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O55201

- SPT5H_MOUSE

UniProt

O55201 - SPT5H_MOUSE

Protein

Transcription elongation factor SPT5

Gene

Supt5h

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    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.By similarity

    GO - Molecular functioni

    1. chromatin binding Source: MGI

    GO - Biological processi

    1. negative regulation of DNA-templated transcription, elongation Source: Ensembl
    2. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    3. positive regulation of DNA-templated transcription, elongation Source: Ensembl
    4. positive regulation of macroautophagy Source: Ensembl
    5. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    6. transcription elongation from RNA polymerase II promoter Source: Ensembl

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_203462. Formation of the Early Elongation Complex.
    REACT_226490. RNA Polymerase II Transcription Elongation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription elongation factor SPT5
    Alternative name(s):
    DRB sensitivity-inducing factor large subunit
    Short name:
    DSIF large subunit
    Gene namesi
    Name:Supt5h
    Synonyms:Supt5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1202400. Supt5.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. DSIF complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10821082Transcription elongation factor SPT5PRO_0000208469Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei664 – 6641Phosphoserine1 Publication
    Modified residuei690 – 6901Asymmetric dimethylarginine; alternateBy similarity
    Modified residuei690 – 6901Omega-N-methylarginine; alternateBy similarity
    Modified residuei690 – 6901Omega-N-methylated arginine; alternateBy similarity
    Modified residuei692 – 6921Asymmetric dimethylarginine; alternateBy similarity
    Modified residuei692 – 6921Omega-N-methylarginine; alternateBy similarity
    Modified residuei692 – 6921Omega-N-methylated arginine; alternateBy similarity
    Modified residuei692 – 6921Symmetric dimethylarginine; alternateBy similarity
    Modified residuei712 – 7121N6-acetyllysine1 Publication
    Modified residuei769 – 7691Phosphothreonine; by CDK9By similarity
    Modified residuei778 – 7781Phosphothreonine; by CDK9By similarity
    Modified residuei1028 – 10281PhosphothreonineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiO55201.
    PaxDbiO55201.
    PRIDEiO55201.

    PTM databases

    PhosphoSiteiO55201.

    Expressioni

    Gene expression databases

    BgeeiO55201.
    CleanExiMM_SUPT5H.
    GenevestigatoriO55201.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    BioGridi203575. 14 interactions.
    IntActiO55201. 1 interaction.
    MINTiMINT-4105191.

    Structurei

    3D structure databases

    ProteinModelPortaliO55201.
    SMRiO55201. Positions 174-309, 411-521, 696-751.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini271 – 30434KOW 1Add
    BLAST
    Domaini418 – 44932KOW 2Add
    BLAST
    Domaini470 – 50132KOW 3Add
    BLAST
    Domaini592 – 62534KOW 4Add
    BLAST
    Domaini698 – 73134KOW 5Add
    BLAST
    Repeati748 – 7536CTR1-1; approximate
    Repeati754 – 7596CTR1-2
    Repeati760 – 7656CTR1-3
    Repeati766 – 7727CTR1-4
    Repeati775 – 7817CTR1-5
    Repeati782 – 7887CTR1-6
    Repeati790 – 7967CTR1-7
    Repeati797 – 8037CTR1-8
    Repeati805 – 8117CTR1-9
    Repeati838 – 8458CTR2-1
    Repeati848 – 8569CTR2-2; approximate
    Repeati857 – 8637CTR2-3; approximate
    Repeati875 – 8795CTR2-4; half-length
    Repeati890 – 8967CTR2-5; approximate
    Repeati898 – 9058CTR2-6
    Repeati910 – 9156CTR2-7; approximate
    Repeati918 – 9247CTR2-8
    Repeati926 – 9338CTR2-9
    Repeati937 – 9448CTR2-10

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni174 – 26895Interaction with SUPT4H1 and SUPT4H2By similarityAdd
    BLAST
    Regioni311 – 418108Interaction with RNA polymerase IIBy similarityAdd
    BLAST
    Regioni748 – 811649 X 7 AA approximate tandem repeats of G-S-[QR]-T-P-X-[YQ], motif CTR1Add
    BLAST
    Regioni838 – 94410710 X 8 AA approximate tandem repeats of P-[TS]-P-S-P-[QA]-[SG]-Y, motif CTR2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi11 – 10494Glu-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SPT5 family.Curated
    Contains 5 KOW domains.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0250.
    GeneTreeiENSGT00440000037640.
    HOVERGENiHBG079775.
    InParanoidiO55201.
    KOiK15172.
    OMAiAFFDIEA.
    OrthoDBiEOG7Z3F3Q.
    PhylomeDBiO55201.
    TreeFamiTF105730.

    Family and domain databases

    InterProiIPR005824. 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]
    PfamiPF00467. KOW. 2 hits.
    PF03439. Spt5-NGN. 1 hit.
    PF11942. Spt5_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036945. Spt5. 1 hit.
    SMARTiSM01104. CTD. 1 hit.
    SM00739. KOW. 6 hits.
    SM00738. NGN. 1 hit.
    [Graphical view]
    SUPFAMiSSF50104. SSF50104. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O55201-1) [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

    MSDSEDSNFS EEEDSERSSE AEEAEVEEDQ RSAAGSEKEE EPEEEEEEEE     50
    EYDEEEEEED DDRPPKKPRH GGFILDEADV DDEYEDEDQW EDGAEDILEK 100
    EEIEASNIDN VVLDEDRSGA RRLQNLWRDQ REEELGEYYM KKYAKSSVGE 150
    TVYGGSDELS DDITQQQLLP GVKDPNLWTV KCKIGEERAT AISLMRKFIA 200
    YQFTDTPLQI KSVVAPEHVK GYIYVEAYKQ THVKQAIEGV GNLRLGYWNQ 250
    QMVPIKEMTD VLKVVKEVAN LKPKSWVRLK RGIYKDDIAQ VDYVEPSQNT 300
    ISLKMIPRID YDRIKARMSL KDWFAKRKKF KRPPQRLFDA EKIRSLGGDV 350
    ASDGDFLIFE GNRYSRKGFL FKSFAMSAVI TEGVKPTLSE LEKFEDQPEG 400
    IDLEVVTEST GKEREHNFQP GDNVEVCEGE LINLQGKVLS VDGNKITIMP 450
    KHEDLKDMLE FPAQELRKYF KMGDHVKVIA GRFEGDTGLI VRVEENFVIL 500
    FSDLTMHELK VLPRDLQLCS ETASGVDVGG QHEWGELVQL DPRTVGVIVR 550
    LERETFQVLN MHGKVVTVRH QAVTQKKDNR FAVALDSDQN NIHVKDIVKV 600
    IDGPHSGREG EIRHLYRSFA FLHCKKLVEN GGMFVCKARH LVLAGGSKPR 650
    DVTNLTVGGF TPMSPRISSP MHPSAEGQHG GFGSPGGMSR GRGRRDNELI 700
    GQTVRISQGP YKGYIGVVKD ATESTARVEL HSTCQTISVD RQRLTTVDSQ 750
    RPGGMTSTYG RTPMYGSQTP MYGSGSRTPM YGSQTPLQDG SRTPHYGSQT 800
    PLHDGSRTPA QSGAWDPNNP NTPSRAEEEY EYAFDDEPTP SPQAYGGTPN 850
    PQTPGYPDPS SPQVNPQYNP QTPGTPAMYN TDQFSPYAAP SPQGSYQPSP 900
    SPQSYHQVAP SPAGYQNTHS PASYHPTPSP MAYQASPSPS PVGYSPMTPG 950
    APSPGGYNPH TPGSGIEQNS SDWVTTDIQV KVRDTYLDTQ IVGQTGVIRS 1000
    VTGGMCSVYL KDSEKVVSIS SEHLEPITPT KNNKVKVILG EDREATGVLL 1050
    SIDGEDGIIR MDLEDQQIKI LNLRFLGKLL EA 1082
    Length:1,082
    Mass (Da):120,664
    Last modified:June 1, 1998 - v1
    Checksum:i109D0D8D2D71DDE7
    GO
    Isoform 2 (identifier: O55201-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-194: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:888
    Mass (Da):98,310
    Checksum:i30E132908E6A5F03
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti30 – 301Q → R in BAE26244. (PubMed:16141072)Curated
    Sequence conflicti51 – 511E → EE in BAE26244. (PubMed:16141072)Curated
    Sequence conflicti111 – 1111V → L in BAE27278. (PubMed:16141072)Curated
    Sequence conflicti229 – 2291K → E in BAE27184. (PubMed:16141072)Curated
    Sequence conflicti265 – 2651V → E in BAE26864. (PubMed:16141072)Curated
    Sequence conflicti416 – 4161H → N in AAH58598. (PubMed:15489334)Curated
    Sequence conflicti775 – 7751G → D in BAE26864. (PubMed:16141072)Curated
    Sequence conflicti1063 – 10631L → I in BAE26864. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 194194Missing in isoform 2. 1 PublicationVSP_016283Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS39857.1. [O55201-1]
    PIRiT42204.
    RefSeqiNP_038704.1. NM_013676.1. [O55201-1]
    UniGeneiMm.285906.

    Genome annotation databases

    EnsembliENSMUST00000003527; ENSMUSP00000003527; ENSMUSG00000003435. [O55201-1]
    GeneIDi20924.
    KEGGimmu:20924.
    UCSCiuc009fyh.1. mouse. [O55201-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS39857.1. [O55201-1 ]
    PIRi T42204.
    RefSeqi NP_038704.1. NM_013676.1. [O55201-1 ]
    UniGenei Mm.285906.

    3D structure databases

    ProteinModelPortali O55201.
    SMRi O55201. Positions 174-309, 411-521, 696-751.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203575. 14 interactions.
    IntActi O55201. 1 interaction.
    MINTi MINT-4105191.

    PTM databases

    PhosphoSitei O55201.

    Proteomic databases

    MaxQBi O55201.
    PaxDbi O55201.
    PRIDEi O55201.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000003527 ; ENSMUSP00000003527 ; ENSMUSG00000003435 . [O55201-1 ]
    GeneIDi 20924.
    KEGGi mmu:20924.
    UCSCi uc009fyh.1. mouse. [O55201-1 ]

    Organism-specific databases

    CTDi 20924.
    MGIi MGI:1202400. Supt5.

    Phylogenomic databases

    eggNOGi COG0250.
    GeneTreei ENSGT00440000037640.
    HOVERGENi HBG079775.
    InParanoidi O55201.
    KOi K15172.
    OMAi AFFDIEA.
    OrthoDBi EOG7Z3F3Q.
    PhylomeDBi O55201.
    TreeFami TF105730.

    Enzyme and pathway databases

    Reactomei REACT_203462. Formation of the Early Elongation Complex.
    REACT_226490. RNA Polymerase II Transcription Elongation.

    Miscellaneous databases

    ChiTaRSi SUPT5H. mouse.
    NextBioi 299833.
    PROi O55201.
    SOURCEi Search...

    Gene expression databases

    Bgeei O55201.
    CleanExi MM_SUPT5H.
    Genevestigatori O55201.

    Family and domain databases

    InterProi IPR005824. 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 ]
    Pfami PF00467. KOW. 2 hits.
    PF03439. Spt5-NGN. 1 hit.
    PF11942. Spt5_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036945. Spt5. 1 hit.
    SMARTi SM01104. CTD. 1 hit.
    SM00739. KOW. 6 hits.
    SM00738. NGN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50104. SSF50104. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    Entry informationi

    Entry nameiSPT5H_MOUSE
    AccessioniPrimary (citable) accession number: O55201
    Secondary accession number(s): Q3UJ77
    , Q3UJH1, Q3UKD7, Q3UM54, Q6PB73, Q6PDP0, Q6PFR4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 117 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3