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Protein

Activated RNA polymerase II transcriptional coactivator p15

Gene

Sub1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi621582. Sub1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: Ensembl
  • nucleolus Source: Ensembl
  • nucleus Source: RGD
  • transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 127126Activated RNA polymerase II transcriptional coactivator p15PRO_0000045173Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41PhosphoserineBy similarity
Modified residuei9 – 91PhosphoserineCombined sources
Modified residuei10 – 101PhosphoserineBy similarity
Modified residuei11 – 111PhosphoserineBy similarity
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei15 – 151PhosphoserineBy similarity
Modified residuei17 – 171PhosphoserineCombined sources
Modified residuei19 – 191PhosphoserineCombined sources
Modified residuei35 – 351N6-acetyllysineBy similarity
Modified residuei53 – 531N6-acetyllysineBy similarity
Modified residuei55 – 551PhosphoserineBy similarity
Modified residuei68 – 681N6-acetyllysineBy similarity
Modified residuei118 – 1181PhosphoserineBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei50 – 512CleavageBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ63396.
PRIDEiQ63396.

PTM databases

iPTMnetiQ63396.

Expressioni

Gene expression databases

GenevisibleiQ63396. RN.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi251393. 1 interaction.
IntActiQ63396. 2 interactions.
MINTiMINT-4598677.
STRINGi10116.ENSRNOP00000067467.

Structurei

3D structure databases

ProteinModelPortaliQ63396.
SMRiQ63396. Positions 63-127.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 5049RegulatoryBy similarityAdd
BLAST
Regioni77 – 10125Interaction with ssDNABy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 1916Ser-richAdd
BLAST
Compositional biasi23 – 5331Lys-richAdd
BLAST
Compositional biasi43 – 5816Ser-richAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2712. Eukaryota.
ENOG410XUB8. LUCA.
GeneTreeiENSGT00390000008802.
HOGENOMiHOG000239157.
HOVERGENiHBG028243.
InParanoidiQ63396.
OMAiQWNQLKD.
OrthoDBiEOG76MKBV.
PhylomeDBiQ63396.
TreeFamiTF313859.

Family and domain databases

Gene3Di2.30.31.10. 1 hit.
InterProiIPR003173. PC4.
IPR009044. ssDNA-bd_transcriptional_reg.
[Graphical view]
PfamiPF02229. PC4. 1 hit.
[Graphical view]
SUPFAMiSSF54447. SSF54447. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431G → S in AAA41758 (PubMed:6208900).Curated
Sequence conflicti99 – 991G → R in AAA41758 (PubMed:6208900).Curated

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_006232043.2.
UniGeneiRn.160776.
Rn.8706.

Genome annotation databases

EnsembliENSRNOT00000074446; ENSRNOP00000067467; ENSRNOG00000050563.
GeneIDi192269.
KEGGirno:192269.

Cross-referencesi

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_006232043.2.
UniGeneiRn.160776.
Rn.8706.

3D structure databases

ProteinModelPortaliQ63396.
SMRiQ63396. Positions 63-127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi251393. 1 interaction.
IntActiQ63396. 2 interactions.
MINTiMINT-4598677.
STRINGi10116.ENSRNOP00000067467.

PTM databases

iPTMnetiQ63396.

Proteomic databases

PaxDbiQ63396.
PRIDEiQ63396.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000074446; ENSRNOP00000067467; ENSRNOG00000050563.
GeneIDi192269.
KEGGirno:192269.

Organism-specific databases

CTDi10923.
RGDi621582. Sub1.

Phylogenomic databases

eggNOGiKOG2712. Eukaryota.
ENOG410XUB8. LUCA.
GeneTreeiENSGT00390000008802.
HOGENOMiHOG000239157.
HOVERGENiHBG028243.
InParanoidiQ63396.
OMAiQWNQLKD.
OrthoDBiEOG76MKBV.
PhylomeDBiQ63396.
TreeFamiTF313859.

Miscellaneous databases

NextBioi622964.
PROiQ63396.

Gene expression databases

GenevisibleiQ63396. RN.

Family and domain databases

Gene3Di2.30.31.10. 1 hit.
InterProiIPR003173. PC4.
IPR009044. ssDNA-bd_transcriptional_reg.
[Graphical view]
PfamiPF02229. PC4. 1 hit.
[Graphical view]
SUPFAMiSSF54447. SSF54447. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Spleen.
  2. "Molecular cloning and characterization of a cDNA clone for a protein specifically expressed in embryo as well as in a chemically induced pancreatic B cell tumor of rat."
    Soma G., Kitahara N., Andoh T.
    Biochem. Biophys. Res. Commun. 124:164-171(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-127.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-17 AND SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTCP4_RAT
AccessioniPrimary (citable) accession number: Q63396
Secondary accession number(s): Q5M805
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 110 of the entry and version 3 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.