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

7 structures for Q04636

Entry ID Method Resolution Chain Position Source
2GCJ X-ray 255 A A/B/C/D 220-478 PDB
2GCL X-ray 221 A A/B 220-478 PDB
3F5R X-ray 170 A A 1-168 PDB
4PQ0 X-ray 165 A A 232-473 PDB
7NKY EM 320 A O 1-552 PDB
8XGC EM 370 A M 1-552 PDB
AF-Q04636-F1 Predicted AlphaFoldDB

2 variants for Q04636

Variant ID(s) Position Change Description Diseaes Association Provenance
s13-136079 194 S>A No SGRP
s13-137105 536 A>T No SGRP

No associated diseases with Q04636

3 regional properties for Q04636

Type Name Position InterPro Accession
domain Histone chaperone RTT106/FACT complex subunit SPT16-like, middle domain 381 - 475 IPR013719
domain SSRP1, dimerization domain 110 - 178 IPR024954
domain FACT complex subunit SSRP1/POB3, N-terminal PH domain 3 - 103 IPR035417

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
  • Chromosome
  • Colocalizes with RNA polymerase II on chromatin (PubMed:10413469, PubMed:14585989, PubMed:14739930)
  • Recruited to actively transcribed loci (PubMed:14585989)
  • Associates with the coding region of HTA1 (PubMed:19683497)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
chromatin The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome.
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.

1 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).

5 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-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 organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of one or more nucleosomes.
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 chromatin organization Any process that modulates the frequency, rate or extent of chromatin organization.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q08945 SSRP1 FACT complex subunit SSRP1 Homo sapiens (Human) PR
10 20 30 40 50 60
MSTDFDRIYL NQSKFSGRFR IADSGLGWKI STSGGSAANQ ARKPFLLPAT ELSTVQWSRG
70 80 90 100 110 120
CRGYDLKINT KNQGVIQLDG FSQDDYNLIK NDFHRRFNIQ VEQREHSLRG WNWGKTDLAR
130 140 150 160 170 180
NEMVFALNGK PTFEIPYARI NNTNLTSKNE VGIEFNIQDE EYQPAGDELV EMRFYIPGVI
190 200 210 220 230 240
QTNVDENMTK KEESSNEVVP KKEDGAEGED VQMAVEEKSM AEAFYEELKE KADIGEVAGD
250 260 270 280 290 300
AIVSFQDVFF TTPRGRYDID IYKNSIRLRG KTYEYKLQHR QIQRIVSLPK ADDIHHLLVL
310 320 330 340 350 360
AIEPPLRQGQ TTYPFLVLQF QKDEETEVQL NLEDEDYEEN YKDKLKKQYD AKTHIVLSHV
370 380 390 400 410 420
LKGLTDRRVI VPGEYKSKYD QCAVSCSFKA NEGYLYPLDN AFFFLTKPTL YIPFSDVSMV
430 440 450 460 470 480
NISRAGQTST SSRTFDLEVV LRSNRGSTTF ANISKEEQQL LEQFLKSKNL RVKNEDREVQ
490 500 510 520 530 540
ERLQTALGSD SDEEDINMGS AGEDDESVDE DFQVSSDNDA DEVAEEFDSD AALSDAEGGS
550
DEERPSKKPK VE