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 Q4H2R2

Entry ID Method Resolution Chain Position Source
AF-Q4H2R2-F1 Predicted AlphaFoldDB

No variants for Q4H2R2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q4H2R2

No associated diseases with Q4H2R2

4 regional properties for Q4H2R2

Type Name Position InterPro Accession
domain High mobility group box domain 553 - 623 IPR009071
domain Histone chaperone RTT106/FACT complex subunit SPT16-like, middle domain 341 - 432 IPR013719
domain SSRP1, dimerization domain 109 - 172 IPR024954
domain FACT complex subunit SSRP1/POB3, N-terminal PH domain 9 - 102 IPR035417

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
  • Chromosome
  • Nucleus, nucleolus
  • Colocalizes with RNA polymerase II on chromatin
  • Recruited to actively transcribed loci
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
FACT complex A histone chaperone complex that facilitates nucleosome disassembly and reassembly upon DNA or RNA polymerase passage.
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.

3 GO annotations of molecular function

Name Definition
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.
nucleosome binding Binding to a nucleosome, a complex comprised of DNA wound around a multisubunit core and associated proteins, which forms the primary packing unit of DNA into higher order structures.

3 GO annotations of biological process

Name Definition
DNA repair The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
DNA replication The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by initiation proteins, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
regulation of chromatin organization Any process that modulates the frequency, rate or extent of chromatin organization.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTENGQFLDY KNVFQENRGA MHDGRLQLLK EKIVFKNNKT GKIDSIQQND LHSALWRRVA
70 80 90 100 110 120
RDFELKFQMN SGQVFRFDGF KEMEFERLKD FVKNYYKIDL EHQELSGKGW NWGTTDFEGN
130 140 150 160 170 180
EMMFQVGQKL SFEIPLNNVS QCTQNKDEVT MEFHQNDDSE LSLMEMRFFI PPSQDEMIDK
190 200 210 220 230 240
VKDFHDNVMA KADVLQVKGT AICVFQDLQC LTPRGRYDIR MYPKFIQLHG KTFDYKITYT
250 260 270 280 290 300
SILRLFLLPH KDQRQIFFVV SLDPPLKQGM TRYHFLILLF YKEDDLAVEL SLPDDEIEER
310 320 330 340 350 360
FGGKLQKDMS GPMYEVVSRV MKHLVQRKIT VPGSFKGLNG VQSITCTYKA SSGFLFPLER
370 380 390 400 410 420
GFMYVHKPPV HIRFDEIAYV NFARGTTKIN KSFDFEIETR SKNNFVFSNI ERDQYASLYD
430 440 450 460 470 480
FVHNKQLKIK NIGKDGADFD LMVDSDEDAD VHDPYMERMK QEAAEREKQV DDDDDDESED
490 500 510 520 530 540
DDFQPETNVA EVEEEYNSDV GSASSGASDE EEEDGEEEVE EKPKKRKKEK VMKERRQKET
550 560 570 580 590 600
PGKVKRKKKD PNAPKRPQSA YFLWLNENRG RFKAENKGIS VTELTKLAGK EWKKIDPDEK
610 620 630 640 650 660
QKFERMYQKS KVKFDAAMKE YKSQGGGRTS SSPAKKMKMK SPKPSKASSS MVSPSKFKSK
670 680 690 700
EFITESDSLS SSDSDAEVKS KNSPPADEES ASESEAASEE EESD