKBiPA30520.
GenAtlasiSearch...

Phylogenomic databases

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

Miscellaneous databases

ChiTaRSiMXD1. human.
EvolutionaryTraceiQ05195.
GeneWikiiMXD1.
GenomeRNAii4084.
NextBioi16006.
PROiQ05195.
SOURCEiSearch...

Gene expression databases

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

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]
ProtoNetiSearch...

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: May 27, 2015
This is version 141 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

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.