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Reviewed, UniProtKB/Swiss-Prot Q9NRL2 (BAZ1A_HUMAN)

Last modified December 15, 2009. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bromodomain adjacent to zinc finger domain protein 1A
Alternative name(s):
    ATP-utilizing chromatin assembly and remodeling factor 1
      Short name=hACF1
    ATP-dependent chromatin-remodeling protein
    Williams syndrome transcription factor-related chromatin-remodeling factor 180
      Short name=WCRF180
      Short name=hWALp1
    CHRAC subunit ACF1
Gene names
Name: BAZ1A
Synonyms: ACF1, WCRF180
ORF Names: HSPC317
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1556 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May play a role in transcriptional regulation. May be involved in the formation or maintenance of heterochromatin playing a critical role in developmental control.

Subunit structure

Together with CHRAC1, POLE3 and SMARCA5 proteins, it forms the ISWI chromatin-remodeling complex, CHRAC.

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 processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainBromodomain
Coiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processregulation of transcription

Inferred from electronic annotation. Source: UniProtKB-KW

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionprotein binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

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 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
Coiled coil306 – 39792 Potential
Coiled coil634 – 70976 Potential

Amino acid modifications

Modified residue2701Phosphoserine
Modified residue6061Phosphotyrosine Ref.7
Modified residue7021Phosphoserine
Modified residue7311Phosphothreonine
Modified residue12791Phosphoserine Ref.8
Modified residue12811Phosphoserine Ref.8
Modified residue13391Phosphoserine Ref.10
Modified residue13531Phosphoserine Ref.10
Modified residue13631Phosphoserine Ref.10
Modified residue13671Phosphothreonine Ref.10
Modified residue13711Phosphoserine Ref.10
Modified residue14021Phosphoserine Ref.10
Modified residue14131Phosphoserine Ref.10 Ref.6 Ref.9
Modified residue14171Phosphoserine Ref.10 Ref.6
Modified residue15471Phosphothreonine Ref.10

Natural variations

Alternative sequence504 – 53532Missing in isoform 2.
VSP_000551
Natural variant3441D → E: dbSNP rs1133285.
VAR_028049
Natural variant13661N → K: dbSNP rs1044140. Ref.1 Ref.5
VAR_048423

Experimental info

Sequence conflict1351R → T in BAA89209. Ref.3
Sequence conflict2361D → E in BAA89209. Ref.3
Sequence conflict4941K → Q in AAF28995. Ref.4
Sequence conflict503 – 5086KDLTEA → QDFTEP in AAF28995. Ref.4
Sequence conflict5251S → P in AAF28995. Ref.4
Sequence conflict536 – 5405GCSLK → AALKF in AAF28995. Ref.4
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.5

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.

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: 10880450] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MASS SPECTROMETRY, 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: 10655480] [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: 10662543] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Testis.
[4]"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.
[5]"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: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 746-1556 (ISOFORM 1), VARIANT LYS-1366.
Tissue: Uterus.
[6]"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-1413 AND SER-1417, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-606, MASS SPECTROMETRY.
[8]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1279 AND SER-1281, MASS SPECTROMETRY.
[9]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1413, MASS SPECTROMETRY.
[10]"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-1339; SER-1353; SER-1363; THR-1367; SER-1371; SER-1402; SER-1413; SER-1417 AND THR-1547, MASS SPECTROMETRY.
[11]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[12]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1402, MASS SPECTROMETRY.
[13]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270; SER-702 AND THR-731, MASS SPECTROMETRY.
Tissue: T-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF213467 mRNA. Translation: AAF70601.1.
AF221130 mRNA. Translation: AAF32366.1.
AB032252 mRNA. Translation: BAA89209.1.
AF161435 mRNA. Translation: AAF28995.1. Frameshift.
AL050089 mRNA. Translation: CAB43261.1.
IPIIPI00383565.
IPI00412415.
PIRT08738.
RefSeqNP_038476.2.
NP_872589.1.
UniGeneHs.509140

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9NRL2. 2 interactions.
STRINGQ9NRL2.

PTM databases

PhosphoSiteQ9NRL2.

Genome annotation databases

EnsemblENST00000360310; ENSP00000353458; ENSG00000198604; Homo sapiens. [Genome view]
ENST00000382422; ENSP00000371859; ENSG00000198604; Homo sapiens. [Genome view]
GeneID11177.
KEGGhsa:11177.
UCSCuc001wsk.1. human.
uc001wsl.1. human.

Organism-specific databases

CTD11177.
GeneCardsGC14M034291.
H-InvDBHIX0011594.
HGNCHGNC:960. BAZ1A.
HPAHPA002730.
MIM605680. gene.
PharmGKBPA25270.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG717122.
HOVERGENQ9NRL2.
InParanoidQ9NRL2.
OMANGARLQC.
OrthoDBEOG9N8TQT.

Gene expression databases

ArrayExpressQ9NRL2.
BgeeQ9NRL2.
CleanExHS_BAZ1A.
GenevestigatorQ9NRL2.
GermOnlineENSG00000198604. Homo sapiens.

Family and domain databases

InterProIPR001487. 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.
[Graphical view]
Gene3DG3DSA:1.20.920.10. Bromodomain. 1 hit.
PfamPF00439. Bromodomain. 1 hit.
PF02791. DDT. 1 hit.
PF00628. PHD. 1 hit.
PF10537. WAC_Acf1_DNA_bd. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 1 hit.
SM00571. DDT. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
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 Resources

NextBio42529.
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: December 15, 2009
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 14

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents