SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q7KZ85

- SPT6H_HUMAN

UniProt

Q7KZ85 - SPT6H_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Transcription elongation factor SPT6
Gene
SUPT6H, KIAA0162, SPT6H
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Transcription elongation factor which binds histone H3 and plays a key role in the regulation of transcription elongation and mRNA processing. Enhances the transcription elongation by RNA polymerase II (RNAPII) and is also required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. Besides chaperoning histones in transcription, acts to transport and splice mRNA by forming a complex with IWS1 and the C-terminal domain (CTD) of the RNAPII subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex recruits mRNA export factors (ALYREF/THOC4, EXOSC10) as well as histone modifying enzymes (such as SETD2), to ensure proper mRNA splicing, efficient mRNA export and elongation-coupled H3K36 methylation, a signature chromatin mark of active transcription. SUPT6H via its association with SETD1A, regulates both class-switch recombination and somatic hypermutation through formation of H3K4me3 epigenetic marks on activation-induced cytidine deaminase (AICDA) target loci. Promotes the activation of the myogenic gene program by entailing erasure of the repressive H3K27me3 epigenetic mark through stabilization of the chromatin interaction of the H3K27 demethylase KDM6A.5 Publications

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. histone binding Source: UniProtKB
  3. hydrolase activity, acting on ester bonds Source: InterPro
  4. poly(A) RNA binding Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  1. RNA splicing Source: UniProtKB-KW
  2. chromatin remodeling Source: UniProtKB
  3. mRNA processing Source: UniProtKB-KW
  4. mRNA transport Source: UniProtKB-KW
  5. negative regulation of histone H3-K27 methylation Source: UniProtKB
  6. positive regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB
  7. regulation of isotype switching Source: UniProtKB
  8. regulation of mRNA export from nucleus Source: UniProtKB
  9. regulation of mRNA processing Source: UniProtKB
  10. regulation of muscle cell differentiation Source: UniProtKB
  11. regulation of transcription, DNA-templated Source: UniProtKB
  12. transcription, DNA-templated Source: UniProtKB-KW
  13. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Host-virus interaction, mRNA processing, mRNA splicing, mRNA transport, Transcription, Transcription regulation, Transport

Enzyme and pathway databases

SignaLinkiQ7KZ85.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription elongation factor SPT6
Short name:
hSPT6
Alternative name(s):
Histone chaperone suppressor of Ty6
Tat-cotransactivator 2 protein
Short name:
Tat-CT2 protein
Gene namesi
Name:SUPT6H
Synonyms:KIAA0162, SPT6H
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:11470. SUPT6H.

Subcellular locationi

Nucleus Inferred

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36256.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 17261725Transcription elongation factor SPT6
PRO_0000072171Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei7 – 71Phosphoserine1 Publication
Modified residuei12 – 121Phosphoserine1 Publication
Modified residuei73 – 731Phosphoserine1 Publication
Modified residuei75 – 751Phosphoserine1 Publication
Modified residuei78 – 781Phosphoserine1 Publication
Modified residuei125 – 1251Phosphoserine3 Publications
Modified residuei267 – 2671Phosphoserine1 Publication
Modified residuei743 – 7431N6-acetyllysine1 Publication
Modified residuei1523 – 15231Phosphothreonine2 Publications
Modified residuei1532 – 15321Phosphothreonine2 Publications
Modified residuei1535 – 15351Phosphoserine4 Publications
Modified residuei1539 – 15391Phosphothreonine3 Publications
Modified residuei1676 – 16761N6-acetyllysine1 Publication
Modified residuei1697 – 16971Phosphothreonine2 Publications
Modified residuei1701 – 17011Phosphoserine3 Publications
Modified residuei1703 – 17031Phosphoserine3 Publications
Modified residuei1718 – 17181Phosphothreonine4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ7KZ85.
PaxDbiQ7KZ85.
PeptideAtlasiQ7KZ85.
PRIDEiQ7KZ85.

PTM databases

PhosphoSiteiQ7KZ85.

Miscellaneous databases

PMAP-CutDBQ7KZ85.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

ArrayExpressiQ7KZ85.
BgeeiQ7KZ85.
GenevestigatoriQ7KZ85.

Organism-specific databases

HPAiCAB012416.
HPA036382.

Interactioni

Subunit structurei

Interacts with RNA polymerase II and the DRB sensitivity-inducing factor complex (DSIF complex), which is composed of SUPT5H and SUPT4H1. Interacts with human cytomegalovirus/HHV-5 protein UL69. Interacts with KDM6A By similarity. Interacts (via SH2 domain) with SETD1A By similarity. Interacts (via SH2 domain) with POLR2A phosphorylated at 'Ser-2'. Interacts with IWS1, AICDA and PAAF1. Interacts with histone H2B and H3.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ERBB2P046262EBI-2515547,EBI-641062

Protein-protein interaction databases

BioGridi112698. 15 interactions.
DIPiDIP-42615N.
IntActiQ7KZ85. 12 interactions.
MINTiMINT-1491202.

Structurei

3D structure databases

ProteinModelPortaliQ7KZ85.
SMRiQ7KZ85. Positions 270-1285, 1326-1512.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1213 – 128270S1 motif
Add
BLAST
Domaini1325 – 1431107SH2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 916915Interaction with PAAF1
Add
BLAST
Regioni2 – 485484Interaction with IWS1 By similarity
Add
BLAST
Regioni317 – 1300984Interaction with KDM6A By similarity
Add
BLAST
Regioni1633 – 172694Interaction with histone H2B and H3
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi6 – 250245Asp/Glu-rich
Add
BLAST
Compositional biasi1525 – 15284Poly-Ser
Compositional biasi1654 – 16574Poly-Ser

Sequence similaritiesi

Belongs to the SPT6 family.
Contains 1 S1 motif domain.
Contains 1 SH2 domain.

Phylogenomic databases

eggNOGiCOG2183.
HOVERGENiHBG093994.
InParanoidiQ7KZ85.
KOiK11292.
OMAiRRSIFEM.
OrthoDBiEOG7DFXBC.
PhylomeDBiQ7KZ85.
TreeFamiTF105956.

Family and domain databases

Gene3Di1.10.150.310. 1 hit.
1.10.3500.10. 2 hits.
2.40.50.140. 1 hit.
3.30.420.140. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
IPR022967. RNA-binding_domain_S1.
IPR012337. RNaseH-like_dom.
IPR010994. RuvA_2-like.
IPR000980. SH2.
IPR028083. Spt6_acidic_N_dom.
IPR027999. Spt6_dom.
IPR028088. Spt6_HTH_DNA-bd_dom.
IPR028231. SPT6_YqgF.
IPR023323. Tex-like_dom.
IPR023097. Tex_RuvX-like_dom.
IPR017072. TF_Spt6.
IPR006641. YqgF/RNaseH-like_dom.
[Graphical view]
PANTHERiPTHR10145. PTHR10145. 1 hit.
PfamiPF14878. DLD. 1 hit.
PF14641. HTH_44. 1 hit.
PF00575. S1. 1 hit.
PF14633. SH2_2. 1 hit.
PF14632. SPT6_acidic. 1 hit.
PF14639. YqgF. 1 hit.
[Graphical view]
PIRSFiPIRSF036947. Spt6. 1 hit.
SMARTiSM00316. S1. 1 hit.
SM00252. SH2. 1 hit.
SM00732. YqgFc. 1 hit.
[Graphical view]
SUPFAMiSSF47781. SSF47781. 2 hits.
SSF50249. SSF50249. 1 hit.
SSF53098. SSF53098. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50126. S1. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q7KZ85-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSDFVESEAE ESEEEYNDEG EVVPRVTKKF VEEEDDDEEE EEENLDDQDE     50
QGNLKGFIND DDDEDEGEED EGSDSGDSED DVGHKKRKRT SFDDRLEDDD 100
FDLIEENLGV KVKRGQKYRR VKKMSDDEDD DEEEYGKEEH EKEAIAEEIF 150
QDGEGEEGQE AMEAPMAPPE EEEEDDEESD IDDFIVDDDG QPLKKPKWRK 200
KLPGYTDAAL QEAQEIFGVD FDYDEFEKYN EYDEELEEEY EYEDDEAEGE 250
IRVRPKKTTK KRVSRRSIFE MYEPSELESS HLTDQDNEIR ATDLPERFQL 300
RSIPVKGAED DELEEEADWI YRNAFATPTI SLQESCDYLD RGQPASSFSR 350
KGPSTIQKIK EALGFMRNQH FEVPFIAFYR KEYVEPELHI NDLWRVWQWD 400
EKWTQLRIRK ENLTRLFEKM QAYQYEQISA DPDKPLADGI RALDTTDMER 450
LKDVQSMDEL KDVYNHFLLY YGRDIPKMQN AAKASRKKLK RVREEGDEEG 500
EGDEAEDEEQ RGPELKQASR RDMYTICQSA GLDGLAKKFG LTPEQFGENL 550
RDSYQRHETE QFPAEPLELA KDYVCSQFPT PEAVLEGARY MVALQIAREP 600
LVRQVLRQTF QERAKLNITP TKKGRKDVDE AHYAYSFKYL KNKPVKELRD 650
DQFLKICLAE DEGLLTTDIS IDLKGVEGYG NDQTYFEEIK QFYYRDEFSH 700
QVQEWNRQRT MAIERALQQF LYVQMAKELK NKLLAEAKEY VIKACSRKLY 750
NWLRVAPYRP DQQVEEDDDF MDENQGKGIR VLGIAFSSAR DHPVFCALVN 800
GEGEVTDFLR LPHFTKRRTA WREEEREKKA QDIETLKKFL LNKKPHVVTV 850
AGENRDAQML IEDVKRIVHE LDQGQQLSSI GVELVDNELA ILYMNSKKSE 900
AEFRDYPPVL RQAVSLARRI QDPLIEFAQV CSSDEDILCL KFHPLQEHVV 950
KEELLNALYC EFINRVNEVG VDVNRAIAHP YSQALIQYVC GLGPRKGTHL 1000
LKILKQNNTR LESRTQLVTM CHMGPKVFMN CAGFLKIDTA SLGDSTDSYI 1050
EVLDGSRVHP ETYEWARKMA VDALEYDESA EDANPAGALE EILENPERLK 1100
DLDLDAFAEE LERQGYGDKH ITLYDIRAEL SCRYKDLRTA YRSPNTEEIF 1150
NMLTKETPET FYIGKLIICN VTGIAHRRPQ GESYDQAIRN DETGLWQCPF 1200
CQQDNFPELS EVWNHFDSGS CPGQAIGVKT RLDNGVTGFI PTKFLSDKVV 1250
KRPEERVKVG MTVHCRIMKI DIEKFSADLT CRTSDLMDRN NEWKLPKDTY 1300
YDFDAEAADH KQEEDMKRKQ QRTTYIKRVI AHPSFHNINF KQAEKMMETM 1350
DQGDVIIRPS SKGENHLTVT WKVSDGIYQH VDVREEGKEN AFSLGATLWI 1400
NSEEFEDLDE IVARYVQPMA SFARDLLNHK YYQDCSGGDR KKLEELLIKT 1450
KKEKPTFIPY FICACKELPG KFLLGYQPRG KPRIEYVTVT PEGFRYRGQI 1500
FPTVNGLFRW FKDHYQDPVP GITPSSSSRT RTPASINATP ANINLADLTR 1550
AVNALPQNMT SQMFSAIAAV TGQGQNPNAT PAQWASSQYG YGGSGGGSSA 1600
YHVFPTPAQQ PVATPLMTPS YSYTTPSQPI TTPQYHQLQA STTPQSAQAQ 1650
PQPSSSSRQR QQQPKSNSHA AIDWGKMAEQ WLQEKEAERR KQKQRLTPRP 1700
SPSPMIESTP MSIAGDATPL LDEMDR 1726
Length:1,726
Mass (Da):199,073
Last modified:August 31, 2004 - v2
Checksum:iF7EB22FA669EB030
GO
Isoform 2 (identifier: Q7KZ85-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1181: Missing.
     1182-1211: ESYDQAIRNDETGLWQCPFCQQDNFPELSE → MPSRGTRPEDSSVLIPTDNSTPHKEDLSSK

Show »
Length:545
Mass (Da):61,301
Checksum:i4BD128B2327CECE4
GO
Isoform 3 (identifier: Q7KZ85-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     617-1616: Missing.

Show »
Length:726
Mass (Da):84,632
Checksum:iBA3499B7CD6743BD
GO

Sequence cautioni

The sequence AAB18949.1 differs from that shown. Reason: Frameshift at position 988.
The sequence AAC50821.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH33074.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAA11479.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11811181Missing in isoform 2.
VSP_011505Add
BLAST
Alternative sequencei617 – 16161000Missing in isoform 3.
VSP_011507Add
BLAST
Alternative sequencei1182 – 121130ESYDQ…PELSE → MPSRGTRPEDSSVLIPTDNS TPHKEDLSSK in isoform 2.
VSP_011506Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 7313DDDED…EDEGS → ATAPGHPKLSEGR in AAC50821. 1 Publication
Add
BLAST
Sequence conflicti100 – 10910DFDLIEENLG → LEDDDFLLNE in AAH33074. 1 Publication
Sequence conflicti988 – 9947YVCGLGP → VCLWPGT in AAB18949. 1 Publication
Sequence conflicti1545 – 15451L → P in AAH17105. 1 Publication
Sequence conflicti1627 – 16271S → I in AAH17105. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U38623 mRNA. Translation: AAC99996.1.
U38658 mRNA. Translation: AAB18949.1. Frameshift.
U46691 mRNA. Translation: AAC50821.1. Different initiation.
D79984 mRNA. Translation: BAA11479.2. Different initiation.
CH471159 Genomic DNA. Translation: EAW51117.1.
BC003692 mRNA. Translation: AAH03692.1.
BC003696 mRNA. Translation: AAH03696.1.
BC017105 mRNA. Translation: AAH17105.1.
BC033074 mRNA. Translation: AAH33074.1. Different initiation.
BC073963 mRNA. Translation: AAH73963.1.
BC136522 mRNA. Translation: AAI36523.1.
BC136524 mRNA. Translation: AAI36525.1.
BC150268 mRNA. Translation: AAI50269.1.
AF070532 mRNA. Translation: AAC28631.1.
CCDSiCCDS32596.1. [Q7KZ85-1]
RefSeqiNP_003161.2. NM_003170.3. [Q7KZ85-1]
XP_005258083.1. XM_005258026.1. [Q7KZ85-1]
XP_005258084.1. XM_005258027.1. [Q7KZ85-1]
XP_006722105.1. XM_006722042.1.
UniGeneiHs.250429.

Genome annotation databases

EnsembliENST00000314616; ENSP00000319104; ENSG00000109111. [Q7KZ85-1]
ENST00000347486; ENSP00000338143; ENSG00000109111. [Q7KZ85-1]
GeneIDi6830.
KEGGihsa:6830.
UCSCiuc002hby.3. human. [Q7KZ85-1]

Polymorphism databases

DMDMi51701986.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U38623 mRNA. Translation: AAC99996.1 .
U38658 mRNA. Translation: AAB18949.1 . Frameshift.
U46691 mRNA. Translation: AAC50821.1 . Different initiation.
D79984 mRNA. Translation: BAA11479.2 . Different initiation.
CH471159 Genomic DNA. Translation: EAW51117.1 .
BC003692 mRNA. Translation: AAH03692.1 .
BC003696 mRNA. Translation: AAH03696.1 .
BC017105 mRNA. Translation: AAH17105.1 .
BC033074 mRNA. Translation: AAH33074.1 . Different initiation.
BC073963 mRNA. Translation: AAH73963.1 .
BC136522 mRNA. Translation: AAI36523.1 .
BC136524 mRNA. Translation: AAI36525.1 .
BC150268 mRNA. Translation: AAI50269.1 .
AF070532 mRNA. Translation: AAC28631.1 .
CCDSi CCDS32596.1. [Q7KZ85-1 ]
RefSeqi NP_003161.2. NM_003170.3. [Q7KZ85-1 ]
XP_005258083.1. XM_005258026.1. [Q7KZ85-1 ]
XP_005258084.1. XM_005258027.1. [Q7KZ85-1 ]
XP_006722105.1. XM_006722042.1.
UniGenei Hs.250429.

3D structure databases

ProteinModelPortali Q7KZ85.
SMRi Q7KZ85. Positions 270-1285, 1326-1512.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112698. 15 interactions.
DIPi DIP-42615N.
IntActi Q7KZ85. 12 interactions.
MINTi MINT-1491202.

PTM databases

PhosphoSitei Q7KZ85.

Polymorphism databases

DMDMi 51701986.

Proteomic databases

MaxQBi Q7KZ85.
PaxDbi Q7KZ85.
PeptideAtlasi Q7KZ85.
PRIDEi Q7KZ85.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000314616 ; ENSP00000319104 ; ENSG00000109111 . [Q7KZ85-1 ]
ENST00000347486 ; ENSP00000338143 ; ENSG00000109111 . [Q7KZ85-1 ]
GeneIDi 6830.
KEGGi hsa:6830.
UCSCi uc002hby.3. human. [Q7KZ85-1 ]

Organism-specific databases

CTDi 6830.
GeneCardsi GC17P026989.
HGNCi HGNC:11470. SUPT6H.
HPAi CAB012416.
HPA036382.
MIMi 601333. gene.
neXtProti NX_Q7KZ85.
PharmGKBi PA36256.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2183.
HOVERGENi HBG093994.
InParanoidi Q7KZ85.
KOi K11292.
OMAi RRSIFEM.
OrthoDBi EOG7DFXBC.
PhylomeDBi Q7KZ85.
TreeFami TF105956.

Enzyme and pathway databases

SignaLinki Q7KZ85.

Miscellaneous databases

ChiTaRSi SUPT6H. human.
GeneWikii SUPT6H.
GenomeRNAii 6830.
NextBioi 26667.
PMAP-CutDB Q7KZ85.
PROi Q7KZ85.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q7KZ85.
Bgeei Q7KZ85.
Genevestigatori Q7KZ85.

Family and domain databases

Gene3Di 1.10.150.310. 1 hit.
1.10.3500.10. 2 hits.
2.40.50.140. 1 hit.
3.30.420.140. 1 hit.
3.30.505.10. 1 hit.
InterProi IPR012340. NA-bd_OB-fold.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
IPR022967. RNA-binding_domain_S1.
IPR012337. RNaseH-like_dom.
IPR010994. RuvA_2-like.
IPR000980. SH2.
IPR028083. Spt6_acidic_N_dom.
IPR027999. Spt6_dom.
IPR028088. Spt6_HTH_DNA-bd_dom.
IPR028231. SPT6_YqgF.
IPR023323. Tex-like_dom.
IPR023097. Tex_RuvX-like_dom.
IPR017072. TF_Spt6.
IPR006641. YqgF/RNaseH-like_dom.
[Graphical view ]
PANTHERi PTHR10145. PTHR10145. 1 hit.
Pfami PF14878. DLD. 1 hit.
PF14641. HTH_44. 1 hit.
PF00575. S1. 1 hit.
PF14633. SH2_2. 1 hit.
PF14632. SPT6_acidic. 1 hit.
PF14639. YqgF. 1 hit.
[Graphical view ]
PIRSFi PIRSF036947. Spt6. 1 hit.
SMARTi SM00316. S1. 1 hit.
SM00252. SH2. 1 hit.
SM00732. YqgFc. 1 hit.
[Graphical view ]
SUPFAMi SSF47781. SSF47781. 2 hits.
SSF50249. SSF50249. 1 hit.
SSF53098. SSF53098. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEi PS50126. S1. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
    DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Tissue: Cervix, Lung, Melanoma, Placenta and Testis.
  5. Yu W., Gibbs R.A.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1460-1726 (ISOFORMS 1/2).
    Tissue: Brain.
  6. "Role of the human homolog of the yeast transcription factor SPT5 in HIV-1 Tat-activation."
    Wu-Baer F., Lane W.S., Gaynor R.B.
    J. Mol. Biol. 277:179-197(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Functional interaction between pleiotropic transactivator pUL69 of human cytomegalovirus and the human homolog of yeast chromatin regulatory protein SPT6."
    Winkler M., aus Dem Siepen T., Stamminger T.
    J. Virol. 74:8053-8064(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HISTONE H2B; H3 AND HHV-5 PROTEIN UL69.
  8. Cited for: FUNCTION, INTERACTION WITH THE DSIF COMPLEX AND RNA POLYMERASE II.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA splicing and export."
    Yoh S.M., Cho H., Pickle L., Evans R.M., Jones K.A.
    Genes Dev. 21:160-174(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH POLR2A.
  11. "The Iws1:Spt6:CTD complex controls cotranscriptional mRNA biosynthesis and HYPB/Setd2-mediated histone H3K36 methylation."
    Yoh S.M., Lucas J.S., Jones K.A.
    Genes Dev. 22:3422-3434(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IWS1.
  12. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1535; THR-1539 AND THR-1718, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267; THR-1523; SER-1535; THR-1539; SER-1701; SER-1703 AND THR-1718, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-75; SER-78; THR-1532; SER-1535; THR-1539; THR-1697; SER-1701; SER-1703 AND THR-1718, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-743 AND LYS-1676, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; THR-1523; THR-1532; THR-1697; SER-1701; SER-1703 AND THR-1718, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Histone chaperones Spt6 and FACT: Similarities and differences in modes of action at transcribed genes."
    Duina A.A.
    Genet. Res. Int. 2011:625210-625210(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  20. Cited for: INTERACTION WITH AICDA.
  21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-12; SER-125 AND SER-1535, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "The cellular protein SPT6 is required for efficient replication of human cytomegalovirus."
    Cygnar D., Hagemeier S., Kronemann D., Bresnahan W.A.
    J. Virol. 86:2011-2020(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HHV-5 PROTEIN UL69.
  23. "Spt6 levels are modulated by PAAF1 and proteasome to regulate the HIV-1 LTR."
    Nakamura M., Basavarajaiah P., Rousset E., Beraud C., Latreille D., Henaoui I.S., Lassot I., Mari B., Kiernan R.
    Retrovirology 9:13-13(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PAAF1.
  24. "The histone chaperone Spt6 coordinates histone H3K27 demethylation and myogenesis."
    Wang A.H., Zare H., Mousavi K., Wang C., Moravec C.E., Sirotkin H.I., Ge K., Gutierrez-Cruz G., Sartorelli V.
    EMBO J. 32:1075-1086(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiSPT6H_HUMAN
AccessioniPrimary (citable) accession number: Q7KZ85
Secondary accession number(s): A7E2B4
, Q15737, Q6GMQ4, Q7KYW9, Q7LDK4, Q8N526, Q92775, Q96AH3, Q9BTH9, Q9BTI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: July 9, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi