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Protein

Metastasis-associated protein MTA1

Gene

MTA1

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

Functioni

Transcriptional coregulator which can act as both a transcriptional corepressor and coactivator. As a part of the histone-deacetylase multiprotein complex (NuRD), regulates transcription of its targets by modifying the acetylation status of the target chromatin and cofactor accessibility to the target DNA. In conjunction with other components of NuRD, acts as a transcriptional corepressor of BRCA1, ESR1, TFF1 and CDKN1A. Acts as a transcriptional coactivator of BCAS3, PAX5 and SUMO2, independent of the NuRD complex. Stimulates the expression of WNT1 by inhibiting the expression of its transcriptional corepressor SIX3. Plays a role in the inflammatory responses, both as a target and as a component of the NF-kappa-B signaling and regulates a subset of proinflammatory cytokines such as IL1B, MIP2, and TNF. Regulates p53-dependent and -independent DNA repair processes following genotoxic stress. Regulates the stability and function of p53/TP53 by inhibiting its ubiquitination by COP1 and MDM2 thereby regulating the p53-dependent DNA repair. Plays an important role in tumorigenesis, tumor invasion, and metastasis. Involved in the epigenetic regulation of ESR1 expression in breast cancer in a TFAP2C, IFI16 and HDAC4/5/6-dependent manner. Plays a role in the regulation of the circadian clock and is essential for the generation and maintenance of circadian rhythms under constant light and for normal entrainment of behavior to light-dark (LD) cycles. Positively regulates the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation of its own transcription and the transcription of CRY1. Regulates deacetylation of ARNTL/BMAL1 by regulating SIRT1 expression, resulting in derepressing CRY1-mediated transcription repression. Isoform Short binds to ESR1 and sequesters it in the cytoplasm and enhances its non-genomic responses.6 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri393 – 420GATA-type; atypicalAdd BLAST28

GO - Molecular functioni

  • chromatin binding Source: InterPro
  • core promoter binding Source: UniProtKB
  • core promoter sequence-specific DNA binding Source: UniProtKB
  • histone deacetylase activity Source: Reactome
  • RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  • transcription coactivator activity Source: UniProtKB
  • transcription corepressor activity Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: InterPro
  • zinc ion binding Source: InterPro

GO - Biological processi

  • circadian regulation of gene expression Source: UniProtKB
  • double-strand break repair Source: UniProtKB
  • entrainment of circadian clock by photoperiod Source: UniProtKB
  • locomotor rhythm Source: UniProtKB
  • positive regulation of protein autoubiquitination Source: UniProtKB
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein sumoylation Source: Reactome
  • regulation of gene expression, epigenetic Source: UniProtKB
  • regulation of inflammatory response Source: UniProtKB
  • response to ionizing radiation Source: UniProtKB
  • response to lipopolysaccharide Source: UniProtKB
  • signal transduction Source: ProtInc
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:G66-33126-MONOMER.
ReactomeiR-HSA-3214815. HDACs deacetylate histones.
R-HSA-3232118. SUMOylation of transcription factors.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
SIGNORiQ13330.

Names & Taxonomyi

Protein namesi
Recommended name:
Metastasis-associated protein MTA1
Gene namesi
Name:MTA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:7410. MTA1.

Subcellular locationi

Isoform Long :

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • microtubule Source: UniProtKB
  • nuclear envelope Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi182K → A: Reduced ubiquitination. Significant reduction in ubiquitination; when associated with A-626. 1 Publication1
Mutagenesisi509K → R: Reduced sumoylation and transcriptional corepressor activity. 1 Publication1
Mutagenesisi626K → A: Loss of acetylation and transcriptional coactivator activity. Reduced ubiquitination. Significant reduction in ubiquitination; when associated with A-182. 3 Publications1
Mutagenesisi711 – 713IVI → AAA: Significant loss of interaction with SUMO1 and SUMO2 and reduced transcriptional corepressor activity. 1 Publication3

Organism-specific databases

DisGeNETi9112.
OpenTargetsiENSG00000182979.
PharmGKBiPA31218.

Polymorphism and mutation databases

BioMutaiMTA1.
DMDMi259016275.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000834931 – 715Metastasis-associated protein MTA1Add BLAST715

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei386PhosphoserineCombined sources1
Modified residuei446PhosphoserineCombined sources1
Modified residuei449PhosphoserineCombined sources1
Cross-linki509Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3)
Modified residuei522PhosphoserineCombined sources1
Modified residuei564PhosphothreonineCombined sources1
Modified residuei576PhosphoserineCombined sources1
Modified residuei578PhosphothreonineCombined sources1
Modified residuei626N6-acetyllysine; alternate3 Publications1
Cross-linki626Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei639PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylation by CSNK1G2/CK1 triggered by estrogen enhances corepression of estrogen receptor (ER).1 Publication
Acetylation is essential for its transcriptional coactivator activity.3 Publications
Sumoylation positively regulates its transcriptional corepressor activity but does not affect the protein stability. Sumoylated preferentially by SUMO2 or SUMO3 than SUMO1. Sumoylation is enhanced by PIAS1/3/4 and preferentially sumoylated by SUMO2 in the presence of PIAS1/3/4. Desumoylated by SENP1.1 Publication
Ubiquitinated by RFWD2, which leads to proteasomal degradation.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ13330.
MaxQBiQ13330.
PaxDbiQ13330.
PeptideAtlasiQ13330.
PRIDEiQ13330.

PTM databases

iPTMnetiQ13330.
PhosphoSitePlusiQ13330.

Expressioni

Tissue specificityi

Widely expressed. High expression in brain, liver, kidney, and cardiac muscle, ovaries, adrenal glands and virgin mammary glands. Higher in tumors than in adjacent normal tissue from the same individual. Up-regulated in a wide variety of cancers including breast, liver, ovarian, and colorectal cancer and its expression levels are closely correlated with tumor aggressiveness and metastasis.2 Publications

Developmental stagei

Highly expressed in metastatic cells.

Gene expression databases

BgeeiENSG00000182979.
CleanExiHS_MTA1.
ExpressionAtlasiQ13330. baseline and differential.
GenevisibleiQ13330. HS.

Organism-specific databases

HPAiCAB004508.
HPA005544.

Interactioni

Subunit structurei

Component of the nucleosome-remodeling and histone-deacetylase multiprotein complex (NuRD). Interacts with HDAC1 and ITGB3BP/CENPR. Binds to CSNK1G2 in the cytoplasm. Interacts with NACC2. Interacts with ARNTL/BMAL1 and CLOCK. Interacts with EP300, TFAP2C, IFI16, TPR, HDAC2, UBE2I/UBC9, PIAS1, PIAS3, PIAS4, p53/TP53, MDM2, RFWD2, SUMO1, SUMO2, SENP1 and SENP2. Interacts with SIX3; facilitates the binding of SIX3 to the core DNA motif of SIX3 promoter (By similarity).By similarity12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EHMT2Q96KQ79EBI-714236,EBI-744366
ESR1P033724EBI-714236,EBI-78473
HDAC1Q1354710EBI-714236,EBI-301834
HDAC2Q927695EBI-714236,EBI-301821
HIF1AQ166656EBI-714236,EBI-447269
IKZF1Q134223EBI-714236,EBI-745305
KHDRBS2Q5VWX13EBI-714236,EBI-742808
KPNA3Q8IYQ93EBI-714236,EBI-742146
KRT40Q6A1623EBI-714236,EBI-10171697
KRTAP10-8P604103EBI-714236,EBI-10171774
LZTS2Q9BRK43EBI-714236,EBI-741037
MAGEA11P43364-23EBI-714236,EBI-10178634
NOTCH2NLQ7Z3S93EBI-714236,EBI-945833
RBBP4Q090288EBI-714236,EBI-620823
SATQ6ICU93EBI-714236,EBI-10178867
SH3GL1Q6FGM03EBI-714236,EBI-10173690
ZEB2O6031512EBI-714236,EBI-717614

GO - Molecular functioni

  • RNA polymerase II repressing transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi114562. 106 interactors.
DIPiDIP-41751N.
IntActiQ13330. 62 interactors.
MINTiMINT-255103.
STRINGi9606.ENSP00000333633.

Structurei

Secondary structure

1715
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni171 – 173Combined sources3
Turni192 – 194Combined sources3
Beta strandi195 – 199Combined sources5
Helixi207 – 224Combined sources18
Helixi238 – 246Combined sources9
Helixi248 – 260Combined sources13
Turni261 – 263Combined sources3
Helixi265 – 272Combined sources8
Helixi284 – 287Combined sources4
Helixi290 – 303Combined sources14
Helixi307 – 313Combined sources7
Helixi320 – 330Combined sources11
Beta strandi472 – 474Combined sources3
Helixi477 – 485Combined sources9
Helixi487 – 490Combined sources4
Helixi492 – 495Combined sources4
Helixi505 – 514Combined sources10
Helixi534 – 543Combined sources10
Helixi674 – 680Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BKXX-ray3.00A162-335[»]
4PBYX-ray2.50C/D656-686[»]
4PBZX-ray2.15B670-695[»]
4PC0X-ray2.50C/D670-711[»]
5FXYX-ray3.20B/D/F/H464-546[»]
5ICNX-ray3.30A162-354[»]
ProteinModelPortaliQ13330.
SMRiQ13330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 164BAHPROSITE-ProRule annotationAdd BLAST164
Domaini165 – 276ELM2PROSITE-ProRule annotationAdd BLAST112
Domaini283 – 335SANTPROSITE-ProRule annotationAdd BLAST53

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi545 – 552SH3-bindingSequence analysis8
Motifi696 – 705SH3-bindingSequence analysis10
Motifi711 – 715SUMO interaction motif 1 (SIM); crucial for efficient sumoylation5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi697 – 705Poly-Pro9

Domaini

Isoform Short contains a Leu-Arg-Ile-Leu-Leu motif (ER binding motif).

Sequence similaritiesi

Contains 1 BAH domain.PROSITE-ProRule annotation
Contains 1 ELM2 domain.PROSITE-ProRule annotation
Contains 1 GATA-type zinc finger.Curated
Contains 1 SANT domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri393 – 420GATA-type; atypicalAdd BLAST28

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3554. Eukaryota.
ENOG410XSAJ. LUCA.
GeneTreeiENSGT00580000081398.
HOGENOMiHOG000045387.
HOVERGENiHBG002598.
InParanoidiQ13330.
KOiK11660.
OMAiDKHATLS.
OrthoDBiEOG091G04Z4.
PhylomeDBiQ13330.
TreeFamiTF106444.

Family and domain databases

InterProiIPR001025. BAH_dom.
IPR000949. ELM2_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR000679. Znf_GATA.
[Graphical view]
PfamiPF01426. BAH. 1 hit.
PF01448. ELM2. 1 hit.
PF00320. GATA. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
SMARTiSM00439. BAH. 1 hit.
SM01189. ELM2. 1 hit.
SM00717. SANT. 1 hit.
SM00401. ZnF_GATA. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS51038. BAH. 1 hit.
PS51156. ELM2. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: Q13330-1) [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
MAANMYRVGD YVYFENSSSN PYLIRRIEEL NKTANGNVEA KVVCFYRRRD
60 70 80 90 100
ISSTLIALAD KHATLSVCYK AGPGADNGEE GEIEEEMENP EMVDLPEKLK
110 120 130 140 150
HQLRHRELFL SRQLESLPAT HIRGKCSVTL LNETESLKSY LEREDFFFYS
160 170 180 190 200
LVYDPQQKTL LADKGEIRVG NRYQADITDL LKEGEEDGRD QSRLETQVWE
210 220 230 240 250
AHNPLTDKQI DQFLVVARSV GTFARALDCS SSVRQPSLHM SAAAASRDIT
260 270 280 290 300
LFHAMDTLHK NIYDISKAIS ALVPQGGPVL CRDEMEEWSA SEANLFEEAL
310 320 330 340 350
EKYGKDFTDI QQDFLPWKSL TSIIEYYYMW KTTDRYVQQK RLKAAEAESK
360 370 380 390 400
LKQVYIPNYN KPNPNQISVN NVKAGVVNGT GAPGQSPGAG RACESCYTTQ
410 420 430 440 450
SYQWYSWGPP NMQCRLCASC WTYWKKYGGL KMPTRLDGER PGPNRSNMSP
460 470 480 490 500
HGLPARSSGS PKFAMKTRQA FYLHTTKLTR IARRLCREIL RPWHAARHPY
510 520 530 540 550
LPINSAAIKA ECTARLPEAS QSPLVLKQAV RKPLEAVLRY LETHPRPPKP
560 570 580 590 600
DPVKSVSSVL SSLTPAKVAP VINNGSPTIL GKRSYEQHNG VDGNMKKRLL
610 620 630 640 650
MPSRGLANHG QARHMGPSRN LLLNGKSYPT KVRLIRGGSL PPVKRRRMNW
660 670 680 690 700
IDAPDDVFYM ATEETRKIRK LLSSSETKRA ARRPYKPIAL RQSQALPPRP
710
PPPAPVNDEP IVIED
Length:715
Mass (Da):80,786
Last modified:September 22, 2009 - v2
Checksum:i2D5330F0489AE62E
GO
Isoform Short (identifier: Q13330-2) [UniParc]FASTAAdd to basket
Also known as: MTA1S

The sequence of this isoform differs from the canonical sequence as follows:
     398-430: TTQSYQWYSWGPPNMQCRLCASCWTYWKKYGGL → MSSLRILLDILEEIWWLENANPVRWREARTKPQ
     431-715: Missing.

Show »
Length:430
Mass (Da):49,017
Checksum:iDE4B752E9476C6CE
GO
Isoform 3 (identifier: Q13330-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     64-81: TLSVCYKAGPGADNGEEG → R

Show »
Length:698
Mass (Da):79,192
Checksum:iBCF775330376172E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti498H → N in AAA78935 (PubMed:8083195).Curated1
Sequence conflicti545P → R in AAI42942 (PubMed:15489334).Curated1
Sequence conflicti655D → G in AAA78935 (PubMed:8083195).Curated1
Sequence conflicti661 – 662AT → PK in AAA78935 (PubMed:8083195).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_055847372V → I.Corresponds to variant rs4983413dbSNPEnsembl.1
Natural variantiVAR_058965612A → T.3 PublicationsCorresponds to variant rs13707dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04220764 – 81TLSVC…NGEEG → R in isoform 3. 1 PublicationAdd BLAST18
Alternative sequenceiVSP_001601398 – 430TTQSY…KYGGL → MSSLRILLDILEEIWWLENA NPVRWREARTKPQ in isoform Short. 1 PublicationAdd BLAST33
Alternative sequenceiVSP_001602431 – 715Missing in isoform Short. 1 PublicationAdd BLAST285

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35113 mRNA. Translation: AAA78935.1.
AF508978 mRNA. Translation: AAN01613.1.
AL928654 Genomic DNA. No translation available.
BC009443 mRNA. Translation: AAH09443.2.
BC142941 mRNA. Translation: AAI42942.1.
BX248776 mRNA. Translation: CAD66583.1.
CCDSiCCDS32169.1. [Q13330-1]
CCDS55954.1. [Q13330-2]
RefSeqiNP_001190187.1. NM_001203258.1. [Q13330-2]
NP_004680.2. NM_004689.3. [Q13330-1]
UniGeneiHs.525629.

Genome annotation databases

EnsembliENST00000331320; ENSP00000333633; ENSG00000182979. [Q13330-1]
ENST00000405646; ENSP00000384180; ENSG00000182979. [Q13330-3]
ENST00000438610; ENSP00000393438; ENSG00000182979. [Q13330-2]
GeneIDi9112.
KEGGihsa:9112.
UCSCiuc001yqx.4. human. [Q13330-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35113 mRNA. Translation: AAA78935.1.
AF508978 mRNA. Translation: AAN01613.1.
AL928654 Genomic DNA. No translation available.
BC009443 mRNA. Translation: AAH09443.2.
BC142941 mRNA. Translation: AAI42942.1.
BX248776 mRNA. Translation: CAD66583.1.
CCDSiCCDS32169.1. [Q13330-1]
CCDS55954.1. [Q13330-2]
RefSeqiNP_001190187.1. NM_001203258.1. [Q13330-2]
NP_004680.2. NM_004689.3. [Q13330-1]
UniGeneiHs.525629.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BKXX-ray3.00A162-335[»]
4PBYX-ray2.50C/D656-686[»]
4PBZX-ray2.15B670-695[»]
4PC0X-ray2.50C/D670-711[»]
5FXYX-ray3.20B/D/F/H464-546[»]
5ICNX-ray3.30A162-354[»]
ProteinModelPortaliQ13330.
SMRiQ13330.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114562. 106 interactors.
DIPiDIP-41751N.
IntActiQ13330. 62 interactors.
MINTiMINT-255103.
STRINGi9606.ENSP00000333633.

PTM databases

iPTMnetiQ13330.
PhosphoSitePlusiQ13330.

Polymorphism and mutation databases

BioMutaiMTA1.
DMDMi259016275.

Proteomic databases

EPDiQ13330.
MaxQBiQ13330.
PaxDbiQ13330.
PeptideAtlasiQ13330.
PRIDEiQ13330.

Protocols and materials databases

DNASUi9112.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331320; ENSP00000333633; ENSG00000182979. [Q13330-1]
ENST00000405646; ENSP00000384180; ENSG00000182979. [Q13330-3]
ENST00000438610; ENSP00000393438; ENSG00000182979. [Q13330-2]
GeneIDi9112.
KEGGihsa:9112.
UCSCiuc001yqx.4. human. [Q13330-1]

Organism-specific databases

CTDi9112.
DisGeNETi9112.
GeneCardsiMTA1.
HGNCiHGNC:7410. MTA1.
HPAiCAB004508.
HPA005544.
MIMi603526. gene.
neXtProtiNX_Q13330.
OpenTargetsiENSG00000182979.
PharmGKBiPA31218.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3554. Eukaryota.
ENOG410XSAJ. LUCA.
GeneTreeiENSGT00580000081398.
HOGENOMiHOG000045387.
HOVERGENiHBG002598.
InParanoidiQ13330.
KOiK11660.
OMAiDKHATLS.
OrthoDBiEOG091G04Z4.
PhylomeDBiQ13330.
TreeFamiTF106444.

Enzyme and pathway databases

BioCyciZFISH:G66-33126-MONOMER.
ReactomeiR-HSA-3214815. HDACs deacetylate histones.
R-HSA-3232118. SUMOylation of transcription factors.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
SIGNORiQ13330.

Miscellaneous databases

ChiTaRSiMTA1. human.
GeneWikiiMTA1.
GenomeRNAii9112.
PROiQ13330.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000182979.
CleanExiHS_MTA1.
ExpressionAtlasiQ13330. baseline and differential.
GenevisibleiQ13330. HS.

Family and domain databases

InterProiIPR001025. BAH_dom.
IPR000949. ELM2_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR000679. Znf_GATA.
[Graphical view]
PfamiPF01426. BAH. 1 hit.
PF01448. ELM2. 1 hit.
PF00320. GATA. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
SMARTiSM00439. BAH. 1 hit.
SM01189. ELM2. 1 hit.
SM00717. SANT. 1 hit.
SM00401. ZnF_GATA. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS51038. BAH. 1 hit.
PS51156. ELM2. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMTA1_HUMAN
AccessioniPrimary (citable) accession number: Q13330
Secondary accession number(s): A5PLK4
, Q86SW2, Q8NFI8, Q96GI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 22, 2009
Last modified: November 30, 2016
This is version 172 of the entry and version 2 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 14
    Human chromosome 14: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.