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 Q6FWT4

Entry ID Method Resolution Chain Position Source
AF-Q6FWT4-F1 Predicted AlphaFoldDB

No variants for Q6FWT4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6FWT4

No associated diseases with Q6FWT4

4 regional properties for Q6FWT4

Type Name Position InterPro Accession
domain Peptidase M24 198 - 423 IPR000994
domain Histone chaperone RTT106/FACT complex subunit SPT16-like, middle domain 830 - 920 IPR013719
domain FACT complex subunit Spt16 domain 549 - 703 IPR013953
domain FACT complex subunit Spt16, N-terminal lobe domain 6 - 169 IPR029148

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
  • Chromosome
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.
replication fork protection complex A protein complex conserved in eukaryotes and associated with the replication fork; the complex stabilizes stalled replication forks and is thought to be involved in coordinating leading- and lagging-strand synthesis and in replication checkpoint signaling.

3 GO annotations of molecular function

Name Definition
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.
protein carrier chaperone Binding to and carrying a protein between two different cellular components by moving along with the target protein.

6 GO annotations of biological process

Name Definition
constitutive heterochromatin assembly The compaction of chromatin into a conformation that is refactory to transcription.
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-templated DNA replication A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands.
nucleosome assembly The aggregation, arrangement and bonding together of a nucleosome, the beadlike structural units of eukaryotic chromatin composed of histones and DNA.
positive regulation of RNA polymerase II transcription preinitiation complex assembly Any process that activates or increases the frequency, rate or extent of RNA polymerase II transcriptional preinitiation complex assembly.
regulation of sister chromatid cohesion Any process that modulates the frequency, rate or extent of sister chromatid cohesion.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSELNIDAEA FKARVELLHG KYREFENEPN SMVFALGSSN PENPYQKTTA LHYWLMGYEF
70 80 90 100 110 120
PATLIVFTPG KVVIITSGPK AKHLEKVVEL FKNNNNGVEL EIWQRNNKDV EHSQKLFKDI
130 140 150 160 170 180
IELINTAGKT VGIPEKDVYE GKFMKEWKPI WDAAIKEHEF KLVDISAGLS STWEVKDDKE
190 200 210 220 230 240
KAYISIASKC SDRFMNLLSD EMVRAVDDEL KITNSKLSDK IENKIDDLKF LKKITNDLSA
250 260 270 280 290 300
MCPPNHKFTL DLLDWTYSPI IQSGNKFDLR VSAHSNNDQL HGNGCILASC GIRYNNYCSN
310 320 330 340 350 360
TTRTFLIDPS EEMVNNYVFL LDLQKHIIEN ELKAGRTGKE VYESVVEFIK KVRPELAGNF
370 380 390 400 410 420
TKNIGSLIGL EFRDSFFVLN SKNDKRKIQV GDCFNISFGF NALKDMKTNT NYALQLADTV
430 440 450 460 470 480
ILNEDGPKIL TEYTKSKSQV SFYFNNDEVE KEKKPAASTK IPTNLDGNSK ILRSKLRGDA
490 500 510 520 530 540
RGESQDAQKE QIRKENQRKL HEKLQKEGLL RFTAEDATTE GSETRQYFKK YESYVRESQI
550 560 570 580 590 600
PNNVRDLRIH VDWRSQTIIV PIYGRPVPFH INSYKNGSKN EEGEYTYLRL NFHSPGSAGG
610 620 630 640 650 660
ISKNVVELPY DDSPDNQFMR SITLRSKDGD RMSETFKQIT DLKKESTKRE QERKALADVV
670 680 690 700 710 720
QQDKLIENKT GRTKRLDQIF VRPSPDTKRV PSTVFIHENG IRYQSPLRTD SRIDILFSNI
730 740 750 760 770 780
KNLIFQSCKG ELIVIIHIHL KNPIMMGKKK IQDVQFYREA SDVSVDETGT GRRNQNKFRK
790 800 810 820 830 840
YGDEDELEQE QEERRKRAML DKEFKYFADA IAEASNGLVS VESTFRDLGF QGVPNRSAVF
850 860 870 880 890 900
CMPTTDCLVQ LIEPPFLVVN LEEIEVAILE RVQFGLKNFD LVFVYKDFKK PVTHINTIPI
910 920 930 940 950 960
ESLDFLKQWL TDMDIPYAIS TINLKWSTIM QSLQEDPHQF FLDGGWSFLN ANSDEEGSDE
970 980 990 1000 1010 1020
SEEEISEYEA SEEEPEDESA YSDEDDYSED ISDGSYSGAD SEEEEGEDWD ELEKKAAKAD
RTAGLRD