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 Q54G78

Entry ID Method Resolution Chain Position Source
AF-Q54G78-F1 Predicted AlphaFoldDB

No variants for Q54G78

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q54G78

No associated diseases with Q54G78

3 regional properties for Q54G78

Type Name Position InterPro Accession
domain Histone chaperone RTT106/FACT complex subunit SPT16-like, middle domain 378 - 474 IPR013719
domain SSRP1, dimerization domain 111 - 180 IPR024954
domain FACT complex subunit SSRP1/POB3, N-terminal PH domain 10 - 100 IPR035417

Functions

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

1 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.

4 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.
identical protein binding Binding to an identical protein or proteins.
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
MSSSSNPVSQ FNNISLGGRI SGTRGILKFT TNNITWKSEN GKIETVSSSD IKRANWARVT
70 80 90 100 110 120
PRIFQLILSI KGGATVKFDG FKEQDYEVVR KYLSDQYNVS PLEIIELSSK GCNWGEVKVN
130 140 150 160 170 180
GPMIQFTTDH GKVGFEFPIS EVSQSVIGAN NKNELTLEFH HDKAMDDDDE TMVEMRFFTP
190 200 210 220 230 240
IRPSKEGEEG GKEKKVGEDG EEDEEDEEDA EKEEEISALE QFQQTIMNKS DMVSNVGKSL
250 260 270 280 290 300
VVFSAIQFLT PRGRIDIEMY PTFLKLHGKT HDYKVPYESI SRLFQFFRPD QKHIFFIISL
310 320 330 340 350 360
DPPIRQGQTK YAHLVIQFQA EENIHLELNL TDELQQKFKD QLSPIMNGNA NALICKILKA
370 380 390 400 410 420
LTGKKITIPG NFQSDSGANS IKCSLKANEG YLYPLERCFF FVHKPPTYIK FEDISNIEFA
430 440 450 460 470 480
RYGAPSVRGG SNRTFDLSIN LKNSTSIQFV NIQREEYPSL FNFLKEKKLS ILNPVTTGPA
490 500 510 520
MIIDDDDSDD DDYEPSESGS ESDEGSASDE SEEESEEDKK AKKKQKK