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P51532 (SMCA4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription activator BRG1

EC=3.6.4.-
Alternative name(s):
ATP-dependent helicase SMARCA4
BRG1-associated factor 190A
Short name=BAF190A
Mitotic growth and transcription activator
Protein BRG-1
Protein brahma homolog 1
SNF2-beta
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
Gene names
Name:SMARCA4
Synonyms:BAF190A, BRG1, SNF2B, SNF2L4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1647 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional coactivator cooperating with nuclear hormone receptors to potentiate transcriptional activation. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves a release of HDAC1 and recruitment of CREBBP. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. SMARCA4/BAF190A may promote neural stem cell self-renewal/proliferation by enhancing Notch-dependent proliferative signals, while concurrently making the neural stem cell insensitive to SHH-dependent differentiating cues By similarity. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene. Acts as a corepressor of ZEB1 to regulate E-cadherin transcription and is required for induction of epithelial-mesenchymal transition (EMT) by ZEB1. Ref.11 Ref.21 Ref.25

Subunit structure

Component of the CREST-BRG1 complex, at least composed of SMARCA4/BRG1/BAF190A, SS18L1/CREST, HDAC1, RB1 and SP1 By similarity. Interacts with NR3C1, PGR, SMARD1, TOPBP1 and ZMIM2/ZIMP7. Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, IKFZ1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. Interacts directly with IKFZ1 in the BAF complex. In muscle cells, the BAF complex also contains DPF3. Component of the BAF53 complex, at least composed of BAF53A, RUVBL1, SMARCA4/BRG1/BAF190A, and TRRAP, which preferentially acetylates histone H4 (and H2A) within nucleosomes. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Interacts with (via the bromodomain) with TERT; the interaction regulates Wnt-mediated signaling. Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin. Interacts with PHF10/BAF45A By similarity. Interacts with MYOG By similarity. Interacts with ZEB1 (via N-terminus). Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.18 Ref.21 Ref.25

Subcellular location

Nucleus Ref.25.

Tissue specificity

Colocalizes with ZEB1 in E-cadherin-negative cells from established lines, and stroma of normal colon as well as in de-differentiated epithelial cells at the invasion front of colorectal carcinomas (at protein level). Ref.25

Involvement in disease

Rhabdoid tumor predisposition syndrome 2 (RTPS2) [MIM:613325]: A familial cancer syndrome predisposing to renal or extrarenal malignant rhabdoid tumors and to a variety of tumors of the central nervous system, including choroid plexus carcinoma, medulloblastoma, and central primitive neuroectodermal tumors. Rhabdoid tumors are the most aggressive and lethal malignancies occurring in early childhood.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24

Mental retardation, autosomal dominant 16 (MRD16) [MIM:614609]: A disease characterized by multiple congenital anomalies and mental retardation. Mental retardation is defined by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD16 patients manifest developmental delay, absent or hypoplastic fifth fingernails or toenails, thick eyebrows and long eyelashes, hirsutism. Additional findings include hypotonia, microcephaly, seizures, a Dandy-Walker malformation, and vision and hearing problems.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.31

Sequence similarities

Belongs to the SNF2/RAD54 helicase family.

Contains 1 bromo domain.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 HSA domain.

Contains 1 QLQ domain.

Ontologies

Keywords
   Biological processNeurogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Mental retardation
   DomainBromodomain
   LigandATP-binding
Nucleotide-binding
   Molecular functionActivator
Chromatin regulator
Helicase
Hydrolase
Repressor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from genetic interaction Ref.1. Source: GOC

ATP-dependent chromatin remodeling

Inferred from direct assay PubMed 16217013. Source: UniProt

DNA methylation on cytosine within a CG sequence

Inferred from electronic annotation. Source: Ensembl

aortic smooth muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

blastocyst growth

Inferred from electronic annotation. Source: Ensembl

blastocyst hatching

Inferred from electronic annotation. Source: Ensembl

cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

chromatin remodeling

Inferred from direct assay PubMed 10943845PubMed 11726552. Source: BHF-UCL

definitive erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

embryonic hindlimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic organ morphogenesis

Inferred from electronic annotation. Source: Ensembl

epidermis morphogenesis

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Inferred from electronic annotation. Source: Ensembl

forebrain development

Inferred from electronic annotation. Source: Ensembl

glial cell fate determination

Inferred from electronic annotation. Source: Ensembl

heart trabecula formation

Inferred from electronic annotation. Source: Ensembl

hindbrain development

Inferred from electronic annotation. Source: Ensembl

histone H3 acetylation

Inferred from electronic annotation. Source: Ensembl

keratinocyte differentiation

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

methylation-dependent chromatin silencing

Inferred from electronic annotation. Source: Ensembl

negative regulation of G1/S transition of mitotic cell cycle

Traceable author statement PubMed 19149898. Source: BHF-UCL

negative regulation of androgen receptor signaling pathway

Inferred from mutant phenotype PubMed 18487222. Source: BHF-UCL

negative regulation of cell growth

Inferred from mutant phenotype PubMed 12065415. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 17938176. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter during mitosis

Traceable author statement PubMed 19149898. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12065415. Source: BHF-UCL

neural retina development

Inferred from expression pattern PubMed 18816825. Source: BHF-UCL

nucleosome disassembly

Inferred from direct assay PubMed 8895581. Source: BHF-UCL

positive regulation by host of viral transcription

Inferred from mutant phenotype PubMed 16687403. Source: BHF-UCL

positive regulation of DNA binding

Inferred from electronic annotation. Source: Ensembl

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 11950834PubMed 17938176. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15774904PubMed 17938176. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.3. Source: BHF-UCL

regulation of transcription from RNA polymerase II promoter

Non-traceable author statement PubMed 8804307. Source: BHF-UCL

stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

vasculogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentSWI/SNF complex

Inferred from direct assay PubMed 11078522. Source: UniProtKB

WINAC complex

Inferred from direct assay. Source: BHF-UCL

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

heterochromatin

Inferred from electronic annotation. Source: Ensembl

nBAF complex

Inferred from sequence or structural similarity. Source: UniProtKB

npBAF complex

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear chromatin

Inferred from direct assay PubMed 12065415PubMed 15774904. Source: BHF-UCL

nuclear euchromatin

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.25. Source: UniProtKB

perichromatin fibrils

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from direct assay PubMed 16217013. Source: UniProt

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-dependent ATPase activity

Inferred from genetic interaction Ref.1. Source: BHF-UCL

RNA polymerase II regulatory region sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II transcription coactivator activity

Inferred from direct assay PubMed 15774904. Source: BHF-UCL

Tat protein binding

Inferred from physical interaction PubMed 16687403. Source: BHF-UCL

androgen receptor binding

Inferred from physical interaction PubMed 18487222. Source: BHF-UCL

chromatin binding

Inferred from electronic annotation. Source: Ensembl

helicase activity

Traceable author statement Ref.3. Source: ProtInc

lysine-acetylated histone binding

Inferred from direct assay Ref.30. Source: BHF-UCL

p53 binding

Inferred from physical interaction PubMed 11950834. Source: BHF-UCL

protein N-terminus binding

Inferred from physical interaction Ref.12. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.12PubMed 14701856Ref.14PubMed 17984088Ref.25. Source: UniProtKB

transcription coactivator activity

Inferred from mutant phenotype PubMed 16687403. Source: BHF-UCL

transcription corepressor activity

Inferred from direct assay Ref.25. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P51532-1)

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: P51532-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1259-1291: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P51532-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1259-1291: Missing.
     1388-1388: W → WLKT
     1475-1475: Missing.
Isoform 4 (identifier: P51532-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1259-1291: Missing.
     1388-1388: W → WLKT
Isoform 5 (identifier: P51532-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1259-1291: Missing.
     1475-1475: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16471647Transcription activator BRG1
PRO_0000074353

Regions

Domain171 – 20636QLQ
Domain460 – 53273HSA
Domain766 – 931166Helicase ATP-binding
Domain1084 – 1246163Helicase C-terminal
Domain1477 – 154771Bromo
Nucleotide binding779 – 7868ATP Potential
Region1 – 282282Necessary for interaction with SS18L1/CREST By similarity
Motif881 – 8844DEGH box
Compositional bias578 – 58811Poly-Lys
Compositional bias663 – 67210Poly-Glu
Compositional bias1360 – 13645Poly-Glu
Compositional bias1571 – 158414Poly-Glu

Sites

Site1539 – 15402Required for binding to 'Lys-15'-acetylated histone 3

Amino acid modifications

Modified residue111Phosphothreonine Ref.15
Modified residue1881N6-acetyllysine Ref.23
Modified residue3531Phosphothreonine Ref.22
Modified residue6091Phosphothreonine Ref.22
Modified residue6101Phosphoserine Ref.22
Modified residue6131Phosphoserine Ref.19 Ref.22 Ref.28
Modified residue6951Phosphoserine Ref.22 Ref.26 Ref.28
Modified residue6991Phosphoserine Ref.22 Ref.26 Ref.28
Modified residue13821Phosphoserine Ref.19 Ref.28
Modified residue14521Phosphoserine Ref.15 Ref.19
Modified residue15701Phosphoserine Ref.19 Ref.22 Ref.26
Modified residue15751Phosphoserine Ref.19 Ref.22 Ref.26
Modified residue15861Phosphoserine Ref.19
Modified residue16271Phosphoserine Ref.22 Ref.28
Modified residue16311Phosphoserine Ref.22 Ref.28

Natural variations

Alternative sequence1259 – 129133Missing in isoform 2, isoform 3, isoform 4 and isoform 5.
VSP_043137
Alternative sequence13881W → WLKT in isoform 3 and isoform 4.
VSP_043677
Alternative sequence14751Missing in isoform 3 and isoform 5.
VSP_043678
Natural variant5461Missing in MRD16. Ref.31
VAR_068209
Natural variant5611V → E.
Corresponds to variant rs1804579 [ dbSNP | Ensembl ].
VAR_028215
Natural variant8591T → M in MRD16. Ref.31
Corresponds to variant rs281875226 [ dbSNP | Ensembl ].
VAR_068210
Natural variant8851R → C in MRD16. Ref.31
Corresponds to variant rs281875227 [ dbSNP | Ensembl ].
VAR_068211
Natural variant9211L → F in MRD16. Ref.31
Corresponds to variant rs281875228 [ dbSNP | Ensembl ].
VAR_068212
Natural variant10111M → T in MRD16. Ref.31
Corresponds to variant rs281875229 [ dbSNP | Ensembl ].
VAR_068213
Natural variant10361M → I.
Corresponds to variant rs1801514 [ dbSNP | Ensembl ].
VAR_028216
Natural variant11571R → G in MRD16. Ref.31
Corresponds to variant rs281875230 [ dbSNP | Ensembl ].
VAR_068214

Experimental info

Mutagenesis14841V → A: No effect on binding to 'Lys-15'-acetylated histone H3. Ref.29
Mutagenesis15391F → A: Abolishes binding to 'Lys-15'-acetylated histone H3. Ref.29
Mutagenesis15401N → A: Abolishes binding to 'Lys-15'-acetylated histone H3. Ref.29
Sequence conflict5691R → P in AAB40977. Ref.1
Sequence conflict5691R → P in BAA05143. Ref.3

Secondary structure

.................. 1647
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: ABDA5EDBF10D7D28

FASTA1,647184,646
        10         20         30         40         50         60 
MSTPDPPLGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SMMGPSPGPP SAGHPIPTQG 

        70         80         90        100        110        120 
PGGYPQDNMH QMHKPMESMH EKGMSDDPRY NQMKGMGMRS GGHAGMGPPP SPMDQHSQGY 

       130        140        150        160        170        180 
PSPLGGSEHA SSPVPASGPS SGPQMSSGPG GAPLDGADPQ ALGQQNRGPT PFNQNQLHQL 

       190        200        210        220        230        240 
RAQIMAYKML ARGQPLPDHL QMAVQGKRPM PGMQQQMPTL PPPSVSATGP GPGPGPGPGP 

       250        260        270        280        290        300 
GPGPAPPNYS RPHGMGGPNM PPPGPSGVPP GMPGQPPGGP PKPWPEGPMA NAAAPTSTPQ 

       310        320        330        340        350        360 
KLIPPQPTGR PSPAPPAVPP AASPVMPPQT QSPGQPAQPA PMVPLHQKQS RITPIQKPRG 

       370        380        390        400        410        420 
LDPVEILQER EYRLQARIAH RIQELENLPG SLAGDLRTKA TIELKALRLL NFQRQLRQEV 

       430        440        450        460        470        480 
VVCMRRDTAL ETALNAKAYK RSKRQSLREA RITEKLEKQQ KIEQERKRRQ KHQEYLNSIL 

       490        500        510        520        530        540 
QHAKDFKEYH RSVTGKIQKL TKAVATYHAN TEREQKKENE RIEKERMRRL MAEDEEGYRK 

       550        560        570        580        590        600 
LIDQKKDKRL AYLLQQTDEY VANLTELVRQ HKAAQVAKEK KKKKKKKKAE NAEGQTPAIG 

       610        620        630        640        650        660 
PDGEPLDETS QMSDLPVKVI HVESGKILTG TDAPKAGQLE AWLEMNPGYE VAPRSDSEES 

       670        680        690        700        710        720 
GSEEEEEEEE EEQPQAAQPP TLPVEEKKKI PDPDSDDVSE VDARHIIENA KQDVDDEYGV 

       730        740        750        760        770        780 
SQALARGLQS YYAVAHAVTE RVDKQSALMV NGVLKQYQIK GLEWLVSLYN NNLNGILADE 

       790        800        810        820        830        840 
MGLGKTIQTI ALITYLMEHK RINGPFLIIV PLSTLSNWAY EFDKWAPSVV KVSYKGSPAA 

       850        860        870        880        890        900 
RRAFVPQLRS GKFNVLLTTY EYIIKDKHIL AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH 

       910        920        930        940        950        960 
YVAPRRLLLT GTPLQNKLPE LWALLNFLLP TIFKSCSTFE QWFNAPFAMT GEKVDLNEEE 

       970        980        990       1000       1010       1020 
TILIIRRLHK VLRPFLLRRL KKEVEAQLPE KVEYVIKCDM SALQRVLYRH MQAKGVLLTD 

      1030       1040       1050       1060       1070       1080 
GSEKDKKGKG GTKTLMNTIM QLRKICNHPY MFQHIEESFS EHLGFTGGIV QGLDLYRASG 

      1090       1100       1110       1120       1130       1140 
KFELLDRILP KLRATNHKVL LFCQMTSLMT IMEDYFAYRG FKYLRLDGTT KAEDRGMLLK 

      1150       1160       1170       1180       1190       1200 
TFNEPGSEYF IFLLSTRAGG LGLNLQSADT VIIFDSDWNP HQDLQAQDRA HRIGQQNEVR 

      1210       1220       1230       1240       1250       1260 
VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ AGMFDQKSSS HERRAFLQAI LEHEEQDESR 

      1270       1280       1290       1300       1310       1320 
HCSTGSGSAS FAHTAPPPAG VNPDLEEPPL KEEDEVPDDE TVNQMIARHE EEFDLFMRMD 

      1330       1340       1350       1360       1370       1380 
LDRRREEARN PKRKPRLMEE DELPSWIIKD DAEVERLTCE EEEEKMFGRG SRHRKEVDYS 

      1390       1400       1410       1420       1430       1440 
DSLTEKQWLK AIEEGTLEEI EEEVRQKKSS RKRKRDSDAG SSTPTTSTRS RDKDDESKKQ 

      1450       1460       1470       1480       1490       1500 
KKRGRPPAEK LSPNPPNLTK KMKKIVDAVI KYKDSSSGRQ LSEVFIQLPS RKELPEYYEL 

      1510       1520       1530       1540       1550       1560 
IRKPVDFKKI KERIRNHKYR SLNDLEKDVM LLCQNAQTFN LEGSLIYEDS IVLQSVFTSV 

      1570       1580       1590       1600       1610       1620 
RQKIEKEDDS EGEESEEEEE GEEEGSESES RSVKVKIKLG RKEKAQDRLK GGRRRPSRGS 

      1630       1640 
RAKPVVSDDD SEEEQEEDRS GSGSEED 

« Hide

Isoform 2 [UniParc].

Checksum: CB7C83C8DC7109CA
Show »

FASTA1,614181,348
Isoform 3 [UniParc].

Checksum: 94455AEA6678D1CC
Show »

FASTA1,616181,603
Isoform 4 [UniParc].

Checksum: 33F65B2C4F6CCCEC
Show »

FASTA1,617181,690
Isoform 5 [UniParc].

Checksum: 9E9DBE797BBDF774
Show »

FASTA1,613181,261

References

« Hide 'large scale' references
[1]"BRG1 contains a conserved domain of the SWI2/SNF2 family necessary for normal mitotic growth and transcription."
Khavari P.A., Peterson C.L., Tamkun J.W., Mendel D.B., Crabtree G.R.
Nature 366:170-174(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]Khavari P.A., Peterson C.L., Tamkun J.W., Mendel D.B., Crabtree G.R.
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and Drosophila brahma are transcriptional coactivators cooperating with the estrogen receptor and the retinoic acid receptor."
Chiba H., Muramatsu M., Nomoto A., Kato H.
Nucleic Acids Res. 22:1815-1820(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal brain.
[4]"BRG1, a component of the SWI-SNF complex, is mutated in multiple human tumor cell lines."
Wong A.K.C., Shanahan F., Chen Y., Lian L., Ha P., Hendricks K., Ghaffari S., Iliev D., Penn B., Woodland A.-M., Smith R., Salada G., Carillo A., Laity K., Gupte J., Swedlund B., Tavtigian S.V., Teng D.H.-F., Lees E.
Cancer Res. 60:6171-6177(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Frequent BRG1/SMARCA4-inactivating mutations in human lung cancer cell lines."
Medina P.P., Romero O.A., Kohno T., Montuenga L.M., Pio R., Yokota J., Sanchez-Cespedes M.
Hum. Mutat. 29:617-622(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5).
Tissue: Lung.
[6]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton 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. expand/collapse author list , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex."
Fryer C.J., Archer T.K.
Nature 393:88-91(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR3C1 AND PGR.
[9]"Ikaros DNA-binding proteins direct formation of chromatin remodeling complexes in lymphocytes."
Kim J., Sif S., Jones B., Jackson A., Koipally J., Heller E., Winandy S., Viel A., Sawyer A., Ikeda T., Kingston R., Georgopoulos K.
Immunity 10:345-355(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IKZF1 IN THE BAF COMPLEX.
[10]"BAF53 forms distinct nuclear complexes and functions as a critical c-Myc-interacting nuclear cofactor for oncogenic transformation."
Park J., Wood M.A., Cole M.D.
Mol. Cell. Biol. 22:1307-1316(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE BAF53 COMPLEX WITH BAF53A; RUVBL1 AND TRRAP.
[11]"The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome."
Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S.
Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
[12]"BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation."
Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.
Mol. Cell. Biol. 23:6210-6220(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR3C1 AND SMARD1.
[13]"TopBP1 recruits Brg1/Brm to repress E2F1-induced apoptosis, a novel pRb-independent and E2F1-specific control for cell survival."
Liu K., Luo Y., Lin F.-T., Lin W.-C.
Genes Dev. 18:673-686(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TOPBP1.
[14]"hZimp7, a novel PIAS-like protein, enhances androgen receptor-mediated transcription and interacts with SWI/SNF-like BAF complexes."
Huang C.-Y., Beliakoff J., Li X., Lee J., Li X., Sharma M., Lim B., Sun Z.
Mol. Endocrinol. 19:2915-2929(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZMIM2.
[15]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11 AND SER-1452, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[18]"Regulation of muscle development by DPF3, a novel histone acetylation and methylation reader of the BAF chromatin remodeling complex."
Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C., Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H., Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.
Genes Dev. 22:2370-2384(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE BAF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[19]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-1382; SER-1452; SER-1570; SER-1575 AND SER-1586, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Telomerase modulates Wnt signalling by association with target gene chromatin."
Park J.I., Venteicher A.S., Hong J.Y., Choi J., Jun S., Shkreli M., Chang W., Meng Z., Cheung P., Ji H., McLaughlin M., Veenstra T.D., Nusse R., McCrea P.D., Artandi S.E.
Nature 460:66-72(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TERT, FUNCTION.
[22]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-353; THR-609; SER-610; SER-613; SER-695; SER-699; SER-1570; SER-1575; SER-1627 AND SER-1631, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[23]"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-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Germline nonsense mutation and somatic inactivation of SMARCA4/BRG1 in a family with rhabdoid tumor predisposition syndrome."
Schneppenheim R., Fruhwald M.C., Gesk S., Hasselblatt M., Jeibmann A., Kordes U., Kreuz M., Leuschner I., Martin Subero J.I., Obser T., Oyen F., Vater I., Siebert R.
Am. J. Hum. Genet. 86:279-284(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN RTPS2.
[25]"ZEB1 represses E-cadherin and induces an EMT by recruiting the SWI/SNF chromatin-remodeling protein BRG1."
Sanchez-Tillo E., Lazaro A., Torrent R., Cuatrecasas M., Vaquero E.C., Castells A., Engel P., Postigo A.
Oncogene 29:3490-3500(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ZEB1, TISSUE SPECIFICITY.
[26]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695; SER-699; SER-1570 AND SER-1575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[27]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-695; SER-699; SER-1382; SER-1627 AND SER-1631, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Solution structure of human Brg1 bromodomain and its specific binding to acetylated histone tails."
Shen W., Xu C., Huang W., Zhang J., Carlson J.E., Tu X., Wu J., Shi Y.
Biochemistry 46:2100-2110(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1452-1570 IN COMPLEX WITH ACETYLATED HISTONES, MUTAGENESIS OF VAL-1484; PHE-1539 AND ASN-1540.
[30]"Structural ramification for acetyl-lysine recognition by the bromodomain of human BRG1 protein, a central ATPase of the SWI/SNF remodeling complex."
Singh M., Popowicz G.M., Krajewski M., Holak T.A.
ChemBioChem 8:1308-1316(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1448-1575 IN COMPLEX WITH ACETYLATED HISTONE 3.
[31]"Mutations affecting components of the SWI/SNF complex cause Coffin-Siris syndrome."
Tsurusaki Y., Okamoto N., Ohashi H., Kosho T., Imai Y., Hibi-Ko Y., Kaname T., Naritomi K., Kawame H., Wakui K., Fukushima Y., Homma T., Kato M., Hiraki Y., Yamagata T., Yano S., Mizuno S., Sakazume S. expand/collapse author list , Ishii T., Nagai T., Shiina M., Ogata K., Ohta T., Niikawa N., Miyatake S., Okada I., Mizuguchi T., Doi H., Saitsu H., Miyake N., Matsumoto N.
Nat. Genet. 44:376-378(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MRD16 LYS-546 DEL; MET-859; CYS-885; PHE-921; THR-1011 AND GLY-1157.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U29175 mRNA. Translation: AAB40977.1.
D26156 mRNA. Translation: BAA05143.1.
AF254822 Genomic DNA. Translation: AAG24789.1.
EU430756 mRNA. Translation: ACA09750.1.
EU430757 mRNA. Translation: ACA09751.1.
EU430758 mRNA. Translation: ACA09752.1.
EU430759 mRNA. Translation: ACA09753.1.
AC006127 Genomic DNA. Translation: AAC97986.1.
AC006127 Genomic DNA. Translation: AAC97987.1.
AC011442 Genomic DNA. No translation available.
AC011485 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84167.1.
CCDSCCDS12253.1. [P51532-1]
CCDS45972.1. [P51532-4]
CCDS45973.1. [P51532-3]
CCDS54217.1. [P51532-2]
CCDS54218.1. [P51532-5]
PIRS45252.
RefSeqNP_001122316.1. NM_001128844.1. [P51532-1]
NP_001122317.1. NM_001128845.1. [P51532-4]
NP_001122318.1. NM_001128846.1. [P51532-3]
NP_001122319.1. NM_001128847.1. [P51532-2]
NP_001122320.1. NM_001128848.1. [P51532-5]
NP_003063.2. NM_003072.3. [P51532-1]
XP_005260089.1. XM_005260032.1. [P51532-4]
XP_005260090.1. XM_005260033.1. [P51532-3]
XP_005260091.1. XM_005260034.1. [P51532-2]
XP_005260092.1. XM_005260035.1. [P51532-5]
UniGeneHs.327527.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GRCX-ray1.50A1448-1575[»]
2H60NMR-A1452-1570[»]
3UVDX-ray1.85A1448-1569[»]
ProteinModelPortalP51532.
SMRP51532. Positions 749-1265, 1449-1569.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112481. 182 interactions.
DIPDIP-24249N.
IntActP51532. 55 interactions.
MINTMINT-204078.
STRING9606.ENSP00000350720.

PTM databases

PhosphoSiteP51532.

Polymorphism databases

DMDM116242792.

Proteomic databases

MaxQBP51532.
PaxDbP51532.
PRIDEP51532.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344626; ENSP00000343896; ENSG00000127616. [P51532-1]
ENST00000413806; ENSP00000414727; ENSG00000127616. [P51532-4]
ENST00000429416; ENSP00000395654; ENSG00000127616. [P51532-1]
ENST00000444061; ENSP00000392837; ENSG00000127616. [P51532-5]
ENST00000450717; ENSP00000397783; ENSG00000127616. [P51532-3]
ENST00000541122; ENSP00000445036; ENSG00000127616. [P51532-4]
ENST00000589677; ENSP00000464778; ENSG00000127616. [P51532-3]
ENST00000590574; ENSP00000466963; ENSG00000127616. [P51532-2]
GeneID6597.
KEGGhsa:6597.
UCSCuc002mqf.4. human. [P51532-1]
uc002mqj.4. human. [P51532-4]
uc010dxq.3. human. [P51532-2]
uc010dxr.3. human. [P51532-5]
uc010dxs.3. human. [P51532-3]

Organism-specific databases

CTD6597.
GeneCardsGC19P011071.
GeneReviewsSMARCA4.
HGNCHGNC:11100. SMARCA4.
HPACAB004208.
HPA048340.
MIM603254. gene.
613325. phenotype.
614609. phenotype.
neXtProtNX_P51532.
Orphanet1465. Coffin-Siris syndrome.
231108. Familial rhabdoid tumor.
PharmGKBPA35950.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0553.
HOGENOMHOG000172363.
HOVERGENHBG056636.
KOK11647.
OrthoDBEOG771265.
PhylomeDBP51532.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkP51532.

Gene expression databases

ArrayExpressP51532.
BgeeP51532.
CleanExHS_SMARCA4.
GenevestigatorP51532.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR006576. BRK_domain.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR014978. Gln-Leu-Gln_QLQ.
IPR013999. HAS_subgr.
IPR014012. Helicase/SANT-assoc_DNA-bd.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR029295. SnAC.
IPR000330. SNF2_N.
[Graphical view]
PfamPF07533. BRK. 1 hit.
PF00439. Bromodomain. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07529. HSA. 1 hit.
PF08880. QLQ. 1 hit.
PF14619. SnAC. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00592. BRK. 1 hit.
SM00297. BROMO. 1 hit.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00573. HSA. 1 hit.
SM00951. QLQ. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51204. HSA. 1 hit.
PS51666. QLQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSMARCA4. human.
EvolutionaryTraceP51532.
GeneWikiSMARCA4.
GenomeRNAi6597.
NextBio25661.
PROP51532.
SOURCESearch...

Entry information

Entry nameSMCA4_HUMAN
AccessionPrimary (citable) accession number: P51532
Secondary accession number(s): B1A8Z4 expand/collapse secondary AC list , B1A8Z5, B1A8Z6, B1A8Z7, E9PBR8, O95052, Q9HBD3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM