SUPT16H | ENSG00000092201 | NCBI 11198

Details for: SUPT16H

Gene ID: 11198

Symbol: SUPT16H

Ensembl ID: ENSG00000092201

Description: SPT16 homolog, facilitates chromatin remodeling subunit

Associated with

Disease
(R-HSA-1643685)
Formation of hiv-1 elongation complex containing hiv-1 tat
(R-HSA-167200)
Formation of hiv elongation complex in the absence of hiv tat
(R-HSA-167152)
Formation of rna pol ii elongation complex
(R-HSA-112382)
Gene expression (transcription)
(R-HSA-74160)
Generic transcription pathway
(R-HSA-212436)
Hiv elongation arrest and recovery
(R-HSA-167287)
Hiv infection
(R-HSA-162906)
Hiv life cycle
(R-HSA-162587)
Hiv transcription elongation
(R-HSA-167169)
Infectious disease
(R-HSA-5663205)
Late phase of hiv life cycle
(R-HSA-162599)
Pausing and recovery of hiv elongation
(R-HSA-167290)
Pausing and recovery of tat-mediated hiv elongation
(R-HSA-167238)
Regulation of tp53 activity
(R-HSA-5633007)
Regulation of tp53 activity through phosphorylation
(R-HSA-6804756)
Rna polymerase ii pre-transcription events
(R-HSA-674695)
Rna polymerase ii transcription
(R-HSA-73857)
Rna polymerase ii transcription elongation
(R-HSA-75955)
Tat-mediated elongation of the hiv-1 transcript
(R-HSA-167246)
Tat-mediated hiv elongation arrest and recovery
(R-HSA-167243)
Tp53 regulates transcription of dna repair genes
(R-HSA-6796648)
Transcriptional regulation by tp53
(R-HSA-3700989)
Transcription of the hiv genome
(R-HSA-167172)
Viral infection pathways
(R-HSA-9824446)
Dna repair
(GO:0006281)
Dna replication
(GO:0006260)
Fact complex
(GO:0035101)
Nucleoplasm
(GO:0005654)
Nucleosome assembly
(GO:0006334)
Nucleosome binding
(GO:0031491)
Nucleosome disassembly
(GO:0006337)
Nucleus
(GO:0005634)
Positive regulation of dna-templated transcription, elongation
(GO:0032786)
Protein binding
(GO:0005515)
Rna binding
(GO:0003723)
Transcription by rna polymerase ii
(GO:0006366)
Transcription elongation by rna polymerase ii
(GO:0006368)

Other Information

Proteins

FACT complex subunit SPT16

Genular Protein ID: 2344652572

Symbol: SP16H_HUMAN

Name: FACT complex subunit SPT16

UniProtKB Accession Codes:

Q9Y5B9 Q6GMT8 Q6P2F1 Q6PJM1 Q9NRX0

Database IDs:

Citations:

PubMed ID: 10421373

Title: The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins.

PubMed ID: 10421373

DOI: 10.1038/22350

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 10792464

Title: Functional interaction of general transcription initiation factor TFIIE with general chromatin factor SPT16/CDC68.

PubMed ID: 10792464

DOI: 10.1046/j.1365-2443.2000.00323.x

PubMed ID: 9489704

Title: FACT, a factor that facilitates transcript elongation through nucleosomes.

PubMed ID: 9489704

DOI: 10.1016/s0092-8674(00)80903-4

PubMed ID: 9836642

Title: Requirement of RSF and FACT for transcription of chromatin templates in vitro.

PubMed ID: 9836642

DOI: 10.1126/science.282.5395.1900

PubMed ID: 10912001

Title: FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH.

PubMed ID: 10912001

DOI: 10.1016/s1097-2765(00)80272-5

PubMed ID: 11239457

Title: A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1.

PubMed ID: 11239457

DOI: 10.1016/s1097-2765(01)00176-9

PubMed ID: 12393879

Title: p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex.

PubMed ID: 12393879

DOI: 10.1074/jbc.m209820200

PubMed ID: 12934006

Title: FACT facilitates transcription-dependent nucleosome alteration.

PubMed ID: 12934006

DOI: 10.1126/science.1085703

PubMed ID: 14660563

Title: Nek9, a novel FACT-associated protein, modulates interphase progression.

PubMed ID: 14660563

DOI: 10.1074/jbc.m311477200

PubMed ID: 16713563

Title: Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II.

PubMed ID: 16713563

DOI: 10.1016/j.cell.2006.04.029

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16682447

Title: Modulation of nucleosome-binding activity of FACT by poly(ADP-ribosyl)ation.

PubMed ID: 16682447

DOI: 10.1093/nar/gkl241

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 27499292

Title: The flexible ends of CENP-A nucleosome are required for mitotic fidelity.

PubMed ID: 27499292

DOI: 10.1016/j.molcel.2016.06.023

PubMed ID: 28611249

Title: A Herpesviral Immediate Early Protein Promotes Transcription Elongation of Viral Transcripts.

PubMed ID: 28611249

DOI: 10.1128/mbio.00745-17

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 31924697

Title: De novo variants in SUPT16H cause neurodevelopmental disorders associated with corpus callosum abnormalities.

PubMed ID: 31924697

DOI: 10.1136/jmedgenet-2019-106193

Sequence Information:

Length: 1047
Mass: 119914
Checksum: 3E1B23C45BDC61C2
Sequence:

MAVTLDKDAY YRRVKRLYSN WRKGEDEYAN VDAIVVSVGV DEEIVYAKST ALQTWLFGYE 
LTDTIMVFCD DKIIFMASKK KVEFLKQIAN TKGNENANGA PAITLLIREK NESNKSSFDK 
MIEAIKESKN GKKIGVFSKD KFPGEFMKSW NDCLNKEGFD KIDISAVVAY TIAVKEDGEL 
NLMKKAASIT SEVFNKFFKE RVMEIVDADE KVRHSKLAES VEKAIEEKKY LAGADPSTVE 
MCYPPIIQSG GNYNLKFSVV SDKNHMHFGA ITCAMGIRFK SYCSNLVRTL MVDPSQEVQE 
NYNFLLQLQE ELLKELRHGV KICDVYNAVM DVVKKQKPEL LNKITKNLGF GMGIEFREGS 
LVINSKNQYK LKKGMVFSIN LGFSDLTNKE GKKPEEKTYA LFIGDTVLVD EDGPATVLTS 
VKKKVKNVGI FLKNEDEEEE EEEKDEAEDL LGRGSRAALL TERTRNEMTA EEKRRAHQKE 
LAAQLNEEAK RRLTEQKGEQ QIQKARKSNV SYKNPSLMPK EPHIREMKIY IDKKYETVIM 
PVFGIATPFH IATIKNISMS VEGDYTYLRI NFYCPGSALG RNEGNIFPNP EATFVKEITY 
RASNIKAPGE QTVPALNLQN AFRIIKEVQK RYKTREAEEK EKEGIVKQDS LVINLNRSNP 
KLKDLYIRPN IAQKRMQGSL EAHVNGFRFT SVRGDKVDIL YNNIKHALFQ PCDGEMIIVL 
HFHLKNAIMF GKKRHTDVQF YTEVGEITTD LGKHQHMHDR DDLYAEQMER EMRHKLKTAF 
KNFIEKVEAL TKEELEFEVP FRDLGFNGAP YRSTCLLQPT SSALVNATEW PPFVVTLDEV 
ELIHFERVQF HLKNFDMVIV YKDYSKKVTM INAIPVASLD PIKEWLNSCD LKYTEGVQSL 
NWTKIMKTIV DDPEGFFEQG GWSFLEPEGE GSDAEEGDSE SEIEDETFNP SEDDYEEEEE 
DSDEDYSSEA EESDYSKESL GSEEESGKDW DELEEEARKA DRESRYEEEE EQSRSMSRKR 
KASVHSSGRG SNRGSRHSSA PPKKKRK

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: SUPT16H

Associated with

Other Information

The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins. PubMed ID: 10421373

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Functional interaction of general transcription initiation factor TFIIE with general chromatin factor SPT16/CDC68. PubMed ID: 10792464

FACT, a factor that facilitates transcript elongation through nucleosomes. PubMed ID: 9489704

Requirement of RSF and FACT for transcription of chromatin templates in vitro. PubMed ID: 9836642

FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH. PubMed ID: 10912001

A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1. PubMed ID: 11239457

p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex. PubMed ID: 12393879

FACT facilitates transcription-dependent nucleosome alteration. PubMed ID: 12934006

Nek9, a novel FACT-associated protein, modulates interphase progression. PubMed ID: 14660563

Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II. PubMed ID: 16713563

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

Modulation of nucleosome-binding activity of FACT by poly(ADP-ribosyl)ation. PubMed ID: 16682447

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features. PubMed ID: 22223895

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. PubMed ID: 22814378

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

Uncovering global SUMOylation signaling networks in a site-specific manner. PubMed ID: 25218447

SUMO-2 orchestrates chromatin modifiers in response to DNA damage. PubMed ID: 25772364

The flexible ends of CENP-A nucleosome are required for mitotic fidelity. PubMed ID: 27499292

A Herpesviral Immediate Early Protein Promotes Transcription Elongation of Viral Transcripts. PubMed ID: 28611249

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733

De novo variants in SUPT16H cause neurodevelopmental disorders associated with corpus callosum abnormalities. PubMed ID: 31924697