Q05195 (MAD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Max dimerization protein 1
Short name=Max dimerizer 1

Alternative name(s):
Protein MAD

Gene names

Name:	MXD1
Synonyms:	MAD

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	221 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX. Interacts with RNF17 By similarity.
Subcellular location	Nucleus.
Post-translational modification	Ubiquitinated by BIRC2/c-IAP1, leading to its subsequent degradation by the proteasome. Ref.7
Sequence similarities	Contains 1 bHLH (basic helix-loop-helix) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
Molecular function	Repressor
PTM	Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell proliferation Traceable author statement PubMed 7829091. Source: ProtInc multicellular organismal development Traceable author statement PubMed 7829091. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrion Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW sequence-specific DNA binding transcription factor activity Traceable author statement PubMed 7829091Ref.1. Source: ProtInc transcription corepressor activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q05195-1)

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.

Isoform 2 (identifier: Q05195-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 221

221

Max dimerization protein 1

PRO_0000127264

Regions

Domain

56 – 108

53

bHLH

Motif

21 – 49

29

Nuclear localization signal Potential

Natural variations

Alternative sequence

58 – 67

10

Missing in isoform 2.

VSP_043074

Secondary structure

1

.

.

.

.

.

.

.

.

.

221

Helix Strand Turn

Details...

Helix

9 – 19

11

Helix

58 – 81

24

Beta strand

87 – 89

3

Helix

95 – 134

40

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: B39FAEBFD708B6AB	FASTA	221	25,254
	10 20 30 40 50 60 MAAAVRMNIQ MLLEAADYLE RREREAEHGY ASMLPYNNKD RDALKRRNKS KKNNSSSRST 70 80 90 100 110 120 HNEMEKNRRA HLRLCLEKLK GLVPLGPESS RHTTLSLLTK AKLHIKKLED CDRKAVHQID 130 140 150 160 170 180 QLQREQRHLK RQLEKLGIER IRMDSIGSTV SSERSDSDRE EIDVDVESTD YLTGDLDWSS 190 200 210 220 SSVSDSDERG SMQSLGSDEG YSSTSIKRIK LQDSHKACLG L
	Isoform 2 [UniParc]. Checksum: 0C30C9CD1A02730B	FASTA	211	24,027
	10 20 30 40 50 60 MAAAVRMNIQ MLLEAADYLE RREREAEHGY ASMLPYNNKD RDALKRRNKS KKNNSSSRRA 70 80 90 100 110 120 HLRLCLEKLK GLVPLGPESS RHTTLSLLTK AKLHIKKLED CDRKAVHQID QLQREQRHLK 130 140 150 160 170 180 RQLEKLGIER IRMDSIGSTV SSERSDSDRE EIDVDVESTD YLTGDLDWSS SSVSDSDERG 190 200 210 SMQSLGSDEG YSSTSIKRIK LQDSHKACLG L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00012034.
IPI00976926.

PIR

A45181.

RefSeq

NP_001189442.1. NM_001202513.1.
NP_001189443.1. NM_001202514.1.
NP_002348.1. NM_002357.3.

UniGene

Hs.468908.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q05195.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-204N.

STRING

9606.ENSP00000264444.

PTM databases

PhosphoSite

Q05195.

Polymorphism databases

DMDM

729978.

Proteomic databases

PaxDb

Q05195.

PRIDE

Q05195.

Protocols and materials databases

DNASU

4084.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264444; ENSP00000264444; ENSG00000059728.
ENST00000540449; ENSP00000443935; ENSG00000059728.

GeneID

4084.

KEGG

hsa:4084.

UCSC

uc002sfy.3. human.

Organism-specific databases

CTD

4084.

GeneCards

GC02P070124.

HGNC

HGNC:6761. MXD1.

HPA

HPA001599.

MIM

600021. gene.

neXtProt

NX_Q05195.

PharmGKB

PA30520.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG238408.

HOGENOM

HOG000247060.

HOVERGEN

HBG006314.

InParanoid

Q05195.

KO

K09114.

OMA

CDRKAIH.

OrthoDB

EOG44XJJ1.

PhylomeDB

Q05195.

Enzyme and pathway databases

Pathway_Interaction_DB

telomerasepathway. Regulation of Telomerase.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.

Gene expression databases

ArrayExpress

Q05195.

Bgee

Q05195.

CleanEx

HS_MXD1.

Genevestigator

Q05195.

GermOnline

ENSG00000059728. Homo sapiens.

Family and domain databases

Gene3D

4.10.280.10. 1 hit.

InterPro

IPR011598. bHLH_dom.
[Graphical view]

Pfam

PF00010. HLH. 1 hit.
[Graphical view]

SMART

SM00353. HLH. 1 hit.
[Graphical view]

SUPFAM

SSF47459. HLH_basic. 1 hit.

PROSITE

PS50888. BHLH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q05195.

GenomeRNAi

4084.

NextBio

16006.

SOURCE

Search...

Entry information

Entry name

MAD1_HUMAN

Accession

Primary (citable) accession number: Q05195
Secondary accession number(s): B2R6V8 , B7ZLI6, D6W5G2, Q6FI41

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 124 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.