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Q02078

- MEF2A_HUMAN

UniProt

Q02078 - MEF2A_HUMAN

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Protein

Myocyte-specific enhancer factor 2A

Gene

MEF2A

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

Functioni

Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT]4TAR-3', found in numerous muscle-specific genes. Also involved in the activation of numerous growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. In cerebellar granule neurons, phosphorylated and sumoylated MEF2A represses transcription of NUR77 promoting synaptic differentiation. Associates with chromatin to the ZNF16 promoter.8 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei176 – 1772CleavageCurated
Sitei213 – 2142CleavageCurated
Sitei466 – 4672CleavageCurated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi58 – 8629Mef2-typeSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. activating transcription factor binding Source: UniProtKB
  2. chromatin binding Source: UniProtKB
  3. histone acetyltransferase binding Source: UniProtKB
  4. histone deacetylase binding Source: UniProtKB
  5. protein heterodimerization activity Source: UniProtKB
  6. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  7. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  8. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: Ensembl
  9. RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
  10. RNA polymerase II transcription coactivator activity Source: BHF-UCL
  11. RNA polymerase II transcription factor binding Source: BHF-UCL
  12. sequence-specific DNA binding Source: UniProtKB
  13. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
  14. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  15. SMAD binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cardiac conduction Source: UniProtKB
  3. cellular response to calcium ion Source: UniProtKB
  4. dendrite morphogenesis Source: UniProtKB
  5. ERK5 cascade Source: UniProtKB
  6. heart development Source: UniProtKB
  7. innate immune response Source: Reactome
  8. MAPK cascade Source: UniProtKB
  9. mitochondrial genome maintenance Source: UniProtKB
  10. mitochondrion distribution Source: UniProtKB
  11. muscle cell differentiation Source: Reactome
  12. muscle organ development Source: UniProtKB
  13. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  14. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  15. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  16. neurotrophin TRK receptor signaling pathway Source: Reactome
  17. positive regulation of muscle cell differentiation Source: Reactome
  18. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  19. stress-activated MAPK cascade Source: Reactome
  20. toll-like receptor 10 signaling pathway Source: Reactome
  21. toll-like receptor 2 signaling pathway Source: Reactome
  22. toll-like receptor 3 signaling pathway Source: Reactome
  23. toll-like receptor 4 signaling pathway Source: Reactome
  24. toll-like receptor 5 signaling pathway Source: Reactome
  25. toll-like receptor 9 signaling pathway Source: Reactome
  26. toll-like receptor signaling pathway Source: Reactome
  27. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  28. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  29. transcription, DNA-templated Source: UniProtKB
  30. transcription from RNA polymerase II promoter Source: GOC
  31. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  32. ventricular cardiac myofibril assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Apoptosis, Differentiation, Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_12599. ERK/MAPK targets.
REACT_21402. CDO in myogenesis.
SignaLinkiQ02078.

Names & Taxonomyi

Protein namesi
Recommended name:
Myocyte-specific enhancer factor 2A
Alternative name(s):
Serum response factor-like protein 1
Gene namesi
Name:MEF2A
Synonyms:MEF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:6993. MEF2A.

Subcellular locationi

Nucleus 2 PublicationsPROSITE-ProRule annotation

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nuclear chromatin Source: BHF-UCL
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Coronary artery disease, autosomal dominant, 1 (ADCAD1) [MIM:608320]: A common heart disease characterized by reduced or absent blood flow in one or more of the arteries that encircle and supply the heart. Its most important complication is acute myocardial infarction.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi176 – 1761D → A: Abolishes cleavage at sites 1 and 2 by caspase 3. Increased cleavage at site 3 by caspase 3. 1 Publication
Mutagenesisi213 – 2131D → A: Abolishes cleavage at sites 2 and 3 by caspase 7. 1 Publication
Mutagenesisi255 – 2551S → A: Slightly increased MEF2A protein level. 1 Publication
Mutagenesisi255 – 2551S → D: Decreased MEF2A protein level. 1 Publication
Mutagenesisi269 – 2691R → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-270. 1 Publication
Mutagenesisi270 – 2701K → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-269. 1 Publication
Mutagenesisi273 – 2731L → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-275. 1 Publication
Mutagenesisi275 – 2751V → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-273. 1 Publication
Mutagenesisi277 – 2771I → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-278. 1 Publication
Mutagenesisi278 – 2781P → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-277. 1 Publication
Mutagenesisi312 – 3121T → A: Greatly reduced p38-mediated phosphorylation. Abolishes p38-mediated transcriptional activation; when associated with A-319. 2 Publications
Mutagenesisi319 – 3191T → A: Greatly reduced p38-mediated phosphorylation. Abolishes P38-mediated transcriptional activation; when associated with A-312. 2 Publications
Mutagenesisi355 – 3551S → A: No effect on p38-mediated transcriptional activity. 2 Publications
Mutagenesisi387 – 3871S → A: No effect on p38-mediated phosphorylation.
Mutagenesisi403 – 4031K → R: Abolishes sumoylation. No change in subcellular location nor in DNA binding. Loss of transcriptional repression. 2 Publications
Mutagenesisi408 – 4081S → A: Loss of sumoylation. 2 Publications
Mutagenesisi408 – 4081S → D: Rescues sumoylation. 2 Publications
Mutagenesisi453 – 4531S → A: No effect on p38-mediated phosphorylation. 1 Publication
Mutagenesisi479 – 4791S → A: No effect on p38-mediated phosphorylation. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi608320. phenotype.
PharmGKBiPA30731.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 507507Myocyte-specific enhancer factor 2APRO_0000199428Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591Phosphoserine; by CK2By similarity
Modified residuei98 – 981Phosphoserine1 Publication
Modified residuei235 – 2351Phosphoserine1 Publication
Modified residuei249 – 2491N6-acetyllysine1 Publication
Modified residuei255 – 2551Phosphoserine; by MAPK142 Publications
Modified residuei312 – 3121Phosphothreonine; by MAPK7 and MAPK14; alternate5 Publications
Modified residuei312 – 3121Phosphothreonine; by NLK; alternate5 Publications
Modified residuei319 – 3191Phosphothreonine; by MAPK7 and MAPK144 Publications
Modified residuei355 – 3551Phosphoserine; by MAPK71 Publication
Modified residuei403 – 4031N6-acetyllysine; alternateBy similarity
Cross-linki403 – 403Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Modified residuei408 – 4081Phosphoserine; by CDK54 Publications
Modified residuei453 – 4531Phosphoserine; by MAPK1 Publication

Post-translational modificationi

Constitutive phosphorylation on Ser-408 promotes Lys-403 sumoylation thus preventing acetylation at this site. Dephosphorylation on Ser-408 by PPP3CA upon neuron depolarization promotes a switch from sumoylation to acetylation on residue Lys-403 leading to inhibition of dendrite claw differentiation. Phosphorylation on Thr-312 and Thr-319 are the main sites involved in p38 MAPK signaling and activate transcription. Phosphorylated on these sites by MAPK14/p38alpha and MAPK11/p38beta, but not by MAPK13/p38delta nor by MAPK12/p38gamma. Phosphorylation on Ser-408 by CDK5 induced by neurotoxicity inhibits MEF2A transcriptional activation leading to apoptosis of cortical neurons. Phosphorylation on Thr-312, Thr-319 and Ser-355 can be induced by EGF.12 Publications
Sumoylation on Lys-403 is enhanced by PIAS1 and represses transcriptional activity. Phosphorylation on Ser-408 is required for sumoylation. Has no effect on nuclear location nor on DNA binding. Sumoylated with SUMO1 and, to a lesser extent with SUMO2 and SUMO3. PIASx facilitates sumoylation in postsynaptic dendrites in the cerebellar cortex and promotes their morphogenesis (By similarity).By similarity
Acetylation on Lys-403 activates transcriptional activity. Acetylated by p300 on several sites in diffentiating myocytes. Acetylation on Lys-4 increases DNA binding and transactivation (By similarity). Hyperacetylation by p300 leads to enhanced cardiac myocyte growth and heart failure.By similarity
Proteolytically cleaved in cerebellar granule neurons on several sites by caspase 3 and caspase 7 following neurotoxicity. Preferentially cleaves the CDK5-mediated hyperphosphorylated form which leads to neuron apoptosis and transcriptional inactivation.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ02078.
PaxDbiQ02078.
PRIDEiQ02078.

PTM databases

PhosphoSiteiQ02078.

Miscellaneous databases

PMAP-CutDBQ02078.

Expressioni

Tissue specificityi

Isoform MEF2 and isoform MEFA are expressed only in skeletal and cardiac muscle and in the brain. Isoform RSRFC4 and isoform RSRFC9 are expressed in all tissues examined.2 Publications

Gene expression databases

BgeeiQ02078.
CleanExiHS_MEF2A.
ExpressionAtlasiQ02078. baseline and differential.
GenevestigatoriQ02078.

Organism-specific databases

HPAiCAB004499.
HPA046597.
HPA056563.

Interactioni

Subunit structurei

Binds DNA as a homo- or heterodimer. Dimerizes with MEF2D. Interacts with HDAC7 (By similarity). Interacts with PIAS1; the interaction enhances sumoylation. Interacts with HDAC4, HDAC9 and SLC2A4RG. Interacts (via the N-terminal) with MAPK7; the interaction results in the phosphorylation and transcriptional activity of MEF2A.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PITX2Q99697-32EBI-2656305,EBI-1175243

Protein-protein interaction databases

BioGridi110369. 30 interactions.
DIPiDIP-40711N.
IntActiQ02078. 11 interactions.
MINTiMINT-104848.
STRINGi9606.ENSP00000346389.

Structurei

Secondary structure

1
507
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 3825Combined sources
Beta strandi42 – 487Combined sources
Turni50 – 523Combined sources
Beta strandi54 – 607Combined sources
Helixi62 – 7110Combined sources
Beta strandi77 – 804Combined sources
Helixi81 – 9010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C7UNMR-A/B2-86[»]
1EGWX-ray1.50A/B/C/D2-78[»]
1LEWX-ray2.30B269-280[»]
3KOVX-ray2.90A/B/I/J2-91[»]
3MU6X-ray2.43A/B/C/D2-70[»]
3P57X-ray2.19A/B/C/D/I/J2-91[»]
ProteinModelPortaliQ02078.
SMRiQ02078. Positions 2-91.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02078.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 5755MADS-boxPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni266 – 28318Required for interaction with MAPKsAdd
BLAST
Regioni289 – 2968Beta domain

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 3128Lys-rich (basic)Add
BLAST
Compositional biasi141 – 18646Ser/Thr-richAdd
BLAST
Compositional biasi420 – 44627Gln/Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the MEF2 family.Curated
Contains 1 MADS-box domain.PROSITE-ProRule annotation
Contains 1 Mef2-type DNA-binding domain.Curated

Phylogenomic databases

eggNOGiCOG5068.
GeneTreeiENSGT00390000011828.
HOGENOMiHOG000230620.
HOVERGENiHBG053944.
InParanoidiQ02078.
KOiK09260.
PhylomeDBiQ02078.
TreeFamiTF314067.

Family and domain databases

InterProiIPR022102. HJURP_C.
IPR002100. TF_MADSbox.
[Graphical view]
PfamiPF12347. HJURP_C. 1 hit.
PF00319. SRF-TF. 1 hit.
[Graphical view]
PRINTSiPR00404. MADSDOMAIN.
SMARTiSM00432. MADS. 1 hit.
[Graphical view]
SUPFAMiSSF55455. SSF55455. 1 hit.
PROSITEiPS00350. MADS_BOX_1. 1 hit.
PS50066. MADS_BOX_2. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. Align

Isoform MEF2 (identifier: Q02078-1) [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
MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS
60 70 80 90 100
SNKLFQYAST DMDKVLLKYT EYNEPHESRT NSDIVEALNK KEHRGCDSPD
110 120 130 140 150
PDTSYVLTPH TEEKYKKINE EFDNMMRNHK IAPGLPPQNF SMSVTVPVTS
160 170 180 190 200
PNALSYTNPG SSLVSPSLAA SSTLTDSSML SPPQTTLHRN VSPGAPQRPP
210 220 230 240 250
STGNAGGMLS TTDLTVPNGA GSSPVGNGFV NSRASPNLIG ATGANSLGKV
260 270 280 290 300
MPTKSPPPPG GGNLGMNSRK PDLRVVIPPS SKGMMPPLSE EEELELNTQR
310 320 330 340 350
ISSSQATQPL ATPVVSVTTP SLPPQGLVYS AMPTAYNTDY SLTSADLSAL
360 370 380 390 400
QGFNSPGMLS LGQVSAWQQH HLGQAALSSL VAGGQLSQGS NLSINTNQNI
410 420 430 440 450
SIKSEPISPP RDRMTPSGFQ QQQQQQQQQQ PPPPPQPQPQ PPQPQPRQEM
460 470 480 490 500
GRSPVDSLSS SSSSYDGSDR EDPRGDFHSP IVLGRPPNTE DRESPSVKRM

RMDAWVT
Length:507
Mass (Da):54,811
Last modified:November 1, 1995 - v1
Checksum:i362BA4FBCC792CE2
GO
Isoform MEFA (identifier: Q02078-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-132: ALNKKEHRGC...DNMMRNHKIA → TLRKKGLNGC...DSDFIFKRGP

Show »
Length:505
Mass (Da):54,442
Checksum:iE0032FA6F955D7F7
GO
Isoform RSRFC4 (identifier: Q02078-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     289-296: Missing.
     420-421: Missing.

Show »
Length:497
Mass (Da):53,596
Checksum:iA255A8EDC8B07FB0
GO
Isoform RSRFC9 (identifier: Q02078-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-132: ALNKKEHRGC...DNMMRNHKIA → TLRKKGLNGC...DSDFIFKRGP
     289-296: Missing.
     420-421: Missing.

Show »
Length:495
Mass (Da):53,227
Checksum:i3C083C4EFC3872F0
GO
Isoform 5 (identifier: Q02078-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     289-296: Missing.

Note: No experimental confirmation available.

Show »
Length:499
Mass (Da):53,852
Checksum:iFE3A83DDCE477C27
GO
Isoform 6 (identifier: Q02078-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-132: ALNKKEHRGC...DNMMRNHKIA → TLRKKGLNGC...DSDFIFKRGP
     289-296: Missing.

Note: No experimental confirmation available.

Show »
Length:497
Mass (Da):53,483
Checksum:iF4A61D805AE448AF
GO
Isoform 7 (identifier: Q02078-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     19-86: Missing.
     87-132: ALNKKEHRGC...DNMMRNHKIA → TLRKKGLNGC...DSDFIFKRGP

Note: No experimental confirmation available. Contains a phosphoserine at position 30.

Show »
Length:437
Mass (Da):46,529
Checksum:iD28A536D0F0188BE
GO
Isoform 8 (identifier: Q02078-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     19-62: VTFTKRKFGL...KLFQYASTDM → TLRKKGLNGC...DSDFIFKRGP
     63-132: Missing.
     289-296: Missing.

Note: No experimental confirmation available. Contains a phosphoserine at position 30.

Show »
Length:429
Mass (Da):45,570
Checksum:iB356416F17385FCD
GO

Sequence cautioni

The sequence AAH53871.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD92222.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti430 – 4301Missing in AAB17195. 1 PublicationCurated
Sequence conflicti430 – 4301Missing in AAB17196. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti263 – 2631N → S.1 Publication
Corresponds to variant rs121918530 [ dbSNP | Ensembl ].
VAR_038407
Natural varianti279 – 2791P → L.3 Publications
Corresponds to variant rs121918529 [ dbSNP | Ensembl ].
VAR_038408
Natural varianti283 – 2831G → D.1 Publication
VAR_038409
Natural varianti440 – 4467Missing Loss of nuclear localization; 66% decrease in transcription activation; loss of synergistic activation by MEF2A and GATA1 through a dominant-negative mechanism.
VAR_017743

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei19 – 8668Missing in isoform 7. 1 PublicationVSP_043338Add
BLAST
Alternative sequencei19 – 6244VTFTK…ASTDM → TLRKKGLNGCESPDADDYFE HSPLSEDRFSKLNEDSDFIF KRGP in isoform 8. 1 PublicationVSP_046018Add
BLAST
Alternative sequencei63 – 13270Missing in isoform 8. 1 PublicationVSP_046019Add
BLAST
Alternative sequencei87 – 13246ALNKK…NHKIA → TLRKKGLNGCESPDADDYFE HSPLSEDRFSKLNEDSDFIF KRGP in isoform MEFA, isoform RSRFC9, isoform 6 and isoform 7. 5 PublicationsVSP_006240Add
BLAST
Alternative sequencei289 – 2968Missing in isoform RSRFC4, isoform RSRFC9, isoform 5, isoform 6 and isoform 8. 5 PublicationsVSP_006241
Alternative sequencei420 – 4212Missing in isoform RSRFC4 and isoform RSRFC9. 3 PublicationsVSP_006242

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16312 mRNA. Translation: CAA76175.1.
X63381 mRNA. Translation: CAA44979.1.
X68503 mRNA. Translation: CAA48516.1.
X68505 mRNA. Translation: CAA48517.1.
U49020
, U44889, U49012, U49013, U49015, U49016, U49017, U49018, U49019 Genomic DNA. Translation: AAB17195.1.
U49020
, U44889, U49012, U49013, U49015, U49016, U49017, U49018, U49019 Genomic DNA. Translation: AAB17196.1.
AK294207 mRNA. Translation: BAG57518.1.
AB208985 mRNA. Translation: BAD92222.1. Different initiation.
AC015660 Genomic DNA. No translation available.
AC022692 Genomic DNA. No translation available.
AC103967 Genomic DNA. No translation available.
BC013437 mRNA. Translation: AAH13437.1.
BC053871 mRNA. Translation: AAH53871.1. Different initiation.
CCDSiCCDS45362.1. [Q02078-5]
CCDS45363.1. [Q02078-7]
CCDS53978.1. [Q02078-6]
CCDS58401.1. [Q02078-8]
PIRiC39481.
S25831.
RefSeqiNP_001124398.1. NM_001130926.1. [Q02078-6]
NP_001124399.1. NM_001130927.1. [Q02078-7]
NP_001124400.1. NM_001130928.1. [Q02078-8]
NP_001165365.1. NM_001171894.1. [Q02078-6]
NP_005578.2. NM_005587.2. [Q02078-5]
XP_005254972.1. XM_005254915.1. [Q02078-6]
UniGeneiHs.268675.

Genome annotation databases

EnsembliENST00000338042; ENSP00000337202; ENSG00000068305. [Q02078-6]
ENST00000354410; ENSP00000346389; ENSG00000068305. [Q02078-5]
ENST00000449277; ENSP00000399460; ENSG00000068305. [Q02078-8]
ENST00000557785; ENSP00000453441; ENSG00000068305. [Q02078-6]
ENST00000557942; ENSP00000453095; ENSG00000068305. [Q02078-2]
ENST00000558812; ENSP00000454120; ENSG00000068305. [Q02078-7]
GeneIDi4205.
KEGGihsa:4205.
UCSCiuc002bve.3. human. [Q02078-2]
uc002bvf.3. human. [Q02078-5]
uc002bvg.3. human. [Q02078-6]
uc010urv.2. human. [Q02078-7]
uc010urw.2. human. [Q02078-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16312 mRNA. Translation: CAA76175.1 .
X63381 mRNA. Translation: CAA44979.1 .
X68503 mRNA. Translation: CAA48516.1 .
X68505 mRNA. Translation: CAA48517.1 .
U49020
, U44889 , U49012 , U49013 , U49015 , U49016 , U49017 , U49018 , U49019 Genomic DNA. Translation: AAB17195.1 .
U49020
, U44889 , U49012 , U49013 , U49015 , U49016 , U49017 , U49018 , U49019 Genomic DNA. Translation: AAB17196.1 .
AK294207 mRNA. Translation: BAG57518.1 .
AB208985 mRNA. Translation: BAD92222.1 . Different initiation.
AC015660 Genomic DNA. No translation available.
AC022692 Genomic DNA. No translation available.
AC103967 Genomic DNA. No translation available.
BC013437 mRNA. Translation: AAH13437.1 .
BC053871 mRNA. Translation: AAH53871.1 . Different initiation.
CCDSi CCDS45362.1. [Q02078-5 ]
CCDS45363.1. [Q02078-7 ]
CCDS53978.1. [Q02078-6 ]
CCDS58401.1. [Q02078-8 ]
PIRi C39481.
S25831.
RefSeqi NP_001124398.1. NM_001130926.1. [Q02078-6 ]
NP_001124399.1. NM_001130927.1. [Q02078-7 ]
NP_001124400.1. NM_001130928.1. [Q02078-8 ]
NP_001165365.1. NM_001171894.1. [Q02078-6 ]
NP_005578.2. NM_005587.2. [Q02078-5 ]
XP_005254972.1. XM_005254915.1. [Q02078-6 ]
UniGenei Hs.268675.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C7U NMR - A/B 2-86 [» ]
1EGW X-ray 1.50 A/B/C/D 2-78 [» ]
1LEW X-ray 2.30 B 269-280 [» ]
3KOV X-ray 2.90 A/B/I/J 2-91 [» ]
3MU6 X-ray 2.43 A/B/C/D 2-70 [» ]
3P57 X-ray 2.19 A/B/C/D/I/J 2-91 [» ]
ProteinModelPortali Q02078.
SMRi Q02078. Positions 2-91.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110369. 30 interactions.
DIPi DIP-40711N.
IntActi Q02078. 11 interactions.
MINTi MINT-104848.
STRINGi 9606.ENSP00000346389.

PTM databases

PhosphoSitei Q02078.

Proteomic databases

MaxQBi Q02078.
PaxDbi Q02078.
PRIDEi Q02078.

Protocols and materials databases

DNASUi 4205.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000338042 ; ENSP00000337202 ; ENSG00000068305 . [Q02078-6 ]
ENST00000354410 ; ENSP00000346389 ; ENSG00000068305 . [Q02078-5 ]
ENST00000449277 ; ENSP00000399460 ; ENSG00000068305 . [Q02078-8 ]
ENST00000557785 ; ENSP00000453441 ; ENSG00000068305 . [Q02078-6 ]
ENST00000557942 ; ENSP00000453095 ; ENSG00000068305 . [Q02078-2 ]
ENST00000558812 ; ENSP00000454120 ; ENSG00000068305 . [Q02078-7 ]
GeneIDi 4205.
KEGGi hsa:4205.
UCSCi uc002bve.3. human. [Q02078-2 ]
uc002bvf.3. human. [Q02078-5 ]
uc002bvg.3. human. [Q02078-6 ]
uc010urv.2. human. [Q02078-7 ]
uc010urw.2. human. [Q02078-1 ]

Organism-specific databases

CTDi 4205.
GeneCardsi GC15P100107.
H-InvDB HIX0012611.
HGNCi HGNC:6993. MEF2A.
HPAi CAB004499.
HPA046597.
HPA056563.
MIMi 600660. gene.
608320. phenotype.
neXtProti NX_Q02078.
PharmGKBi PA30731.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5068.
GeneTreei ENSGT00390000011828.
HOGENOMi HOG000230620.
HOVERGENi HBG053944.
InParanoidi Q02078.
KOi K09260.
PhylomeDBi Q02078.
TreeFami TF314067.

Enzyme and pathway databases

Reactomei REACT_12599. ERK/MAPK targets.
REACT_21402. CDO in myogenesis.
SignaLinki Q02078.

Miscellaneous databases

ChiTaRSi MEF2A. human.
EvolutionaryTracei Q02078.
GeneWikii Myocyte-specific_enhancer_factor_2A.
GenomeRNAii 4205.
NextBioi 16568.
PMAP-CutDB Q02078.
PROi Q02078.
SOURCEi Search...

Gene expression databases

Bgeei Q02078.
CleanExi HS_MEF2A.
ExpressionAtlasi Q02078. baseline and differential.
Genevestigatori Q02078.

Family and domain databases

InterProi IPR022102. HJURP_C.
IPR002100. TF_MADSbox.
[Graphical view ]
Pfami PF12347. HJURP_C. 1 hit.
PF00319. SRF-TF. 1 hit.
[Graphical view ]
PRINTSi PR00404. MADSDOMAIN.
SMARTi SM00432. MADS. 1 hit.
[Graphical view ]
SUPFAMi SSF55455. SSF55455. 1 hit.
PROSITEi PS00350. MADS_BOX_1. 1 hit.
PS50066. MADS_BOX_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human SRF-related proteins: DNA-binding properties and potential regulatory targets."
    Pollock R., Treisman R.
    Genes Dev. 5:2327-2341(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MEF2; RSRFC4 AND RSRFC9), DNA-BINDING, TISSUE SPECIFICITY, DIMERIZATION.
    Tissue: Placenta.
  2. Treisman R.
    Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RSRFC9), SEQUENCE REVISION.
  3. "Human myocyte-specific enhancer factor 2 comprises a group of tissue-restricted MADS box transcription factors."
    Yu Y.-T., Breitbart R.E., Smoot L.B., Lee Y., Mahdavi V., Nadal-Ginard B.
    Genes Dev. 6:1783-1798(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MEF2 AND RSRFC9), TISSUE SPECIFICITY.
    Tissue: Heart and Skeletal muscle.
  4. Suzuki E., Lowry J., Sonoda G., Testa J.R., Walsh K.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS RSRFC4 AND RSRFC9).
  5. "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 7).
    Tissue: Amygdala.
  6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno F.R.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
    Tissue: Brain.
  7. "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].
  8. "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 5 AND 8).
    Tissue: Pancreas and Uterus.
  9. "Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1."
    Yang C.-C., Ornatsky O.I., McDermott J.C., Cruz T.F., Prody C.A.
    Nucleic Acids Res. 26:4771-4777(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAPK7, PHOSPHORYLATION.
  10. "HDAC4 deacetylase associates with and represses the MEF2 transcription factor."
    Miska E.A., Karlsson C., Langley E., Nielsen S.J., Pines J., Kouzarides T.
    EMBO J. 18:5099-5107(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC4 AND HDAC9.
  11. "Regulation of the MEF2 family of transcription factors by p38."
    Zhao M., New L., Kravchenko V.V., Kato Y., Gram H., di Padova F., Olson E.N., Ulevitch R.J., Han J.-D.
    Mol. Cell. Biol. 19:21-30(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-312; THR-319 AND SER-453, FUNCTION, HETERODIMERIZATION, MUTAGENESIS OF THR-312; THR-319; SER-355; SER-453 AND SER-479.
  12. "Targeting of p38 mitogen-activated protein kinases to MEF2 transcription factors."
    Yang S.-H., Galanis A., Sharrocks A.D.
    Mol. Cell. Biol. 19:4028-4038(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAPK14, PHOSPHORYLATION AT THR-312 AND THR-319, MUTAGENESIS OF ARG-269; LYS-270; LEU-273; VAL-275; ILE-277 AND PRO-278.
  13. "Big mitogen-activated kinase regulates multiple members of the MEF2 protein family."
    Kato Y., Zhao M., Morikawa A., Sugiyama T., Chakravortty D., Koide N., Yoshida T., Tapping R.I., Yang Y., Yokochi T., Lee J.D.
    J. Biol. Chem. 275:18534-18540(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-312; THR-319 AND SER-355, MUTAGENESIS OF THR-312; THR-319 AND SER-355.
  14. "Dominant-interfering forms of MEF2 generated by caspase cleavage contribute to NMDA-induced neuronal apoptosis."
    Okamoto S., Li Z., Ju C., Scholzke M.N., Mathews E., Cui J., Salvesen G.S., Bossy-Wetzel E., Lipton S.A.
    Proc. Natl. Acad. Sci. U.S.A. 99:3974-3979(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING AT ASP-176; ASP-213 AND ASP-466, FUNCTION, MUTAGENESIS OF ASP-176 AND ASP-213.
  15. "Phosphorylation motifs regulating the stability and function of myocyte enhancer factor 2A."
    Cox D.M., Du M., Marback M., Yang E.C.C., Chan J., Siu K.W.M., McDermott J.C.
    J. Biol. Chem. 278:15297-15303(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-255; THR-312; THR-319 AND SER-408, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-255.
  16. "Cdk5-mediated inhibition of the protective effects of transcription factor MEF2 in neurotoxicity-induced apoptosis."
    Gong X., Tang X., Wiedmann M., Wang X., Peng J., Zheng D., Blair L.A.C., Marshall J., Mao Z.
    Neuron 38:33-46(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-408, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-408.
  17. "Regulation of the human GLUT4 gene promoter: interaction between a transcriptional activator and myocyte enhancer factor 2A."
    Knight J.B., Eyster C.A., Griesel B.A., Olson A.L.
    Proc. Natl. Acad. Sci. U.S.A. 100:14725-14730(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC2A4RG.
  18. "Alternative pre-mRNA splicing governs expression of a conserved acidic transactivation domain in myocyte enhancer factor 2 factors of striated muscle and brain."
    Zhu B., Ramachandran B., Gulick T.
    J. Biol. Chem. 280:28749-28760(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF BETA DOMAIN.
  19. "Cyclin-dependent kinase 5 mediates neurotoxin-induced degradation of the transcription factor myocyte enhancer factor 2."
    Tang X., Wang X., Gong X., Tong M., Park D., Xia Z., Mao Z.
    J. Neurosci. 25:4823-4834(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING, PHOSPHORYLATION.
  20. "SUMO-1 modification of MEF2A regulates its transcriptional activity."
    Riquelme C., Barthel K.K., Liu X.
    J. Cell. Mol. Med. 10:132-144(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-403, INTERACTION WITH PIAS1, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-403.
  21. Cited for: SUMOYLATION AT LYS-403, PHOSPHORYLATION AT SER-408, FUNCTION, MUTAGENESIS OF LYS-403 AND SER-408.
  22. "A calcium-regulated MEF2 sumoylation switch controls postsynaptic differentiation."
    Shalizi A., Gaudilliere B., Yuan Z., Stegmueller J., Shirogane T., Ge Q., Tan Y., Schulman B., Harper J.W., Bonni A.
    Science 311:1012-1017(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-408, FUNCTION.
  23. "Nemo-like kinase-myocyte enhancer factor 2A signaling regulates anterior formation in Xenopus development."
    Satoh K., Ohnishi J., Sato A., Takeyama M., Iemura S., Natsume T., Shibuya H.
    Mol. Cell. Biol. 27:7623-7630(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-312 BY NLK.
  24. "Quantitative control of adaptive cardiac hypertrophy by acetyltransferase p300."
    Wei J.Q., Shehadeh L.A., Mitrani J.M., Pessanha M., Slepak T.I., Webster K.A., Bishopric N.H.
    Circulation 118:934-946(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION, INVOLVEMENT IN CARDIAC HYPERTROPHY.
  25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-235 AND SER-255, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 (ISOFORMS 7 AND 8), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "Identification of HZF1 as a novel target gene of the MEF2 transcription factor."
    Liu X., Jin E.Z., Zhi J.X., Li X.Q.
    Mol. Med. Report. 4:465-469(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHROMATIN BINDING.
  29. "Transcription factor MEF2A mutations in patients with coronary artery disease."
    Bhagavatula M.R.K., Fan C., Shen G.-Q., Cassano J., Plow E.F., Topol E.J., Wang Q.
    Hum. Mol. Genet. 13:3181-3188(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SER-263; LEU-279 AND ASP-283, CHARACTERIZATION OF VARIANTS SER-263; LEU-279 AND ASP-283.
  30. "The Pro279Leu variant in the transcription factor MEF2A is associated with myocardial infarction."
    Gonzalez P., Garcia-Castro M., Reguero J.R., Batalla A., Ordonez A.G., Palop R.L., Lozano I., Montes M., Alvarez V., Coto E.
    J. Med. Genet. 43:167-169(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LEU-279, ASSOCIATION WITH SUSCEPTIBILITY TO MYOCARDIAL INFARCTION.
  31. Cited for: VARIANT LEU-279, LACK OF ASSOCIATION WITH MYOCARDIAL INFARCTION.
  32. "Solution structure of the MEF2A-DNA complex: structural basis for the modulation of DNA bending and specificity by MADS-box transcription factors."
    Huang K., Louis J.M., Donaldson L., Lim F.L., Sharrocks A.D., Clore G.M.
    EMBO J. 19:2615-2628(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-86 IN COMPLEX WITH DNA.
  33. "Crystal structure of MEF2A core bound to DNA at 1.5 A resolution."
    Santelli E., Richmond T.J.
    J. Mol. Biol. 297:437-449(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-78 IN COMPLEX WITH DNA, DIMERIZATION.

Entry informationi

Entry nameiMEF2A_HUMAN
AccessioniPrimary (citable) accession number: Q02078
Secondary accession number(s): B4DFQ7
, F6XG23, O43814, Q14223, Q14224, Q59GX4, Q7Z6C9, Q96D14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 153 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 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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