P15919
Gene name |
Rag1 |
Protein name |
V(D)J recombination-activating protein 1 |
Names |
RAG-1 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:19373 |
EC number |
2.3.2.27: Aminoacyltransferases |
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
26 structures for P15919
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1RMD | X-ray | 210 A | A | 265-380 | PDB |
| 3GNA | X-ray | 240 A | A | 389-464 | PDB |
| 3GNB | X-ray | 300 A | A | 389-464 | PDB |
| 4WWX | X-ray | 320 A | B/E | 392-1008 | PDB |
| 5ZDZ | X-ray | 280 A | A/C | 384-1008 | PDB |
| 5ZE0 | X-ray | 275 A | A/C | 384-1008 | PDB |
| 5ZE1 | X-ray | 300 A | A/C | 384-1008 | PDB |
| 5ZE2 | X-ray | 330 A | A/C | 384-1008 | PDB |
| 6CG0 | EM | 317 A | A/C | 265-1039 | PDB |
| 6CIJ | EM | 390 A | A/C | 265-1040 | PDB |
| 6CIK | X-ray | 315 A | A/C | 384-1008 | PDB |
| 6CIL | X-ray | 415 A | A/C | 384-1008 | PDB |
| 6CIM | X-ray | 360 A | A/C | 384-1008 | PDB |
| 6OEM | EM | 360 A | A/C | 1-1040 | PDB |
| 6OEN | EM | 430 A | A/C | 1-1040 | PDB |
| 6OEO | EM | 369 A | A/C | 1-1040 | PDB |
| 6OEP | EM | 370 A | A/C | 1-1040 | PDB |
| 6OEQ | EM | 430 A | A/C | 1-1040 | PDB |
| 6OER | EM | 329 A | A/C | 1-1040 | PDB |
| 6OES | EM | 306 A | A/C | 1-1040 | PDB |
| 6OET | EM | 340 A | A/C | 1-1040 | PDB |
| 6V0V | EM | 361 A | A | 265-1039 | PDB |
| 6XNX | EM | 270 A | A/C | 261-1008 | PDB |
| 6XNY | EM | 290 A | A/C | 261-1008 | PDB |
| 6XNZ | EM | 380 A | A/C | 261-1008 | PDB |
| AF-P15919-F1 | Predicted | AlphaFoldDB |
46 variants for P15919
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs234458221 | 23 | I>M | No | EVA | |
| rs3391994911 | 34 | R>G | No | EVA | |
| rs224434232 | 96 | S>P | No | EVA | |
| rs3388567168 | 114 | G>E | No | EVA | |
| rs3388562664 | 136 | T>I | No | EVA | |
| rs3388569549 | 161 | D>V | No | EVA | |
| rs3388572717 | 163 | K>E | No | EVA | |
| rs3388569169 | 163 | K>R | No | EVA | |
| rs27362079 | 189 | S>A | No | EVA | |
| rs27362080 | 198 | K>N | No | EVA | |
| rs251051961 | 217 | H>Y | No | EVA | |
| rs3388562688 | 225 | H>L | No | EVA | |
| rs3388567152 | 252 | A>V | No | EVA | |
| rs3388576711 | 256 | S>I | No | EVA | |
| rs3391883642 | 290 | C>S | No | EVA | |
| rs27362086 | 346 | N>S | No | EVA | |
| rs27362087 | 375 | S>I | No | EVA | |
| rs3388566135 | 475 | F>L | No | EVA | |
| rs3388569609 | 485 | Y>C | No | EVA | |
| rs3388567466 | 491 | I>N | No | EVA | |
| rs3388567427 | 648 | S>Y | No | EVA | |
| rs3388576213 | 659 | L>M | No | EVA | |
| rs3388576723 | 662 | E>D | No | EVA | |
| rs3388573022 | 671 | I>F | No | EVA | |
| rs3388571468 | 711 | L>V | No | EVA | |
| rs3388572547 | 723 | S>T | No | EVA | |
| rs3388573071 | 729 | L>V | No | EVA | |
| rs3388573108 | 731 | D>V | No | EVA | |
| rs27362096 | 732 | T>A | No | EVA | |
| rs864277759 | 789 | P>A | No | EVA | |
| rs27362098 | 805 | Y>F | No | EVA | |
| rs3388566145 | 829 | W>R | No | EVA | |
| rs3388569548 | 841 | M>L | No | EVA | |
| rs3388567163 | 915 | R>S | No | EVA | |
| rs3391986199 | 923 | K>M | No | EVA | |
| rs3413100877 | 925 | K>N | No | EVA | |
| rs3388576159 | 933 | T>A | No | EVA | |
| rs3388566123 | 934 | N>Y | No | EVA | |
| rs3388573651 | 942 | H>Y | No | EVA | |
| rs3388572788 | 955 | A>T | No | EVA | |
| rs3388569235 | 980 | K>* | No | EVA | |
| rs3388573092 | 996 | S>* | No | EVA | |
| rs3388572753 | 1006 | H>Y | No | EVA | |
| rs3388576892 | 1008 | A>T | No | EVA | |
| rs224942264 | 1025 | P>T | No | EVA | |
| rs3388572789 | 1041 | F>K | No | EVA |
No associated diseases with P15919
6 regional properties for P15919
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Zinc finger, RING-type | 290 - 329 | IPR001841 |
| conserved_site | Zinc finger, RING-type, conserved site | 305 - 314 | IPR017907 |
| domain | Zinc finger, C3HC4 RING-type | 290 - 328 | IPR018957 |
| domain | V(D)J recombination-activating protein 1, Zinc finger | 351 - 380 | IPR019485 |
| domain | RAG nonamer-binding domain | 389 - 456 | IPR023336 |
| domain | RAG1 importin-binding | 12 - 288 | IPR035714 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.2.27 | Aminoacyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| DNA recombinase complex | A protein-DNA complex consisting of a higher-order oligomer of strand exchange proteins (recombinases) on single-stranded DNA. |
| endodeoxyribonuclease complex | A protein complex which is capable of endodeoxyribonuclease activity. |
| 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. |
9 GO annotations of molecular function
| Name | Definition |
|---|---|
| endonuclease activity | Catalysis of the hydrolysis of ester linkages within nucleic acids by creating internal breaks. |
| 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. |
| identical protein binding | Binding to an identical protein or proteins. |
| metal ion binding | Binding to a metal ion. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
| sequence-specific DNA binding | Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding. |
| ubiquitin protein ligase activity | Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues. |
| ubiquitin-protein transferase activity | Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages. |
| zinc ion binding | Binding to a zinc ion (Zn). |
18 GO annotations of biological process
| Name | Definition |
|---|---|
| adaptive immune response | An immune response mediated by cells expressing specific receptors for antigen produced through a somatic diversification process, and allowing for an enhanced secondary response to subsequent exposures to the same antigen (immunological memory). |
| B cell differentiation | The process in which a precursor cell type acquires the specialized features of a B cell. A B cell is a lymphocyte of B lineage with the phenotype CD19-positive and capable of B cell mediated immunity. |
| chromatin organization | The assembly or remodeling of chromatin composed of DNA complexed with histones, other associated proteins, and sometimes RNA. |
| DNA recombination | Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction. |
| histone monoubiquitination | The modification of histones by addition of a single ubiquitin group. |
| negative regulation of cysteine-type endopeptidase activity involved in apoptotic process | Any process that stops, prevents, or reduces the frequency, rate or extent of a cysteine-type endopeptidase activity involved in the apoptotic process. |
| negative regulation of T cell apoptotic process | Any process that stops, prevents, or reduces the frequency, rate or extent of T cell death by apoptotic process. |
| negative regulation of thymocyte apoptotic process | Any process that stops, prevents, or reduces the frequency, rate or extent of thymocyte death by apoptotic process. |
| positive regulation of T cell differentiation | Any process that activates or increases the frequency, rate or extent of T cell differentiation. |
| pre-B cell allelic exclusion | Expression of a single heavy chain allele during pre-B cell differentiation. |
| protein autoubiquitination | The ubiquitination by a protein of one or more of its own amino acid residues, or residues on an identical protein. Ubiquitination occurs on the lysine residue by formation of an isopeptide crosslink. |
| regulation of behavioral fear response | Any process that modulates the frequency, rate or extent of behavioral fear response. |
| regulation of T cell differentiation | Any process that modulates the frequency, rate or extent of T cell differentiation. |
| T cell differentiation in thymus | The process in which a precursor cell type acquires the specialized features of a T cell via a differentiation pathway dependent upon transit through the thymus. |
| T cell homeostasis | The process of regulating the proliferation and elimination of T cells such that the total number of T cells within a whole or part of an organism is stable over time in the absence of an outside stimulus. |
| thymus development | The process whose specific outcome is the progression of the thymus over time, from its formation to the mature structure. The thymus is a symmetric bi-lobed organ involved primarily in the differentiation of immature to mature T cells, with unique vascular, nervous, epithelial, and lymphoid cell components. |
| V(D)J recombination | The process in which immune receptor V, D, and J, or V and J gene segments, depending on the specific receptor, are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS). |
| visual learning | Any process in an organism in which a change in behavior of an individual occurs in response to repeated exposure to a visual cue. |
3 homologous proteins in AiPD
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAASLPSTLS | FSSAPDEIQH | PQIKFSEWKF | KLFRVRSFEK | APEEAQKEKD | SSEGKPYLEQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SPVVPEKPGG | QNSILTQRAL | KLHPKFSKKF | HADGKSSDKA | VHQARLRHFC | RICGNRFKSD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GHSRRYPVHG | PVDAKTQSLF | RKKEKRVTSW | PDLIARIFRI | DVKADVDSIH | PTEFCHDCWS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IMHRKFSSSH | SQVYFPRKVT | VEWHPHTPSC | DICFTAHRGL | KRKRHQPNVQ | LSKKLKTVLN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| HARRDRRKRT | QARVSSKEVL | KKISNCSKIH | LSTKLLAVDF | PAHFVKSISC | QICEHILADP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VETSCKHLFC | RICILRCLKV | MGSYCPSCRY | PCFPTDLESP | VKSFLNILNS | LMVKCPAQDC |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NEEVSLEKYN | HHVSSHKESK | ETLVHINKGG | RPRQHLLSLT | RRAQKHRLRE | LKIQVKEFAD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KEEGGDVKAV | CLTLFLLALR | ARNEHRQADE | LEAIMQGRGS | GLQPAVCLAI | RVNTFLSCSQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| YHKMYRTVKA | ITGRQIFQPL | HALRNAEKVL | LPGYHPFEWQ | PPLKNVSSRT | DVGIIDGLSG |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LASSVDEYPV | DTIAKRFRYD | SALVSALMDM | EEDILEGMRS | QDLDDYLNGP | FTVVVKESCD |
| 610 | 620 | 630 | 640 | 650 | 660 |
| GMGDVSEKHG | SGPAVPEKAV | RFSFTVMRIT | IEHGSQNVKV | FEEPKPNSEL | CCKPLCLMLA |
| 670 | 680 | 690 | 700 | 710 | 720 |
| DESDHETLTA | ILSPLIAERE | AMKSSELTLE | MGGIPRTFKF | IFRGTGYDEK | LVREVEGLEA |
| 730 | 740 | 750 | 760 | 770 | 780 |
| SGSVYICTLC | DTTRLEASQN | LVFHSITRSH | AENLQRYEVW | RSNPYHESVE | ELRDRVKGVS |
| 790 | 800 | 810 | 820 | 830 | 840 |
| AKPFIETVPS | IDALHCDIGN | AAEFYKIFQL | EIGEVYKHPN | ASKEERKRWQ | ATLDKHLRKR |
| 850 | 860 | 870 | 880 | 890 | 900 |
| MNLKPIMRMN | GNFARKLMTQ | ETVDAVCELI | PSEERHEALR | ELMDLYLKMK | PVWRSSCPAK |
| 910 | 920 | 930 | 940 | 950 | 960 |
| ECPESLCQYS | FNSQRFAELL | STKFKYRYEG | KITNYFHKTL | AHVPEIIERD | GSIGAWASEG |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| NESGNKLFRR | FRKMNARQSK | CYEMEDVLKH | HWLYTSKYLQ | KFMNAHNALK | SSGFTMNSKE |
| 1030 | |||||
| TLGDPLGIED | SLESQDSMEF |