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Q9UIF9 (BAZ2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 2A
Alternative name(s):
Transcription termination factor I-interacting protein 5
Short name=TTF-I-interacting protein 5
Short name=Tip5
hWALp3
Gene names
Name:BAZ2A
Synonyms:KIAA0314, TIP5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1905 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential component of the NoRC (nucleolar remodeling complex) complex, a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing. In the complex, it plays a central role by being recruited to rDNA and by targeting chromatin modifying enzymes such as HDAC1, leading to repress RNA polymerase I transcription. Recruited to rDNA via its interaction with TTF1 and its ability to recognize and bind histone H4 acetylated on 'Lys-16' (H4K16ac), leading to deacetylation of H4K5ac, H4K8ac, H4K12ac but not H4K16ac. Specifically binds pRNAs, 150-250 nucleotide RNAs that are complementary in sequence to the rDNA promoter; pRNA-binding is required for heterochromatin formation and rDNA silencing By similarity.

Subunit structure

Component of the NoRC complex, at least composed of SMARCA5/SNF2H and BAZ2A/TIP5. Interacts with TTF1; required for recruitment of the NoRC complex to rDNA. Interacts with DNMT1, DNM3B, HDAC1 and SIN3A By similarity.

Subcellular location

Nucleusnucleolus By similarity. Note: Colocalizes with the basal RNA polymerase I transcription factor UBF in the nucleolus By similarity.

Tissue specificity

Expressed at moderate levels in most tissues analyzed, including heart, brain, placenta, lung, skeletal muscle, kidney and pancreas.

Domain

The bromo domain and the PHD-type zinc finger recognize and bind histone H4 acetylated on 'Lys-16' (H4K16ac). These 2 domains play a central role in the recritment of chromatin silencing proteins such as DNMT1, DNMT3B and HDAC1.

The MBD (methyl-CpG-binding) domain, also named TAM domain, specifically recognizes and binds a conserved stem-loop structure the association within pRNA. Binding to pRNA induces a conformational change of BAZ2A/TIP5 and is essential for targeting the NoRC complex to the nucleolus By similarity.

Post-translational modification

Acetylation at Lys-680 by KAT8/MOF promotes its dissociation from pRNA, affecting heterochromatin formation, nucleosome positioning and rDNA silencing. Deacetylation by SIRT1 in late S phase enhances pRNA-binding, allowing de novo DNA methylation and heterochromatin formation. Acetylation is high during S phase and declines to background levels in late S phase when the silent copies of rRNA genes are replicated By similarity. Ref.13

Sequence similarities

Belongs to the WAL family.

Contains 4 A.T hook DNA-binding domains.

Contains 1 bromo domain.

Contains 1 DDT domain.

Contains 1 MBD (methyl-CpG-binding) domain.

Contains 1 PHD-type zinc finger.

Sequence caution

The sequence AAB60864.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAG51228.1 differs from that shown. Reason: Erroneous termination at position 168. Translated as Tyr.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainBromodomain
Coiled coil
Repeat
Zinc-finger
   LigandDNA-binding
Metal-binding
RNA-binding
Zinc
   Molecular functionChromatin regulator
Repressor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA methylation

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin remodeling

Non-traceable author statement PubMed 11532953. Source: UniProtKB

chromatin silencing at rDNA

Inferred from sequence or structural similarity. Source: UniProtKB

heterochromatin assembly involved in chromatin silencing

Inferred from electronic annotation. Source: Ensembl

histone H3-K9 methylation

Inferred from electronic annotation. Source: Ensembl

histone H4 deacetylation

Inferred from electronic annotation. Source: Ensembl

histone H4-K20 methylation

Inferred from electronic annotation. Source: Ensembl

histone deacetylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Non-traceable author statement Ref.1. Source: UniProtKB

transcription, DNA-templated

Non-traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentchromatin silencing complex

Inferred from sequence or structural similarity. Source: UniProtKB

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

rDNA heterochromatin

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone acetyl-lysine binding

Inferred from sequence or structural similarity. Source: UniProtKB

ligand-dependent nuclear receptor binding

Non-traceable author statement Ref.1. Source: BHF-UCL

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCK1P163332EBI-934890,EBI-389883

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: Q9UIF9-1)

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 1 (identifier: Q9UIF9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     6-6: N → NEAN
     178-207: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9UIF9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1434-1437: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19051905Bromodomain adjacent to zinc finger domain protein 2A
PRO_0000211172

Regions

Domain546 – 61772MBD
Domain848 – 91366DDT
Domain1810 – 188071Bromo
DNA binding649 – 66113A.T hook 1
DNA binding670 – 68213A.T hook 2
DNA binding1186 – 119813A.T hook 3
DNA binding1404 – 141613A.T hook 4
Zinc finger1676 – 172651PHD-type
Coiled coil693 – 792100 Potential
Compositional bias660 – 799140Lys-rich
Compositional bias1212 – 127766Glu-rich
Compositional bias1290 – 1411122Pro-rich
Compositional bias1759 – 17624Poly-Arg

Amino acid modifications

Modified residue1341Phosphoserine Ref.16
Modified residue5091Phosphoserine Ref.15 Ref.16
Modified residue6801N6-acetyllysine; by KAT8 Ref.13
Modified residue7991N6-acetyllysine By similarity
Modified residue13971Phosphoserine Ref.14 Ref.15 Ref.16
Modified residue15591Phosphoserine Ref.10
Modified residue17471Phosphoserine Ref.11
Modified residue17701Phosphoserine Ref.11 Ref.15
Modified residue17831Phosphoserine Ref.11 Ref.14 Ref.15 Ref.16
Modified residue17851Phosphoserine Ref.16

Natural variations

Alternative sequence61N → NEAN in isoform 1.
VSP_037960
Alternative sequence178 – 20730Missing in isoform 1.
VSP_019111
Alternative sequence1434 – 14374Missing in isoform 3.
VSP_037961
Natural variant4981V → E.
Corresponds to variant rs2230579 [ dbSNP | Ensembl ].
VAR_055548

Experimental info

Sequence conflict1061N → S in CAH18232. Ref.2
Sequence conflict1481E → K in BAA89211. Ref.1
Sequence conflict1551Q → H in BAA89211. Ref.1
Sequence conflict2071Q → P in CAH18232. Ref.2
Sequence conflict2101G → C in BAA89211. Ref.1
Sequence conflict2361G → C in BAA89211. Ref.1
Sequence conflict5031A → T in CAH18232. Ref.2
Sequence conflict6011V → L in BAA89211. Ref.1
Sequence conflict7271Q → L in BAA89211. Ref.1
Sequence conflict7471Q → H in BAA89211. Ref.1
Sequence conflict8121R → K in BAA89211. Ref.1
Sequence conflict9781L → P in BAA89211. Ref.1
Sequence conflict1032 – 10332EG → GR in BAA89211. Ref.1
Sequence conflict11901G → S in BAA89211. Ref.1
Sequence conflict11931R → L in BAA89211. Ref.1
Sequence conflict11991S → F in BAA89211. Ref.1
Sequence conflict12051L → F in BAA89211. Ref.1
Sequence conflict12291A → V in BAA89211. Ref.1
Sequence conflict12741S → N in CAH18232. Ref.2
Sequence conflict13191P → L in BAA89211. Ref.1
Sequence conflict13221L → F in BAA89211. Ref.1
Sequence conflict13401P → L in BAA89211. Ref.1
Sequence conflict14431R → P in BAA89211. Ref.1
Sequence conflict15681R → P in BAA89211. Ref.1
Sequence conflict15981E → K in BAA89211. Ref.1
Sequence conflict16431V → I in BAA89211. Ref.1
Sequence conflict16491E → Q in BAA89211. Ref.1
Sequence conflict16561Q → H in BAA89211. Ref.1
Sequence conflict16631Q → H in BAA89211. Ref.1
Sequence conflict17661R → K in BAA89211. Ref.1
Sequence conflict17811G → R in BAA89211. Ref.1

Secondary structure

............... 1905
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified September 1, 2009. Version 4.
Checksum: F364E2AC4BF89EA2

FASTA1,905211,198
        10         20         30         40         50         60 
MEMEANDHFN FTGLPPAPAA SGLKPSPSSG EGLYTNGSPM NFPQQGKSLN GDVNVNGLST 

        70         80         90        100        110        120 
VSHTTTSGIL NSAPHSSSTS HLHHPSVAYD CLWNYSQYPS ANPGSNLKDP PLLSQFSGGQ 

       130        140        150        160        170        180 
YPLNGILGGS RQPSSPSHNT NLRAGSQEFW ANGTQSPMGL NFDSQELYDS FPDQNFEVMP 

       190        200        210        220        230        240 
NGPPSFFTSP QTSPMLGSSI QTFAPSQEVG SGIHPDEAAE KEMTSVVAEN GTGLVGSLEL 

       250        260        270        280        290        300 
EEEQPELKMC GYNGSVPSVE SLHQEVSVLV PDPTVSCLDD PSHLPDQLED TPILSEDSLE 

       310        320        330        340        350        360 
PFNSLAPEPV SGGLYGIDDT ELMGAEDKLP LEDSPVISAL DCPSLNNATA FSLLADDSQT 

       370        380        390        400        410        420 
STSIFASPTS PPVLGESVLQ DNSFDLNNGS DAEQEEMETQ SSDFPPSLTQ PAPDQSSTIQ 

       430        440        450        460        470        480 
LHPATSPAVS PTTSPAVSLV VSPAASPEIS PEVCPAASTV VSPAVFSVVS PASSAVLPAV 

       490        500        510        520        530        540 
SLEVPLTASV TSPKASPVTS PAAAFPTASP ANKDVSSFLE TTADVEEITG EGLTASGSGD 

       550        560        570        580        590        600 
VMRRRIATPE EVRLPLQHGW RREVRIKKGS HRWQGETWYY GPCGKRMKQF PEVIKYLSRN 

       610        620        630        640        650        660 
VVHSVRREHF SFSPRMPVGD FFEERDTPEG LQWVQLSAEE IPSRIQAITG KRGRPRNTEK 

       670        680        690        700        710        720 
AKTKEVPKVK RGRGRPPKVK ITELLNKTDN RPLKKLEAQE TLNEEDKAKI AKSKKKMRQK 

       730        740        750        760        770        780 
VQRGECQTTI QGQARNKRKQ ETKSLKQKEA KKKSKAEKEK GKTKQEKLKE KVKREKKEKV 

       790        800        810        820        830        840 
KMKEKEEVTK AKPACKADKT LATQRRLEER QRQQMILEEM KKPTEDMCLT DHQPLPDFSR 

       850        860        870        880        890        900 
VPGLTLPSGA FSDCLTIVEF LHSFGKVLGF DPAKDVPSLG VLQEGLLCQG DSLGEVQDLL 

       910        920        930        940        950        960 
VRLLKAALHD PGFPSYCQSL KILGEKVSEI PLTRDNVSEI LRCFLMAYGV EPALCDRLRT 

       970        980        990       1000       1010       1020 
QPFQAQPPQQ KAAVLAFLVH ELNGSTLIIN EIDKTLESMS SYRKNKWIVE GRLRRLKTVL 

      1030       1040       1050       1060       1070       1080 
AKRTGRSEVE MEGPEECLGR RRSSRIMEET SGMEEEEEEE SIAAVPGRRG RRDGEVDATA 

      1090       1100       1110       1120       1130       1140 
SSIPELERQI EKLSKRQLFF RKKLLHSSQM LRAVSLGQDR YRRRYWVLPY LAGIFVEGTE 

      1150       1160       1170       1180       1190       1200 
GNLVPEEVIK KETDSLKVAA HASLNPALFS MKMELAGSNT TASSPARARG RPRKTKPGSM 

      1210       1220       1230       1240       1250       1260 
QPRHLKSPVR GQDSEQPQAQ LQPEAQLHAP AQPQPQLQLQ LQSHKGFLEQ EGSPLSLGQS 

      1270       1280       1290       1300       1310       1320 
QHDLSQSAFL SWLSQTQSHS SLLSSSVLTP DSSPGKLDPA PSQPPEEPEP DEAESSPDPQ 

      1330       1340       1350       1360       1370       1380 
ALWFNISAQM PCNAAPTPPP AVSEDQPTPS PQQLASSKPM NRPSAANPCS PVQFSSTPLA 

      1390       1400       1410       1420       1430       1440 
GLAPKRRAGD PGEMPQSPTG LGQPKRRGRP PSKFFKQMEQ RYLTQLTAQP VPPEMCSGWW 

      1450       1460       1470       1480       1490       1500 
WIRDPEMLDA MLKALHPRGI REKALHKHLN KHRDFLQEVC LRPSADPIFE PRQLPAFQEG 

      1510       1520       1530       1540       1550       1560 
IMSWSPKEKT YETDLAVLQW VEELEQRVIM SDLQIRGWTC PSPDSTREDL AYCEHLSDSQ 

      1570       1580       1590       1600       1610       1620 
EDITWRGRGR EGLAPQRKTT NPLDLAVMRL AALEQNVERR YLREPLWPTH EVVLEKALLS 

      1630       1640       1650       1660       1670       1680 
TPNGAPEGTT TEISYEITPR IRVWRQTLER CRSAAQVCLC LGQLERSIAW EKSVNKVTCL 

      1690       1700       1710       1720       1730       1740 
VCRKGDNDEF LLLCDGCDRG CHIYCHRPKM EAVPEGDWFC TVCLAQQVEG EFTQKPGFPK 

      1750       1760       1770       1780       1790       1800 
RGQKRKSGYS LNFSEGDGRR RRVLLRGRES PAAGPRYSEE GLSPSKRRRL SMRNHHSDLT 

      1810       1820       1830       1840       1850       1860 
FCEIILMEME SHDAAWPFLE PVNPRLVSGY RRIIKNPMDF STMRERLLRG GYTSSEEFAA 

      1870       1880       1890       1900 
DALLVFDNCQ TFNEDDSEVG KAGHIMRRFF ESRWEEFYQG KQANL 

« Hide

Isoform 1 [UniParc].

Checksum: 8F197C2BE4F4EB4A
Show »

FASTA1,878208,390
Isoform 3 [UniParc].

Checksum: 00A922530275504E
Show »

FASTA1,901210,747

References

« Hide 'large scale' references
[1]"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.
[2]"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] (ISOFORM 2).
Tissue: Fetal kidney.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-1905 (ISOFORM 2).
Tissue: Brain.
[5]Ohara O., Nagase T., Kikuno R., Nomura N.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-1905 (ISOFORMS 1/2).
Tissue: Placenta.
[7]Jansa P., Grummt I.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 359-753.
Tissue: Lung.
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1065-1905.
Tissue: Lymph.
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1559, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[11]"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-1747; SER-1770 AND SER-1783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Reversible acetylation of the chromatin remodelling complex NoRC is required for non-coding RNA-dependent silencing."
Zhou Y., Schmitz K.M., Mayer C., Yuan X., Akhtar A., Grummt I.
Nat. Cell Biol. 11:1010-1016(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-680.
[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-1397 AND SER-1783, 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-509; SER-1397; SER-1770 AND SER-1783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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 SER-134; SER-509; SER-1397; SER-1783 AND SER-1785, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB032254 mRNA. Translation: BAA89211.1.
CR749379 mRNA. Translation: CAH18232.1.
AC090681 Genomic DNA. No translation available.
AB002312 mRNA. Translation: BAA20773.2.
AK023830 mRNA. Translation: BAG51228.1. Sequence problems.
AF000422 mRNA. Translation: AAB60864.1. Sequence problems.
BC008965 mRNA. Translation: AAH08965.2.
RefSeqNP_038477.2. NM_013449.3.
UniGeneHs.314263.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4LZ2X-ray1.76A1796-1899[»]
ProteinModelPortalQ9UIF9.
SMRQ9UIF9. Positions 554-614, 1673-1898.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116346. 10 interactions.
IntActQ9UIF9. 7 interactions.
MINTMINT-7240976.
STRING9606.ENSP00000368754.

PTM databases

PhosphoSiteQ9UIF9.

Polymorphism databases

DMDM257051081.

Proteomic databases

PaxDbQ9UIF9.
PRIDEQ9UIF9.

Protocols and materials databases

DNASU11176.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000549787; ENSP00000448760; ENSG00000076108.
ENST00000551812; ENSP00000446880; ENSG00000076108. [Q9UIF9-1]
GeneID11176.
KEGGhsa:11176.
UCSCuc001slp.1. human. [Q9UIF9-1]

Organism-specific databases

CTD11176.
GeneCardsGC12M056954.
H-InvDBHIX0010736.
HGNCHGNC:962. BAZ2A.
HPAHPA005782.
MIM605682. gene.
neXtProtNX_Q9UIF9.
PharmGKBPA25272.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5076.
HOGENOMHOG000169644.
HOVERGENHBG107494.
KOK15224.
OMAAFSDCLT.
PhylomeDBQ9UIF9.
TreeFamTF329083.

Gene expression databases

ArrayExpressQ9UIF9.
BgeeQ9UIF9.
CleanExHS_BAZ2A.
GenevestigatorQ9UIF9.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
3.30.890.10. 1 hit.
InterProIPR017956. AT_hook_DNA-bd_motif.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR004022. DDT_dom.
IPR018500. DDT_dom_subgr.
IPR018501. DDT_dom_superfamily.
IPR016177. DNA-bd_dom.
IPR001739. Methyl_CpG_DNA-bd.
IPR028940. TIP5.
IPR028942. WHIM1_dom.
IPR028935. WHIM3_domain.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERPTHR22880:SF2. PTHR22880:SF2. 1 hit.
PfamPF00439. Bromodomain. 1 hit.
PF02791. DDT. 1 hit.
PF01429. MBD. 1 hit.
PF00628. PHD. 1 hit.
PF15612. WHIM1. 1 hit.
PF15614. WHIM3. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00384. AT_hook. 4 hits.
SM00297. BROMO. 1 hit.
SM00571. DDT. 1 hit.
SM00391. MBD. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF54171. SSF54171. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS50827. DDT. 1 hit.
PS50982. MBD. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBAZ2A. human.
GeneWikiBAZ2A.
GenomeRNAi11176.
NextBio42525.
PROQ9UIF9.
SOURCESearch...

Entry information

Entry nameBAZ2A_HUMAN
AccessionPrimary (citable) accession number: Q9UIF9
Secondary accession number(s): B3KN66 expand/collapse secondary AC list , O00536, O15030, Q68DI8, Q96H26
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: September 1, 2009
Last modified: April 16, 2014
This is version 136 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 12

Human chromosome 12: entries, gene names and cross-references to MIM