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Protein

Activated RNA polymerase II transcriptional coactivator p15

Gene

Sub1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA) (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActivator, DNA-binding
Biological processTranscription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Activated RNA polymerase II transcriptional coactivator p15
Alternative name(s):
Positive cofactor 4
Short name:
PC4
SUB1 homolog
p14
Gene namesi
Name:Sub1
Synonyms:Pc4, Rpo2tc1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi

Organism-specific databases

RGDi621582 Sub1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000451731 – 127Activated RNA polymerase II transcriptional coactivator p15Add BLAST127

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei4PhosphoserineBy similarity1
Modified residuei9PhosphoserineCombined sources1
Modified residuei10PhosphoserineBy similarity1
Modified residuei11PhosphoserineBy similarity1
Modified residuei13PhosphoserineBy similarity1
Modified residuei15PhosphoserineBy similarity1
Modified residuei17PhosphoserineCombined sources1
Modified residuei19PhosphoserineCombined sources1
Modified residuei35N6-acetyllysineBy similarity1
Modified residuei53N6-acetyllysineBy similarity1
Modified residuei55PhosphoserineBy similarity1
Modified residuei56PhosphoserineBy similarity1
Modified residuei57PhosphoserineBy similarity1
Modified residuei58PhosphoserineBy similarity1
Modified residuei68N6-acetyllysine; alternateBy similarity1
Cross-linki68Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki68Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei118PhosphoserineBy similarity1

Post-translational modificationi

Activity is controlled by protein kinases that target the regulatory region. Phosphorylation inactivates both ds DNA-binding and cofactor function, but does not affect binding to ssDNA (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei50 – 51CleavageBy similarity2

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ63396
PRIDEiQ63396

PTM databases

iPTMnetiQ63396
PhosphoSitePlusiQ63396

Expressioni

Gene expression databases

BgeeiENSRNOG00000050563
GenevisibleiQ63396 RN

Interactioni

Subunit structurei

Homodimer. Interacts with CSTF2 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi251393, 1 interactor
IntActiQ63396, 2 interactors
MINTiQ63396
STRINGi10116.ENSRNOP00000067467

Structurei

3D structure databases

ProteinModelPortaliQ63396
SMRiQ63396
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 50RegulatoryBy similarityAdd BLAST50
Regioni77 – 101Interaction with ssDNABy similarityAdd BLAST25

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi4 – 19Ser-richAdd BLAST16
Compositional biasi23 – 53Lys-richAdd BLAST31
Compositional biasi43 – 58Ser-richAdd BLAST16

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2712 Eukaryota
ENOG410XUB8 LUCA
GeneTreeiENSGT00390000008802
HOGENOMiHOG000239157
HOVERGENiHBG028243
InParanoidiQ63396
OMAiMVDIREH
OrthoDBiEOG091G14VO
PhylomeDBiQ63396
TreeFamiTF313859

Family and domain databases

Gene3Di2.30.31.10, 1 hit
InterProiView protein in InterPro
IPR003173 PC4
IPR009044 ssDNA-bd_transcriptional_reg
PfamiView protein in Pfam
PF02229 PC4, 1 hit
SUPFAMiSSF54447 SSF54447, 1 hit

Sequencei

Sequence statusi: Complete.

Q63396-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKSKELVSS SSSGSDSDSE VEKKLKRKKQ VVPEKPVKKQ KPGESSRALA
60 70 80 90 100
SSKQSSSSRD DNMFQIGKMR YVSVRDFKGK ILIDIREYWM DSEGEMKPGR
110 120
KGISLNMEQW SQLKEQISDI DDAVRKL
Length:127
Mass (Da):14,441
Last modified:January 23, 2007 - v3
Checksum:i7B2B8CF34A54105C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti43G → S in AAA41758 (PubMed:6208900).Curated1
Sequence conflicti99G → R in AAA41758 (PubMed:6208900).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC088346 mRNA Translation: AAH88346.1
K02816 mRNA Translation: AAA41758.1
PIRiA23063
RefSeqiNP_001009618.1, NM_001009618.1
XP_006232105.1, XM_006232043.3
UniGeneiRn.160776
Rn.8706

Genome annotation databases

EnsembliENSRNOT00000074446; ENSRNOP00000067467; ENSRNOG00000050563
GeneIDi192269
KEGGirno:192269

Entry informationi

Entry nameiTCP4_RAT
AccessioniPrimary (citable) accession number: Q63396
Secondary accession number(s): Q5M805
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 126 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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