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 Q9V460

Entry ID Method Resolution Chain Position Source
AF-Q9V460-F1 Predicted AlphaFoldDB

No variants for Q9V460

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9V460

No associated diseases with Q9V460

17 regional properties for Q9V460

Type Name Position InterPro Accession
domain NGN domain 215 - 301 IPR005100
domain KOW 309 - 336 IPR005824-1
domain KOW 460 - 487 IPR005824-2
domain KOW 512 - 542 IPR005824-3
domain KOW 634 - 661 IPR005824-4
domain KOW 739 - 766 IPR005824-5
domain KOW 1026 - 1053 IPR005824-6
domain NusG-like, N-terminal 213 - 304 IPR006645
domain Spt5 transcription elongation factor, N-terminal 114 - 209 IPR022581
domain Spt5 C-terminal domain 812 - 929 IPR024945
domain NGN domain, eukaryotic 215 - 302 IPR039385
domain Spt5, KOW domain repeat 1 313 - 350 IPR041973
domain Spt5, KOW domain repeat 2 461 - 511 IPR041975
domain Spt5, KOW domain repeat 3 512 - 562 IPR041976
domain Spt5, KOW domain repeat 4 638 - 680 IPR041977
domain Spt5, KOW domain repeat 5 737 - 788 IPR041978
domain Spt5, KOW domain repeat 6 1020 - 1075 IPR041980

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
  • Chromosome
  • Localizes predominantly to transcriptionally active regions of polytene chromosomes
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
DSIF complex A heterodimeric protein complex formed of Spt4 and Spt5 proteins which is expressed in eukaryotes from yeast to man. DSIF is an inhibitory elongation factor that promotes RNA polymerase II transcriptional pausing, but can also stimulate transcriptional elongation under certain conditions, and may play a role in RNA processing via its physical association with mRNA capping enzymes.
polytene chromosome A type of chromosome in a polyploid cell, formed when multiple copies of homologous chromosomes are aligned side by side to give a giant chromosome in which distinct chromosome bands are readily visible.
polytene chromosome interband A stretch of less tightly packed chromatin along the polytene chromosome, found between bands.
polytene chromosome puff A swelling at a site along the length of a polytene chromosome, thought to be the site of active transcription.
transcription elongation factor complex Any protein complex that interacts with RNA polymerase II to increase (positive transcription elongation factor) or reduce (negative transcription elongation factor) the rate of transcription elongation.

5 GO annotations of molecular function

Name Definition
chromatin binding Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.
mRNA binding Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns.
protein heterodimerization activity Binding to a nonidentical protein to form a heterodimer.
protein-containing complex binding Binding to a macromolecular complex.
RNA polymerase II complex binding Binding to an RNA polymerase II core enzyme, a multisubunit eukaryotic nuclear RNA polymerase typically composed of twelve subunits.

7 GO annotations of biological process

Name Definition
dosage compensation Compensating for the variation in the unpaired sex chromosome:autosome chromosome ratios between sexes by activation or inactivation of genes on one or both of the sex chromosomes.
negative regulation of DNA-templated transcription, elongation Any process that stops, prevents, or reduces the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
negative regulation of transcription by RNA polymerase II Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II.
positive regulation of DNA-templated transcription, elongation Any process that activates or increases the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
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.
regulation of transcription by RNA polymerase II Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.
transcription elongation by RNA polymerase II promoter The extension of an RNA molecule after transcription initiation and promoter clearance at an RNA polymerase II promoter by the addition of ribonucleotides catalyzed by RNA polymerase II.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O00267 SUPT5H Transcription elongation factor SPT5 Homo sapiens (Human) PR
O55201 Supt5h Transcription elongation factor SPT5 Mus musculus (Mouse) PR
Q9STN3 At4g08350 Putative transcription elongation factor SPT5 homolog 1 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MSDSEVSNMS DSGSEDGSIS NKSQRSARSK SRSRSRSGSR GSRSVSRSRS RSQSGHSRSG
70 80 90 100 110 120
SESPQRRDNR GKSDESGEEE EEPPGEDIDS EEYDEEENDD HPRKKKKKER FGGFIIDEAE
130 140 150 160 170 180
VDDEVDEDDE WEEGANEIGI VGNEIDELGP TARDIEIRRR GTNLWDTQKE DEIEEYLRKK
190 200 210 220 230 240
YADESIAKRH FGDGGEEMSD EITQQTLLPG IKDPNLWMVK CRIGEEKATA LLLMRKYLTY
250 260 270 280 290 300
LNTDDPLQIK SIIAPEGVKG YIYLEAYKQT HVKTCIDNVG NLRMGKWKQE MVPIKEMTDV
310 320 330 340 350 360
LKVVKEQVGL KVKQWVRLKR GLYKDDIAQV DYVDLAQNQV HLKLLPRIDY TRMRGALRTT
370 380 390 400 410 420
ATESDDSKRK KKRRPAAKPF DPEAVRAIGG EVHSDGDFLL FEGNRYSRKG FLYKNFTMSA
430 440 450 460 470 480
ILSDGVKPTL AELERFEESP EEVNLEIMGT VKDDPTMAHS FSMGDNVEVC VGDLENLQAK
490 500 510 520 530 540
IVAIDGTMIT VMPKHQDLKD PLIFKASELR KYFKTGDHAR VLAGRYEGET GLIIRVEPTR
550 560 570 580 590 600
VVLVSDLTNH ELEVLPRDLQ LCSDVATGVD CLGQFQWGDM VQLDSQNVGV IVRLERENFH
610 620 630 640 650 660
VLGMNGKCIE CKPTALHKRK ENRHTVALDA DQNQIRRRDV VKVMEGPHAG RSGEIKHLYR
670 680 690 700 710 720
SLAFLHCRMY TENGGIFVCK TRHLQLAGGS KTTVSNAGIV GGLGFMSPRI QSPMHPSGGR
730 740 750 760 770 780
GARGGARGGR GGFRVTRDRE ILGKTIKISG GPYKGAVGIV KDATESTARV ELHTSCQTIS
790 800 810 820 830 840
VDRNHIAIVG VTGKEGSVST YGRTPARTPG YGAQTPSYTA AGSKTPLVGS QTPNWDTDTR
850 860 870 880 890 900
TPYGTMTPSH DGSMTPRHGA WDPTANTTPA RNNDFDYSLE EPSPSPGYNP STPGYQMTSQ
910 920 930 940 950 960
FAPQTPGTLY GSDRSYSPFN PSPSPAPSPY PVGYMNTPSP STYSPNTPGG IPQSPYNPQT
970 980 990 1000 1010 1020
PGASLDSSMG DWCTTDIEVR IHTHDDTDLV GQTGIIRTVS NGVCSVFLRQ EDRSVSIVSE
1030 1040 1050 1060 1070
HLAPVLPCNG DEFKIIYGDD RESVGRVLSK DGDVFVCRIN EEIKLLPINF LCKMKSID