PHD zinc finger-containing protein [General function prediction only];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  182 YDLDQCDEAWLKVFNgERNLSGlvPVTDEQFERVVEELEvRCWDKIQAIM--KSEEGLGIEYDENVICDVCRSPDSEEAN 259
Cdd:COG5141    133 YDLDEYDTMWLRYLN-ESAIDE--NVSEEAFEIIVTRLE-KEWFFFEHGLpdKHVEPIEPSDEFDDICTKCTSTHNENSN 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  260 EMVFCDNCNICVHQACYGITNIPSGQWMCRTCSMG--QKPDCVLCPNKGGAMKSTRSGqKWAHVSCALWIPEVSIGSVDR 337
Cdd:COG5141    209 AIVFCDGCEICVHQSCYGIQFLPEGFWLCRKCIYGeyQIRCCSFCPSSDGAFKQTSDG-RWGHVICAMFNPELSFGHLLS 287

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  338 MEPITKISSIPASRWALICVLCRERVGACIQCSVKTCKTAYHVTCAFQHGLEMRAIIEDENAEDGVKLRSYCQKHgtnkS 417
Cdd:COG5141    288 KDPIDNIASVSSSRWKLGCLICKEFGGTCIQCSYFNCTRAYHVTCARRAGYFDLNIYSHNGISYCIDHEPLCRKH----Y 363

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  418 KRDNKNSNNNAGSGTEEEGATTTSAAGTGAGTGGGEMKRKKRKdmTSEERNQARALRMAEIEAEFDKHVSVKDISCHLLD 497
Cdd:COG5141    364 PLGYGRMNGLRYFGYEKLRYKNPPTAIPRKVRAARPRATLFMK--LCWKQPPATPSVLSRVEACDLKEKDRQDLPVNIFD 441

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  498 VDQdaipyiynYWVLKRKSFHNRPLLppKSDDVDLAAQNQEQADDLEKMKMFVHLRQDLERVRNLCYMVSRREKLSRSFF 577
Cdd:COG5141    442 ICK--------YWEMKRKSEIGGPLV--ILPDIVYSLKTLEDWMSKRRMREVAKALQDQYQLLTLVESTAKRQLLKCQLS 511

                   ....*..
gi 1988305676  578 RMREQTF 584
Cdd:COG5141    512 NLRKKFL 518

PHD zinc finger-containing protein [General function prediction only];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  182 YDLDQCDEAWLKVFNgERNLSGlvPVTDEQFERVVEELEvRCWDKIQAIM--KSEEGLGIEYDENVICDVCRSPDSEEAN 259
Cdd:COG5141    133 YDLDEYDTMWLRYLN-ESAIDE--NVSEEAFEIIVTRLE-KEWFFFEHGLpdKHVEPIEPSDEFDDICTKCTSTHNENSN 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  260 EMVFCDNCNICVHQACYGITNIPSGQWMCRTCSMG--QKPDCVLCPNKGGAMKSTRSGqKWAHVSCALWIPEVSIGSVDR 337
Cdd:COG5141    209 AIVFCDGCEICVHQSCYGIQFLPEGFWLCRKCIYGeyQIRCCSFCPSSDGAFKQTSDG-RWGHVICAMFNPELSFGHLLS 287

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  338 MEPITKISSIPASRWALICVLCRERVGACIQCSVKTCKTAYHVTCAFQHGLEMRAIIEDENAEDGVKLRSYCQKHgtnkS 417
Cdd:COG5141    288 KDPIDNIASVSSSRWKLGCLICKEFGGTCIQCSYFNCTRAYHVTCARRAGYFDLNIYSHNGISYCIDHEPLCRKH----Y 363

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  418 KRDNKNSNNNAGSGTEEEGATTTSAAGTGAGTGGGEMKRKKRKdmTSEERNQARALRMAEIEAEFDKHVSVKDISCHLLD 497
Cdd:COG5141    364 PLGYGRMNGLRYFGYEKLRYKNPPTAIPRKVRAARPRATLFMK--LCWKQPPATPSVLSRVEACDLKEKDRQDLPVNIFD 441

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  498 VDQdaipyiynYWVLKRKSFHNRPLLppKSDDVDLAAQNQEQADDLEKMKMFVHLRQDLERVRNLCYMVSRREKLSRSFF 577
Cdd:COG5141    442 ICK--------YWEMKRKSEIGGPLV--ILPDIVYSLKTLEDWMSKRRMREVAKALQDQYQLLTLVESTAKRQLLKCQLS 511

                   ....*..
gi 1988305676  578 RMREQTF 584
Cdd:COG5141    512 NLRKKFL 518

PHD finger found in proteins Jade-1, Jade-2, Jade-3, and similar proteins; This family includes proteins Jade-1 (PHF17), Jade-2 (PHF15), and Jade-3 (PHF16), each of which is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and EAF6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. This family also contains Drosophila melanogaster PHD finger protein rhinoceros (RNO). It is a novel plant homeodomain (PHD)-containing nuclear protein that may function as a transcription factor that antagonizes Ras signaling by regulating transcription of key EGFR/Ras pathway regulators in the Drosophila eye. All Jade proteins contain a canonical Cys4HisCys3 PHD finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1988305676  246 ICDVCRSPDSEEANEMVFCDNCNICVHQACYGITNIPSGQWMCRTC 291
Cdd:cd15573      1 VCDVCRSPDSEEGNEMVFCDKCNICVHQACYGIQKIPEGSWLCRTC 46

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1988305676   246 ICDVCRSPDSEEanEMVFCDNCNICVHQACYGIT---NIPSGQWMCRTC 291
Cdd:smart00249    1 YCSVCGKPDDGG--ELLQCDGCDRWYHQTCLGPPlleEEPDGKWYCPKC 47

Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-1 (PHF17), Jade-2 (PHF15), and Jade-3 (PHF16); each of these proteins is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and EAF6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, has reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. This family also contains Drosophila melanogaster PHD finger protein rhinoceros (RNO). It is a novel plant homeodomain (PHD)-containing nuclear protein that may function as a transcription factor that antagonizes Ras signaling by regulating transcription of key EGFR/Ras pathway regulators in the Drosophila eye. All Jade proteins contain a canonical PHD finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  299 CVLCPNKGGAMKSTRSGQKWAHVSCALWIPEVSIGSVDRMEPITKISSIPASRWALICVLCRERVGACIQCSVKTCKTAY 378
Cdd:cd15671      1 CVLCPKKGGAMKSTKSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPMSRWALVCVLCKEKTGACIQCSVKSCKTAF 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1988305676  379 HVTCAFQHGLEMRAIIEDENaeDGVKLRSYCQKH 412
Cdd:cd15671     81 HVTCAFQHGLEMKTILEDED--DEVKFKSYCPKH 112

Extended PHD finger found in protein Jade-3 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-3. Jade-3, also termed PHD finger protein 16 (PHF16), is a plant homeodomain (PHD) zinc finger protein that is close related to Jade-1, which functions as an essential regulator of multiple cell signaling pathways. Like Jade-1, Jade-3 is required for ING4 and ING5 to associate with histone acetyl transferase (HAT) HBO1 and Eaf6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. Jade-3 contains a canonical PHD domain followed by this non-canonical ePHD domain, both of which are zinc-binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  299 CVLCPNKGGAMKSTRSGQKWAHVSCALWIPEVSIGSVDRMEPITKISSIPASRWALICVLCRERVGACIQCSVKTCKTAY 378
Cdd:cd15706      1 CLLCPKTGGAMKATRTGTKWAHVSCALWIPEVSIACPERMEPITKVSHIPPSRWALVCSLCKLKTGACIQCSVKSCITAF 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1988305676  379 HVTCAFQHGLEMRAIIEDenaEDGVKLRSYCQKH 412
Cdd:cd15706     81 HVTCAFEHSLEMKTILDE---GDEVKFKSYCLKH 111

Extended PHD finger found in protein Jade-1 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-1. Jade-1, also termed PHD finger protein 17 (PHF17), is a novel binding partner of von Hippel-Lindau (VHL) tumor suppressor Pvhl, a key regulator of cellular oxygen sensing pathway. It is highly expressed in renal proximal tubules. Jade-1 functions as an essential regulator of multiple cell signaling pathways. It may be involved in the Serine/threonine kinase AKT/AKT1 pathway during renal cancer pathogenesis and normally prevents renal epithelial cell proliferation and transformation. It also acts as a pro-apoptotic and growth suppressive ubiquitin ligase to inhibit canonical Wnt downstream effector beta-catenin for proteasomal degradation and ASA transcription factor associated with histone acetyltransferase activity and with increased abundance of cyclin-dependent kinase inhibitor p21. Moreover, Jade-1 is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and Eaf6 to form a HBO1 complex, and plays a role in epithelial cell regeneration. It has also been identified as a novel component of the nephrocystin protein (NPHP) complex and interacts with the ciliary protein nephrocystin-4 (NPHP4). Jade-1 contains a canonical plant homeodomain (PHD) finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  296 KPDCVLCPNKGGAMKSTRSGQKWAHVSCALWIPEVSIGSVDRMEPITKISSIPASRWALICVLCRERVGACIQCSVKTCK 375
Cdd:cd15704      1 QPKCLLCPKKGGAMKPTRSGTKWVHVSCALWIPEVSIGSPEKMEPITKVSHIPSSRWALVCSLCNEKVGASIQCSVKNCR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1988305676  376 TAYHVTCAFQHGLEMRAIIEDenaEDGVKLRSYCQKHGTNK 416
Cdd:cd15704     81 TAFHVTCAFDRGLEMKTILAE---NDEVKFKSYCPKHSSTK 118

PHD-zinc-finger like domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  297 PDCVLCPNKGGAMKSTrSGQKWAHVSCALWIPEVSIGSVDRMEPITkISSIPASRWALICVLCRERVGACIQCSVKTCKT 376
Cdd:pfam13832    1 VRCCLCPLRGGALKQT-SDGRWVHVLCAIFVPEVRFGNVATMEPID-VSRIPPERWKLKCVFCKKRSGACIQCSKGRCTT 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1988305676  377 AYHVTCAFQHGLEMRaiIEDenaEDGVKLRSYCQKH 412
Cdd:pfam13832   79 AFHVTCAQAAGVYME--PED---WPNVVVIAYCQKH 109

Extended PHD finger found in Arabidopsis thaliana ATX1, -2, and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of A. thaliana histone-lysine N-methyltransferase arabidopsis trithorax-like proteins ATX1, -2, and similar proteins. ATX1 and -2 are sister paralogs originating from a segmental chromosomal duplication; they are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1 (also known as protein SET domain group 27, or trithorax-homolog protein 1/TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1 regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2 (also known as protein SET domain group 30, or trithorax-homolog protein 2/TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). ATX1 and ATX2 are multi-domain proteins that consist of an N-terminal PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical PHD finger, this non-canonical ePHD finger, and a C-terminal SET domain.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  299 CVLCPNKGGAMKSTRSGqKWAHVSCALWIPEVSIGSVDRMEPITKISSIPASRWALICVLCRERVGACIQCSVKTCKTAY 378
Cdd:cd15662      1 CCLCPVVGGALKPTTDG-RWAHLACAIWIPETCLLDVKTMEPVDGINAISKERWELSCTICKQRYGACIQCSNNSCRVAY 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1988305676  379 HVTCAFQHGLEMRAIIE--DENAEDGVKLRSYCQKH 412
Cdd:cd15662     80 HPLCARAAGLCMEVADEggEDPGDQGLRLLSYCPRH 115

Extended PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of BRPF1. BRPF1, also termed peregrin, or protein Br140, is a multi-domain protein that binds histones, mediates monocytic leukemic zinc-finger protein (MOZ) -dependent histone acetylation, and is required for Hox gene expression and segmental identity. It is a close partner of the MOZ histone acetyltransferase (HAT) complex and a novel Trithorax group (TrxG) member with a central role during development. BRPF1 is primarily a nuclear protein that has a broad tissue distribution and is abundant in testes and spermatogonia. It contains a plant homeodomain (PHD) zinc finger followed by a non-canonical ePHD finger, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. This PHD finger binds to methylated lysine 4 of histone H3 (H3K4me), the bromodomain interacts with acetylated lysines on N-terminal tails of histones and other proteins, and the PWWP domain shows histone-binding and chromatin association properties. BRPF1 may be involved in chromatin remodeling.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  299 CVLCPNKGGAMKSTRSGqKWAHVSCALWIPEVSIGSVDRMEPITKISSIPASRWALICVLCRER-VGACIQCSVKTCKTA 377
Cdd:cd15701      1 CALCPNKGGAFKQTDDG-RWAHVVCALWIPEVCFANTVFLEPIDSIEHIPPARWKLTCYICKQRgSGACIQCHKANCYTA 79

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1988305676  378 YHVTCAFQHGLEMRAIIEDENAEDG----VKLRSYCQKH 412
Cdd:cd15701     80 FHVTCAQQAGLYMKMEPVRETGANGtsfsVRKTAYCDIH 118

Extended PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of BRPF3. BRF3 is a homolog of BRPF1 and BRPF2. It is a scaffold protein that forms a novel monocytic leukemic zinc finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complex with other regulatory subunits. BRPF3 contains a plant homeodomain (PHD) finger followed by this non-canonical ePHD finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  299 CVLCPNKGGAMKSTRSGqKWAHVSCALWIPEVSIGSVDRMEPITKISSIPASRWALICVLCRER-VGACIQCSVKTCKTA 377
Cdd:cd15703      1 CVLCPNKGGAFKQTSDG-RWAHVVCAIWIPEVCFANTVFLEPVEGVNNIPPARWKLTCYLCKQKgRGAAIQCHKVNCYTA 79

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1988305676  378 YHVTCAFQHGLEMRAIIEDENAEDG----VKLRSYCQKH 412
Cdd:cd15703     80 FHVTCAQRAGLFMKIEPVRETGLNGttftVRKTAYCENH 118

Extended PHD finger found in protein AF-10 and AF-17; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of AF-10 and AF-17. AF-10, also termed ALL1 (acute lymphoblastic leukaemia)-fused gene from chromosome 10 protein, is a transcription factor encoded by gene AF10, a translocation partner of the MLL (mixed-lineage leukaemia) oncogene in leukaemia. AF-10 has been implicated in the development of leukemia following chromosomal rearrangements between the AF10 gene and one of at least two other genes, MLL and CALM. It plays a key role in the survival of uncommitted hematopoietic cells. Moreover, AF-10 functions as a follistatin-related gene (FLRG)-interacting protein. The interaction with FLRG enhances AF10-dependent transcription. It interacts with the human counterpart of yeast Dot1, hDOT1L, and may act as a bridge for the recruitment of hDOT1L to the genes targeted by MLL-AF10. It also interacts with the synovial sarcoma associated protein SYT protein and may play a role in synovial sarcomas and acute leukemias. AF-17, also termed ALL1-fused gene from chromosome 17 protein, is encoded by gene AF17 that has been identified in hematological malignancies as translocation partners of the mixed lineage leukemia gene MLL. It is a putative transcription factor that may play a role in multiple signaling pathways. It is involved in chromatin-mediated gene regulation mechanisms. It functions as a component of the multi-subunit Dot1 complex (Dotcom) and plays a role in the Wnt/Wingless signaling pathway. It also seems to be a downstream target of the beta-catenin/T-cell factor pathway, and participates in G2-M progression. Moreover, it may function as an important regulator of ENaC-mediated Na+ transport and thus blood pressure. Both AF-10 and AF-17 contain an N-terminal plant homeodomain (PHD) finger followed by this non-canonical ePHD finger. The PHD finger is involved in their homo-oligomerization. In the C-terminal region, they possess a leucine zipper domain and a glutamine-rich region. This family also includes ZFP-1, the Caenorhabditis elegans AF10 homolog. It was originally identified as a factor promoting RNAi interference in C. elegans. It also acts as Dot1-interacting protein that opposes H2B ubiquitination to reduce polymerase II (Pol II) transcription.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  299 CVLCPNKGGAMKSTRSGqKWAHVSCALWIPEVSIGSVDRMEPITkISSIPASRWALICVLCRER-------VGACIQCSV 371
Cdd:cd15672      1 CELCPHKDGALKRTDNG-GWAHVVCALYIPEVRFGNVATMEPII-LQDVPQDRFNKTCYICEEQgreskasTGACMQCNK 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1988305676  372 KTCKTAYHVTCAFQHGLemraIIEDE-NAEDGVKLRSYCQKH 412
Cdd:cd15672     79 SGCKQSFHVTCAQMAGL----LCEEAgNYSDNVKYCGYCSYH 116

Extended PHD finger found in Arabidopsis thaliana ATX3, -4, -5, and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of A. thaliana histone-lysine N-methyltransferase arabidopsis trithorax-like proteins ATX3 (also termed protein SET domain group 14, or trithorax-homolog protein 3), ATX4 (also termed protein SET domain group 16, or trithorax-homolog protein 4) and ATX5 (also termed protein SET domain group 29, or trithorax-homolog protein 5), which belong to the histone-lysine methyltransferase family. These proteins show distinct phylogenetic origins from the family of ATX1 and ATX2. They are multi-domain proteins that consist of an N-terminal PWWP domain, a canonical PHD finger, this non-canonical extended PHD finger, and a C-terminal SET domain.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  299 CVLCPNKGGAMKSTRSGQKWAHVSCALWIPEVSIGSVDRMEPITKISSIPASRWALICVLCRERVGACIQCSvkTCKTAY 378
Cdd:cd15663      1 CCLCPVKGGALKPTDVEGLWVHVTCAWFRPEVCFKNEEKMEPAVGLLRIPLSTFLKACVICKQIHGSCTQCC--KCATYF 78

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1988305676  379 HVTCAFQHGLEMRAIIEDENAEDGVKLRSYCQKH 412
Cdd:cd15663     79 HAMCASRAGYHMELHCLEKNGVQITRMVSYCSFH 112

PHD finger found in protein Jade-3 and similar proteins; Jade-3, also termed PHD finger protein 16 (PHF16), is a plant homeodomain (PHD) zinc finger protein that is closely related to Jade-1, which functions as an essential regulator of multiple cell signaling pathways. Like Jade-1, Jade-3 is required for ING4 and ING5 to associate with histone acetyl transferase (HAT) HBO1 and Eaf6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. Jade-3 contains a canonical Cys4HisCys3 PHD domain followed by a non-canonical extended PHD (ePHD) domain, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1988305676  246 ICDVCRSPDSEEANEMVFCDNCNICVHQACYGITNIPSGQWMCRTCSMG 294
Cdd:cd15681      1 ICDVCRSPDSEEGNDMVFCDKCNICVHQACYGILKVPEGSWLCRTCVLG 49

PHD finger found in protein Jade-2 and similar proteins; Jade-2, also termed PHD finger protein 15 (PHF15), is a plant homeodomain (PHD) zinc finger protein that is closely related to Jade-1, which functions as an essential regulator of multiple cell signaling pathways. Like Jade-1, Jade-2 is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and Eaf6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. Jade-2 contains a canonical Cys4HisCys3 PHD finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1988305676  246 ICDVCRSPDSEEANEMVFCDNCNICVHQACYGITNIPSGQWMCRTC 291
Cdd:cd15680      1 VCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVPTGSWLCRTC 46

Extended PHD finger found in protein AF-10 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of AF-10. AF-10, also termed ALL1 (acute lymphoblastic leukaemia)-fused gene from chromosome 10 protein, is a transcription factor encoded by gene AF10, a translocation partner of the MLL (mixed-lineage leukaemia) oncogene in leukaemia. AF-10 has been implicated in the development of leukemia following chromosomal rearrangements between the AF10 gene and one of at least two other genes, MLL and CALM. It plays a key role in the survival of uncommitted hematopoietic cells. Moreover, AF-10 functions as a follistatin-related gene (FLRG)-interacting protein. The interaction with FLRG enhances AF10-dependent transcription. It interacts with human counterpart of the yeast Dot1, hDOT1L, and may act as a bridge for the recruitment of hDOT1L to the genes targeted by MLL-AF10. It also interacts with the synovial sarcoma associated protein SYT protein and may play a role in synovial sarcomas and acute leukemias. AF-10 contains an N-terminal plant homeodomain (PHD) finger followed by this non-canonical ePHD finger.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  299 CVLCPNKGGAMKSTRSGqKWAHVSCALWIPEVSIGSVDRMEPITkISSIPASRWALICVLCRER-------VGACIQCSV 371
Cdd:cd15708      5 CELCPHKDGALKRTDNG-GWAHVVCALYIPEVQFANVSTMEPIV-LQSVPHERYNKTCYICDEQgreskaaTGACMTCNK 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1988305676  372 KTCKTAYHVTCAFQHGLEMRaiiEDENAEDGVKLRSYCQKH 412
Cdd:cd15708     83 HGCRQAFHVTCAQLAGLLCE---EEGNGADNVQYCGYCKYH 120

PHD finger found in protein Jade-1 and similar proteins; Jade-1, also termed PHD finger protein 17 (PHF17), is a novel binding partner of von Hippel-Lindau (VHL) tumor suppressor Pvhl, a key regulator of the cellular oxygen sensing pathway. It is highly expressed in renal proximal tubules. Jade-1 functions as an essential regulator of multiple cell signaling pathways. It may be involved in the serine/threonine kinase AKT/AKT1 pathway during renal cancer pathogenesis and normally prevents renal epithelial cell proliferation and transformation. It also acts as a pro-apoptotic and growth suppressive ubiquitin ligase to inhibit canonical Wnt downstream effector beta-catenin for proteasomal degradation, and as a transcription factor associated with histone acetyltransferase activity and with increased abundance of cyclin-dependent kinase inhibitor p21. Moreover, Jade-1 is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and Eaf6 to form a HBO1 complex, and plays a role in epithelial cell regeneration. It has also been identified as a novel component of the nephrocystin protein (NPHP) complex and interacts with the ciliary protein nephrocystin-4 (NPHP4). Jade-1 contains a canonical Cys4HisCys3 plant homeodomain (PHD) finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1988305676  246 ICDVCRSPDSEEANEMVFCDNCNICVHQACYGITNIPSGQWMCRTC 291
Cdd:cd15679      1 VCDVCQSPDGEDGNEMVFCDKCNICVHQACYGILKVPEGSWLCRTC 46

Extended PHD finger (ePHD) found in Jumonji domain-containing protein 2A (JMJD2A); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of JMJD2A. JMJD2A, also termed lysine-specific demethylase 4A (KDM4A), or JmjC domain-containing histone demethylation protein 3A (JHDM3A), catalyzes the demethylation of di- and trimethylated H3K9 and H3K36. It is involved in carcinogenesis and functions as a transcription regulator that may either stimulate or repress gene transcription. It associates with nuclear receptor co-repressor complex or histone deacetylases. Moreover, JMJD2A forms complexes with both the androgen and estrogen receptor (ER) and plays an essential role in growth of both ER-positive and -negative breast tumors. It is also involved in prostate, colon, and lung cancer progression. JMJD2A contains jmjN and jmjC domains in the N-terminal region, followed by a canonical PHD finger, this non-canonical ePHD finger, and a Tudor domain.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  299 CVLCPNKGGAMKSTrSGQKWAHVSCALWIPEVSIGSVDRMEPItKISSIPASRWALICVLCRERV----GACIQCSVKTC 374
Cdd:cd15713      1 CCLCSLRGGALQRA-NDDKWVHVMCAVAVLEARFVNIAERSPV-DVSKIPLQRFKLKCIFCKKRRkrtaGCCVQCSHGRC 78

                           90
                   ....*....|....*..
gi 1988305676  375 KTAYHVTCAFQHGLEMR 391
Cdd:cd15713     79 PTSFHASCAQAAGVMMQ 95

Extended PHD finger found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Snt2p. Sntp2 is a yeast protein that may function in multiple stress pathways. It coordinates the transcriptional response to hydrogen peroxide-mediated oxidative stress through interaction with Ecm5 and the Rpd3 deacetylase. Snt2p contains a bromo adjacent homology (BAH) domain, two canonical PHD fingers, a non-canonical ePHD finger, and a SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domain.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  299 CVLCPNKGG---------------AMKSTRSGqKWAHVSCALWIPEVSIGSVDRMEPITKISSIPASRWALICVLCRERV 363
Cdd:cd15667      1 CSLCNAKESnyelakkqsprtrpdALKCTSNG-TWCHVLCALFNEDIKFGNSKSLQPILNTESVLLKGSRQKCEICKVSG 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988305676  364 GACIQCSVktCKTAYHVTCA-----FQHGLEMRAIIEDENAE---DGVKLRSY-------CQKH 412
Cdd:cd15667     80 GGLVKCEV--CDDRFHVSCAqdtpgFKLGFKKEYLSDDTENPfitDKVDNESYtlkpiivCPKH 141

PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and similar proteins; BRPF1, also termed peregrin or protein Br140, is a multi-domain protein that binds histones, mediates monocytic leukemic zinc-finger protein (MOZ)-dependent histone acetylation, and is required for Hox gene expression and segmental identity. It is a close partner of the MOZ histone acetyltransferase (HAT) complex and a novel Trithorax group (TrxG) member with a central role during development. BRPF1 is primarily a nuclear protein that has a broad tissue distribution and is abundant in testes and spermatogonia. It contains a canonical Cys4HisCys3 plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. PHD and ePHD fingers both bind to lysine 4 of histone H3 (K4H3), bromodomains interact with acetylated lysines on N-terminal tails of histones and other proteins, and PWWP domains show histone-binding and chromatin association properties. BRPF1 may be involved in chromatin remodeling. This model corresponds to the canonical Cys4HisCys3 PHD finger.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1988305676  242 DENVICDVCRSPDSEEANEMVFCDNCNICVHQACYGITNIPSGQWMCRTC 291
Cdd:cd15676      5 DEDAVCCICNDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRRC 54

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains. Several PHD fingers have been identified as binding modules of methylated histone H3.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1988305676  246 ICDVCRSPDseEANEMVFCDNCNICVHQACYGIT----NIPSGQWMCRTCS 292
Cdd:pfam00628    1 YCAVCGKSD--DGGELVQCDGCDDWFHLACLGPPldpaEIPSGEWLCPECK 49

PHD finger found in protein AF-10 and AF-17; This family includes protein AF-10 and AF-17. AF-10, also termed ALL1 (acute lymphoblastic leukemia)-fused gene from chromosome 10 protein, is a transcription factor encoded by gene AF10, a translocation partner of the MLL (mixed-lineage leukemia) oncogene in leukemia. AF-10 has been implicated in the development of leukemia following chromosomal rearrangements between the AF10 gene and one of at least two other genes, MLL and CALM. It plays a key role in the survival of uncommitted hematopoietic cells. Moreover, AF-10 functions as a follistatin-related gene (FLRG)-interacting protein. The interaction with FLRG enhances AF10-dependent transcription. It interacts with the human counterpart of the yeast Dot1, hDOT1L, and may act as a bridge for the recruitment of hDOT1L to the genes targeted by MLL-AF10. It also interacts with the synovial sarcoma associated SYT protein and may play a role in synovial sarcomas and acute leukemias. AF-17, also termed ALL1-fused gene from chromosome 17 protein, is encoded by gene AF17 that has been identified in hematological malignancies as translocation partners of the mixed lineage leukemia gene MLL. It is a putative transcription factor that may play a role in multiple signaling pathways. It is involved in chromatin-mediated gene regulation mechanisms. It functions as a component of the multi-subunit Dot1 complex (Dotcom) and plays a role in the Wnt/Wingless signaling pathway. It also seems to be a downstream target of the beta-catenin/T-cell factor pathway, and participates in G2-M progression. Moreover, it may function as an important regulator of ENaC-mediated Na+ transport and thus blood pressure. Both AF-10 and AF-17 contain an N-terminal canonical Cys4HisCys3 plant homeodomain (PHD) finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His. The PHD finger is involved in their homo-oligomerization. In the C-terminal region, they possess a leucine zipper domain and a glutamine-rich region. This family also includes ZFP-1, the Caenorhabditis elegans AF10 homolog. It was originally identified as a factor promoting RNAi interference in C. elegans. It also acts as a Dot1-interacting protein that opposes H2B ubiquitination to reduce polymerase II (Pol II) transcription. This model corresponds to the canonical Cys4HisCys3 PHD finger.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1988305676  247 CDVCRSPDSEEANEMVFCD--NCNICVHQACYGITNIPSGQWMCRTC 291
Cdd:cd15574      2 CCVCSDERGWAENPLVYCDghGCNVAVHQACYGIVQVPTGPWFCRKC 48

PHD finger 2 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed BRG1-associated factor 45a (BAF45a), or XAP135, is a ubiquitously expressed transcriptional regulator that is required for maintaining the undifferentiated status of neuroblasts. It contains a SAY (supporter of activation of yellow) domain and two adjacent plant homeodomain (PHD) fingers. This model corresponds to the second PHD finger.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1988305676  247 CDVCRSPDSEEanEMVFCDNCNICVHQACYGITNIPSGQWMCRTC 291
Cdd:cd15529      2 CTKCGDPHDED--KMMFCDQCDRGYHTFCVGLRSIPDGRWICPLC 44

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) finger typically characterized as Cys4HisCys3, and a non-canonical extended PHD finger, characterized as Cys2HisCys5HisCys2His. Variations include the RAG2 PHD finger characterized by Cys3His2Cys2His and the PHD finger 5 found in nuclear receptor-binding SET domain-containing proteins characterized by Cys4HisCys2His. The PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. Single or multiple copies of PHD fingers have been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors. The PHD finger domain SF is structurally similar to the RING and FYVE_like superfamilies.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1988305676  246 ICDVCRSPDSEEaNEMVFCDNCNICVHQACYGI---TNIPSGQWMCRTC 291
Cdd:cd15489      1 SCIVCGKGGDLG-GELLQCDGCGKWFHADCLGPplsSFVPNGKWICPVC 48

PHD finger 2 found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and similar proteins; This group corresponds to Snt2p and similar proteins. Snt2p is a yeast protein that may function in multiple stress pathways. It coordinates the transcriptional response to hydrogen peroxide-mediated oxidative stress through interaction with Ecm5 and the Rpd3 deacetylase. Snt2p contains a bromo adjacent homology (BAH) domain, two canonical Cys4HisCys3 plant homeodomain (PHD) fingers, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domain; this model corresponds to the second canonical Cys4HisCys3 PHD finger.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1988305676  247 CDVCRSPDSEEANEMVFCDNCNICVHQACYGIT---------NIPSGQWMCRTC 291
Cdd:cd15498      2 CSVCSEQFASNFNTSLSCYNCGLNVHASCYGITvpgkmnkvkNLKSYKWLCDPC 55

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second ePHD finger of KMT2C, and KMT2D. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, five PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobilitygroup)-binding motif, and two FY-rich regions.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  299 CVLCPNKGGAMKSTRSG------QKWAHVSCALWIPEV------SIGSVDRmepitkissipASRWAL--ICVLCReRVG 364
Cdd:cd15666      1 CVLCGGEGDGDTDGPGRllnldvDKWVHLNCALWSYEVyetqngALMNVEE-----------ALRRALttTCSHCG-RTG 68

                           90       100
                   ....*....|....*....|...
gi 1988305676  365 ACIQCSVKTCKTAYHVTCAFQHG 387
Cdd:cd15666     69 ATVPCFKPRCANVYHLPCAIKDG 91

PHD finger 1 found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) family proteins MTF2, PHF19, and similar proteins; The family includes two PCL family proteins, metal-response element-binding transcription factor 2 (MTF2/PCL2) and PHF19/PCL3, which are homologs of PHD finger protein1 (PHF1). PCL family proteins are accessory components of the polycomb repressive complex 2 (PRC2) core complex and all contain an N-terminal Tudor domain followed by two PHD fingers, and a C-terminal MTF2 domain. They specifically recognize tri-methylated H3K36 (H3K36me3) through their N-terminal Tudor domains. The interaction between their Tudor domains and H3K36me3 is critical for both the targeting and spreading of PRC2 into active chromatin regions and for the maintenance of optimal repression of poised developmental genes where PCL proteins, H3K36me3, and H3K27me3 coexist. Moreover, unlike other PHD finger-containing proteins, the first PHD fingers of PCL proteins do not display histone H3K4 binding affinity and they do not affect the Tudor domain binding to histones. This model corresponds to the first PHD finger.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1988305676  247 CDVCRSPDSEEANEMVFCDNCNICVHQACYG--ITNIP---SGQWMCRTC 291
Cdd:cd15499      2 CSICGGAEARDGNEILICDKCDKGYHQLCHSpkVRTSPlegDEKWFCSRC 51

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of KMT2A. KMT2A also termed ALL-1, or CXXC-type zinc finger protein 7, or myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), or trithorax-like protein (Htrx), or zinc finger protein HRX, is a histone methyltransferase that belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2). It regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex, which also contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL1 complex is highly active and specific for H3K4methylation. KMT2A contains a CxxC (x for any residue) zinc finger domain, three PHD fingers, a Bromodomain domain, this extended PHD finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988305676  299 CVLCPNKGGAmKSTRSGQ-------KWAHVSCALWIPEVsIGSVDRMEPITKISSIPASRwaLICVLCrERVGACIQCSV 371
Cdd:cd15693      3 CALCLKYGDD-SANDAGRllyigqnEWTHVNCALWSAEV-FEDDDGSLKNVHMAVIRGKQ--LRCEFC-QKPGATVGCCL 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1988305676  372 KTCKTAYHVTCAFQHGLemrAIIEDEnaedgvklRSYCQKH 412
Cdd:cd15693     78 TSCTSNYHFMCSRAKNC---VFLEDK--------KVYCQRH 107

PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A) and 2B (BAZ2B); BAZ2A, also termed transcription termination factor I-interacting protein 5 (TTF-I-interacting protein 5, or Tip5), or WALp3, is an epigenetic regulator. It has been implicated in epigenetic rRNA gene silencing, as the large subunit of the SNF2h-containing chromatin-remodeling complex NoRC that induces nucleosome sliding in an ATP- and histone H4 tail-dependent fashion. BAZ2A has also been shown to be broadly overexpressed in prostate cancer, to regulate numerous protein-coding genes and to cooperate with EZH2 (enhancer of zeste homolog 2) to maintain epigenetic silencing at genes repressed in prostate cancer metastasis. Its overexpression is tightly associated with a prostate cancer subtype displaying CpG island methylator phenotype (CIMP) in tumors and with prostate cancer recurrence in patients. BAZ2B, also termed WALp4, is a bromodomain-containing protein whose biological role is still elusive. It shows high sequence similarly with BAZ2A. Both BAZ2A and BAZ2B contain a TAM (TIP5/ARBP/MBD) domain, a DDT domain, four AT-hooks, BAZ 1 and BAZ 2 motifs, a WAKZ (WSTF/Acf1/KIAA0314/ZK783.4) motif, a plant homeodomain (PHD) finger, and a bromodomain. BAZ2B also harbors an extra Apolipophorin-III like domain in its N-terminal region.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1988305676  247 CDVCRSPDSEEanEMVFCDNCNICVHQACYG--ITNIPSGQWMCRTC 291
Cdd:cd15545      2 CQICRSGDNED--QLLLCDGCDRGYHTYCFKpkMTNVPEGDWFCPEC 46