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Reviewed, UniProtKB/Swiss-Prot Q9W420 (SPT6H_DROME)

Last modified June 16, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Transcription elongation factor SPT6
Gene names
Name: Spt6
ORF Names: CG12225
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1831 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Acts to stimulate transcriptional elongation by RNA polymerase II By similarity.

Subunit structure

Self associates. Interacts with RNA polymerase II. Interacts with the FACT complex, which is composed of dre4/Spt16 and Ssrp/Ssrp1. Interacts with the exosome, a complex with 3'-5' exoribonuclease activity which is composed of at least Csl4, Dis3, Mtr3, Rrp4, Rrp6, Rrp40, Rrp42, Rrp46 and Ski6. Interacts with the DRB sensitivity-inducing factor complex (the DSIF complex), which is composed of Spt4 and Spt5. Ref.7 Ref.8

Subcellular location

Nucleus. Note: Recruited to sites of active transcription where it colocalizes with the elongating form of RNA polymerase II. Ref.7 Ref.8 Ref.5 Ref.6

Sequence similarities

Belongs to the SPT6 family.

Contains 1 S1 motif domain.

Contains 1 SH2 domain.

Sequence caution

The sequence AAF14115.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18311831Transcription elongation factor SPT6
PRO_0000072170

Regions

Domain1217 – 128670S1 motif
Domain1329 – 1440112SH2 1
Coiled coil7 – 5953 Potential
Coiled coil467 – 49428 Potential
Compositional bias6 – 245240Asp/Glu-rich
Compositional bias489 – 51224Glu-rich
Compositional bias1552 – 1682131Ser-rich
Compositional bias1675 – 170228Gly-rich
Compositional bias1771 – 178313Poly-Gly

Amino acid modifications

Modified residue341Phosphoserine Ref.10
Modified residue361Phosphoserine Ref.10
Modified residue371Phosphoserine Ref.10
Modified residue661Phosphoserine Ref.10
Modified residue701Phosphoserine Ref.10
Modified residue751Phosphoserine Ref.10
Modified residue1241Phosphoserine Ref.9
Modified residue1511Phosphoserine Ref.10
Modified residue1561Phosphoserine Ref.10
Modified residue1591Phosphoserine Ref.10
Modified residue1711Phosphothreonine Ref.10
Modified residue1731Phosphoserine Ref.10
Modified residue16611Phosphoserine Ref.10
Modified residue16641Phosphoserine Ref.10
Modified residue18151Phosphoserine Ref.10

Experimental info

Sequence conflict11941L → I in AAF14114. Ref.1
Sequence conflict11941L → I in AAF14115. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9W420-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 005FC78C83EF744D

FASTA1,831208,599
        10         20         30         40         50         60 
MAEFLDSEAE ESEEEEELDV NERKRLKKLK AAVSDSSEEE EDDEERLREE LKDLIDDNPI 

        70         80         90        100        110        120 
EEDDGSGYDS DGVGSGKKRK KHEDDDLDDR LEDDDYDLIE ENLGVKVERR KRFKRLRRIH 

       130        140        150        160        170        180 
DNESDGEEQH VDEGLVREQI AEQLFDENDE SIGHRSERSH READDYDDVD TESDADDFIV 

       190        200        210        220        230        240 
DDNGRPIAEK KKKRRPIFTD ASLQEGQDIF GVDFDYDDFS KYEEDDYEDD SEGDEYDEDL 

       250        260        270        280        290        300 
GVGDDTRVKK KKALKKKVVK KTIFDIYEPS ELKRGHFTDM DNEIRKTDIP ERMQLREVPV 

       310        320        330        340        350        360 
TPVPEGSDEL DLEAEWIYKY AFCKHTVSEQ EKPESREKMR KPPTTVNKIK QTLEFIRNQQ 

       370        380        390        400        410        420 
LEVPFIAFYR KEYVKPELNI DDLWKVYYYD GIWCQLNERK RKLKVLFEKM RQFQLDTLCA 

       430        440        450        460        470        480 
DTDQPVPDDV RLILDSDFER LADVQSMEEL KDVHMYFLLN YSHELPRMQA EQRRKAIQER 

       490        500        510        520        530        540 
REAKARRQAA AAENGDDAAE AIVVPEPEDD DDPELIDYQL KQASNSSPYA VFRKAGICGF 

       550        560        570        580        590        600 
AKHFGLTPEQ YAENLRDNYQ RNEITQESIG PTELAKQYLS PRFMTTDEVI HAAKYVVARQ 

       610        620        630        640        650        660 
LAQEPLLRKT MREVYFDRAR INIRPTKNGM VLIDENSPVY SMKYVAKKPV SDLFGDQFIK 

       670        680        690        700        710        720 
LMMAEEEKLL EITFLEEFEG NACANGTPGD YVEESKALYQ LDQFAKHVQE WNKLRAECVQ 

       730        740        750        760        770        780 
LALQKWVIPD LIKELRSTLH EEAQQFVLRS CTGKLYKWLK VAPYKPQLPP DFGYEEWSTL 

       790        800        810        820        830        840 
RGIRVLGLAY DPDHSVAAFC AVTTVEGDIS DYLRLPNILK RKNSYNLEEK AQKLADLRKL 

       850        860        870        880        890        900 
SDFIKMKKPH IVVIGAESRD AQNIQADIKE ILHELETSEQ FPPIEVEIID NELAKIYANS 

       910        920        930        940        950        960 
KKGESDFKEY PPLLKQAASL ARKMQDPLVE YSQLCDADDE ILCLRYHPLQ ERVPREQLLE 

       970        980        990       1000       1010       1020 
QLSLQFINRT SEVGLDINLM VQNSRTINLL QYICGLGPRK GQALLKLLKQ SNQRLENRTQ 

      1030       1040       1050       1060       1070       1080 
LVTVCHLGPR VFINCSGFIK IDTSSLGDST EAYVEVLDGS RVHPETYEWA RKMAIDAMEY 

      1090       1100       1110       1120       1130       1140 
DDEETNPAGA LEEILESPER LKDLDLDAFA VELERQGFGS KSITLYDIRN ELSCLYKDYR 

      1150       1160       1170       1180       1190       1200 
TPYTKPSAEE LFDMLTKETP DSFYVGKCVT AMVTGFTYRR PQGDQLDSAN PVRLDSNESW 

      1210       1220       1230       1240       1250       1260 
QCPFCHKDDF PELSEVWNHF DANACPGQPS GVRVRLENGL PGFIHIKNLS DRQVRNPEER 

      1270       1280       1290       1300       1310       1320 
VRVSQMIHVR IIKIDIDRFS VECSSRTADL KDVNNEWRPR RDNYYDYVTE EQDNRKVSDA 

      1330       1340       1350       1360       1370       1380 
KARALKRKIY ARRVIAHPSF FNKSYAEVVA MLAEADQGEV ALRPSSKSKD HLTATWKVAD 

      1390       1400       1410       1420       1430       1440 
DIFQHIDVRE EGKENDFSLG RSLWIGTEEF EDLDEIIARH IMPMALAARE LIQYKYYKPN 

      1450       1460       1470       1480       1490       1500 
MVTGDENERD VMEKLLREEK ANDPKKIHYF FTASRAMPGK FLLSYLPKTK VRHEYVTVMP 

      1510       1520       1530       1540       1550       1560 
EGYRFRGQIF DTVNSLLRWF KEHWLDPTAT PASASASNLT PLHLMRPPPT ISSSSQTSLG 

      1570       1580       1590       1600       1610       1620 
PQAPYSVTGS VTGGTPRSGI SSAVGGGGSS AYSITQSITG YGTSGSSAPG AGVSSSHYGS 

      1630       1640       1650       1660       1670       1680 
SSTPSFGAIN TPYTPSGQTP FMTPYTPHAS QTPRYGHNVP SPSSQSSSSQ RHHYGSSSGT 

      1690       1700       1710       1720       1730       1740 
GSTPRYHDMG GGGGGGVGGG GGSNAYSMQP HHQQRAKENL DWQLANDAWA RRRPQQHQSH 

      1750       1760       1770       1780       1790       1800 
QSYHAQQQHH HSQQQPHMGM SMNMGITMSL GRGTGGGGGG GYGSTPVNDY STGGGHNRGM 

      1810       1820       1830 
SSKASVRSTP RTNASPHSMN LGDATPLYDE N 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of Drosophila SPT6 homolog."
Chiang P.-W.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 400-1831.
Strain: Berkeley.
Tissue: Embryo.
[5]"Spt5 and spt6 are associated with active transcription and have characteristics of general elongation factors in D. melanogaster."
Kaplan C.D., Morris J.R., Wu C.-T., Winston F.
Genes Dev. 14:2623-2634(2000) [PubMed: 11040216] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"High-resolution localization of Drosophila Spt5 and Spt6 at heat shock genes in vivo: roles in promoter proximal pausing and transcription elongation."
Andrulis E.D., Guzman E., Doering P., Werner J., Lis J.T.
Genes Dev. 14:2635-2649(2000) [PubMed: 11040217] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila."
Andrulis E.D., Werner J., Nazarian A., Erdjument-Bromage H., Tempst P., Lis J.T.
Nature 420:837-841(2002) [PubMed: 12490954] [Abstract]
Cited for: SELF-ASSOCIATION, INTERACTION WITH SPT5 AND THE EXOSOME COMPLEX, SUBCELLULAR LOCATION.
[8]"Tracking FACT and the RNA polymerase II elongation complex through chromatin in vivo."
Saunders A., Werner J., Andrulis E.D., Nakayama T., Hirose S., Reinberg D., Lis J.T.
Science 301:1094-1096(2003) [PubMed: 12934007] [Abstract]
Cited for: INTERACTION WITH SPT5; RNA POLYMERASE II AND THE FACT COMPLEX, SUBCELLULAR LOCATION.
[9]"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
Mol. Biosyst. 3:275-286(2007) [PubMed: 17372656] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, MASS SPECTROMETRY.
[10]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-36; SER-37; SER-66; SER-70; SER-75; SER-151; SER-156; SER-159; THR-171; SER-173; SER-1661; SER-1664 AND SER-1815, MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF104400 mRNA. Translation: AAF14114.1.
AF104401 Genomic DNA. Translation: AAF14115.1. Sequence problems.
AE014298 Genomic DNA. Translation: AAF46140.1.
AY052030 mRNA. Translation: AAK93454.1. Different initiation.
RefSeqNP_651962.2.
UniGeneDm.7373

3D structure databases

HSSPHSSP built from PDB template 5RXN based on UniProtKB P00268.
ModBaseSearch...

Proteomic databases

PRIDEQ9W420.

Genome annotation databases

EnsemblFBgn0028982. Drosophila melanogaster. [Contig view]
GeneID44000.
KEGGdme:Dmel_CG12225.
NMPDRfig|7227.3.peg.16696.

Organism-specific databases

FlyBaseFBgn0028982. Spt6.

Phylogenomic databases

HOGENOMQ9W420.
OMAQ9W420. QHFEVPF.

Gene expression databases

ArrayExpressQ9W420.
GermOnlineCG12225. Drosophila melanogaster.

Family and domain databases

InterProIPR012340. NA-bd_OB-fold.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
IPR006641. Resolv_RNaseH-like.
IPR000980. SH2.
IPR017072. TF_Spt6.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
PfamPF00575. S1. 1 hit.
[Graphical view]
PIRSFPIRSF036947. Spt6. 1 hit.
SMARTSM00252. SH2. 2 hits.
SM00732. YqgFc. 1 hit.
[Graphical view]
PROSITEPS50126. S1. 1 hit.
PS50001. SH2. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio836551.

Entry information

Entry nameSPT6H_DROME
AccessionPrimary (citable) accession number: Q9W420
Secondary accession number(s): Q960J2, Q9U8B5, Q9U8B6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents