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Database: UniProt
Entry: F1S8K5_PIG
LinkDB: F1S8K5_PIG
Original site: F1S8K5_PIG 
ID   F1S8K5_PIG              Unreviewed;      1083 AA.
AC   F1S8K5;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   24-JAN-2024, entry version 83.
DE   RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN   Name=SUPT16H {ECO:0000313|Ensembl:ENSSSCP00000022646.2,
GN   ECO:0000313|VGNC:VGNC:93622};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000022646.2, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000022646.2, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000022646.2,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:HDA51427.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
RN   [3] {ECO:0000313|Ensembl:ENSSSCP00000022646.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: Component of the FACT complex, a general chromatin factor
CC       that acts to reorganize nucleosomes. The FACT complex is involved in
CC       multiple processes that require DNA as a template such as mRNA
CC       elongation, DNA replication and DNA repair. During transcription
CC       elongation the FACT complex acts as a histone chaperone that both
CC       destabilizes and restores nucleosomal structure. It facilitates the
CC       passage of RNA polymerase II and transcription by promoting the
CC       dissociation of one histone H2A-H2B dimer from the nucleosome, then
CC       subsequently promotes the reestablishment of the nucleosome following
CC       the passage of RNA polymerase II. {ECO:0000256|RuleBase:RU367052}.
CC   -!- SUBUNIT: Component of the FACT complex.
CC       {ECO:0000256|RuleBase:RU367052}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367052}.
CC       Chromosome {ECO:0000256|RuleBase:RU367052}.
CC   -!- SIMILARITY: Belongs to the peptidase M24 family. SPT16 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010779, ECO:0000256|RuleBase:RU367052}.
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DR   EMBL; DQIR01095951; HDA51427.1; -; Transcribed_RNA.
DR   EMBL; DQIR01167597; HDB23074.1; -; Transcribed_RNA.
DR   RefSeq; XP_001929215.3; XM_001929180.5.
DR   STRING; 9823.ENSSSCP00000022646; -.
DR   PaxDb; 9823-ENSSSCP00000022646; -.
DR   Ensembl; ENSSSCT00000031400.3; ENSSSCP00000022646.2; ENSSSCG00000022900.3.
DR   GeneID; 100155525; -.
DR   KEGG; ssc:100155525; -.
DR   CTD; 11198; -.
DR   VGNC; VGNC:93622; SUPT16H.
DR   eggNOG; KOG1189; Eukaryota.
DR   GeneTree; ENSGT00390000014495; -.
DR   HOGENOM; CLU_004627_0_0_1; -.
DR   OMA; GKNNLQW; -.
DR   OrthoDB; 169847at2759; -.
DR   TreeFam; TF300341; -.
DR   Reactome; R-SSC-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-SSC-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-SSC-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-SSC-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   Reactome; R-SSC-75955; RNA Polymerase II Transcription Elongation.
DR   Proteomes; UP000008227; Chromosome 7.
DR   Bgee; ENSSSCG00000022900; Expressed in hindlimb bud and 45 other cell types or tissues.
DR   GO; GO:0035101; C:FACT complex; IBA:GO_Central.
DR   GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006337; P:nucleosome disassembly; IEA:Ensembl.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd01091; CDC68-like; 1.
DR   Gene3D; 2.30.29.150; -; 1.
DR   Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR   Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR   Gene3D; 2.30.29.210; FACT complex subunit Spt16p/Cdc68p; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR029148; FACT-Spt16_Nlobe.
DR   InterPro; IPR013953; FACT_Spt16.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR   InterPro; IPR040258; Spt16.
DR   InterPro; IPR048969; SPT16_C.
DR   InterPro; IPR033825; Spt16_M24.
DR   PANTHER; PTHR13980; CDC68 RELATED; 1.
DR   PANTHER; PTHR13980:SF15; FACT COMPLEX SUBUNIT SPT16; 1.
DR   Pfam; PF14826; FACT-Spt16_Nlob; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF08512; Rttp106-like_middle; 1.
DR   Pfam; PF08644; SPT16; 1.
DR   Pfam; PF21091; SPT16_C; 1.
DR   SMART; SM01285; FACT-Spt16_Nlob; 1.
DR   SMART; SM01287; Rtt106; 1.
DR   SMART; SM01286; SPT16; 1.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
PE   1: Evidence at protein level;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU367052};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367052};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU367052};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU367052};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367052};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F1S8K5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU367052};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU367052}.
FT   DOMAIN          41..204
FT                   /note="FACT complex subunit Spt16 N-terminal lobe"
FT                   /evidence="ECO:0000259|SMART:SM01285"
FT   DOMAIN          565..725
FT                   /note="FACT complex subunit Spt16"
FT                   /evidence="ECO:0000259|SMART:SM01286"
FT   DOMAIN          842..932
FT                   /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT                   like middle"
FT                   /evidence="ECO:0000259|SMART:SM01287"
FT   REGION          528..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          954..1083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        965..1007
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1008..1054
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1083 AA;  123660 MW;  AF2D2F11218768B9 CRC64;
     MLPGHWESAG FRGRERVAEP GPRVILGTRG GAASVAMAVT LDKDAYYRRV KRLYSNWRKG
     EDEYANVDAI VVSVGVDEEI VYAKSTALQT WLFGYELTDT IMVFCDDKII FMASKKKVEF
     LKQIANTKGN ENANGAPAIT LLIREKNESN KSSFDKMIEA IKESKNGKKI GVFSKDKFPG
     EFMKSWNDCL NKEGFDKIDI SAVVAYTIAV KEDGELNLMK KAASITSEVF NKFFKERVME
     IVDADEKVRH SKLAESVEKA IEEKKYLAGA DPSTVEMCYP PIIQSGGNYN LKFSVVSDKN
     HMHFGAITCA MGIRFKSYCS NLVRTLMVDP SQEVQENYNF LLQLQEELLK ELRHGVKICD
     VYNAVMDVVK KQKPELLNKI TKNLGFGMGI EFREGSLVIN SKNQYKLKKG MVFSINLGFS
     DLTNKEGKKP EEKTYALFIG DTVLVDEDGP ATVLTSVKKK VKNVGIFLKN EDEEEEEEEK
     DEAEDLLGRG SRAALLTERT RNEMTAEEKR RAHQKELAAQ LNEEAKRRLT EQKGEQQIQK
     ARKSNVSYKN PSLMPKEPHI REMKIYIDKK YETVIMPVFG IATPFHIATI KNISMSVEGD
     YTYLRINFYC PGSALGRNEG NIFPNPEATF VKEITYRASN MKAPGEQTVP ALNLQNAFRI
     IKEVQKRYKT REAEEKEKEG IVKQDSLVIN LNRSNPKLKD LYIRPNIAQK RMQGSLEAHV
     NGFRFTSVRG DKVDILYNNI KHALFQPCDG EMIIVLHFHL KNAIMFGKKR HTDVQFYTEV
     GEITTDLGKH QHMHDRDDLY AEQMEREMRH KLKTAFKNFI EKVEALTKEE LEFEVPFRDL
     GFNGAPYRST CLLQPTSSAL VNATEWPPFV VTLDEVELIH FERVQFHLKN FDMVIVYKDY
     SKKVTMINAI PVASLDPIKE WLNSCDLKYT EGVQSLNWTK IMKTIVDDPE GFFEQGGWSF
     LEPEGEGSDA EEGDSESEIE DETFNPSEDD YEEEEEDSDE DYSSEAEESD YSKESLGSEE
     ESGKDWDELE EEARKADRES RYEEEEEQSR SMSRKRKASV HSSGRGSNRG SRHSSAPPKK
     KRK
//
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