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Q9NRL2 (BAZ1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1556 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HTTP428584EBI-927511,EBI-466029

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15561556Bromodomain adjacent to zinc finger domain protein 1A
PRO_0000211167

Regions

Domain22 – 128107WAC
Domain422 – 48766DDT
Domain1446 – 151671Bromo
Zinc finger1148 – 119851PHD-type
Region1 – 133133Required for interaction with NCOR1
Region1 – 128128Required for association with the CHRAC1/POLE3 complex
Region667 – 933267Interaction with SMARCA5
Coiled coil306 – 39792 Potential
Coiled coil634 – 70976 Potential
Compositional bias487 – 4915Poly-Glu
Compositional bias1239 – 125719Glu-rich

Amino acid modifications

Modified residue2701Phosphoserine Ref.14 Ref.15
Modified residue7021Phosphoserine Ref.14
Modified residue7311Phosphothreonine Ref.17
Modified residue12811Phosphoserine Ref.17
Modified residue13711Phosphoserine Ref.15
Modified residue14021Phosphoserine Ref.13 Ref.15
Modified residue14131Phosphoserine Ref.10 Ref.13 Ref.17
Modified residue14171Phosphoserine Ref.10 Ref.13

Natural variations

Alternative sequence504 – 53532Missing in isoform 2.
VSP_000551
Natural variant3441D → E.
Corresponds to variant rs1133285 [ dbSNP | Ensembl ].
VAR_028049
Natural variant13661N → K. Ref.1 Ref.7
Corresponds to variant rs1044140 [ dbSNP | Ensembl ].
VAR_048423

Experimental info

Sequence conflict1351R → T in BAA89209. Ref.3
Sequence conflict2361D → E in BAA89209. Ref.3
Sequence conflict4941K → Q in AAF28995. Ref.6
Sequence conflict503 – 5086KDLTEA → QDFTEP in AAF28995. Ref.6
Sequence conflict5251S → P in AAF28995. Ref.6
Sequence conflict536 – 5405GCSLK → AALKF in AAF28995. Ref.6
Sequence conflict5511E → D in AAF70601. Ref.1
Sequence conflict7301V → F in BAA89209. Ref.3
Sequence conflict7691P → L in BAA89209. Ref.3
Sequence conflict12011S → C in BAA89209. Ref.3
Sequence conflict12061S → F in BAA89209. Ref.3
Sequence conflict14091R → K in AAF70601. Ref.1
Sequence conflict14091R → K in CAB43261. Ref.7

Sequences

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

Last modified October 17, 2006. Version 2.
Checksum: 4D78B9A8ADBF715B

FASTA1,556178,702
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 2DB787369178282B
Show »

FASTA1,524175,385

References

« Hide '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 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. expand/collapse author list , 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. 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 (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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRT08738.
RefSeqNP_038476.2. NM_013448.2.
NP_872589.1. NM_182648.1.
UniGeneHs.509140.

3D structure databases

ProteinModelPortalQ9NRL2.
SMRQ9NRL2. Positions 1149-1197, 1433-1551.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116347. 19 interactions.
IntActQ9NRL2. 7 interactions.
MINTMINT-1183777.
STRING9606.ENSP00000353458.

PTM databases

PhosphoSiteQ9NRL2.

Polymorphism databases

DMDM116241266.

Proteomic databases

PaxDbQ9NRL2.
PRIDEQ9NRL2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358716; ENSP00000351555; ENSG00000198604. [Q9NRL2-2]
ENST00000360310; ENSP00000353458; ENSG00000198604. [Q9NRL2-1]
ENST00000382422; ENSP00000371859; ENSG00000198604. [Q9NRL2-1]
GeneID11177.
KEGGhsa:11177.
UCSCuc001wsk.3. human. [Q9NRL2-1]
uc001wsl.3. human. [Q9NRL2-2]

Organism-specific databases

CTD11177.
GeneCardsGC14M035221.
H-InvDBHIX0037904.
HGNCHGNC:960. BAZ1A.
HPAHPA002730.
MIM605680. gene.
neXtProtNX_Q9NRL2.
PharmGKBPA25270.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5076.
HOGENOMHOG000095179.
HOVERGENHBG080889.
InParanoidQ9NRL2.
KOK11655.
OMAAYDPSQM.
OrthoDBEOG7D59MK.
PhylomeDBQ9NRL2.
TreeFamTF316326.

Gene expression databases

ArrayExpressQ9NRL2.
BgeeQ9NRL2.
CleanExHS_BAZ1A.
GenevestigatorQ9NRL2.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
InterProIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR004022. DDT_dom.
IPR018500. DDT_dom_subgr.
IPR018501. DDT_dom_superfamily.
IPR028942. WHIM1_dom.
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]
PfamPF00439. Bromodomain. 1 hit.
PF02791. DDT. 1 hit.
PF00628. PHD. 1 hit.
PF10537. WAC_Acf1_DNA_bd. 1 hit.
PF15612. WHIM1. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 1 hit.
SM00571. DDT. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEPS00633. 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]
ProtoNetSearch...

Other

ChiTaRSBAZ1A. human.
GenomeRNAi11177.
NextBio42529.
PROQ9NRL2.
SOURCESearch...

Entry information

Entry nameBAZ1A_HUMAN
AccessionPrimary (citable) accession number: Q9NRL2
Secondary accession number(s): Q9NZ15 expand/collapse secondary AC list , Q9P065, Q9UIG1, Q9Y3V3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 141 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

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 14

Human chromosome 14: entries, gene names and cross-references to MIM