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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei50 – 512Cleavage

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi68 – 681K → G: Reduced ssDNA binding. 1 Publication
Mutagenesisi75 – 751R → G: Reduced ssDNA binding. 1 Publication
Mutagenesisi77 – 804FKGK → AGG: Loss of ssDNA binding. 1 Publication
Mutagenesisi86 – 861R → G: Loss of ssDNA binding. 1 Publication
Mutagenesisi101 – 1011K → G: Loss of ssDNA binding. 1 Publication

Organism-specific databases

PharmGKBiPA142670858.

Polymorphism and mutation databases

BioMutaiSUB1.
DMDMi1709514.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 127126Activated RNA polymerase II transcriptional coactivator p15PRO_0000215944Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41Phosphoserine1 Publication
Modified residuei9 – 91Phosphoserine1 Publication
Modified residuei10 – 101Phosphoserine1 Publication
Modified residuei11 – 111Phosphoserine1 Publication
Modified residuei13 – 131Phosphoserine2 Publications
Modified residuei15 – 151Phosphoserine2 Publications
Modified residuei17 – 171Phosphoserine3 Publications
Modified residuei19 – 191Phosphoserine3 Publications
Modified residuei35 – 351N6-acetyllysine1 Publication
Modified residuei53 – 531N6-acetyllysineBy similarity
Modified residuei68 – 681N6-acetyllysine1 Publication
Modified residuei118 – 1181Phosphoserine4 Publications

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP53999.
PaxDbiP53999.
PeptideAtlasiP53999.
PRIDEiP53999.

PTM databases

PhosphoSiteiP53999.

Expressioni

Gene expression databases

BgeeiP53999.
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. 32 interactions.
DIPiDIP-29044N.
IntActiP53999. 11 interactions.
MINTiMINT-138673.
STRINGi9606.ENSP00000265073.

Structurei

Secondary structure

1
127
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi63 – 675Combined sources
Beta strandi70 – 778Combined sources
Beta strandi80 – 9011Combined sources
Beta strandi92 – 943Combined sources
Beta strandi96 – 10510Combined sources
Helixi107 – 12620Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 63-127.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53999.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 5049RegulatoryAdd
BLAST
Regioni77 – 10125Interaction with ssDNAAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 1916Ser-richAdd
BLAST
Compositional biasi23 – 5331Lys-richAdd
BLAST
Compositional biasi50 – 589Ser-rich

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG299238.
GeneTreeiENSGT00390000008802.
HOVERGENiHBG028243.
InParanoidiP53999.
OMAiQWNQLKD.
OrthoDBiEOG76MKBV.
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111S → G.1 Publication
Corresponds to variant rs17850527 [ dbSNP | Ensembl ].
VAR_032870

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_011512245.1. XM_011513943.1.
XP_011512246.1. XM_011513944.1.
UniGeneiHs.229641.

Genome annotation databases

EnsembliENST00000265073; ENSP00000265073; ENSG00000113387.
ENST00000502897; ENSP00000427100; ENSG00000113387.
ENST00000506237; ENSP00000422078; ENSG00000113387.
ENST00000512913; ENSP00000422806; ENSG00000113387.
ENST00000515355; ENSP00000426850; ENSG00000113387.
GeneIDi10923.
KEGGihsa:10923.
UCSCiuc003jhs.2. human.

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_011512245.1. XM_011513943.1.
XP_011512246.1. XM_011513944.1.
UniGeneiHs.229641.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 63-127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116127. 32 interactions.
DIPiDIP-29044N.
IntActiP53999. 11 interactions.
MINTiMINT-138673.
STRINGi9606.ENSP00000265073.

PTM databases

PhosphoSiteiP53999.

Polymorphism and mutation databases

BioMutaiSUB1.
DMDMi1709514.

Proteomic databases

MaxQBiP53999.
PaxDbiP53999.
PeptideAtlasiP53999.
PRIDEiP53999.

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.
UCSCiuc003jhs.2. human.

Organism-specific databases

CTDi10923.
GeneCardsiGC05P032533.
HGNCiHGNC:19985. SUB1.
HPAiCAB015351.
HPA001311.
MIMi600503. gene.
neXtProtiNX_P53999.
PharmGKBiPA142670858.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG299238.
GeneTreeiENSGT00390000008802.
HOVERGENiHBG028243.
InParanoidiP53999.
OMAiQWNQLKD.
OrthoDBiEOG76MKBV.
PhylomeDBiP53999.
TreeFamiTF313859.

Miscellaneous databases

ChiTaRSiSUB1. human.
EvolutionaryTraceiP53999.
GeneWikiiSUB1.
GenomeRNAii10923.
NextBioi41499.
PROiP53999.
SOURCEiSearch...

Gene expression databases

BgeeiP53999.
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...

Publicationsi

« Hide 'large scale' publications
  1. "A novel mediator of class II gene transcription with homology to viral immediate-early transcriptional regulators."
    Kretzschmar M., Kaiser K., Lottspeich F., Meisterernst M.
    Cell 78:525-534(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION.
  2. "Purification, cloning, and characterization of a human coactivator, PC4, that mediates transcriptional activation of class II genes."
    Ge H., Roeder R.G.
    Cell 78:513-523(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-11 AND 81-97, FUNCTION.
  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], VARIANT GLY-11.
    Tissue: Bone marrow, Cervix, Lung and Prostate.
  4. "Phosphorylation negatively regulates the function of coactivator PC4."
    Ge H., Zhao Y., Chait B.T., Roeder R.G.
    Proc. Natl. Acad. Sci. U.S.A. 91:12691-12695(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, MASS SPECTROMETRY.
  5. "The coactivator p15 (PC4) initiates transcriptional activation during TFIIA-TFIID-promoter complex formation."
    Kaiser K., Stelzer G., Meisterernst M.
    EMBO J. 14:3520-3527(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
  6. "A dynamic model for PC4 coactivator function in RNA polymerase II transcription."
    Malik S., Guermah M., Roeder R.G.
    Proc. Natl. Acad. Sci. U.S.A. 95:2192-2197(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION BY CK2.
  7. "Evolutionarily conserved interaction between CstF-64 and PC4 links transcription, polyadenylation, and termination."
    Calvo O., Manley J.L.
    Mol. Cell 7:1013-1023(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSTF2.
  8. "Gradual phosphorylation regulates PC4 coactivator function."
    Jonker H.R.A., Wechselberger R.W., Pinkse M., Kaptein R., Folkers G.E.
    FEBS J. 273:1430-1444(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY, FUNCTION, DNA-BINDING, PHOSPHORYLATION AT SER-11; SER-13; SER-15; SER-17 AND SER-19.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-35 AND LYS-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-9; SER-10; SER-13; SER-15; SER-17; SER-19 AND SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "C-terminal domain of transcription cofactor PC4 reveals dimeric ssDNA binding site."
    Brandsen J., Werten S., van der Vliet P.C., Meisterernst M., Kroon J., Gros P.
    Nat. Struct. Biol. 4:900-903(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 63-127, FUNCTION, SUBUNIT.
  18. "The intrinsically unstructured domain of PC4 modulates the activity of the structured core through inter- and intramolecular interactions."
    Jonker H.R.A., Wechselberger R.W., Boelens R., Kaptein R., Folkers G.E.
    Biochemistry 45:5067-5081(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, FUNCTION, MUTAGENESIS OF LYS-68; ARG-75; 77-PHE--LYS-80; ARG-86 AND LYS-101.
  19. "A global transcription cofactor bound to juxtaposed strands of unwound DNA."
    Werten S., Moras D.
    Nat. Struct. Biol. 13:181-182(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 63-127 IN COMPLEX WITH SINGLE-STRANDED DNA, SUBUNIT.

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: July 22, 2015
This is version 144 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

External Data

Dasty 3

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 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.