Q9NRL2 (BAZ1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bromodomain adjacent to zinc finger domain protein 1A

Alternative name(s):
ATP-dependent chromatin-remodeling protein
ATP-utilizing chromatin assembly and remodeling factor 1
Short name=hACF1
CHRAC subunit ACF1
Williams syndrome transcription factor-related chromatin-remodeling factor 180
Short name=WCRF180
hWALp1

Gene names

Name:	BAZ1A
Synonyms:	ACF1, WCRF180
ORF Names:	HSPC317

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1556 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the ACF complex, an ATP-dependent chromatin remodeling complex, that regulates spacing of nucleosomes using ATP to generate evenly spaced nucleosomes along the chromatin. The ATPase activity of the complex is regulated by the length of flanking DNA. Also involved in facilitating the DNA replication process. BAZ1A is the accessory, non-catalytic subunit of the complex which can enhance and direct the process provided by the ATPase subunit, SMARCA5, probably through targeting pericentromeric heterochromatin in late S phase. Moves end-positioned nucleosomes to a predominantly central position. May have a role in nuclear receptor-mediated transcription repression. Ref.8 Ref.9 Ref.11 Ref.12 Component of the histone-fold protein complex CHRAC complex which faciliates nucleosome sliding by the ACF complex and enhances ACF-mediated chromatin assembly. The C-terminal regions of both CHRAC1 and POLE1 are required for these functions. Ref.8 Ref.9 Ref.11 Ref.12
Subunit structure	Component of the ACF chromatin remodeling complex that includes BAZ1A and SMARCA5. Additional this complex can form, together with CHRAC1 and POLE1, the histone-fold protein complex, CHRAC. Interacts with NCOR1 (via its RD1 domain); the interaction corepresses a number of NCOR1-regulated genes. Ref.1 Ref.8 Ref.12
Subcellular location	Nucleus. Note: May target the CHRAC complex to heterochromatin.
Tissue specificity	Highly expressed in testis and at low or undetectable levels in other tissues analyzed.
Miscellaneous	Stimulated by double-stranded DNA and nucleosomal DNA.
Sequence similarities	Belongs to the WAL family. Contains 1 bromo domain. Contains 1 DDT domain. Contains 1 PHD-type zinc finger. Contains 1 WAC domain.
Sequence caution	The sequence AAF28995.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Bromodomain Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA-dependent DNA replication Inferred from direct assay Ref.8. Source: UniProtKB chromatin remodeling Traceable author statement Ref.3. Source: BHF-UCL regulation of transcription, DNA-dependent Non-traceable author statement Ref.3. Source: BHF-UCL transcription, DNA-dependent Non-traceable author statement Ref.3. Source: BHF-UCL
Cellular_component	ACF complex Traceable author statement Ref.3. Source: BHF-UCL CHRAC Inferred from direct assay Ref.1. Source: UniProtKB nuclear chromosome Inferred from electronic annotation. Source: Compara
Molecular_function	zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9NRL2-1)

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: Q9NRL2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     504-535: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1556	1556	Bromodomain adjacent to zinc finger domain protein 1A		PRO_0000211167
Regions
	Domain	22 – 128	107	WAC
	Domain	422 – 487	66	DDT
	Domain	1446 – 1516	71	Bromo
	Zinc finger	1148 – 1198	51	PHD-type
	Region	1 – 133	133	Required for interaction with NCOR1
	Region	1 – 128	128	Required for association with the CHRAC1/POLE3 complex
	Region	667 – 933	267	Interaction with SMARCA5
	Coiled coil	306 – 397	92	Potential
	Coiled coil	634 – 709	76	Potential
	Compositional bias	487 – 491	5	Poly-Glu
	Compositional bias	1239 – 1257	19	Glu-rich
Amino acid modifications
	Modified residue	270	1	Phosphoserine Ref.14 Ref.15
	Modified residue	702	1	Phosphoserine Ref.14
	Modified residue	731	1	Phosphothreonine Ref.17
	Modified residue	1281	1	Phosphoserine Ref.17
	Modified residue	1371	1	Phosphoserine Ref.15
	Modified residue	1402	1	Phosphoserine Ref.13 Ref.15
	Modified residue	1413	1	Phosphoserine Ref.10 Ref.13 Ref.17
	Modified residue	1417	1	Phosphoserine Ref.10 Ref.13
Natural variations
	Alternative sequence	504 – 535	32	Missing in isoform 2.		VSP_000551
	Natural variant	344	1	D → E. Corresponds to variant rs1133285 [ dbSNP | Ensembl ].		VAR_028049
	Natural variant	1366	1	N → K. Ref.1 Ref.7 Corresponds to variant rs1044140 [ dbSNP | Ensembl ].		VAR_048423
Experimental info
	Sequence conflict	135	1	R → T in BAA89209. Ref.3
	Sequence conflict	236	1	D → E in BAA89209. Ref.3
	Sequence conflict	494	1	K → Q in AAF28995. Ref.6
	Sequence conflict	503 – 508	6	KDLTEA → QDFTEP in AAF28995. Ref.6
	Sequence conflict	525	1	S → P in AAF28995. Ref.6
	Sequence conflict	536 – 540	5	GCSLK → AALKF in AAF28995. Ref.6
	Sequence conflict	551	1	E → D in AAF70601. Ref.1
	Sequence conflict	730	1	V → F in BAA89209. Ref.3
	Sequence conflict	769	1	P → L in BAA89209. Ref.3
	Sequence conflict	1201	1	S → C in BAA89209. Ref.3
	Sequence conflict	1206	1	S → F in BAA89209. Ref.3
	Sequence conflict	1409	1	R → K in AAF70601. Ref.1
	Sequence conflict	1409	1	R → K in CAB43261. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 4D78B9A8ADBF715B	FASTA	1,556	178,702
	10 20 30 40 50 60 MPLLHRKPFV RQKPPADLRP DEEVFYCKVT NEIFRHYDDF FERTILCNSL VWSCAVTGRP 70 80 90 100 110 120 GLTYQEALES EKKARQNLQS FPEPLIIPVL YLTSLTHRSR LHEICDDIFA YVKDRYFVEE 130 140 150 160 170 180 TVEVIRNNGA RLQCRILEVL PPSHQNGFAN GHVNSVDGET IIISDSDDSE TQSCSFQNGK 190 200 210 220 230 240 KKDAIDPLLF KYKVQPTKKE LHESAIVKAT QISRRKHLFS RDKLKLFLKQ HCEPQDGVIK 250 260 270 280 290 300 IKASSLSTYK IAEQDFSYFF PDDPPTFIFS PANRRRGRPP KRIHISQEDN VANKQTLASY 310 320 330 340 350 360 RSKATKERDK LLKQEEMKSL AFEKAKLKRE KADALEAKKK EKEDKEKKRE ELKKIVEEER 370 380 390 400 410 420 LKKKEEKERL KVEREKEREK LREEKRKYVE YLKQWSKPRE DMECDDLKEL PEPTPVKTRL 430 440 450 460 470 480 PPEIFGDALM VLEFLNAFGE LFDLQDEFPD GVTLEVLEEA LVGNDSEGPL CELLFFFLTA 490 500 510 520 530 540 IFQAIAEEEE EVAKEQLTDA DTKDLTEALD EDADPTKSAL SAVASLAAAW PQLHQGCSLK 550 560 570 580 590 600 SLDLDSCTLS EILRLHILAS GADVTSANAK YRYQKRGGFD ATDDACMELR LSNPSLVKKL 610 620 630 640 650 660 SSTSVYDLTP GEKMKILHAL CGKLLTLVST RDFIEDYVDI LRQAKQEFRE LKAEQHRKER 670 680 690 700 710 720 EEAAARIRKR KEEKLKEQEQ KMKEKQEKLK EDEQRNSTAD ISIGEEERED FDTSIESKDT 730 740 750 760 770 780 EQKELDQDMV TEDEDDPGSH KRGRRGKRGQ NGFKEFTRQE QINCVTREPL TADEEEALKQ 790 800 810 820 830 840 EHQRKEKELL EKIQSAIACT NIFPLGRDRM YRRYWIFPSI PGLFIEEDYS GLTEDMLLPR 850 860 870 880 890 900 PSSFQNNVQS QDPQVSTKTG EPLMSESTSN IDQGPRDHSV QLPKPVHKPN RWCFYSSCEQ 910 920 930 940 950 960 LDQLIEALNS RGHRESALKE TLLQEKSRIC AQLARFSEEK FHFSDKPQPD SKPTYSRGRS 970 980 990 1000 1010 1020 SNAYDPSQMC AEKQLELRLR DFLLDIEDRI YQGTLGAIKV TDRHIWRSAL ESGRYELLSE 1030 1040 1050 1060 1070 1080 ENKENGIIKT VNEDVEEMEI DEQTKVIVKD RLLGIKTETP STVSTNASTP QSVSSVVHYL 1090 1100 1110 1120 1130 1140 AMALFQIEQG IERRFLKAPL DASDSGRSYK TVLDRWRESL LSSASLSQVF LHLSTLDRSV 1150 1160 1170 1180 1190 1200 IWSKSILNAR CKICRKKGDA ENMVLCDGCD RGHHTYCVRP KLKTVPEGDW FCPECRPKQR 1210 1220 1230 1240 1250 1260 SRRLSSRQRP SLESDEDVED SMGGEDDEVD GDEEEGQSEE EEYEVEQDED DSQEEEEVSL 1270 1280 1290 1300 1310 1320 PKRGRPQVRL PVKTRGKLSS SFSSRGQQQE PGRYPSRSQQ STPKTTVSSK TGRSLRKINS 1330 1340 1350 1360 1370 1380 APPTETKSLR IASRSTRHSH GPLQADVFVE LLSPRRKRRG RKSANNTPEN SPNFPNFRVI 1390 1400 1410 1420 1430 1440 ATKSSEQSRS VNIASKLSLQ ESESKRRCRK RQSPEPSPVT LGRRSSGRQG GVHELSAFEQ 1450 1460 1470 1480 1490 1500 LVVELVRHDD SWPFLKLVSK IQVPDYYDII KKPIALNIIR EKVNKCEYKL ASEFIDDIEL 1510 1520 1530 1540 1550 MFSNCFEYNP RNTSEAKAGT RLQAFFHIQA QKLGLHVTPS NVDQVSTPPA AKKSRI
	Isoform 2 [UniParc]. Checksum: 2DB787369178282B	FASTA	1,524	175,385
	10 20 30 40 50 60 MPLLHRKPFV RQKPPADLRP DEEVFYCKVT NEIFRHYDDF FERTILCNSL VWSCAVTGRP 70 80 90 100 110 120 GLTYQEALES EKKARQNLQS FPEPLIIPVL YLTSLTHRSR LHEICDDIFA YVKDRYFVEE 130 140 150 160 170 180 TVEVIRNNGA RLQCRILEVL PPSHQNGFAN GHVNSVDGET IIISDSDDSE TQSCSFQNGK 190 200 210 220 230 240 KKDAIDPLLF KYKVQPTKKE LHESAIVKAT QISRRKHLFS RDKLKLFLKQ HCEPQDGVIK 250 260 270 280 290 300 IKASSLSTYK IAEQDFSYFF PDDPPTFIFS PANRRRGRPP KRIHISQEDN VANKQTLASY 310 320 330 340 350 360 RSKATKERDK LLKQEEMKSL AFEKAKLKRE KADALEAKKK EKEDKEKKRE ELKKIVEEER 370 380 390 400 410 420 LKKKEEKERL KVEREKEREK LREEKRKYVE YLKQWSKPRE DMECDDLKEL PEPTPVKTRL 430 440 450 460 470 480 PPEIFGDALM VLEFLNAFGE LFDLQDEFPD GVTLEVLEEA LVGNDSEGPL CELLFFFLTA 490 500 510 520 530 540 IFQAIAEEEE EVAKEQLTDA DTKGCSLKSL DLDSCTLSEI LRLHILASGA DVTSANAKYR 550 560 570 580 590 600 YQKRGGFDAT DDACMELRLS NPSLVKKLSS TSVYDLTPGE KMKILHALCG KLLTLVSTRD 610 620 630 640 650 660 FIEDYVDILR QAKQEFRELK AEQHRKEREE AAARIRKRKE EKLKEQEQKM KEKQEKLKED 670 680 690 700 710 720 EQRNSTADIS IGEEEREDFD TSIESKDTEQ KELDQDMVTE DEDDPGSHKR GRRGKRGQNG 730 740 750 760 770 780 FKEFTRQEQI NCVTREPLTA DEEEALKQEH QRKEKELLEK IQSAIACTNI FPLGRDRMYR 790 800 810 820 830 840 RYWIFPSIPG LFIEEDYSGL TEDMLLPRPS SFQNNVQSQD PQVSTKTGEP LMSESTSNID 850 860 870 880 890 900 QGPRDHSVQL PKPVHKPNRW CFYSSCEQLD QLIEALNSRG HRESALKETL LQEKSRICAQ 910 920 930 940 950 960 LARFSEEKFH FSDKPQPDSK PTYSRGRSSN AYDPSQMCAE KQLELRLRDF LLDIEDRIYQ 970 980 990 1000 1010 1020 GTLGAIKVTD RHIWRSALES GRYELLSEEN KENGIIKTVN EDVEEMEIDE QTKVIVKDRL 1030 1040 1050 1060 1070 1080 LGIKTETPST VSTNASTPQS VSSVVHYLAM ALFQIEQGIE RRFLKAPLDA SDSGRSYKTV 1090 1100 1110 1120 1130 1140 LDRWRESLLS SASLSQVFLH LSTLDRSVIW SKSILNARCK ICRKKGDAEN MVLCDGCDRG 1150 1160 1170 1180 1190 1200 HHTYCVRPKL KTVPEGDWFC PECRPKQRSR RLSSRQRPSL ESDEDVEDSM GGEDDEVDGD 1210 1220 1230 1240 1250 1260 EEEGQSEEEE YEVEQDEDDS QEEEEVSLPK RGRPQVRLPV KTRGKLSSSF SSRGQQQEPG 1270 1280 1290 1300 1310 1320 RYPSRSQQST PKTTVSSKTG RSLRKINSAP PTETKSLRIA SRSTRHSHGP LQADVFVELL 1330 1340 1350 1360 1370 1380 SPRRKRRGRK SANNTPENSP NFPNFRVIAT KSSEQSRSVN IASKLSLQES ESKRRCRKRQ 1390 1400 1410 1420 1430 1440 SPEPSPVTLG RRSSGRQGGV HELSAFEQLV VELVRHDDSW PFLKLVSKIQ VPDYYDIIKK 1450 1460 1470 1480 1490 1500 PIALNIIREK VNKCEYKLAS EFIDDIELMF SNCFEYNPRN TSEAKAGTRL QAFFHIQAQK 1510 1520 LGLHVTPSNV DQVSTPPAAK KSRI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"HuCHRAC, a human ISWI chromatin remodelling complex contains hACF1 and two novel histone-fold proteins." Poot R.A., Dellaire G., Huelsmann B.B., Grimaldi M.A., Corona D.F.V., Becker P.B., Bickmore W.A., Varga-Weisz P.D. EMBO J. 19:3377-3387(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE THE CHRAC COMPLEX, VARIANT LYS-1366. Tissue: Cervix carcinoma.
[2]	"A family of chromatin remodeling factors related to Williams syndrome transcription factor." Bochar D.A., Savard J., Wang W., Lafleur D.W., Moore P., Cote J., Shiekhattar R. Proc. Natl. Acad. Sci. U.S.A. 97:1038-1043(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]	"A novel family of bromodomain genes." Jones M.H., Hamana N., Nezu J., Shimane M. Genomics 63:40-45(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Testis.
[4]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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].
[6]	"Human partial CDS from CD34+ stem cells." Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-540 (ISOFORM 1). Tissue: Umbilical cord blood.
[7]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 746-1556 (ISOFORM 1), VARIANT LYS-1366. Tissue: Uterus.
[8]	"An ACF1-ISWI chromatin-remodeling complex is required for DNA replication through heterochromatin." Collins N., Poot R.A., Kukimoto I., Garcia-Jimenez C., Dellaire G., Varga-Weisz P.D. Nat. Genet. 32:627-632(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SMARCA5 IN THE AFC COMPLEX.
[9]	"The histone-fold protein complex CHRAC-15/17 enhances nucleosome sliding and assembly mediated by ACF." Kukimoto I., Elderkin S., Grimaldi M., Oelgeschlager T., Varga-Weisz P.D. Mol. Cell 13:265-277(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION WITH THE CHRAC1/POLE3 COMPLEX, FUNCTION OF THE CHRAC COMPLEX.
[10]	"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 SER-1413 AND SER-1417, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"The chromatin-remodeling enzyme ACF is an ATP-dependent DNA length sensor that regulates nucleosome spacing." Yang J.G., Madrid T.S., Sevastopoulos E., Narlikar G.J. Nat. Struct. Mol. Biol. 13:1078-1083(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF ACF COMPLEX.
[12]	"Novel regulatory role for human Acf1 in transcriptional repression of vitamin D3 receptor-regulated genes." Ewing A.K., Attner M., Chakravarti D. Mol. Endocrinol. 21:1791-1806(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NCOR1, POSSIBLE FUNCTION.
[13]	"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-1402; SER-1413 AND SER-1417, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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 SER-270 AND SER-702, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"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-270; SER-1371 AND SER-1402, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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].
[17]	"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 THR-731; SER-1281 AND SER-1413, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF213467 mRNA. Translation: AAF70601.1. AF221130 mRNA. Translation: AAF32366.1. AB032252 mRNA. Translation: BAA89209.1. AL121603 Genomic DNA. No translation available. AL355885 Genomic DNA. No translation available. CH471078 Genomic DNA. Translation: EAW65900.1. AF161435 mRNA. Translation: AAF28995.1. Frameshift. AL050089 mRNA. Translation: CAB43261.1.
IPI	IPI00383565. IPI00412415.
PIR	T08738.
RefSeq	NP_038476.2. NM_013448.2. NP_872589.1. NM_182648.1.
UniGene	Hs.509140.
3D structure databases
ProteinModelPortal	Q9NRL2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NRL2. 2 interactions.
MINT	MINT-1183777.
STRING	9606.ENSP00000353458.
PTM databases
PhosphoSite	Q9NRL2.
Polymorphism databases
DMDM	116241266.
Proteomic databases
PaxDb	Q9NRL2.
PRIDE	Q9NRL2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000358716; ENSP00000351555; ENSG00000198604. ENST00000360310; ENSP00000353458; ENSG00000198604. ENST00000382422; ENSP00000371859; ENSG00000198604.
GeneID	11177.
KEGG	hsa:11177.
UCSC	uc001wsk.3. human. uc001wsl.3. human.
Organism-specific databases
CTD	11177.
GeneCards	GC14M035221.
H-InvDB	HIX0037904.
HGNC	HGNC:960. BAZ1A.
HPA	HPA002730.
MIM	605680. gene.
neXtProt	NX_Q9NRL2.
PharmGKB	PA25270.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5076.
HOGENOM	HOG000095179.
HOVERGEN	HBG080889.
InParanoid	Q9NRL2.
KO	K11655.
OMA	SSFQNNV.
OrthoDB	EOG49GKFR.
PhylomeDB	Q9NRL2.
Gene expression databases
ArrayExpress	Q9NRL2.
Bgee	Q9NRL2.
CleanEx	HS_BAZ1A.
Genevestigator	Q9NRL2.
GermOnline	ENSG00000198604. Homo sapiens.
Family and domain databases
Gene3D	1.20.920.10. 1 hit. 3.30.40.10. 1 hit.
InterPro	IPR001487. Bromodomain. IPR018359. Bromodomain_CS. IPR004022. DDT_dom. IPR018500. DDT_dom_subgr. IPR018501. DDT_dom_superfamily. IPR013136. WSTF_Acf1_Cbp146. IPR019786. Zinc_finger_PHD-type_CS. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF00439. Bromodomain. 1 hit. PF02791. DDT. 1 hit. PF00628. PHD. 1 hit. PF10537. WAC_Acf1_DNA_bd. 1 hit. [Graphical view]
PRINTS	PR00503. BROMODOMAIN.
SMART	SM00297. BROMO. 1 hit. SM00571. DDT. 1 hit. SM00249. PHD. 1 hit. SM00184. RING. 1 hit. [Graphical view]
SUPFAM	SSF47370. Bromodomain. 1 hit. SSF57903. FYVE_PHD_ZnF. 1 hit.
PROSITE	PS00633. BROMODOMAIN_1. 1 hit. PS50014. BROMODOMAIN_2. 1 hit. PS50827. DDT. 1 hit. PS51136. WAC. 1 hit. PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	BAZ1A. human.
GenomeRNAi	11177.
NextBio	42529.
SOURCE	Search...

Entry information

Entry name

BAZ1A_HUMAN

Accession

Primary (citable) accession number: Q9NRL2
Secondary accession number(s): Q9NZ15 , Q9P065, Q9UIG1, Q9Y3V3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2002
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.