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P11031 (TCP4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Activated RNA polymerase II transcriptional coactivator p15
Alternative name(s):
Positive cofactor 4
Short name=PC4
SUB1 homolog
Single-stranded DNA-binding protein p9
p14
Gene names
Name:Sub1
Synonyms:Pc4, Rpo2tc1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length127 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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).

Subunit structure

Homodimer. Interacts with CSTF2 By similarity.

Subcellular location

Nucleus.

Post-translational modification

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.

Sequence similarities

Belongs to the transcriptional coactivator PC4 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 127126Activated RNA polymerase II transcriptional coactivator p15
PRO_0000023286

Regions

Region2 – 5049Regulatory
Region77 – 10125Interaction with ssDNA By similarity
Compositional bias4 – 1916Ser-rich
Compositional bias23 – 5331Lys-rich
Compositional bias51 – 588Ser-rich

Sites

Site50 – 512Cleavage

Amino acid modifications

Modified residue111Phosphoserine By similarity
Modified residue131Phosphoserine By similarity
Modified residue151Phosphoserine By similarity
Modified residue171Phosphoserine By similarity
Modified residue191Phosphoserine By similarity
Modified residue351N6-acetyllysine By similarity
Modified residue531N6-acetyllysine Ref.4
Modified residue681N6-acetyllysine By similarity
Modified residue1181Phosphoserine By similarity

Experimental info

Sequence conflict461S → P in BAE27090. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P11031 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 12D58716F40FEB1C

FASTA12714,427
        10         20         30         40         50         60 
MPKSKELVSS SSSGSDSDSE VEKKLKRKKQ AVPEKPVKKQ KPGETSRALA SSKQSSSSRD 

        70         80         90        100        110        120 
DNMFQIGKMR YVSVRDFKGK ILIDIREYWM DSEGEMKPGR KGISLNMEQW SQLKEQISDI 


DDAVRKL 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a novel 9-kDa polypeptide from nuclear extracts. DNA binding properties, primary structure, and in vitro expression."
Ballard D.W., Philbrick W.M., Bothwell A.L.M.
J. Biol. Chem. 263:8450-8457(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 51-81 AND 108-127, PROTEOLYTIC PROCESSING, DNA-BINDING.
[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. expand/collapse author list , 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].
Strain: C57BL/6J, DBA/2 and NOD.
Tissue: Bone marrow.
[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].
Strain: Czech II.
Tissue: Mammary gland.
[4]"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-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03750 mRNA. Translation: AAA37317.1.
AK048371 mRNA. Translation: BAC33314.1.
AK049260 mRNA. Translation: BAC33642.1.
AK132021 mRNA. Translation: BAE20946.1.
AK146335 mRNA. Translation: BAE27090.1.
AK151734 mRNA. Translation: BAE30649.1.
AK154114 mRNA. Translation: BAE32384.1.
BC010967 mRNA. Translation: AAH10967.1.
CCDSCCDS27387.1.
PIRA28084.
RefSeqNP_035424.1. NM_011294.3.
XP_006520105.1. XM_006520042.1.
UniGeneMm.41746.

3D structure databases

ProteinModelPortalP11031.
SMRP11031. Positions 63-127.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202999. 2 interactions.
IntActP11031. 2 interactions.
MINTMINT-4137265.

PTM databases

PhosphoSiteP11031.

Proteomic databases

MaxQBP11031.
PaxDbP11031.
PRIDEP11031.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022816; ENSMUSP00000022816; ENSMUSG00000022205.
ENSMUST00000110504; ENSMUSP00000106130; ENSMUSG00000022205.
GeneID20024.
KEGGmmu:20024.
UCSCuc007vhj.1. mouse.

Organism-specific databases

CTD10923.
MGIMGI:104811. Sub1.

Phylogenomic databases

eggNOGNOG299238.
GeneTreeENSGT00390000008802.
HOGENOMHOG000239157.
HOVERGENHBG028243.
InParanoidP11031.
OMAREYWMNQ.
OrthoDBEOG76MKBV.
PhylomeDBP11031.
TreeFamTF313859.

Gene expression databases

BgeeP11031.
CleanExMM_SUB1.
GenevestigatorP11031.

Family and domain databases

Gene3D2.30.31.10. 1 hit.
InterProIPR003173. PC4.
IPR009044. ssDNA-bd_transcriptional_reg.
[Graphical view]
PfamPF02229. PC4. 1 hit.
[Graphical view]
SUPFAMSSF54447. SSF54447. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSUB1. mouse.
NextBio297547.
PROP11031.
SOURCESearch...

Entry information

Entry nameTCP4_MOUSE
AccessionPrimary (citable) accession number: P11031
Secondary accession number(s): Q3UJR5, Q543N2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot