Reviewed, UniProtKB/Swiss-Prot P51532 (SMCA4_HUMAN)

Names and origin

Protein names

Recommended name:
    Probable global transcription activator SNF2L4
    EC=3.6.1.-
Alternative name(s):
    ATP-dependent helicase SMARCA4
    SNF2-beta
    BRG-1 protein
    Mitotic growth and transcription activator
    Brahma protein homolog 1
    SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4

Gene names

Name:	SMARCA4
Synonyms:	BRG1, SNF2B, SNF2L4

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1647 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Transcriptional coactivator cooperating with nuclear hormone receptors to potentiate transcriptional activation. 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.
Subunit structure	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, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Component of the BAF53 complex, at least composed of BAF53A, RUVBL1, SMARCA4/BRG1, 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. Ref.6 Ref.9 Ref.10 Ref.12
Subcellular location	Nucleus.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.11 Ref.13 Ref.14 Ref.16
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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Bromodomain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Activator Helicase Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	chromatin remodeling Inferred from direct assay. Source: UniProtKB negative regulation of S phase of mitotic cell cycle Traceable author statement. Source: UniProtKB negative regulation of specific transcription from RNA polymerase II promoter Traceable author statement. Source: UniProtKB positive regulation of specific transcription from RNA polymerase II promoter Inferred from direct assay. Source: UniProtKB positive regulation of transcription factor activity Inferred from direct assay. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	SWI/SNF complex Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Ref.1 Inferred by curator. Source: UniProtKB DNA binding Inferred from electronic annotation. Source: InterPro DNA-dependent ATPase activity Ref.1 Inferred from genetic interaction. Source: UniProtKB helicase activity Ref.3 Traceable author statement. Source: ProtInc histone binding Inferred from direct assay. Source: UniProtKB identical protein binding Ref.9 Inferred from physical interaction. Source: IntAct p53 binding Inferred from physical interaction. Source: UniProtKB protein N-terminus binding Ref.9 Inferred from physical interaction. Source: UniProtKB transcription activator activity Ref.3 Inferred from mutant phenotype. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-302489,EBI-302489
ARID1A	O14497	4	EBI-302489,EBI-637887
ARID1B	Q8NFD5	2	EBI-302489,EBI-679921
ARID2	Q68CP9	1	EBI-302489,EBI-637818
MPHOSPH6	Q99547	1	EBI-302489,EBI-373187
NR3C1	P04150	1	EBI-302489,EBI-493507
Nr3c1	P06536	3	EBI-302489,EBI-1187143	From a different organism.
PBRM1	Q86U86	1	EBI-302489,EBI-637807
PPARG	P37231	1	EBI-302489,EBI-781384
RCOR1	Q9UKL0	1	EBI-302489,EBI-926563
REST	Q13127	1	EBI-302489,EBI-926706
SMARCC1	Q92922	1	EBI-302489,EBI-355653
SMARCD1	Q96GM5	2	EBI-302489,EBI-358489
SMARCE1	Q969G3-1	1	EBI-302489,EBI-455091
SMARCE1	Q969G3-2	1	EBI-302489,EBI-455096

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1647

1647

Probable global transcription activator SNF2L4

PRO_0000074353

Regions

Domain

460 – 532

73

HSA

Domain

766 – 931

166

Helicase ATP-binding

Domain

1084 – 1246

163

Helicase C-terminal

Domain

1477 – 1547

71

Bromo

Nucleotide binding

779 – 786

8

ATP Potential

Motif

881 – 884

4

DEGH box

Compositional bias

578 – 588

11

Poly-Lys

Compositional bias

663 – 672

10

Poly-Glu

Compositional bias

1360 – 1364

5

Poly-Glu

Compositional bias

1571 – 1584

14

Poly-Glu

Amino acid modifications

Modified residue

11

1

Phosphothreonine Ref.13

Modified residue

610

1

Phosphoserine Ref.14

Modified residue

613

1

Phosphoserine Ref.16

Modified residue

655

1

Phosphoserine Ref.13

Modified residue

657

1

Phosphoserine Ref.13

Modified residue

660

1

Phosphoserine Ref.13

Modified residue

662

1

Phosphoserine Ref.13

Modified residue

695

1

Phosphoserine Ref.11

Modified residue

721

1

Phosphoserine Ref.14

Modified residue

1382

1

Phosphoserine Ref.11 Ref.16

Modified residue

1452

1

Phosphoserine Ref.13 Ref.16

Modified residue

1570

1

Phosphoserine Ref.16

Modified residue

1575

1

Phosphoserine Ref.16

Modified residue

1586

1

Phosphoserine Ref.16

Modified residue

1627

1

Phosphoserine Ref.16

Modified residue

1631

1

Phosphoserine Ref.16

Modified residue

1640

1

Phosphoserine Ref.16

Modified residue

1642

1

Phosphoserine Ref.16

Modified residue

1644

1

Phosphoserine Ref.16

Natural variations

Natural variant

561

1

V → E: dbSNP rs1804579.

VAR_028215

Natural variant

1036

1

M → I: dbSNP rs1801514.

VAR_028216

Experimental info

Sequence conflict

569

1

R → P in AAB40977. Ref.1

Sequence conflict

569

1

R → P in BAA05143. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1647

Helix Strand Turn

Details...

Helix

1462 – 1471

10

Turn

1475 – 1478

4

Helix

1481 – 1485

5

Turn

1491 – 1493

3

Helix

1495 – 1500

6

Helix

1507 – 1514

8

Turn

1515 – 1517

3

Helix

1522 – 1539

18

Beta strand

1542 – 1544

3

Helix

1545 – 1564

20

Sequences

	Sequence		Length	Mass (Da)
	P51532-1 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: ABDA5EDBF10D7D28	FASTA	1,647	184,646
	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

References

	« Hide 'large scale' referencesShow '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: 8232556] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 8208605] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 11085541] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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. , 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: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex." Fryer C.J., Archer T.K. Nature 393:88-91(1998) [PubMed: 9590696] [Abstract] Cited for: INTERACTION WITH NR3C1 AND PGR.
[7]	"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: 11839798] [Abstract] Cited for: IDENTIFICATION IN THE BAF53 COMPLEX WITH BAF53A; RUVBL1 AND TRRAP.
[8]	"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: 12837248] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
[9]	"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: 12917342] [Abstract] Cited for: INTERACTION WITH NR3C1 AND SMARD1.
[10]	"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: 15075294] [Abstract] Cited for: INTERACTION WITH TOPBP1.
[11]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695 AND SER-1382, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"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: 16051670] [Abstract] Cited for: INTERACTION WITH ZMIM2.
[13]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; SER-655; SER-657; SER-660; SER-662 AND SER-1452, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610 AND SER-721, MASS SPECTROMETRY.
[15]	"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: 18765789] [Abstract] Cited for: IDENTIFICATION IN THE BAF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[16]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-1382; SER-1452; SER-1570; SER-1575; SER-1586; SER-1627; SER-1631; SER-1640; SER-1642 AND SER-1644, MASS SPECTROMETRY.
[17]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

U29175 mRNA. Translation: AAB40977.1.
D26156 mRNA. Translation: BAA05143.1.
AF254822 Genomic DNA. Translation: AAG24789.1.
AC006127 Genomic DNA. Translation: AAC97986.1.
AC006127 Genomic DNA. Translation: AAC97987.1.
AC011442 Genomic DNA. No translation available.
AC011485 Genomic DNA. No translation available.

IPI

IPI00293426.

PIR

S45252.

RefSeq

NP_001122316.1.
NP_003063.2.

UniGene

Hs.327527

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GRC	X-ray	1.50	A	1448-1575	[»]
2H60	NMR	-	A	1452-1570	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:24249N.

IntAct

P51532. 33 interactions.

PTM databases

PhosphoSite

P51532.

Proteomic databases

PRIDE

P51532.

Genome annotation databases

Ensembl

ENSG00000127616. Homo sapiens. [Contig view]

GeneID

6597.

KEGG

hsa:6597.

Organism-specific databases

GeneCards

GC19P010932.

HGNC

HGNC:11100. SMARCA4.

HPA

CAB004208.

MIM

603254. gene.

PharmGKB

PA35950.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P51532.

Gene expression databases

ArrayExpress

P51532.

Bgee

P51532.

CleanEx

HS_SMARCA4.

GermOnline

ENSG00000127616. Homo sapiens.

Family and domain databases

InterPro

IPR006576. BRK_domain.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR014001. DEAD-like_N.
IPR001650. DNA/RNA_helicase_C.
IPR014978. Gln-Leu-Gln_QLQ.
IPR013999. HAS_subgroup.
IPR014012. Helicase/SANT-assoc_DNA_bd.
IPR014021. Helicase_SF1/SF2_ATP-bd.
IPR006562. HSA.
IPR000330. SNF2_N.
[Graphical view]

Gene3D

G3DSA:1.20.920.10. Bromodomain. 1 hit.

Pfam

PF07533. BRK. 1 hit.
PF00439. Bromodomain. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07529. HSA. 1 hit.
PF08880. QLQ. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00592. BRK. 1 hit.
SM00297. BROMO. 1 hit.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00573. HSA. 1 hit.
[Graphical view]

PROSITE

PS00633. 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.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

25661.

SOURCE

Search...

Entry information

Entry name

SMCA4_HUMAN

Accession

Primary (citable) accession number: P51532
Secondary accession number(s): O95052, Q9HBD3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 17, 2006
Last modified:	June 16, 2009
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)