Q9Z277
PR
Gene name |
Baz1b (Wbscr9, Wstf) |
Protein name |
Tyrosine-protein kinase BAZ1B |
Names |
Bromodomain adjacent to zinc finger domain protein 1B, Williams syndrome transcription factor homolog, Williams-Beuren syndrome chromosomal region 9 protein homolog |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:22385 |
EC number |
2.7.10.2: Protein-tyrosine kinases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q9Z277
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9Z277-F1 | Predicted | AlphaFoldDB |
45 variants for Q9Z277
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388799669 | 50 | W>* | No | EVA | |
| rs3388802407 | 56 | G>* | No | EVA | |
| rs3388790636 | 86 | K>R | No | EVA | |
| rs3388790626 | 92 | V>L | No | EVA | |
| rs3388796735 | 94 | H>Q | No | EVA | |
| rs3388794753 | 105 | S>Y | No | EVA | |
| rs3388804319 | 112 | T>S | No | EVA | |
| rs3388778918 | 320 | K>N | No | EVA | |
| rs3388799665 | 337 | W>R | No | EVA | |
| rs1135180682 | 357 | K>R | No | EVA | |
| rs13502646 | 368 | G>E | No | EVA | |
| rs3388789057 | 493 | K>M | No | EVA | |
| rs3388786429 | 507 | L>I | No | EVA | |
| rs3388797538 | 577 | K>R | No | EVA | |
| rs3388799424 | 606 | T>I | No | EVA | |
| rs3388793251 | 608 | F>L | No | EVA | |
| rs3388789063 | 631 | Y>H | No | EVA | |
| rs3388792705 | 704 | E>K | No | EVA | |
| rs3388783808 | 706 | S>G | No | EVA | |
| rs3388768427 | 713 | D>V | No | EVA | |
| rs32233982 | 716 | D>E | No | EVA | |
| rs3388794762 | 724 | E>K | No | EVA | |
| rs3388789061 | 725 | V>M | No | EVA | |
| rs3388804448 | 728 | E>K | No | EVA | |
| rs3388793235 | 732 | K>M | No | EVA | |
| rs3388793220 | 748 | R>W | No | EVA | |
| rs3388804398 | 750 | L>S | No | EVA | |
| rs32235204 | 773 | V>M | No | EVA | |
| rs3388793283 | 777 | L>S | No | EVA | |
| rs3388783769 | 844 | K>M | No | EVA | |
| rs3388793202 | 850 | S>R | No | EVA | |
| rs13497540 | 970 | A>V | No | EVA | |
| rs3388798620 | 1022 | E>D | No | EVA | |
| rs3388783817 | 1159 | A>T | No | EVA | |
| rs13497542 | 1216 | P>L | No | EVA | |
| rs3388768415 | 1220 | E>D | No | EVA | |
| rs3388786383 | 1302 | G>C | No | EVA | |
| rs3388799682 | 1302 | G>V | No | EVA | |
| rs3388786360 | 1303 | R>L | No | EVA | |
| rs3388804420 | 1372 | Y>* | No | EVA | |
| rs3388797615 | 1415 | N>Y | No | EVA | |
| rs3388804365 | 1416 | C>Y | No | EVA | |
| rs13461186 | 1442 | G>C | No | EVA | |
| rs3388796668 | 1460 | D>V | No | EVA | |
| rs3388804697 | 1474 | G>R | No | EVA |
3 associated diseases with Q9Z277
[MIM: 217400]: Corneal dystrophy and perceptive deafness (CDPD)
An ocular disease characterized by the association of corneal clouding with progressive perceptive hearing loss. {ECO:0000269|PubMed:17220209}. Note=The disease is caused by variants affecting the gene represented in this entry.
[MIM: 217700]: Corneal endothelial dystrophy (CHED)
A congenital corneal dystrophy characterized by thickening and opacification of the cornea, altered morphology of the endothelium, and secretion of an abnormal collagenous layer at the Descemet membrane. {ECO:0000269|PubMed:16767101, ECO:0000269|PubMed:16825429, ECO:0000269|PubMed:17220209, ECO:0000269|PubMed:17397048, ECO:0000269|PubMed:17679935, ECO:0000269|PubMed:18474783, ECO:0000269|PubMed:19369245, ECO:0000269|PubMed:20108384, ECO:0000269|PubMed:20185830, ECO:0000269|PubMed:21203343, ECO:0000269|PubMed:21288032, ECO:0000269|PubMed:22072594, ECO:0000269|PubMed:23813972, ECO:0000269|PubMed:26286922, ECO:0000269|PubMed:27581649}. Note=The disease is caused by variants affecting the gene represented in this entry.
[MIM: 613268]: Corneal dystrophy, Fuchs endothelial, 4 (FECD4)
A corneal disease caused by loss of endothelium of the central cornea. It is characterized by focal wart-like guttata that arise from Descemet membrane and develop in the central cornea, epithelial blisters, reduced vision and pain. Descemet membrane is thickened by abnormal collagenous deposition. {ECO:0000269|PubMed:18024964, ECO:0000269|PubMed:20848555, ECO:0000269|PubMed:22072594, ECO:0000269|PubMed:25007886}. Note=The disease is caused by variants affecting the gene represented in this entry.
Without disease ID
- An ocular disease characterized by the association of corneal clouding with progressive perceptive hearing loss. {ECO:0000269|PubMed:17220209}. Note=The disease is caused by variants affecting the gene represented in this entry.
- A congenital corneal dystrophy characterized by thickening and opacification of the cornea, altered morphology of the endothelium, and secretion of an abnormal collagenous layer at the Descemet membrane. {ECO:0000269|PubMed:16767101, ECO:0000269|PubMed:16825429, ECO:0000269|PubMed:17220209, ECO:0000269|PubMed:17397048, ECO:0000269|PubMed:17679935, ECO:0000269|PubMed:18474783, ECO:0000269|PubMed:19369245, ECO:0000269|PubMed:20108384, ECO:0000269|PubMed:20185830, ECO:0000269|PubMed:21203343, ECO:0000269|PubMed:21288032, ECO:0000269|PubMed:22072594, ECO:0000269|PubMed:23813972, ECO:0000269|PubMed:26286922, ECO:0000269|PubMed:27581649}. Note=The disease is caused by variants affecting the gene represented in this entry.
- A corneal disease caused by loss of endothelium of the central cornea. It is characterized by focal wart-like guttata that arise from Descemet membrane and develop in the central cornea, epithelial blisters, reduced vision and pain. Descemet membrane is thickened by abnormal collagenous deposition. {ECO:0000269|PubMed:18024964, ECO:0000269|PubMed:20848555, ECO:0000269|PubMed:22072594, ECO:0000269|PubMed:25007886}. Note=The disease is caused by variants affecting the gene represented in this entry.
1 regional properties for Q9Z277
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Bicarbonate transporter-like, transmembrane domain | 328 - 818 | IPR011531 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.10.2 | Protein-tyrosine kinases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
8 GO annotations of cellular component
| Name | Definition |
|---|---|
| B-WICH complex | A chromatin remodeling complex that positively regulates histone H3 acetylation, in particular H3K9, by recruiting histone acetyltransferases to rDNA gene regions. Located in the nucleolus where it assembles on RNA Polymerase I (Pol I) and possibly on RNA Polymerase III (Pol III) promoter and coding regions during early G1 phase and activates the post-initiation phases of Pol I transcription. May also activate RNA Polymerase II (Pol II) gene transcription. In mammals, B-WICH contains the WICH complex core of BAZ1B and SMARCA5, additional protein subunits and possibly rRNAs. Although it contains several catalytic subunits it is not clear which functions are carried out by the complex itself. |
| condensed chromosome | A highly compacted molecule of DNA and associated proteins resulting in a cytologically distinct structure. |
| nuclear replication fork | The Y-shaped region of a nuclear replicating DNA molecule, resulting from the separation of the DNA strands and in which the synthesis of new strands takes place. Also includes associated protein complexes. |
| nucleolus | A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
| pericentric heterochromatin | Heterochromatin that is located adjacent to the CENP-A rich centromere 'central core' and characterized by methylated H3 histone at lysine 9 (H3K9me2/H3K9me3). |
| WICH complex | An ISWI complex that contains an ATPase subunit of the ISWI family (specifically SNF2H in mammals, which contain two ISWI homologs) and WSTF (Williams Syndrome Transcription Factor). WICH plays roles in regulation of RNAP I and III transcription and in DNA replication and repair. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| histone binding | Binding to a histone, any of a group of water-soluble proteins found in association with the DNA of eukaryotic or archaeal chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in gene regulation and DNA replication. They may be chemically modified (methylated, acetlyated and others) to regulate gene transcription. |
| histone kinase activity | Catalysis of the transfer of a phosphate group to a histone. |
| histone kinase activity (H2A-Y142 specific) | Catalysis of the transfer of a phosphate group to the tyrosine-142 residue of the C-terminal tail of histone H2A. |
| metal ion binding | Binding to a metal ion. |
| protein tyrosine kinase activity | Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate. |
10 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to DNA damage stimulus | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism. |
| chromatin organization | The assembly or remodeling of chromatin composed of DNA complexed with histones, other associated proteins, and sometimes RNA. |
| chromatin remodeling | A dynamic process of chromatin reorganization resulting in changes to chromatin structure. These changes allow DNA metabolic processes such as transcriptional regulation, DNA recombination, DNA repair, and DNA replication. |
| negative regulation of mitotic chromosome condensation | Any process that stops, prevents or reduces the frequency, rate or extent of mitotic chromosome condensation. |
| positive regulation of histone acetylation | Any process that activates or increases the frequency, rate or extent of the addition of an acetyl group to a histone protein. |
| positive regulation of transcription by RNA polymerase I | Any process that activates or increases the frequency, rate or extent of transcription mediated by RNA polymerase I. |
| positive regulation of transcription by RNA polymerase II | Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter. |
| positive regulation of transcription by RNA polymerase III | Any process that activates or increases the frequency, rate or extent of transcription mediated by RNA polymerase III. |
| post-translational protein modification | The process of covalently altering one or more amino acids in a protein after the protein has been completely translated and released from the ribosome. |
| regulation of response to DNA damage stimulus | Any process that modulates the frequency, rate or extent of response to DNA damage stimulus. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAPLLGRKPF | PLVKPLPGEE | PLFTIPHTQE | AFRTREEYEA | RLERYSERIW | TCKSTGSSQL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| THKEAWEEEQ | EVAELLKEEF | PNWYEKLVLE | MVHHNTASLE | KLVDSAWLEI | MTKYAVGEEC |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DFEVGKEKML | KVKIVKIHPL | EKVDEEAVEK | KSDGACDSPS | SDKENSSQMA | QDLQKKETVV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KEDEGRRESI | NDRARRSPRK | LPTSLKKGER | KWAPPKFLPH | KYDVKLQNED | KIISNVPADS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LIRTERPPNK | EILRYFIRHN | ALRAGTGENA | PWVVEDELVK | KYSLPSKFSD | FLLDPYKYMT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LNPSTKRRNT | GSPDRKPSKK | PKRDSSSLSS | PLNPKLWCHV | HLEKSLNGPP | LKVKNSKNSK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SPEEHLEGVM | KIMSPNNNKL | HSFHIPKKGP | AAKKPGKHSD | KPLKAKGRGK | GILNGQKSTG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NSKSPSKCVK | TPKTKMKQMT | LLDMAKGTQK | MTRTPRSSGG | VPRSSGKPHK | HLPPAALHLI |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AYYKENKDKE | DKKSALSCVI | SKTARLLSNE | DRARLPEELR | ALVQKRYELL | EHKKRWASMS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EEQRKEYLKK | KRQELKERLR | EKAKERRERE | MLERLEKQKR | FEDQELGGRN | LPAFRLVDTP |
| 610 | 620 | 630 | 640 | 650 | 660 |
| EGLPNTLFGD | VALVVEFLSC | YSGLLLPDAQ | YPITAVSLME | ALSADKGGFL | YLNRVLVILL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| QTLLQDEIAE | DYGELGMKLS | EIPLTLHSVS | ELVRLCLRRC | DVQEDSEGSE | TDDNKDSTPF |
| 730 | 740 | 750 | 760 | 770 | 780 |
| EDNEVQDEFL | EKLETSEFFE | LTSEEKLRIL | TALCHRILMT | YSVQDHMETR | QQVSAELWKE |
| 790 | 800 | 810 | 820 | 830 | 840 |
| RLAVLKEEND | KKRAEKQKRK | EMEARNKENG | KEENVLGKVD | RKKEIVKIEQ | QVEVEADDMI |
| 850 | 860 | 870 | 880 | 890 | 900 |
| SAVKSRRLLS | MQAKRKREIQ | ERETKVRLER | EAEEERMRKH | KAAAEKAFQE | GIAKAKLVLR |
| 910 | 920 | 930 | 940 | 950 | 960 |
| RTPIGTDRNH | NRYWLFSNEV | PGLFIEKGWV | HNSIDYRFKH | HRKDHSNLPD | DDYCPRSKKA |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| NLGKNASVNA | HHGPALEAVE | TTVPKQGQNL | WFLCDSQKEL | DELLSCLHPQ | GIRESQLKER |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| LEKRYQEITH | SIYLARKPNL | GLKSCDGNQE | LLNFLRSDLI | EVATRLQKGG | LGYMEGTSEF |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| EARVISLEKL | KDFGECVIAL | QASVIKKFLQ | GFMAPKQKKR | KLQSEDSTKS | EEVDEEKKMV |
| 1150 | 1160 | 1170 | 1180 | 1190 | 1200 |
| EEAKVASALE | KWKTAIREAQ | TFSRMHVLLG | MLDACIKWDM | SAENARCKVC | RKKGEDDKLI |
| 1210 | 1220 | 1230 | 1240 | 1250 | 1260 |
| LCDECNKAFH | LFCLRPALYE | VPDGEWQCPA | CQPPTARRNS | RGRNYTEEST | SEGSEGDESG |
| 1270 | 1280 | 1290 | 1300 | 1310 | 1320 |
| EEEEEEEEEE | EEEEDYEVAG | LRLRPRKTIR | GKQSVIPAAR | PGRPPGKKSH | PARRSRPKDD |
| 1330 | 1340 | 1350 | 1360 | 1370 | 1380 |
| PEVDDLVLQT | KRISRRQSLE | LQKCEDILHK | LVKYRFSWPF | REPVTRDEAE | DYYDVIEHPM |
| 1390 | 1400 | 1410 | 1420 | 1430 | 1440 |
| DFQTIQNKCS | CGNYRSVQEF | LTDMKQVFAN | AELYNCRGSH | VLSCMEKTEQ | CLLALLQKHL |
| 1450 | 1460 | 1470 | |||
| PGHPYVRRKR | RKFPDRLADD | EGDSDSESVG | QSRGRRQKK |