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 A0JMR6

Entry ID Method Resolution Chain Position Source
AF-A0JMR6-F1 Predicted AlphaFoldDB

No variants for A0JMR6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A0JMR6

No associated diseases with A0JMR6

6 regional properties for A0JMR6

Type Name Position InterPro Accession
domain JAB1/MPN/MOV34 metalloenzyme domain 547 - 671 IPR000555
domain SANT/Myb domain 104 - 156 IPR001005
domain SWIRM domain 344 - 442 IPR007526
domain SANT domain 107 - 158 IPR017884
domain Myb domain 111 - 158 IPR017930
domain MPN domain 548 - 680 IPR037518

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
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.

6 GO annotations of molecular function

Name Definition
cysteine-type deubiquitinase activity An thiol-dependent isopeptidase activity that cleaves ubiquitin from a target protein to which it is conjugated.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
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.
metal ion binding Binding to a metal ion.
metal-dependent deubiquitinase activity An metal-dependent isopeptidase activity that cleaves ubiquitin from a target protein to which it is conjugated.
transcription coactivator activity A transcription coregulator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coactivators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator.

3 GO annotations of biological process

Name Definition
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.
monoubiquitinated histone H2A deubiquitination The removal of the ubiquitin group from a monoubiquitinated histone H2A protein.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAEEAADVDI DIEGDINESS KSIYDSLNTG FAPEHYIESA WQNEEGLAPW ALDSSISEEN
70 80 90 100 110 120
REAIKKMLLE EEYYLSNKPL AVKFWSDSQE GEKQCIKRVR SPAKASSSPV KWTKEEKNLF
130 140 150 160 170 180
EQGLATFGRR WTSIARLIGS RSVLQVKNYA RHYFKNKCKL EGFVKEEAKI GSLQIPNLQD
190 200 210 220 230 240
YENEPDITDE PTTFRGRADP NLNAIKIEKL SDDEEIDITD EVDELLSNKT NLDTIIIAKT
250 260 270 280 290 300
DKVKETKVET EVQQKSHSTT EHSQTDIPKL VLQQTETECL DSVNPLTCIT SPKWTLSPQQ
310 320 330 340 350 360
CEEDDYDQPD VQDCLQEKCL SPHAEDLTVL CENENDSQDE DDEIKPPDQE LEIDRNFILD
370 380 390 400 410 420
EEKQAIPEFF EGRQAKTPDR YLRIRNYILD QWENCKPKYL NKTSVRPGLK NCGDVNCIGR
430 440 450 460 470 480
IHTYLELIGA INFGCEQAIY NRPRPVDKTK CKEGKDTLEA YKLAHRLQSM RTRKRRVRDP
490 500 510 520 530 540
WGNWCDAKDL EGQTYEHLSA EELARRHEDK IKSYKYSKGT RQVRSSFDPF QLIPCSAFSE
550 560 570 580 590 600
EKKAPFQVKV SCEAMLVLDL HAHVSMAEVI GLLGGRYTES ESVVEICAVE PCNSLSTGLQ
610 620 630 640 650 660
CEMDPVSQTQ ASEALASRGY SVIGWYHSHP AFDPNPSIRD IDTQAKYQNY FSRGGAKFLG
670 680 690 700 710 720
MIISPYNRRN PHPQSQVACL IISDELSNDG SYRIPYKFEI EYMQGEPQWE LVFAKTRWII
730 740 750 760 770 780
EKYRSSHSSV SMDKRFRHDS ELTCLQKLLM CMKKTLGNTA CPLITEEFLH RIEEYFRTSY
790 800 810
KKESNYQIED NDPCKQHSDT TFTMDSFQDY EPNGRPSL