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O55201 (SPT5H_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription elongation factor SPT5
Alternative name(s):
DRB sensitivity-inducing factor large subunit
Short name=DSIF large subunit
Gene names
Name:Supt5h
Synonyms:Supt5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1082 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites By similarity.

Subunit structure

Interacts with SUPT4H1 to form DSIF. DSIF interacts with the positive transcription elongation factor b complex (P-TEFb complex), which is composed of CDK9 and cyclin-T (CCNT1 or CCNT2). DSIF interacts with RNA polymerase II, and this interaction is reduced by phosphorylation of the C-terminal domain (CTD) of POLR2A by P-TEFb. DSIF also interacts with the NELF complex, which is composed of WHSC2/NELFA, COBRA1/NELFB, TH1L/NELFD and RDBP/NELFE, and this interaction occurs following prior binding of DSIF to RNA polymerase II. Also interacts with PRMT1/HRMT1L2, HTATSF1/TATSF1, RNGTT/CAP1A, PRMT5/SKB1, SUPT6H, and can interact with PIN1. Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin By similarity.

Subcellular location

Nucleus By similarity.

Post-translational modification

Methylated by PRMT1/HRMT1L2 and PRMT5/SKB1. Methylation negatively regulates interaction with P-TEFb and RNA polymerase II By similarity.

Phosphorylated by CDK7 and CDK9. Phosphorylation by P-TEFb alleviates transcriptional pausing. Phosphorylation may also stimulate interaction with PIN1. Bulk phosphorylation occurs predominantly in mitosis By similarity.

Sequence similarities

Belongs to the SPT5 family.

Contains 5 KOW domains.

Sequence caution

The sequence AAH57449.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O55201-1)

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: O55201-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-194: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10821082Transcription elongation factor SPT5
PRO_0000208469

Regions

Domain271 – 30434KOW 1
Domain418 – 44932KOW 2
Domain470 – 50132KOW 3
Domain592 – 62534KOW 4
Domain698 – 73134KOW 5
Repeat748 – 7536CTR1-1; approximate
Repeat754 – 7596CTR1-2
Repeat760 – 7656CTR1-3
Repeat766 – 7727CTR1-4
Repeat775 – 7817CTR1-5
Repeat782 – 7887CTR1-6
Repeat790 – 7967CTR1-7
Repeat797 – 8037CTR1-8
Repeat805 – 8117CTR1-9
Repeat838 – 8458CTR2-1
Repeat848 – 8569CTR2-2; approximate
Repeat857 – 8637CTR2-3; approximate
Repeat875 – 8795CTR2-4; half-length
Repeat890 – 8967CTR2-5; approximate
Repeat898 – 9058CTR2-6
Repeat910 – 9156CTR2-7; approximate
Repeat918 – 9247CTR2-8
Repeat926 – 9338CTR2-9
Repeat937 – 9448CTR2-10
Region174 – 26895Interaction with SUPT4H1 and SUPT4H2 By similarity
Region311 – 418108Interaction with RNA polymerase II By similarity
Region748 – 811649 X 7 AA approximate tandem repeats of G-S-[QR]-T-P-X-[YQ], motif CTR1
Region838 – 94410710 X 8 AA approximate tandem repeats of P-[TS]-P-S-P-[QA]-[SG]-Y, motif CTR2
Compositional bias11 – 10494Glu-rich

Amino acid modifications

Modified residue6641Phosphoserine Ref.4
Modified residue6901Asymmetric dimethylarginine; alternate By similarity
Modified residue6901Omega-N-methylarginine; alternate By similarity
Modified residue6901Omega-N-methylated arginine; alternate By similarity
Modified residue6921Asymmetric dimethylarginine; alternate By similarity
Modified residue6921Omega-N-methylarginine; alternate By similarity
Modified residue6921Omega-N-methylated arginine; alternate By similarity
Modified residue6921Symmetric dimethylarginine; alternate By similarity
Modified residue7121N6-acetyllysine Ref.5
Modified residue7691Phosphothreonine; by CDK9 By similarity
Modified residue7781Phosphothreonine; by CDK9 By similarity
Modified residue10281Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 194194Missing in isoform 2.
VSP_016283

Experimental info

Sequence conflict301Q → R in BAE26244. Ref.2
Sequence conflict511E → EE in BAE26244. Ref.2
Sequence conflict1111V → L in BAE27278. Ref.2
Sequence conflict2291K → E in BAE27184. Ref.2
Sequence conflict2651V → E in BAE26864. Ref.2
Sequence conflict4161H → N in AAH58598. Ref.3
Sequence conflict7751G → D in BAE26864. Ref.2
Sequence conflict10631L → I in BAE26864. Ref.2

Sequences

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

Last modified June 1, 1998. Version 1.
Checksum: 109D0D8D2D71DDE7

FASTA1,082120,664
        10         20         30         40         50         60 
MSDSEDSNFS EEEDSERSSE AEEAEVEEDQ RSAAGSEKEE EPEEEEEEEE EYDEEEEEED 

        70         80         90        100        110        120 
DDRPPKKPRH GGFILDEADV DDEYEDEDQW EDGAEDILEK EEIEASNIDN VVLDEDRSGA 

       130        140        150        160        170        180 
RRLQNLWRDQ REEELGEYYM KKYAKSSVGE TVYGGSDELS DDITQQQLLP GVKDPNLWTV 

       190        200        210        220        230        240 
KCKIGEERAT AISLMRKFIA YQFTDTPLQI KSVVAPEHVK GYIYVEAYKQ THVKQAIEGV 

       250        260        270        280        290        300 
GNLRLGYWNQ QMVPIKEMTD VLKVVKEVAN LKPKSWVRLK RGIYKDDIAQ VDYVEPSQNT 

       310        320        330        340        350        360 
ISLKMIPRID YDRIKARMSL KDWFAKRKKF KRPPQRLFDA EKIRSLGGDV ASDGDFLIFE 

       370        380        390        400        410        420 
GNRYSRKGFL FKSFAMSAVI TEGVKPTLSE LEKFEDQPEG IDLEVVTEST GKEREHNFQP 

       430        440        450        460        470        480 
GDNVEVCEGE LINLQGKVLS VDGNKITIMP KHEDLKDMLE FPAQELRKYF KMGDHVKVIA 

       490        500        510        520        530        540 
GRFEGDTGLI VRVEENFVIL FSDLTMHELK VLPRDLQLCS ETASGVDVGG QHEWGELVQL 

       550        560        570        580        590        600 
DPRTVGVIVR LERETFQVLN MHGKVVTVRH QAVTQKKDNR FAVALDSDQN NIHVKDIVKV 

       610        620        630        640        650        660 
IDGPHSGREG EIRHLYRSFA FLHCKKLVEN GGMFVCKARH LVLAGGSKPR DVTNLTVGGF 

       670        680        690        700        710        720 
TPMSPRISSP MHPSAEGQHG GFGSPGGMSR GRGRRDNELI GQTVRISQGP YKGYIGVVKD 

       730        740        750        760        770        780 
ATESTARVEL HSTCQTISVD RQRLTTVDSQ RPGGMTSTYG RTPMYGSQTP MYGSGSRTPM 

       790        800        810        820        830        840 
YGSQTPLQDG SRTPHYGSQT PLHDGSRTPA QSGAWDPNNP NTPSRAEEEY EYAFDDEPTP 

       850        860        870        880        890        900 
SPQAYGGTPN PQTPGYPDPS SPQVNPQYNP QTPGTPAMYN TDQFSPYAAP SPQGSYQPSP 

       910        920        930        940        950        960 
SPQSYHQVAP SPAGYQNTHS PASYHPTPSP MAYQASPSPS PVGYSPMTPG APSPGGYNPH 

       970        980        990       1000       1010       1020 
TPGSGIEQNS SDWVTTDIQV KVRDTYLDTQ IVGQTGVIRS VTGGMCSVYL KDSEKVVSIS 

      1030       1040       1050       1060       1070       1080 
SEHLEPITPT KNNKVKVILG EDREATGVLL SIDGEDGIIR MDLEDQQIKI LNLRFLGKLL 


EA 

« Hide

Isoform 2 [UniParc].

Checksum: 30E132908E6A5F03
Show »

FASTA88898,310

References

« Hide 'large scale' references
[1]"Isolation of murine SPT5 homologue: completion of the isolation and characterization of human and murine homologues of yeast chromatin structural protein complex SPT4, SPT5, and SPT6."
Chiang P.-W., Stubbs L., Zhang L., Kurnit D.M.
Genomics 47:426-428(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Heart, Mammary gland and Placenta.
[3]"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 AND 2).
Strain: C57BL/6 and FVB/N.
Tissue: Brain, Mammary tumor, Olfactory epithelium and Salivary gland.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-712, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U88539 mRNA. Translation: AAC40052.1.
AK145117 mRNA. Translation: BAE26244.1.
AK146055 mRNA. Translation: BAE26864.1.
AK146453 mRNA. Translation: BAE27184.1.
AK146583 mRNA. Translation: BAE27278.1.
AK146650 mRNA. Translation: BAE27330.1.
BC007132 mRNA. Translation: AAH07132.1.
BC057449 mRNA. Translation: AAH57449.1. Different initiation.
BC058598 mRNA. Translation: AAH58598.1.
BC059849 mRNA. Translation: AAH59849.1.
CCDSCCDS39857.1. [O55201-1]
PIRT42204.
RefSeqNP_038704.1. NM_013676.1. [O55201-1]
UniGeneMm.285906.

3D structure databases

ProteinModelPortalO55201.
SMRO55201. Positions 174-309, 411-521, 696-751.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203575. 14 interactions.
IntActO55201. 1 interaction.
MINTMINT-4105191.

PTM databases

PhosphoSiteO55201.

Proteomic databases

MaxQBO55201.
PaxDbO55201.
PRIDEO55201.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003527; ENSMUSP00000003527; ENSMUSG00000003435. [O55201-1]
GeneID20924.
KEGGmmu:20924.
UCSCuc009fyh.1. mouse. [O55201-1]

Organism-specific databases

CTD20924.
MGIMGI:1202400. Supt5.

Phylogenomic databases

eggNOGCOG0250.
GeneTreeENSGT00440000037640.
HOVERGENHBG079775.
InParanoidO55201.
KOK15172.
OMAAFFDIEA.
OrthoDBEOG7Z3F3Q.
PhylomeDBO55201.
TreeFamTF105730.

Gene expression databases

BgeeO55201.
CleanExMM_SUPT5H.
GenevestigatorO55201.

Family and domain databases

InterProIPR005824. KOW.
IPR006645. NGN_dom.
IPR024945. Spt5_C_dom.
IPR022581. Spt5_N.
IPR017071. TF_Spt5.
IPR005100. TF_Spt5_NGN-domain.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamPF00467. KOW. 2 hits.
PF03439. Spt5-NGN. 1 hit.
PF11942. Spt5_N. 1 hit.
[Graphical view]
PIRSFPIRSF036945. Spt5. 1 hit.
SMARTSM01104. CTD. 1 hit.
SM00739. KOW. 6 hits.
SM00738. NGN. 1 hit.
[Graphical view]
SUPFAMSSF50104. SSF50104. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSUPT5H. mouse.
NextBio299833.
PROO55201.
SOURCESearch...

Entry information

Entry nameSPT5H_MOUSE
AccessionPrimary (citable) accession number: O55201
Secondary accession number(s): Q3UJ77 expand/collapse secondary AC list , Q3UJH1, Q3UKD7, Q3UM54, Q6PB73, Q6PDP0, Q6PFR4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot