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Q7KZ85 (SPT6H_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SUPT6H
Synonyms:KIAA0162, SPT6H
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1726 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.8 Ref.10 Ref.23 Ref.24

Subunit structure

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. Ref.7 Ref.8 Ref.10 Ref.11 Ref.20 Ref.22 Ref.23

Subcellular location

Nucleus Probable.

Tissue specificity

Ubiquitously expressed.

Sequence similarities

Belongs to the SPT6 family.

Contains 1 S1 motif domain.

Contains 1 SH2 domain.

Sequence caution

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.

Ontologies

Keywords
   Biological processHost-virus interaction
mRNA processing
mRNA splicing
mRNA transport
Transcription
Transcription regulation
Transport
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin remodeling

Non-traceable author statement Ref.1. Source: UniProtKB

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of histone H3-K27 methylation

Inferred from mutant phenotype Ref.24. Source: UniProtKB

positive regulation of transcription elongation from RNA polymerase II promoter

Inferred from mutant phenotype Ref.10. Source: UniProtKB

regulation of isotype switching

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of mRNA export from nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of mRNA processing

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of muscle cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Non-traceable author statement Ref.1. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

histone binding

Inferred from direct assay Ref.7. Source: UniProtKB

hydrolase activity, acting on ester bonds

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ERBB2P046262EBI-2515547,EBI-641062

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7KZ85-1)

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.
Isoform 2 (identifier: Q7KZ85-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1181: Missing.
     1182-1211: ESYDQAIRNDETGLWQCPFCQQDNFPELSE → MPSRGTRPEDSSVLIPTDNSTPHKEDLSSK
Isoform 3 (identifier: Q7KZ85-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 17261725Transcription elongation factor SPT6
PRO_0000072171

Regions

Domain1213 – 128270S1 motif
Domain1325 – 1431107SH2
Region2 – 916915Interaction with PAAF1
Region2 – 485484Interaction with IWS1 By similarity
Region317 – 1300984Interaction with KDM6A By similarity
Region1633 – 172694Interaction with histone H2B and H3
Compositional bias6 – 250245Asp/Glu-rich
Compositional bias1525 – 15284Poly-Ser
Compositional bias1654 – 16574Poly-Ser

Amino acid modifications

Modified residue21N-acetylserine Ref.14 Ref.21
Modified residue71Phosphoserine Ref.21
Modified residue121Phosphoserine Ref.21
Modified residue731Phosphoserine Ref.15
Modified residue751Phosphoserine Ref.15
Modified residue781Phosphoserine Ref.15
Modified residue1251Phosphoserine Ref.9 Ref.17 Ref.21
Modified residue2671Phosphoserine Ref.13
Modified residue7431N6-acetyllysine Ref.16
Modified residue15231Phosphothreonine Ref.13 Ref.17
Modified residue15321Phosphothreonine Ref.15 Ref.17
Modified residue15351Phosphoserine Ref.12 Ref.13 Ref.15 Ref.21
Modified residue15391Phosphothreonine Ref.12 Ref.13 Ref.15
Modified residue16761N6-acetyllysine Ref.16
Modified residue16971Phosphothreonine Ref.15 Ref.17
Modified residue17011Phosphoserine Ref.13 Ref.15 Ref.17
Modified residue17031Phosphoserine Ref.13 Ref.15 Ref.17
Modified residue17181Phosphothreonine Ref.12 Ref.13 Ref.15 Ref.17

Natural variations

Alternative sequence1 – 11811181Missing in isoform 2.
VSP_011505
Alternative sequence617 – 16161000Missing in isoform 3.
VSP_011507
Alternative sequence1182 – 121130ESYDQ…PELSE → MPSRGTRPEDSSVLIPTDNS TPHKEDLSSK in isoform 2.
VSP_011506

Experimental info

Sequence conflict61 – 7313DDDED…EDEGS → ATAPGHPKLSEGR in AAC50821. Ref.1
Sequence conflict100 – 10910DFDLIEENLG → LEDDDFLLNE in AAH33074. Ref.4
Sequence conflict988 – 9947YVCGLGP → VCLWPGT in AAB18949. Ref.1
Sequence conflict15451L → P in AAH17105. Ref.4
Sequence conflict16271S → I in AAH17105. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 31, 2004. Version 2.
Checksum: F7EB22FA669EB030

FASTA1,726199,073
        10         20         30         40         50         60 
MSDFVESEAE ESEEEYNDEG EVVPRVTKKF VEEEDDDEEE EEENLDDQDE QGNLKGFIND 

        70         80         90        100        110        120 
DDDEDEGEED EGSDSGDSED DVGHKKRKRT SFDDRLEDDD FDLIEENLGV KVKRGQKYRR 

       130        140        150        160        170        180 
VKKMSDDEDD DEEEYGKEEH EKEAIAEEIF QDGEGEEGQE AMEAPMAPPE EEEEDDEESD 

       190        200        210        220        230        240 
IDDFIVDDDG QPLKKPKWRK KLPGYTDAAL QEAQEIFGVD FDYDEFEKYN EYDEELEEEY 

       250        260        270        280        290        300 
EYEDDEAEGE IRVRPKKTTK KRVSRRSIFE MYEPSELESS HLTDQDNEIR ATDLPERFQL 

       310        320        330        340        350        360 
RSIPVKGAED DELEEEADWI YRNAFATPTI SLQESCDYLD RGQPASSFSR KGPSTIQKIK 

       370        380        390        400        410        420 
EALGFMRNQH FEVPFIAFYR KEYVEPELHI NDLWRVWQWD EKWTQLRIRK ENLTRLFEKM 

       430        440        450        460        470        480 
QAYQYEQISA DPDKPLADGI RALDTTDMER LKDVQSMDEL KDVYNHFLLY YGRDIPKMQN 

       490        500        510        520        530        540 
AAKASRKKLK RVREEGDEEG EGDEAEDEEQ RGPELKQASR RDMYTICQSA GLDGLAKKFG 

       550        560        570        580        590        600 
LTPEQFGENL RDSYQRHETE QFPAEPLELA KDYVCSQFPT PEAVLEGARY MVALQIAREP 

       610        620        630        640        650        660 
LVRQVLRQTF QERAKLNITP TKKGRKDVDE AHYAYSFKYL KNKPVKELRD DQFLKICLAE 

       670        680        690        700        710        720 
DEGLLTTDIS IDLKGVEGYG NDQTYFEEIK QFYYRDEFSH QVQEWNRQRT MAIERALQQF 

       730        740        750        760        770        780 
LYVQMAKELK NKLLAEAKEY VIKACSRKLY NWLRVAPYRP DQQVEEDDDF MDENQGKGIR 

       790        800        810        820        830        840 
VLGIAFSSAR DHPVFCALVN GEGEVTDFLR LPHFTKRRTA WREEEREKKA QDIETLKKFL 

       850        860        870        880        890        900 
LNKKPHVVTV AGENRDAQML IEDVKRIVHE LDQGQQLSSI GVELVDNELA ILYMNSKKSE 

       910        920        930        940        950        960 
AEFRDYPPVL RQAVSLARRI QDPLIEFAQV CSSDEDILCL KFHPLQEHVV KEELLNALYC 

       970        980        990       1000       1010       1020 
EFINRVNEVG VDVNRAIAHP YSQALIQYVC GLGPRKGTHL LKILKQNNTR LESRTQLVTM 

      1030       1040       1050       1060       1070       1080 
CHMGPKVFMN CAGFLKIDTA SLGDSTDSYI EVLDGSRVHP ETYEWARKMA VDALEYDESA 

      1090       1100       1110       1120       1130       1140 
EDANPAGALE EILENPERLK DLDLDAFAEE LERQGYGDKH ITLYDIRAEL SCRYKDLRTA 

      1150       1160       1170       1180       1190       1200 
YRSPNTEEIF NMLTKETPET FYIGKLIICN VTGIAHRRPQ GESYDQAIRN DETGLWQCPF 

      1210       1220       1230       1240       1250       1260 
CQQDNFPELS EVWNHFDSGS CPGQAIGVKT RLDNGVTGFI PTKFLSDKVV KRPEERVKVG 

      1270       1280       1290       1300       1310       1320 
MTVHCRIMKI DIEKFSADLT CRTSDLMDRN NEWKLPKDTY YDFDAEAADH KQEEDMKRKQ 

      1330       1340       1350       1360       1370       1380 
QRTTYIKRVI AHPSFHNINF KQAEKMMETM DQGDVIIRPS SKGENHLTVT WKVSDGIYQH 

      1390       1400       1410       1420       1430       1440 
VDVREEGKEN AFSLGATLWI NSEEFEDLDE IVARYVQPMA SFARDLLNHK YYQDCSGGDR 

      1450       1460       1470       1480       1490       1500 
KKLEELLIKT KKEKPTFIPY FICACKELPG KFLLGYQPRG KPRIEYVTVT PEGFRYRGQI 

      1510       1520       1530       1540       1550       1560 
FPTVNGLFRW FKDHYQDPVP GITPSSSSRT RTPASINATP ANINLADLTR AVNALPQNMT 

      1570       1580       1590       1600       1610       1620 
SQMFSAIAAV TGQGQNPNAT PAQWASSQYG YGGSGGGSSA YHVFPTPAQQ PVATPLMTPS 

      1630       1640       1650       1660       1670       1680 
YSYTTPSQPI TTPQYHQLQA STTPQSAQAQ PQPSSSSRQR QQQPKSNSHA AIDWGKMAEQ 

      1690       1700       1710       1720 
WLQEKEAERR KQKQRLTPRP SPSPMIESTP MSIAGDATPL LDEMDR 

« Hide

Isoform 2 [UniParc].

Checksum: 4BD128B2327CECE4
Show »

FASTA54561,301
Isoform 3 [UniParc].

Checksum: BA3499B7CD6743BD
Show »

FASTA72684,632

References

« Hide 'large scale' references
[1]"Identification and analysis of the human and murine putative chromatin structure regulator SUPT6H and Supt6h."
Chiang P.-W., Wang S., Smithivas P., Song W.-J., Ramamoorthy S., Hillman J., Puett S., Van Keuren M.L., Crombez E., Kumar A., Glover T.W., Miller D.E., Tsai C.-H., Blackburn C.C., Chen X.-N., Sun Z., Cheng J.-F., Korenberg J.R., Kurnit D.M.
Genomics 34:328-333(1996) [PubMed] [Europe PMC] [Abstract]
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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Human Spt6 stimulates transcription elongation by RNA polymerase II in vitro."
Endoh M., Zhu W., Hasegawa J., Watanabe H., Kim D.-K., Aida M., Inukai N., Narita T., Yamada T., Furuya A., Sato H., Yamaguchi Y., Mandal S.S., Reinberg D., Wada T., Handa H.
Mol. Cell. Biol. 24:3324-3336(2004) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Histone chaperone Spt6 is required for class switch recombination but not somatic hypermutation."
Okazaki I.M., Okawa K., Kobayashi M., Yoshikawa K., Kawamoto S., Nagaoka H., Shinkura R., Kitawaki Y., Taniguchi H., Natsume T., Iemura S., Honjo T.
Proc. Natl. Acad. Sci. U.S.A. 108:7920-7925(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_003161.2. NM_003170.3.
XP_005258083.1. XM_005258026.1.
XP_005258084.1. XM_005258027.1.
UniGeneHs.250429.

3D structure databases

ProteinModelPortalQ7KZ85.
SMRQ7KZ85. Positions 270-1285, 1326-1512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112698. 13 interactions.
DIPDIP-42615N.
IntActQ7KZ85. 11 interactions.
MINTMINT-1491202.

PTM databases

PhosphoSiteQ7KZ85.

Polymorphism databases

DMDM51701986.

Proteomic databases

PaxDbQ7KZ85.
PeptideAtlasQ7KZ85.
PRIDEQ7KZ85.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314616; ENSP00000319104; ENSG00000109111. [Q7KZ85-1]
ENST00000347486; ENSP00000338143; ENSG00000109111. [Q7KZ85-1]
GeneID6830.
KEGGhsa:6830.
UCSCuc002hby.3. human. [Q7KZ85-1]

Organism-specific databases

CTD6830.
GeneCardsGC17P026989.
HGNCHGNC:11470. SUPT6H.
HPACAB012416.
HPA036382.
MIM601333. gene.
neXtProtNX_Q7KZ85.
PharmGKBPA36256.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2183.
HOVERGENHBG093994.
InParanoidQ7KZ85.
KOK11292.
OMARDIPKMQ.
OrthoDBEOG7DFXBC.
PhylomeDBQ7KZ85.
TreeFamTF105956.

Enzyme and pathway databases

SignaLinkQ7KZ85.

Gene expression databases

ArrayExpressQ7KZ85.
BgeeQ7KZ85.
GenevestigatorQ7KZ85.

Family and domain databases

Gene3D1.10.150.310. 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.
InterProIPR012340. 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]
PANTHERPTHR10145. PTHR10145. 1 hit.
PfamPF14878. 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]
PIRSFPIRSF036947. Spt6. 1 hit.
SMARTSM00316. S1. 1 hit.
SM00252. SH2. 1 hit.
SM00732. YqgFc. 1 hit.
[Graphical view]
SUPFAMSSF47781. SSF47781. 2 hits.
SSF50249. SSF50249. 1 hit.
SSF53098. SSF53098. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEPS50126. S1. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSUPT6H. human.
GeneWikiSUPT6H.
GenomeRNAi6830.
NextBio26667.
PMAP-CutDBQ7KZ85.
PROQ7KZ85.
SOURCESearch...

Entry information

Entry nameSPT6H_HUMAN
AccessionPrimary (citable) accession number: Q7KZ85
Secondary accession number(s): A7E2B4 expand/collapse secondary AC list , Q15737, Q6GMQ4, Q7KYW9, Q7LDK4, Q8N526, Q92775, Q96AH3, Q9BTH9, Q9BTI2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: April 16, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM