Reviewed, UniProtKB/Swiss-Prot P51531 (SMCA2_HUMAN)

Names and origin

Protein names

Recommended name:
    Probable global transcription activator SNF2L2
    EC=3.6.1.-
Alternative name(s):
    ATP-dependent helicase SMARCA2
    SNF2-alpha
    SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2
      Short name=hBRM

Gene names

Name:	SMARCA2
Synonyms:	BRM, SNF2A, SNF2L2

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	1590 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.
Subunit structure	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. Binds TOPBP1.
Subcellular location	Nucleus.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR.
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	Alternative splicing
Domain	Bromodomain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Activator Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	regulation of transcription from RNA polymerase II promoter Ref.1 Traceable author statement. Source: ProtInc
Cellular component	SWI/SNF complex Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro DNA binding Inferred from electronic annotation. Source: InterPro helicase activity Ref.1 Traceable author statement. Source: ProtInc transcription coactivator activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACTL6B	O94805	1	EBI-679562,EBI-724528
Actl6b	Q99MR0	1	EBI-679562,EBI-371554	From a different organism.
ARID1A	O14497	3	EBI-679562,EBI-637887
ARID1B	Q8NFD5	3	EBI-679562,EBI-679921
KHDRBS1	Q07666	2	EBI-679562,EBI-1364
MECP2	P51608	2	EBI-679562,EBI-1189067
PRPF6	O94906	1	EBI-679562,EBI-536755
Smarcb1	Q9Z0H3	1	EBI-679562,EBI-689365	From a different organism.
SMARCD3	Q6STE5-1	1	EBI-679562,EBI-488506

Alternative products

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

Isoform Long (identifier: P51531-1)

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 Short (identifier: P51531-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1400-1417: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1590	1590	Probable global transcription activator SNF2L2		PRO_0000074352
Regions
	Domain	436 – 508	73	HSA
	Domain	736 – 901	166	Helicase ATP-binding
	Domain	1054 – 1216	163	Helicase C-terminal
	Domain	1419 – 1489	71	Bromo
	Nucleotide binding	749 – 756	8	ATP Potential
	Motif	851 – 854	4	DEGH box
	Compositional bias	216 – 238	23	Poly-Gln
	Compositional bias	245 – 253	9	Poly-Gln
	Compositional bias	559 – 562	4	Poly-Arg
	Compositional bias	643 – 650	8	Poly-Glu
	Compositional bias	1297 – 1301	5	Poly-Glu
	Compositional bias	1518 – 1529	12	Poly-Glu
Amino acid modifications
	Modified residue	329	1	Phosphoserine
	Modified residue	591	1	Phosphoserine
	Modified residue	956	1	Phosphoserine
	Modified residue	1377	1	Phosphoserine
	Modified residue	1410	1	Phosphoserine
	Modified residue	1418	1	Phosphoserine
	Modified residue	1419	1	Phosphoserine
	Modified residue	1551	1	N6-acetyllysine
	Modified residue	1553	1	N6-acetyllysine
	Modified residue	1555	1	N6-acetyllysine
	Modified residue	1568	1	Phosphoserine
	Modified residue	1572	1	Phosphoserine
Natural variations
	Alternative sequence	1400 – 1417	18	Missing in isoform Short.		VSP_000577
Experimental info
	Sequence conflict	237 – 240	4	Missing in CAA51407. Ref.1
	Sequence conflict	394	1	Q → E in BAA05142. Ref.2
	Sequence conflict	513	1	G → S in BAA05142. Ref.2
	Sequence conflict	711	1	R → W in CAA51407. Ref.1
	Sequence conflict	1139	1	D → H in BAA05142. Ref.2
	Sequence conflict	1394	1	V → C in CAA51407. Ref.1
	Sequence conflict	1400	1	R → S in CAA51407. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified November 4, 2008. Version 2. Checksum: CE69BBB287D35AB5	FASTA	1,590	181,279
	10 20 30 40 50 60 MSTPTDPGAM PHPGPSPGPG PSPGPILGPS PGPGPSPGSV HSMMGPSPGP PSVSHPMPTM 70 80 90 100 110 120 GSTDFPQEGM HQMHKPIDGI HDKGIVEDIH CGSMKGTGMR PPHPGMGPPQ SPMDQHSQGY 130 140 150 160 170 180 MSPHPSPLGA PEHVSSPMSG GGPTPPQMPP SQPGALIPGD PQAMSQPNRG PSPFSPVQLH 190 200 210 220 230 240 QLRAQILAYK MLARGQPLPE TLQLAVQGKR TLPGLQQQQQ QQQQQQQQQQ QQQQQQQQPQ 250 260 270 280 290 300 QQPPQPQTQQ QQQPALVNYN RPSGPGPELS GPSTPQKLPV PAPGGRPSPA PPAAAQPPAA 310 320 330 340 350 360 AVPGPSVPQP APGQPSPVLQ LQQKQSRISP IQKPQGLDPV EILQEREYRL QARIAHRIQE 370 380 390 400 410 420 LENLPGSLPP DLRTKATVEL KALRLLNFQR QLRQEVVACM RRDTTLETAL NSKAYKRSKR 430 440 450 460 470 480 QTLREARMTE KLEKQQKIEQ ERKRRQKHQE YLNSILQHAK DFKEYHRSVA GKIQKLSKAV 490 500 510 520 530 540 ATWHANTERE QKKETERIEK ERMRRLMAED EEGYRKLIDQ KKDRRLAYLL QQTDEYVANL 550 560 570 580 590 600 TNLVWEHKQA QAAKEKKKRR RRKKKAEENA EGGESALGPD GEPIDESSQM SDLPVKVTHT 610 620 630 640 650 660 ETGKVLFGPE APKASQLDAW LEMNPGYEVA PRSDSEESDS DYEEEDEEEE SSRQETEEKI 670 680 690 700 710 720 LLDPNSEEVS EKDAKQIIET AKQDVDDEYS MQYSARGSQS YYTVAHAISE RVEKQSALLI 730 740 750 760 770 780 NGTLKHYQLQ GLEWMVSLYN NNLNGILADE MGLGKTIQTI ALITYLMEHK RLNGPYLIIV 790 800 810 820 830 840 PLSTLSNWTY EFDKWAPSVV KISYKGTPAM RRSLVPQLRS GKFNVLLTTY EYIIKDKHIL 850 860 870 880 890 900 AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH YVAPRRILLT GTPLQNKLPE LWALLNFLLP 910 920 930 940 950 960 TIFKSCSTFE QWFNAPFAMT GERVDLNEEE TILIIRRLHK VLRPFLLRRL KKEVESQLPE 970 980 990 1000 1010 1020 KVEYVIKCDM SALQKILYRH MQAKGILLTD GSEKDKKGKG GAKTLMNTIM QLRKICNHPY 1030 1040 1050 1060 1070 1080 MFQHIEESFA EHLGYSNGVI NGAELYRASG KFELLDRILP KLRATNHRVL LFCQMTSLMT 1090 1100 1110 1120 1130 1140 IMEDYFAFRN FLYLRLDGTT KSEDRAALLK KFNEPGSQYF IFLLSTRAGG LGLNLQAADT 1150 1160 1170 1180 1190 1200 VVIFDSDWNP HQDLQAQDRA HRIGQQNEVR VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ 1210 1220 1230 1240 1250 1260 AGMFDQKSSS HERRAFLQAI LEHEEENEEE DEVPDDETLN QMIARREEEF DLFMRMDMDR 1270 1280 1290 1300 1310 1320 RREDARNPKR KPRLMEEDEL PSWIIKDDAE VERLTCEEEE EKIFGRGSRQ RRDVDYSDAL 1330 1340 1350 1360 1370 1380 TEKQWLRAIE DGNLEEMEEE VRLKKRKRRR NVDKDPAKED VEKAKKRRGR PPAEKLSPNP 1390 1400 1410 1420 1430 1440 PKLTKQMNAI IDTVINYKDR CNVEKVPSNS QLEIEGNSSG RQLSEVFIQL PSRKELPEYY 1450 1460 1470 1480 1490 1500 ELIRKPVDFK KIKERIRNHK YRSLGDLEKD VMLLCHNAQT FNLEGSQIYE DSIVLQSVFK 1510 1520 1530 1540 1550 1560 SARQKIAKEE ESEDESNEEE EEEDEEESES EAKSVKVKIK LNKKDDKGRD KGKGKKRPNR 1570 1580 1590 GKAKPVVSDF DSDEEQDERE QSEGSGTDDE
	Isoform Short [UniParc]. Checksum: BBD4488C2861C270		1,572	179,281
	10 20 30 40 50 60 MSTPTDPGAM PHPGPSPGPG PSPGPILGPS PGPGPSPGSV HSMMGPSPGP PSVSHPMPTM 70 80 90 100 110 120 GSTDFPQEGM HQMHKPIDGI HDKGIVEDIH CGSMKGTGMR PPHPGMGPPQ SPMDQHSQGY 130 140 150 160 170 180 MSPHPSPLGA PEHVSSPMSG GGPTPPQMPP SQPGALIPGD PQAMSQPNRG PSPFSPVQLH 190 200 210 220 230 240 QLRAQILAYK MLARGQPLPE TLQLAVQGKR TLPGLQQQQQ QQQQQQQQQQ QQQQQQQQPQ 250 260 270 280 290 300 QQPPQPQTQQ QQQPALVNYN RPSGPGPELS GPSTPQKLPV PAPGGRPSPA PPAAAQPPAA 310 320 330 340 350 360 AVPGPSVPQP APGQPSPVLQ LQQKQSRISP IQKPQGLDPV EILQEREYRL QARIAHRIQE 370 380 390 400 410 420 LENLPGSLPP DLRTKATVEL KALRLLNFQR QLRQEVVACM RRDTTLETAL NSKAYKRSKR 430 440 450 460 470 480 QTLREARMTE KLEKQQKIEQ ERKRRQKHQE YLNSILQHAK DFKEYHRSVA GKIQKLSKAV 490 500 510 520 530 540 ATWHANTERE QKKETERIEK ERMRRLMAED EEGYRKLIDQ KKDRRLAYLL QQTDEYVANL 550 560 570 580 590 600 TNLVWEHKQA QAAKEKKKRR RRKKKAEENA EGGESALGPD GEPIDESSQM SDLPVKVTHT 610 620 630 640 650 660 ETGKVLFGPE APKASQLDAW LEMNPGYEVA PRSDSEESDS DYEEEDEEEE SSRQETEEKI 670 680 690 700 710 720 LLDPNSEEVS EKDAKQIIET AKQDVDDEYS MQYSARGSQS YYTVAHAISE RVEKQSALLI 730 740 750 760 770 780 NGTLKHYQLQ GLEWMVSLYN NNLNGILADE MGLGKTIQTI ALITYLMEHK RLNGPYLIIV 790 800 810 820 830 840 PLSTLSNWTY EFDKWAPSVV KISYKGTPAM RRSLVPQLRS GKFNVLLTTY EYIIKDKHIL 850 860 870 880 890 900 AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH YVAPRRILLT GTPLQNKLPE LWALLNFLLP 910 920 930 940 950 960 TIFKSCSTFE QWFNAPFAMT GERVDLNEEE TILIIRRLHK VLRPFLLRRL KKEVESQLPE 970 980 990 1000 1010 1020 KVEYVIKCDM SALQKILYRH MQAKGILLTD GSEKDKKGKG GAKTLMNTIM QLRKICNHPY 1030 1040 1050 1060 1070 1080 MFQHIEESFA EHLGYSNGVI NGAELYRASG KFELLDRILP KLRATNHRVL LFCQMTSLMT 1090 1100 1110 1120 1130 1140 IMEDYFAFRN FLYLRLDGTT KSEDRAALLK KFNEPGSQYF IFLLSTRAGG LGLNLQAADT 1150 1160 1170 1180 1190 1200 VVIFDSDWNP HQDLQAQDRA HRIGQQNEVR VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ 1210 1220 1230 1240 1250 1260 AGMFDQKSSS HERRAFLQAI LEHEEENEEE DEVPDDETLN QMIARREEEF DLFMRMDMDR 1270 1280 1290 1300 1310 1320 RREDARNPKR KPRLMEEDEL PSWIIKDDAE VERLTCEEEE EKIFGRGSRQ RRDVDYSDAL 1330 1340 1350 1360 1370 1380 TEKQWLRAIE DGNLEEMEEE VRLKKRKRRR NVDKDPAKED VEKAKKRRGR PPAEKLSPNP 1390 1400 1410 1420 1430 1440 PKLTKQMNAI IDTVINYKDS SGRQLSEVFI QLPSRKELPE YYELIRKPVD FKKIKERIRN 1450 1460 1470 1480 1490 1500 HKYRSLGDLE KDVMLLCHNA QTFNLEGSQI YEDSIVLQSV FKSARQKIAK EEESEDESNE 1510 1520 1530 1540 1550 1560 EEEEEDEEES ESEAKSVKVK IKLNKKDDKG RDKGKGKKRP NRGKAKPVVS DFDSDEEQDE 1570 REQSEGSGTD DE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and Drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor." Muchardt C., Yaniv M. EMBO J. 12:4279-4290(1993) [PubMed: 8223438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG). Tissue: Liver.
[2]	"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] (ISOFORM SHORT). Tissue: Brain.
[3]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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.
[6]	"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-591, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC." Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J. Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1568 AND SER-1572, MASS SPECTROMETRY. Tissue: Hepatocyte.
[8]	"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 SER-329; SER-956; SER-1377; SER-1418; SER-1419; SER-1568 AND SER-1572, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1551; LYS-1553 AND LYS-1555, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"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-1410, MASS SPECTROMETRY.
[11]	"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.
[12]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1568 AND SER-1572, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X72889 mRNA. Translation: CAA51407.1.
D26155 mRNA. Translation: BAA05142.1.
AL359076, AL138755 Genomic DNA. Translation: CAI12967.1.
AL359076, AL138755 Genomic DNA. Translation: CAI12968.1.
AL138755, AL359076 Genomic DNA. Translation: CAI14599.1.
AL138755, AL359076 Genomic DNA. Translation: CAI14600.1.
CH471071 Genomic DNA. Translation: EAW58811.1.
CH471071 Genomic DNA. Translation: EAW58813.1.

PIR

S39580.
S45251.

RefSeq

NP_003061.3.

UniGene

Hs.298990

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DAT	NMR	-	A	1377-1486	[»]

SMR

P51531. Positions 1384-1500.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:29005N.

IntAct

P51531.

PTM databases

PhosphoSite

P51531.