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
  • Nucleus
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

UniProt AC Gene Name Protein Name Species Evidence Code
P24271 RAG1 V(D)J recombination-activating protein 1 Gallus gallus (Chicken) PR
P15918 RAG1 V(D)J recombination-activating protein 1 Homo sapiens (Human) PR
Q867B5 RAG1 V(D)J recombination-activating protein 1 Sus scrofa (Pig) PR
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