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Conserved domains on  [gi|768004472|ref|XP_011526678|]
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hepatoma-derived growth factor-related protein 2 isoform X2 [Homo sapiens]

Protein Classification

PWWP and LEDGF domain-containing protein( domain architecture ID 10245936)

PWWP and LEDGF domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PWWP super family cl02554
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
 49-112 8.09e-42

PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids and is composed of a five-stranded antiparallel beta-barrel followed by a helical region. It is found in numerous proteins that are involved in cell division, growth, and differentiation. Most PWWP-domain proteins seem to be nuclear, often DNA-binding, proteins that function as transcription factors regulating a variety of developmental processes. PWWP domains specifically recognize DNA and histone methylated lysines at the level of the nucleosome. Based on the fact that other regions of PWWP-domain proteins are responsible for nuclear localization and DNA-binding, is likely that the PWWP domain acts as a site for protein-protein binding interactions, influencing chromatin remodeling and thereby regulating transcriptional processes. Some PWWP-domain proteins have been linked to cancer or other diseases; some are known to function as growth factors.


The actual alignment was detected with superfamily member cd20149:

Pssm-ID: 470613 [Multi-domain]  Cd Length: 84  Bit Score: 146.59  E-value: 8.09e-42
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768004472  49 IDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEGLWEIQNNP 112
Cdd:cd20149   21 IDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKYKDKYGKPNKRKGFNEGLWEIQNNP 84
LEDGF pfam11467
Lens epithelium-derived growth factor (LEDGF); LEDGF is a chromatin-associated protein that ...
 495-592 5.54e-33

Lens epithelium-derived growth factor (LEDGF); LEDGF is a chromatin-associated protein that protects cells from stress-induced apoptosis. It is the binding partner of HIV-1 integrase in human cells. The integrase binding domain (IBD) of LEDGF is a compact right-handed bundle composed of five alpha-helices. The residues essential for the interaction with the integrase are present in the inter-helical loop regions of the bundle structure.


:

Pssm-ID: 463284 [Multi-domain]  Cd Length: 120  Bit Score: 122.82  E-value: 5.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  495 EEKLQKLHSEIKFALKVDSPDVKRCLNALEELGTLQVTSQILQKNTDVVATLKKIRRYKAN------------------K 556
Cdd:pfam11467   1 ERKLQELDLDIKSCLKLDNADVDKCLEALDELKSLQVTPLMLKKNPECVETIKKLRRYVGNleewkmdeeeeaefkekaQ 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 768004472  557 DVMEKAAEVYTRLKSRVLGPKIEAVQKVNKAGMEKE 592
Cdd:pfam11467  81 LIRDKATEIYNKFKSLFLVPEGEVNFWPDFNEEVKE 116
PTZ00121 super family cl31754
MAEBL; Provisional
 122-650 1.45e-04

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  122 VSSSDSEAPEANPADGSDADEDDEDRGVMAVTAVTATAASDRMESDSDSDKSSDNSGLKRKTPALKMSVSKRARKASSDL 201
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  202 DQASVSPSEEENSESSSESEKTSDQDFTPEKKAAVRAPRRGPLGGRKKKAPSASDSDSKADSDGAKPEPVAMARSASSSS 281
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  282 SSSSSSDSDVSVKKPPRGRKPAEKPLPKPRGRKPKPERPPSSSSSDSDSDEVDRISEWKRRDEARRRELEARRRREQEEE 361
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  362 LRRLREQEKEEKERRRERADRGEAERgsggsSGDELREDDEPvkkrgrkgrgrgpPSSSDSEPEAELEREAKKSAKKPQS 441
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKK-----KADEAKKAAEA-------------KKKADEAKKAEEAKKADEAKKAEEA 1533

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  442 SSTEPARKPGQKEKrvrPEEKQQAKPVKVERTRKRSEgfsMDRKVEKKKEPSV---EEKLQKLHSEIKFALKVDSPDVKR 518
Cdd:PTZ00121 1534 KKADEAKKAEEKKK---ADELKKAEELKKAEEKKKAE---EAKKAEEDKNMALrkaEEAKKAEEARIEEVMKLYEEEKKM 1607

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  519 CLNALEELGTLQVTSQILQKNTDVvatLKKIRRYKANKDVMEKAAEvytRLKSRVLGPKIEAVQKVNKAGMEKEKAEE-- 596
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELKKAEEE---KKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEAKKAEEDKKKAEEak 1681

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768004472  597 KLAGEELAGEEAPQEKAEDKPSTDlsapvngeaTSQKGESAEDKEHEEGRDSEE 650
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAE---------ELKKKEAEEKKKAEELKKAEE 1726
 
Name Accession Description Interval E-value
PWWP_HDGFL2 cd20149
PWWP domain found in Hepatoma-derived growth factor-related protein 2 (HDGFL2); HDGFL2, also ...
 49-112 8.09e-42

PWWP domain found in Hepatoma-derived growth factor-related protein 2 (HDGFL2); HDGFL2, also called HDGF-related protein 2 (HRP-2), or Hepatoma-derived growth factor 2 (HDGF-2), is involved in cellular growth control, through the regulation of cyclin D1 expression. It contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438977 [Multi-domain]  Cd Length: 84  Bit Score: 146.59  E-value: 8.09e-42
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768004472  49 IDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEGLWEIQNNP 112
Cdd:cd20149   21 IDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKYKDKYGKPNKRKGFNEGLWEIQNNP 84
LEDGF pfam11467
Lens epithelium-derived growth factor (LEDGF); LEDGF is a chromatin-associated protein that ...
 495-592 5.54e-33

Lens epithelium-derived growth factor (LEDGF); LEDGF is a chromatin-associated protein that protects cells from stress-induced apoptosis. It is the binding partner of HIV-1 integrase in human cells. The integrase binding domain (IBD) of LEDGF is a compact right-handed bundle composed of five alpha-helices. The residues essential for the interaction with the integrase are present in the inter-helical loop regions of the bundle structure.


Pssm-ID: 463284 [Multi-domain]  Cd Length: 120  Bit Score: 122.82  E-value: 5.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  495 EEKLQKLHSEIKFALKVDSPDVKRCLNALEELGTLQVTSQILQKNTDVVATLKKIRRYKAN------------------K 556
Cdd:pfam11467   1 ERKLQELDLDIKSCLKLDNADVDKCLEALDELKSLQVTPLMLKKNPECVETIKKLRRYVGNleewkmdeeeeaefkekaQ 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 768004472  557 DVMEKAAEVYTRLKSRVLGPKIEAVQKVNKAGMEKE 592
Cdd:pfam11467  81 LIRDKATEIYNKFKSLFLVPEGEVNFWPDFNEEVKE 116
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 58-112 2.92e-06

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyzes all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organizing higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression.


Pssm-ID: 459964 [Multi-domain]  Cd Length: 92  Bit Score: 45.88  E-value: 2.92e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472   58 KPPPNKYPIFFFGTHETAFLGPKDLFPYD-----KCKDKYGKPNKRKGFNEGLWEIQNNP 112
Cdd:pfam00855  32 KKKDGEYLVRFFGDSEFAWVKPKDLKPFDegdefEYLKKKKKKKKKKAFKKALEEAEEAL 91
PTZ00121 PTZ00121
MAEBL; Provisional
 122-650 1.45e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  122 VSSSDSEAPEANPADGSDADEDDEDRGVMAVTAVTATAASDRMESDSDSDKSSDNSGLKRKTPALKMSVSKRARKASSDL 201
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  202 DQASVSPSEEENSESSSESEKTSDQDFTPEKKAAVRAPRRGPLGGRKKKAPSASDSDSKADSDGAKPEPVAMARSASSSS 281
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  282 SSSSSSDSDVSVKKPPRGRKPAEKPLPKPRGRKPKPERPPSSSSSDSDSDEVDRISEWKRRDEARRRELEARRRREQEEE 361
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  362 LRRLREQEKEEKERRRERADRGEAERgsggsSGDELREDDEPvkkrgrkgrgrgpPSSSDSEPEAELEREAKKSAKKPQS 441
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKK-----KADEAKKAAEA-------------KKKADEAKKAEEAKKADEAKKAEEA 1533

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  442 SSTEPARKPGQKEKrvrPEEKQQAKPVKVERTRKRSEgfsMDRKVEKKKEPSV---EEKLQKLHSEIKFALKVDSPDVKR 518
Cdd:PTZ00121 1534 KKADEAKKAEEKKK---ADELKKAEELKKAEEKKKAE---EAKKAEEDKNMALrkaEEAKKAEEARIEEVMKLYEEEKKM 1607

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  519 CLNALEELGTLQVTSQILQKNTDVvatLKKIRRYKANKDVMEKAAEvytRLKSRVLGPKIEAVQKVNKAGMEKEKAEE-- 596
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELKKAEEE---KKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEAKKAEEDKKKAEEak 1681

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768004472  597 KLAGEELAGEEAPQEKAEDKPSTDlsapvngeaTSQKGESAEDKEHEEGRDSEE 650
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAE---------ELKKKEAEEKKKAEELKKAEE 1726
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 61-86 2.42e-04

domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 39.64  E-value: 2.42e-04
                           10        20
                   ....*....|....*....|....*.
gi 768004472    61 PNKYPIFFFGTHETAFLGPKDLFPYD 86
Cdd:smart00293  38 ENLYPVLFFGDKDTAWIPSSKLFPLT 63
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 426-691 3.56e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 40.75  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472   426 AELEREAKKSAKKPQSSSTEPARKPGQKEKRVRPEEKQQAKpvkverTRKRSEG-FSMDRKVEKKKEPSVEEKLQKLHSE 504
Cdd:TIGR00927  636 AEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETK------GENESEGeIPAERKGEQEGEGEIEAKEADHKGE 709

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472   505 IKFALKVDSPDVKRCLNALEELGTLQVTSQILQKNTDVVATLKKIRRYKANKDVMEKAAEVYTRLKSRVLGPKIEAVQKV 584
Cdd:TIGR00927  710 TEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDG 789

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472   585 NKAGMEKEKAEEKLAGEELAGEEAPQEKAEDKPSTDLSAPV-NGEATSQKGESAEDKEHEEGRDSEEGPRCGSSEDLHDS 663
Cdd:TIGR00927  790 EMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDeTGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEE 869

                          250       260
                   ....*....|....*....|....*...
gi 768004472   664 VREGPDLDRPGSDRQERERARGDSEALD 691
Cdd:TIGR00927  870 EEEEEEEEEEEEEEEEEEEENEEPLSLE 897
 
Name Accession Description Interval E-value
PWWP_HDGFL2 cd20149
PWWP domain found in Hepatoma-derived growth factor-related protein 2 (HDGFL2); HDGFL2, also ...
 49-112 8.09e-42

PWWP domain found in Hepatoma-derived growth factor-related protein 2 (HDGFL2); HDGFL2, also called HDGF-related protein 2 (HRP-2), or Hepatoma-derived growth factor 2 (HDGF-2), is involved in cellular growth control, through the regulation of cyclin D1 expression. It contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438977 [Multi-domain]  Cd Length: 84  Bit Score: 146.59  E-value: 8.09e-42
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768004472  49 IDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEGLWEIQNNP 112
Cdd:cd20149   21 IDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKYKDKYGKPNKRKGFNEGLWEIQNNP 84
PWWP_PSIP cd20151
PWWP domain found in PC4 and SFRS1-interacting protein (PSIP); PSIP, also called ...
 49-116 5.90e-35

PWWP domain found in PC4 and SFRS1-interacting protein (PSIP); PSIP, also called CLL-associated antigen KW-7, dense fine speckles 70 kDa protein (DFS 70), lens epithelium-derived growth factor (LEDGF), or transcriptional coactivator p75/p52, acts as a transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. It contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438979 [Multi-domain]  Cd Length: 88  Bit Score: 127.41  E-value: 5.90e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768004472  49 IDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEGLWEIQNNPHASY 116
Cdd:cd20151   21 VDEVPDGAVKPPTNKLPIFFFGTHETAFLGPKDIFPYSENKEKYGKPNKRKGFNEGLWEIDNNPKVKF 88
PWWP_HRP cd05834
PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The ...
 49-111 2.89e-33

PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The HRP family includes hepatoma-derived growth factor (HDGF), and HDGF-related proteins (HRPs). HDGF, also called high mobility group protein 1-like 2 (HMG-1L2), is a heparin-binding protein that acts as a transcriptional repressor with mitogenic activity for fibroblasts. It is a prognostic factor in several types of cancer. HDGFL1 is also called PWWP domain-containing protein 1 (PWWP1). Its biological function remains unclear. HDGFL2, also called HDGF-related protein 2 (HRP-2), or hepatoma-derived growth factor 2 (HDGF-2), is involved in cellular growth control, through the regulation of cyclin D1 expression. HDGFL3, also called HDGF-related protein 3 (HRP-3), enhances DNA synthesis and may play a role in cell proliferation. The family also includes PC4 and SFRS1-interacting protein (PSIP) and similar proteins. PSIP, also called CLL-associated antigen KW-7, dense fine speckles 70 kDa protein (DFS 70), lens epithelium-derived growth factor (LEDGF), or transcriptional coactivator p75/p52, acts as a transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Members of the HRP family contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438959 [Multi-domain]  Cd Length: 82  Bit Score: 122.28  E-value: 2.89e-33
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768004472  49 IDDIADGAvKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEGLWEIQNN 111
Cdd:cd05834   21 IDEIPEGA-KIPKNKYPVFFYGTHETAFLKPKDLFPYEENKEKYGKPRKRKGFNEGLWEIENN 82
LEDGF pfam11467
Lens epithelium-derived growth factor (LEDGF); LEDGF is a chromatin-associated protein that ...
 495-592 5.54e-33

Lens epithelium-derived growth factor (LEDGF); LEDGF is a chromatin-associated protein that protects cells from stress-induced apoptosis. It is the binding partner of HIV-1 integrase in human cells. The integrase binding domain (IBD) of LEDGF is a compact right-handed bundle composed of five alpha-helices. The residues essential for the interaction with the integrase are present in the inter-helical loop regions of the bundle structure.


Pssm-ID: 463284 [Multi-domain]  Cd Length: 120  Bit Score: 122.82  E-value: 5.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  495 EEKLQKLHSEIKFALKVDSPDVKRCLNALEELGTLQVTSQILQKNTDVVATLKKIRRYKAN------------------K 556
Cdd:pfam11467   1 ERKLQELDLDIKSCLKLDNADVDKCLEALDELKSLQVTPLMLKKNPECVETIKKLRRYVGNleewkmdeeeeaefkekaQ 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 768004472  557 DVMEKAAEVYTRLKSRVLGPKIEAVQKVNKAGMEKE 592
Cdd:pfam11467  81 LIRDKATEIYNKFKSLFLVPEGEVNFWPDFNEEVKE 116
PWWP_HDGF cd20148
PWWP domain found in Hepatoma-derived growth factor (HDGF); HDGF, also called high mobility ...
 49-112 1.13e-31

PWWP domain found in Hepatoma-derived growth factor (HDGF); HDGF, also called high mobility group protein 1-like 2 (HMG-1L2), is a heparin-binding protein that acts as a transcriptional repressor with mitogenic activity for fibroblasts. It contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438976 [Multi-domain]  Cd Length: 87  Bit Score: 118.20  E-value: 1.13e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768004472  49 IDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEGLWEIQNNP 112
Cdd:cd20148   21 IDEMPEAAVKSTANKYQVFFFGTHETAFLGPKDLFPYEESKEKFGKPNKRKGFSEGLWEIENNP 84
PWWP_HDGFL3 cd20150
PWWP domain found in Hepatoma-derived growth factor-related protein 3 (HDGFL3); HDGFL3, also ...
 49-116 2.48e-30

PWWP domain found in Hepatoma-derived growth factor-related protein 3 (HDGFL3); HDGFL3, also called HDGF-related protein 3 (HRP-3), is the only hepatoma-derived growth factor (HDGF)-related protein (HRP) family member whose expression is almost restricted to the nervous tissue. It enhances DNA synthesis and may play a role in cell proliferation. It contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438978 [Multi-domain]  Cd Length: 93  Bit Score: 114.39  E-value: 2.48e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768004472  49 IDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEGLWEIQNNPHASY 116
Cdd:cd20150   26 IDELPEGAVKPPANKYPIFFFGTHETAFLGPKDLFPYKEYKDKFGKSNKRKGFNEGLWEIENNPGVKF 93
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 58-112 2.92e-06

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyzes all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organizing higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression.


Pssm-ID: 459964 [Multi-domain]  Cd Length: 92  Bit Score: 45.88  E-value: 2.92e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472   58 KPPPNKYPIFFFGTHETAFLGPKDLFPYD-----KCKDKYGKPNKRKGFNEGLWEIQNNP 112
Cdd:pfam00855  32 KKKDGEYLVRFFGDSEFAWVKPKDLKPFDegdefEYLKKKKKKKKKKAFKKALEEAEEAL 91
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 57-108 6.29e-06

PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called 3-hydroxyisobutyrate dehydrogenase-like protein, cytokine-like nuclear factor N-PAC, nuclear protein NP60, or nuclear protein of 60 kDa, is a putative oxidoreductase that is recruited on chromatin and promotes KDM1B demethylase activity. It recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3). GLYR1 enhances the activity of MAP2K4 and MAP2K6 kinases to phosphorylate p38-alpha. In addition to the PWWP domain, GLYR1 also contains an AT-hook and a C-terminal NAD-binding domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438961 [Multi-domain]  Cd Length: 86  Bit Score: 44.90  E-value: 6.29e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768004472  57 VKPPPNKYP---IFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEGLWEI 108
Cdd:cd05836   28 LKKPPRKKKmhcVYFFGSENYAWIEDENIKPYEEFKEEMLKSKKSAGFKDAVEAI 82
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
 58-100 2.81e-05

PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids and is composed of a five-stranded antiparallel beta-barrel followed by a helical region. It is found in numerous proteins that are involved in cell division, growth, and differentiation. Most PWWP-domain proteins seem to be nuclear, often DNA-binding, proteins that function as transcription factors regulating a variety of developmental processes. PWWP domains specifically recognize DNA and histone methylated lysines at the level of the nucleosome. Based on the fact that other regions of PWWP-domain proteins are responsible for nuclear localization and DNA-binding, is likely that the PWWP domain acts as a site for protein-protein binding interactions, influencing chromatin remodeling and thereby regulating transcriptional processes. Some PWWP-domain proteins have been linked to cancer or other diseases; some are known to function as growth factors.


Pssm-ID: 438958 [Multi-domain]  Cd Length: 86  Bit Score: 42.87  E-value: 2.81e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 768004472  58 KPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKG 100
Cdd:cd05162   31 KKKKGGVLVQFFGDNDYAWVKSKNIKPFEEGFKKEFKKKKKKS 73
PTZ00121 PTZ00121
MAEBL; Provisional
 122-650 1.45e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  122 VSSSDSEAPEANPADGSDADEDDEDRGVMAVTAVTATAASDRMESDSDSDKSSDNSGLKRKTPALKMSVSKRARKASSDL 201
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  202 DQASVSPSEEENSESSSESEKTSDQDFTPEKKAAVRAPRRGPLGGRKKKAPSASDSDSKADSDGAKPEPVAMARSASSSS 281
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  282 SSSSSSDSDVSVKKPPRGRKPAEKPLPKPRGRKPKPERPPSSSSSDSDSDEVDRISEWKRRDEARRRELEARRRREQEEE 361
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  362 LRRLREQEKEEKERRRERADRGEAERgsggsSGDELREDDEPvkkrgrkgrgrgpPSSSDSEPEAELEREAKKSAKKPQS 441
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKK-----KADEAKKAAEA-------------KKKADEAKKAEEAKKADEAKKAEEA 1533

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  442 SSTEPARKPGQKEKrvrPEEKQQAKPVKVERTRKRSEgfsMDRKVEKKKEPSV---EEKLQKLHSEIKFALKVDSPDVKR 518
Cdd:PTZ00121 1534 KKADEAKKAEEKKK---ADELKKAEELKKAEEKKKAE---EAKKAEEDKNMALrkaEEAKKAEEARIEEVMKLYEEEKKM 1607

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  519 CLNALEELGTLQVTSQILQKNTDVvatLKKIRRYKANKDVMEKAAEvytRLKSRVLGPKIEAVQKVNKAGMEKEKAEE-- 596
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELKKAEEE---KKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEAKKAEEDKKKAEEak 1681

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768004472  597 KLAGEELAGEEAPQEKAEDKPSTDlsapvngeaTSQKGESAEDKEHEEGRDSEE 650
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAE---------ELKKKEAEEKKKAEELKKAEE 1726
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 61-86 2.42e-04

domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 39.64  E-value: 2.42e-04
                           10        20
                   ....*....|....*....|....*.
gi 768004472    61 PNKYPIFFFGTHETAFLGPKDLFPYD 86
Cdd:smart00293  38 ENLYPVLFFGDKDTAWIPSSKLFPLT 63
PWWP_NSD_rpt2 cd05838
second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 57-107 3.80e-04

second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein family consists of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising in suppressing cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play nonredundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (C5HCH). This model corresponds to the second PWWP domain. The family also includes Drosophila melanogaster maternal-effect sterile 4 (dMes4) that may act as a histone-lysine N-methyltransferase required for wing morphogenesis. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438963 [Multi-domain]  Cd Length: 96  Bit Score: 39.92  E-value: 3.80e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768004472  57 VKPPPNKYPIFFFGTHETAFLGPKDLFPY---DKCKDKYGKPNKRKGFNEGLWE 107
Cdd:cd05838   33 LPHPPGEFPVRFFGSHDYYWVHRGRVFLFeegDKGSKEKSKKSLDKSFKRALKE 86
PTZ00121 PTZ00121
MAEBL; Provisional
 163-653 1.76e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  163 RMESDSDSDKSSDNSGLKRKTPALKMSVSKRARKASSDLDQASVSPSEEENSESSSESEKTSDQDFTPEKKAAVRAPRRG 242
Cdd:PTZ00121 1201 KAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA 1280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  243 PlggRKKKAPSASDSDSKADSDGAKPEPVAMARSASSSSSSSSSSDSDVSVKKPPRGRKPAEKPLPKPRGRKPKPERPPS 322
Cdd:PTZ00121 1281 D---ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  323 SSSSDSDSDEVDRISEWKRRDEARRRELEARRRREQEEELRRLREQEKEEKERRRERADRGEAERGSggSSGDELREDDE 402
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK--KKAEEKKKADE 1435

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  403 pvkkrgRKGRGRGPPSSSDSEPEAELEREAKKSAKKPQSSSTEPARKPGQKEKRVRPEEKQQAKPVK--VERTRKRSEGF 480
Cdd:PTZ00121 1436 ------AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKkkADEAKKAAEAK 1509

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  481 SMDRKVEKKKEPSVEEKLQKLHSEIKFALKVDSPDVKRC--LNALEELGTLQVTSQILQKNTDVVATLKKIRRYKANKDV 558
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdeLKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472  559 MEKAAEVYTRLKSRvlgpkieavQKVNKAGMEKEKAEEKLAGEELAGEEAPQEKAEDKPSTDLSAPVNGEATSQKGESAE 638
Cdd:PTZ00121 1590 EEARIEEVMKLYEE---------EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660

                         490
                  ....*....|....*
gi 768004472  639 DKEHEEGRDSEEGPR 653
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKK 1675
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 426-691 3.56e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 40.75  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472   426 AELEREAKKSAKKPQSSSTEPARKPGQKEKRVRPEEKQQAKpvkverTRKRSEG-FSMDRKVEKKKEPSVEEKLQKLHSE 504
Cdd:TIGR00927  636 AEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETK------GENESEGeIPAERKGEQEGEGEIEAKEADHKGE 709

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472   505 IKFALKVDSPDVKRCLNALEELGTLQVTSQILQKNTDVVATLKKIRRYKANKDVMEKAAEVYTRLKSRVLGPKIEAVQKV 584
Cdd:TIGR00927  710 TEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDG 789

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004472   585 NKAGMEKEKAEEKLAGEELAGEEAPQEKAEDKPSTDLSAPV-NGEATSQKGESAEDKEHEEGRDSEEGPRCGSSEDLHDS 663
Cdd:TIGR00927  790 EMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDeTGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEE 869

                          250       260
                   ....*....|....*....|....*...
gi 768004472   664 VREGPDLDRPGSDRQERERARGDSEALD 691
Cdd:TIGR00927  870 EEEEEEEEEEEEEEEEEEEENEEPLSLE 897
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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