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Q9NRL2

- BAZ1A_HUMAN

UniProt

Q9NRL2 - BAZ1A_HUMAN

Protein

Bromodomain adjacent to zinc finger domain protein 1A

Gene

BAZ1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    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.
    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.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1148 – 119851PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. chromatin remodeling Source: BHF-UCL
    2. DNA-dependent DNA replication Source: UniProtKB
    3. regulation of transcription, DNA-templated Source: BHF-UCL
    4. transcription, DNA-templated Source: BHF-UCL

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:BAZ1A
    Synonyms:ACF1, WCRF180
    ORF Names:HSPC317
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:960. BAZ1A.

    Subcellular locationi

    Nucleus
    Note: May target the CHRAC complex to heterochromatin.

    GO - Cellular componenti

    1. ACF complex Source: BHF-UCL
    2. CHRAC Source: UniProtKB
    3. nuclear chromosome Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25270.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15561556Bromodomain adjacent to zinc finger domain protein 1APRO_0000211167Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei270 – 2701Phosphoserine2 Publications
    Modified residuei702 – 7021Phosphoserine1 Publication
    Modified residuei731 – 7311Phosphothreonine1 Publication
    Modified residuei1281 – 12811Phosphoserine1 Publication
    Modified residuei1371 – 13711Phosphoserine1 Publication
    Modified residuei1402 – 14021Phosphoserine2 Publications
    Modified residuei1413 – 14131Phosphoserine3 Publications
    Modified residuei1417 – 14171Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NRL2.
    PaxDbiQ9NRL2.
    PRIDEiQ9NRL2.

    PTM databases

    PhosphoSiteiQ9NRL2.

    Expressioni

    Tissue specificityi

    Highly expressed in testis and at low or undetectable levels in other tissues analyzed.

    Gene expression databases

    ArrayExpressiQ9NRL2.
    BgeeiQ9NRL2.
    CleanExiHS_BAZ1A.
    GenevestigatoriQ9NRL2.

    Organism-specific databases

    HPAiHPA002730.

    Interactioni

    Subunit structurei

    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.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HTTP428584EBI-927511,EBI-466029

    Protein-protein interaction databases

    BioGridi116347. 19 interactions.
    IntActiQ9NRL2. 7 interactions.
    MINTiMINT-1183777.
    STRINGi9606.ENSP00000353458.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NRL2.
    SMRiQ9NRL2. Positions 1149-1197, 1433-1551.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 128107WACPROSITE-ProRule annotationAdd
    BLAST
    Domaini422 – 48766DDTPROSITE-ProRule annotationAdd
    BLAST
    Domaini1446 – 151671BromoPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 133133Required for interaction with NCOR1Add
    BLAST
    Regioni1 – 128128Required for association with the CHRAC1/POLE3 complexAdd
    BLAST
    Regioni667 – 933267Interaction with SMARCA5Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili306 – 39792Sequence AnalysisAdd
    BLAST
    Coiled coili634 – 70976Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi487 – 4915Poly-Glu
    Compositional biasi1239 – 125719Glu-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the WAL family.Curated
    Contains 1 bromo domain.PROSITE-ProRule annotation
    Contains 1 DDT domain.PROSITE-ProRule annotation
    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
    Contains 1 WAC domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1148 – 119851PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Bromodomain, Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5076.
    HOGENOMiHOG000095179.
    HOVERGENiHBG080889.
    InParanoidiQ9NRL2.
    KOiK11655.
    OMAiATACTNI.
    OrthoDBiEOG7D59MK.
    PhylomeDBiQ9NRL2.
    TreeFamiTF316326.

    Family and domain databases

    Gene3Di1.20.920.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR001487. 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]
    PfamiPF00439. Bromodomain. 1 hit.
    PF02791. DDT. 1 hit.
    PF00628. PHD. 1 hit.
    PF10537. WAC_Acf1_DNA_bd. 1 hit.
    PF15612. WHIM1. 1 hit.
    [Graphical view]
    PRINTSiPR00503. BROMODOMAIN.
    SMARTiSM00297. BROMO. 1 hit.
    SM00571. DDT. 1 hit.
    SM00249. PHD. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEiPS00633. 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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NRL2-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MPLLHRKPFV RQKPPADLRP DEEVFYCKVT NEIFRHYDDF FERTILCNSL     50
    VWSCAVTGRP GLTYQEALES EKKARQNLQS FPEPLIIPVL YLTSLTHRSR 100
    LHEICDDIFA YVKDRYFVEE TVEVIRNNGA RLQCRILEVL PPSHQNGFAN 150
    GHVNSVDGET IIISDSDDSE TQSCSFQNGK KKDAIDPLLF KYKVQPTKKE 200
    LHESAIVKAT QISRRKHLFS RDKLKLFLKQ HCEPQDGVIK IKASSLSTYK 250
    IAEQDFSYFF PDDPPTFIFS PANRRRGRPP KRIHISQEDN VANKQTLASY 300
    RSKATKERDK LLKQEEMKSL AFEKAKLKRE KADALEAKKK EKEDKEKKRE 350
    ELKKIVEEER LKKKEEKERL KVEREKEREK LREEKRKYVE YLKQWSKPRE 400
    DMECDDLKEL PEPTPVKTRL PPEIFGDALM VLEFLNAFGE LFDLQDEFPD 450
    GVTLEVLEEA LVGNDSEGPL CELLFFFLTA IFQAIAEEEE EVAKEQLTDA 500
    DTKDLTEALD EDADPTKSAL SAVASLAAAW PQLHQGCSLK SLDLDSCTLS 550
    EILRLHILAS GADVTSANAK YRYQKRGGFD ATDDACMELR LSNPSLVKKL 600
    SSTSVYDLTP GEKMKILHAL CGKLLTLVST RDFIEDYVDI LRQAKQEFRE 650
    LKAEQHRKER EEAAARIRKR KEEKLKEQEQ KMKEKQEKLK EDEQRNSTAD 700
    ISIGEEERED FDTSIESKDT EQKELDQDMV TEDEDDPGSH KRGRRGKRGQ 750
    NGFKEFTRQE QINCVTREPL TADEEEALKQ EHQRKEKELL EKIQSAIACT 800
    NIFPLGRDRM YRRYWIFPSI PGLFIEEDYS GLTEDMLLPR PSSFQNNVQS 850
    QDPQVSTKTG EPLMSESTSN IDQGPRDHSV QLPKPVHKPN RWCFYSSCEQ 900
    LDQLIEALNS RGHRESALKE TLLQEKSRIC AQLARFSEEK FHFSDKPQPD 950
    SKPTYSRGRS SNAYDPSQMC AEKQLELRLR DFLLDIEDRI YQGTLGAIKV 1000
    TDRHIWRSAL ESGRYELLSE ENKENGIIKT VNEDVEEMEI DEQTKVIVKD 1050
    RLLGIKTETP STVSTNASTP QSVSSVVHYL AMALFQIEQG IERRFLKAPL 1100
    DASDSGRSYK TVLDRWRESL LSSASLSQVF LHLSTLDRSV IWSKSILNAR 1150
    CKICRKKGDA ENMVLCDGCD RGHHTYCVRP KLKTVPEGDW FCPECRPKQR 1200
    SRRLSSRQRP SLESDEDVED SMGGEDDEVD GDEEEGQSEE EEYEVEQDED 1250
    DSQEEEEVSL PKRGRPQVRL PVKTRGKLSS SFSSRGQQQE PGRYPSRSQQ 1300
    STPKTTVSSK TGRSLRKINS APPTETKSLR IASRSTRHSH GPLQADVFVE 1350
    LLSPRRKRRG RKSANNTPEN SPNFPNFRVI ATKSSEQSRS VNIASKLSLQ 1400
    ESESKRRCRK RQSPEPSPVT LGRRSSGRQG GVHELSAFEQ LVVELVRHDD 1450
    SWPFLKLVSK IQVPDYYDII KKPIALNIIR EKVNKCEYKL ASEFIDDIEL 1500
    MFSNCFEYNP RNTSEAKAGT RLQAFFHIQA QKLGLHVTPS NVDQVSTPPA 1550
    AKKSRI 1556
    Length:1,556
    Mass (Da):178,702
    Last modified:October 17, 2006 - v2
    Checksum:i4D78B9A8ADBF715B
    GO
    Isoform 2 (identifier: Q9NRL2-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,524
    Mass (Da):175,385
    Checksum:i2DB787369178282B
    GO

    Sequence cautioni

    The sequence AAF28995.1 differs from that shown. Reason: Frameshift at several positions.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti135 – 1351R → T in BAA89209. (PubMed:10662543)Curated
    Sequence conflicti236 – 2361D → E in BAA89209. (PubMed:10662543)Curated
    Sequence conflicti494 – 4941K → Q in AAF28995. 1 PublicationCurated
    Sequence conflicti503 – 5086KDLTEA → QDFTEP in AAF28995. 1 PublicationCurated
    Sequence conflicti525 – 5251S → P in AAF28995. 1 PublicationCurated
    Sequence conflicti536 – 5405GCSLK → AALKF in AAF28995. 1 PublicationCurated
    Sequence conflicti551 – 5511E → D in AAF70601. (PubMed:10880450)Curated
    Sequence conflicti730 – 7301V → F in BAA89209. (PubMed:10662543)Curated
    Sequence conflicti769 – 7691P → L in BAA89209. (PubMed:10662543)Curated
    Sequence conflicti1201 – 12011S → C in BAA89209. (PubMed:10662543)Curated
    Sequence conflicti1206 – 12061S → F in BAA89209. (PubMed:10662543)Curated
    Sequence conflicti1409 – 14091R → K in AAF70601. (PubMed:10880450)Curated
    Sequence conflicti1409 – 14091R → K in CAB43261. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti344 – 3441D → E.
    Corresponds to variant rs1133285 [ dbSNP | Ensembl ].
    VAR_028049
    Natural varianti1366 – 13661N → K.2 Publications
    Corresponds to variant rs1044140 [ dbSNP | Ensembl ].
    VAR_048423

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei504 – 53532Missing in isoform 2. 1 PublicationVSP_000551Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS41943.1. [Q9NRL2-2]
    CCDS9651.1. [Q9NRL2-1]
    PIRiT08738.
    RefSeqiNP_038476.2. NM_013448.2. [Q9NRL2-1]
    NP_872589.1. NM_182648.1. [Q9NRL2-2]
    UniGeneiHs.509140.

    Genome annotation databases

    EnsembliENST00000358716; ENSP00000351555; ENSG00000198604. [Q9NRL2-2]
    ENST00000360310; ENSP00000353458; ENSG00000198604. [Q9NRL2-1]
    ENST00000382422; ENSP00000371859; ENSG00000198604. [Q9NRL2-1]
    GeneIDi11177.
    KEGGihsa:11177.
    UCSCiuc001wsk.3. human. [Q9NRL2-1]
    uc001wsl.3. human. [Q9NRL2-2]

    Polymorphism databases

    DMDMi116241266.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS41943.1. [Q9NRL2-2 ]
    CCDS9651.1. [Q9NRL2-1 ]
    PIRi T08738.
    RefSeqi NP_038476.2. NM_013448.2. [Q9NRL2-1 ]
    NP_872589.1. NM_182648.1. [Q9NRL2-2 ]
    UniGenei Hs.509140.

    3D structure databases

    ProteinModelPortali Q9NRL2.
    SMRi Q9NRL2. Positions 1149-1197, 1433-1551.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116347. 19 interactions.
    IntActi Q9NRL2. 7 interactions.
    MINTi MINT-1183777.
    STRINGi 9606.ENSP00000353458.

    PTM databases

    PhosphoSitei Q9NRL2.

    Polymorphism databases

    DMDMi 116241266.

    Proteomic databases

    MaxQBi Q9NRL2.
    PaxDbi Q9NRL2.
    PRIDEi Q9NRL2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358716 ; ENSP00000351555 ; ENSG00000198604 . [Q9NRL2-2 ]
    ENST00000360310 ; ENSP00000353458 ; ENSG00000198604 . [Q9NRL2-1 ]
    ENST00000382422 ; ENSP00000371859 ; ENSG00000198604 . [Q9NRL2-1 ]
    GeneIDi 11177.
    KEGGi hsa:11177.
    UCSCi uc001wsk.3. human. [Q9NRL2-1 ]
    uc001wsl.3. human. [Q9NRL2-2 ]

    Organism-specific databases

    CTDi 11177.
    GeneCardsi GC14M035221.
    H-InvDB HIX0037904.
    HGNCi HGNC:960. BAZ1A.
    HPAi HPA002730.
    MIMi 605680. gene.
    neXtProti NX_Q9NRL2.
    PharmGKBi PA25270.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5076.
    HOGENOMi HOG000095179.
    HOVERGENi HBG080889.
    InParanoidi Q9NRL2.
    KOi K11655.
    OMAi ATACTNI.
    OrthoDBi EOG7D59MK.
    PhylomeDBi Q9NRL2.
    TreeFami TF316326.

    Miscellaneous databases

    ChiTaRSi BAZ1A. human.
    GenomeRNAii 11177.
    NextBioi 42529.
    PROi Q9NRL2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NRL2.
    Bgeei Q9NRL2.
    CleanExi HS_BAZ1A.
    Genevestigatori Q9NRL2.

    Family and domain databases

    Gene3Di 1.20.920.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProi IPR001487. 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 ]
    Pfami PF00439. Bromodomain. 1 hit.
    PF02791. DDT. 1 hit.
    PF00628. PHD. 1 hit.
    PF10537. WAC_Acf1_DNA_bd. 1 hit.
    PF15612. WHIM1. 1 hit.
    [Graphical view ]
    PRINTSi PR00503. BROMODOMAIN.
    SMARTi SM00297. BROMO. 1 hit.
    SM00571. DDT. 1 hit.
    SM00249. PHD. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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. 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. 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].

    Entry informationi

    Entry nameiBAZ1A_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRL2
    Secondary accession number(s): Q9NZ15
    , Q9P065, Q9UIG1, Q9Y3V3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2002
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 145 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Miscellaneous

    Stimulated by double-stranded DNA and nucleosomal DNA.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3