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Q9NRL2

- BAZ1A_HUMAN

UniProt

Q9NRL2 - BAZ1A_HUMAN

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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

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. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9NRL2.
CleanExiHS_BAZ1A.
ExpressionAtlasiQ9NRL2. baseline and differential.
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.
GeneTreeiENSGT00760000119099.
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

        10         20         30         40         50
MPLLHRKPFV RQKPPADLRP DEEVFYCKVT NEIFRHYDDF FERTILCNSL
60 70 80 90 100
VWSCAVTGRP GLTYQEALES EKKARQNLQS FPEPLIIPVL YLTSLTHRSR
110 120 130 140 150
LHEICDDIFA YVKDRYFVEE TVEVIRNNGA RLQCRILEVL PPSHQNGFAN
160 170 180 190 200
GHVNSVDGET IIISDSDDSE TQSCSFQNGK KKDAIDPLLF KYKVQPTKKE
210 220 230 240 250
LHESAIVKAT QISRRKHLFS RDKLKLFLKQ HCEPQDGVIK IKASSLSTYK
260 270 280 290 300
IAEQDFSYFF PDDPPTFIFS PANRRRGRPP KRIHISQEDN VANKQTLASY
310 320 330 340 350
RSKATKERDK LLKQEEMKSL AFEKAKLKRE KADALEAKKK EKEDKEKKRE
360 370 380 390 400
ELKKIVEEER LKKKEEKERL KVEREKEREK LREEKRKYVE YLKQWSKPRE
410 420 430 440 450
DMECDDLKEL PEPTPVKTRL PPEIFGDALM VLEFLNAFGE LFDLQDEFPD
460 470 480 490 500
GVTLEVLEEA LVGNDSEGPL CELLFFFLTA IFQAIAEEEE EVAKEQLTDA
510 520 530 540 550
DTKDLTEALD EDADPTKSAL SAVASLAAAW PQLHQGCSLK SLDLDSCTLS
560 570 580 590 600
EILRLHILAS GADVTSANAK YRYQKRGGFD ATDDACMELR LSNPSLVKKL
610 620 630 640 650
SSTSVYDLTP GEKMKILHAL CGKLLTLVST RDFIEDYVDI LRQAKQEFRE
660 670 680 690 700
LKAEQHRKER EEAAARIRKR KEEKLKEQEQ KMKEKQEKLK EDEQRNSTAD
710 720 730 740 750
ISIGEEERED FDTSIESKDT EQKELDQDMV TEDEDDPGSH KRGRRGKRGQ
760 770 780 790 800
NGFKEFTRQE QINCVTREPL TADEEEALKQ EHQRKEKELL EKIQSAIACT
810 820 830 840 850
NIFPLGRDRM YRRYWIFPSI PGLFIEEDYS GLTEDMLLPR PSSFQNNVQS
860 870 880 890 900
QDPQVSTKTG EPLMSESTSN IDQGPRDHSV QLPKPVHKPN RWCFYSSCEQ
910 920 930 940 950
LDQLIEALNS RGHRESALKE TLLQEKSRIC AQLARFSEEK FHFSDKPQPD
960 970 980 990 1000
SKPTYSRGRS SNAYDPSQMC AEKQLELRLR DFLLDIEDRI YQGTLGAIKV
1010 1020 1030 1040 1050
TDRHIWRSAL ESGRYELLSE ENKENGIIKT VNEDVEEMEI DEQTKVIVKD
1060 1070 1080 1090 1100
RLLGIKTETP STVSTNASTP QSVSSVVHYL AMALFQIEQG IERRFLKAPL
1110 1120 1130 1140 1150
DASDSGRSYK TVLDRWRESL LSSASLSQVF LHLSTLDRSV IWSKSILNAR
1160 1170 1180 1190 1200
CKICRKKGDA ENMVLCDGCD RGHHTYCVRP KLKTVPEGDW FCPECRPKQR
1210 1220 1230 1240 1250
SRRLSSRQRP SLESDEDVED SMGGEDDEVD GDEEEGQSEE EEYEVEQDED
1260 1270 1280 1290 1300
DSQEEEEVSL PKRGRPQVRL PVKTRGKLSS SFSSRGQQQE PGRYPSRSQQ
1310 1320 1330 1340 1350
STPKTTVSSK TGRSLRKINS APPTETKSLR IASRSTRHSH GPLQADVFVE
1360 1370 1380 1390 1400
LLSPRRKRRG RKSANNTPEN SPNFPNFRVI ATKSSEQSRS VNIASKLSLQ
1410 1420 1430 1440 1450
ESESKRRCRK RQSPEPSPVT LGRRSSGRQG GVHELSAFEQ LVVELVRHDD
1460 1470 1480 1490 1500
SWPFLKLVSK IQVPDYYDII KKPIALNIIR EKVNKCEYKL ASEFIDDIEL
1510 1520 1530 1540 1550
MFSNCFEYNP RNTSEAKAGT RLQAFFHIQA QKLGLHVTPS NVDQVSTPPA

AKKSRI
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
GeneTreei ENSGT00760000119099.
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

Bgeei Q9NRL2.
CleanExi HS_BAZ1A.
ExpressionAtlasi Q9NRL2. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 147 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