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Q7KZ85

- SPT6H_HUMAN

UniProt

Q7KZ85 - SPT6H_HUMAN

Protein

Transcription elongation factor SPT6

Gene

SUPT6H

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (31 Aug 2004)
      Previous versions | rss
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    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. chromatin remodeling Source: UniProtKB
    2. mRNA processing Source: UniProtKB-KW
    3. mRNA transport Source: UniProtKB-KW
    4. negative regulation of histone H3-K27 methylation Source: UniProtKB
    5. positive regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB
    6. regulation of isotype switching Source: UniProtKB
    7. regulation of mRNA export from nucleus Source: UniProtKB
    8. regulation of mRNA processing Source: UniProtKB
    9. regulation of muscle cell differentiation Source: UniProtKB
    10. regulation of transcription, DNA-templated Source: UniProtKB
    11. RNA splicing Source: UniProtKB-KW
    12. transcription, DNA-templated Source: UniProtKB-KW
    13. viral process Source: UniProtKB-KW

    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 Curated

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36256.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 17261725Transcription elongation factor SPT6PRO_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.By similarity7 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi112698. 15 interactions.
    DIPiDIP-42615N.
    IntActiQ7KZ85. 13 interactions.
    MINTiMINT-1491202.

    Structurei

    3D structure databases

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

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1213 – 128270S1 motifPROSITE-ProRule annotationAdd
    BLAST
    Domaini1325 – 1431107SH2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 916915Interaction with PAAF1Add
    BLAST
    Regioni2 – 485484Interaction with IWS1By similarityAdd
    BLAST
    Regioni317 – 1300984Interaction with KDM6ABy similarityAdd
    BLAST
    Regioni1633 – 172694Interaction with histone H2B and H3Add
    BLAST

    Compositional bias

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

    Sequence similaritiesi

    Belongs to the SPT6 family.Curated
    Contains 1 S1 motif domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 7313DDDED…EDEGS → ATAPGHPKLSEGR in AAC50821. (PubMed:8786132)CuratedAdd
    BLAST
    Sequence conflicti100 – 10910DFDLIEENLG → LEDDDFLLNE in AAH33074. (PubMed:15489334)Curated
    Sequence conflicti988 – 9947YVCGLGP → VCLWPGT in AAB18949. (PubMed:8786132)Curated
    Sequence conflicti1545 – 15451L → P in AAH17105. (PubMed:15489334)Curated
    Sequence conflicti1627 – 16271S → I in AAH17105. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11811181Missing in isoform 2. 1 PublicationVSP_011505Add
    BLAST
    Alternative sequencei617 – 16161000Missing in isoform 3. 1 PublicationVSP_011507Add
    BLAST
    Alternative sequencei1182 – 121130ESYDQ…PELSE → MPSRGTRPEDSSVLIPTDNS TPHKEDLSSK in isoform 2. 1 PublicationVSP_011506Add
    BLAST

    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. 13 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

    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: October 1, 2014
    This is version 112 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