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Protein

Activated RNA polymerase II transcriptional coactivator p15

Gene

SUB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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).7 Publications

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • single-stranded DNA binding Source: UniProtKB
  • transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific binding Source: Ensembl
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000113387-MONOMER.
SIGNORiP53999.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:19985. SUB1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • nucleolus Source: HPA
  • nucleus Source: HPA
  • transcription factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi68K → G: Reduced ssDNA binding. 1 Publication1
Mutagenesisi75R → G: Reduced ssDNA binding. 1 Publication1
Mutagenesisi77 – 80FKGK → AGG: Loss of ssDNA binding. 1 Publication4
Mutagenesisi86R → G: Loss of ssDNA binding. 1 Publication1
Mutagenesisi101K → G: Loss of ssDNA binding. 1 Publication1

Organism-specific databases

DisGeNETi10923.
OpenTargetsiENSG00000113387.
PharmGKBiPA142670858.

Polymorphism and mutation databases

BioMutaiSUB1.
DMDMi1709514.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002159442 – 127Activated RNA polymerase II transcriptional coactivator p15Add BLAST126

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei4PhosphoserineCombined sources1
Modified residuei9PhosphoserineCombined sources1
Modified residuei10PhosphoserineCombined sources1
Modified residuei11Phosphoserine1 Publication1
Modified residuei13PhosphoserineCombined sources1 Publication1
Modified residuei15PhosphoserineCombined sources1 Publication1
Modified residuei17PhosphoserineCombined sources1 Publication1
Modified residuei19PhosphoserineCombined sources1 Publication1
Modified residuei35N6-acetyllysineCombined sources1
Modified residuei53N6-acetyllysineBy similarity1
Modified residuei55PhosphoserineCombined sources1
Modified residuei56PhosphoserineCombined sources1
Modified residuei57PhosphoserineCombined sources1
Modified residuei58PhosphoserineCombined sources1
Modified residuei68N6-acetyllysine; alternateCombined sources1
Cross-linki68Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Modified residuei118PhosphoserineCombined sources1

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. Seems to be phosphorylated in vivo by CK2 in at least 7 sites in the N-terminal Ser-rich region.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei50 – 51Cleavage2

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP53999.
PaxDbiP53999.
PeptideAtlasiP53999.
PRIDEiP53999.
TopDownProteomicsiP53999.

PTM databases

iPTMnetiP53999.
PhosphoSitePlusiP53999.
SwissPalmiP53999.

Expressioni

Gene expression databases

BgeeiENSG00000113387.
CleanExiHS_SUB1.
ExpressionAtlasiP53999. baseline and differential.
GenevisibleiP53999. HS.

Organism-specific databases

HPAiCAB015351.
HPA001311.

Interactioni

Subunit structurei

Homodimer. Interacts with CSTF2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CSTF2P33240-13EBI-998260,EBI-711374
Rep68P031323EBI-998260,EBI-7387242From a different organism.

Protein-protein interaction databases

BioGridi116127. 64 interactors.
DIPiDIP-29044N.
IntActiP53999. 12 interactors.
MINTiMINT-138673.
STRINGi9606.ENSP00000265073.

Structurei

Secondary structure

1127
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi63 – 67Combined sources5
Beta strandi70 – 77Combined sources8
Beta strandi80 – 90Combined sources11
Beta strandi92 – 94Combined sources3
Beta strandi96 – 105Combined sources10
Helixi107 – 126Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PCFX-ray1.74A/B/C/D/E/F/G/H63-127[»]
2C62X-ray1.74A/B63-127[»]
2PHENMR-A/B63-127[»]
4USGX-ray1.97A/B63-127[»]
ProteinModelPortaliP53999.
SMRiP53999.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53999.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 50RegulatoryAdd BLAST49
Regioni77 – 101Interaction with ssDNAAdd BLAST25

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi4 – 19Ser-richAdd BLAST16
Compositional biasi23 – 53Lys-richAdd BLAST31
Compositional biasi50 – 58Ser-rich9

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2712. Eukaryota.
ENOG410XUB8. LUCA.
GeneTreeiENSGT00390000008802.
HOVERGENiHBG028243.
InParanoidiP53999.
OMAiQWNQLKD.
OrthoDBiEOG091G14VO.
PhylomeDBiP53999.
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.

P53999-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKSKELVSS SSSGSDSDSE VDKKLKRKKQ VAPEKPVKKQ KTGETSRALS
60 70 80 90 100
SSKQSSSSRD DNMFQIGKMR YVSVRDFKGK VLIDIREYWM DPEGEMKPGR
110 120
KGISLNPEQW SQLKEQISDI DDAVRKL
Length:127
Mass (Da):14,395
Last modified:January 23, 2007 - v3
Checksum:i0DAE0CAAAD5E4E15
GO

Mass spectrometryi

Molecular mass is 14266±4 Da from positions 2 - 127. Determined by MALDI. 1 Publication
Molecular mass is 14263 Da from positions 2 - 127. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03287011S → G.1 PublicationCorresponds to variant rs17850527dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79805 mRNA. Translation: CAA56200.1.
U12979 mRNA. Translation: AAA20980.1.
BC009610 mRNA. Translation: AAH09610.1.
BC010537 mRNA. Translation: AAH10537.1.
BC018189 mRNA. Translation: AAH18189.1.
BC022339 mRNA. Translation: AAH22339.1.
CCDSiCCDS3897.1.
PIRiA54670.
RefSeqiNP_006704.3. NM_006713.3.
XP_011512246.1. XM_011513944.2.
XP_016864475.1. XM_017008986.1.
XP_016864476.1. XM_017008987.1.
UniGeneiHs.229641.

Genome annotation databases

EnsembliENST00000265073; ENSP00000265073; ENSG00000113387.
ENST00000502897; ENSP00000427100; ENSG00000113387.
ENST00000506237; ENSP00000422078; ENSG00000113387.
ENST00000512913; ENSP00000422806; ENSG00000113387.
ENST00000515355; ENSP00000426850; ENSG00000113387.
GeneIDi10923.
KEGGihsa:10923.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79805 mRNA. Translation: CAA56200.1.
U12979 mRNA. Translation: AAA20980.1.
BC009610 mRNA. Translation: AAH09610.1.
BC010537 mRNA. Translation: AAH10537.1.
BC018189 mRNA. Translation: AAH18189.1.
BC022339 mRNA. Translation: AAH22339.1.
CCDSiCCDS3897.1.
PIRiA54670.
RefSeqiNP_006704.3. NM_006713.3.
XP_011512246.1. XM_011513944.2.
XP_016864475.1. XM_017008986.1.
XP_016864476.1. XM_017008987.1.
UniGeneiHs.229641.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PCFX-ray1.74A/B/C/D/E/F/G/H63-127[»]
2C62X-ray1.74A/B63-127[»]
2PHENMR-A/B63-127[»]
4USGX-ray1.97A/B63-127[»]
ProteinModelPortaliP53999.
SMRiP53999.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116127. 64 interactors.
DIPiDIP-29044N.
IntActiP53999. 12 interactors.
MINTiMINT-138673.
STRINGi9606.ENSP00000265073.

PTM databases

iPTMnetiP53999.
PhosphoSitePlusiP53999.
SwissPalmiP53999.

Polymorphism and mutation databases

BioMutaiSUB1.
DMDMi1709514.

Proteomic databases

EPDiP53999.
PaxDbiP53999.
PeptideAtlasiP53999.
PRIDEiP53999.
TopDownProteomicsiP53999.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265073; ENSP00000265073; ENSG00000113387.
ENST00000502897; ENSP00000427100; ENSG00000113387.
ENST00000506237; ENSP00000422078; ENSG00000113387.
ENST00000512913; ENSP00000422806; ENSG00000113387.
ENST00000515355; ENSP00000426850; ENSG00000113387.
GeneIDi10923.
KEGGihsa:10923.

Organism-specific databases

CTDi10923.
DisGeNETi10923.
GeneCardsiSUB1.
HGNCiHGNC:19985. SUB1.
HPAiCAB015351.
HPA001311.
MIMi600503. gene.
neXtProtiNX_P53999.
OpenTargetsiENSG00000113387.
PharmGKBiPA142670858.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2712. Eukaryota.
ENOG410XUB8. LUCA.
GeneTreeiENSGT00390000008802.
HOVERGENiHBG028243.
InParanoidiP53999.
OMAiQWNQLKD.
OrthoDBiEOG091G14VO.
PhylomeDBiP53999.
TreeFamiTF313859.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000113387-MONOMER.
SIGNORiP53999.

Miscellaneous databases

ChiTaRSiSUB1. human.
EvolutionaryTraceiP53999.
GeneWikiiSUB1.
GenomeRNAii10923.
PROiP53999.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000113387.
CleanExiHS_SUB1.
ExpressionAtlasiP53999. baseline and differential.
GenevisibleiP53999. HS.

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...

Entry informationi

Entry nameiTCP4_HUMAN
AccessioniPrimary (citable) accession number: P53999
Secondary accession number(s): Q96L29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.