Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
PAF1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
PAF1 Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non- phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of MLL1; it promotes leukemogenesis though association with MLL-rearranged oncoproteins, such as MLL-MLLT3/AF9 and MLL-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Connects PAF1C with the RNF20/40 E3 ubiquitin-protein ligase complex. Involved in polyadenylation of mRNA precursors. Has oncogenic activity in vivo and in vitro. Belongs to the PAF1 family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Transcription regulation
Molecular Function: protein binding; chromatin binding
Biological Process: histone monoubiquitination; Wnt receptor signaling pathway; negative regulation of myeloid cell differentiation; endodermal cell fate commitment; transcription, DNA-dependent; positive regulation of RNA elongation from RNA polymerase II promoter; histone H2B ubiquitination; stem cell maintenance; positive regulation of mRNA 3'-end processing; mRNA polyadenylation; positive regulation of transcription from RNA polymerase II promoter; negative regulation of transcription from RNA polymerase II promoter
Reference #:  Q9H166 (UniProtKB)
Alt. Names/Synonyms: F23149_1; FLJ11123; hPAF1; PAF1; Paf1, RNA polymerase II associated factor, homolog (S. cerevisiae); Pancreatic differentiation protein 2; PD2; RNA polymerase II-associated factor 1 homolog
Gene Symbols: PAF1
Molecular weight: 59,976 Da
Basal Isoelectric point: 4.53  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PAF1

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 Y61-p DQNRFVQykATSLEK
0 1 K62-u QNRFVQykATSLEKQ
0 2 K106-u LLDPADEkLLEEEIQ
0 2 S117-p EEIQAPTsSkRSQQH
0 1 K119-u IQAPTsSkRSQQHAK
0 1 K133-u KVVPWMRkTEyISTE
0 3 Y136-p PWMRkTEyISTEFNR
0 1 K150-u RYGISNEkPEVKIGV
0 1 K181-u SQITAIEkTFEDAQK
0 1 K269-u LPVEETLkKRkRDQE
0 1 K272-u EETLkKRkRDQEEEM
0 2 K290-u PDDVYDYkIAREYNW
0 1 K305-u NVKNKASkGYEENYF
0 1 K352-u TNALLVVkHRDMNEk
0 1 K359-u kHRDMNEkELEAQEA
0 1 T386-p EEEEEMEtEEKEAGG
0 4 S456-p DKEEIFGsDADsEDD
0 4 S460-p IFGsDADsEDDADsD
0 6 S466-p DsEDDADsDDEDRGQ
0 1 S516-p HSAQEDGsEAAASDS
  mouse

 
Y61 DQNRFVQYKATSLEK
K62 QNRFVQYKATSLEKQ
K106 LLDPADEKLLEEEIQ
S117 EEIQAPTSSKRSQQH
K119 IQAPTSSKRSQQHAK
K133 KVVPWMRKTEYISTE
Y136 PWMRKTEYISTEFNR
K150 RYGISNEKPEVKIGV
K181 SQITAIEKTFEDAQK
K269 LPVEETLKKRKRDQE
K272 EETLKKRKRDQEEEM
K290 PDDVYDYKIAREYNW
K305 NVKNKASKGYEENYF
K352 TNALLVVKHRDMNEK
K359 KHRDMNEKELEAQEA
A386 EEEEEMEAEEKEAGG
S456-p DKEEIFGsDADsEDD
S460-p IFGsDADsEDDADsD
S466-p DsEDDADsDDEDRGQ
S520 HSAQEDGSEAAASDS
  rat

 
Y61 DQNRFVQYKATSLEK
K62 QNRFVQYKATSLEKQ
K106 LLDPADEKLLEEEIQ
S117 EEIQAPTSSKRSQQH
K119 IQAPTSSKRSQQHAK
K133 KVVPWMRKTEYISTE
Y136 PWMRKTEYISTEFNR
K150 RYGISNEKPEVKIGV
K181 SQITAIEKTFEDAQK
K269 LPVEETLKKRKRDQE
K272 EETLKKRKRDQEEEM
K290 PDDVYDYKIAREYNW
K305 NVKNKASKGYEENYF
K352 TNALLVVKHRDMNEK
K359 KHRDMNEKELEAQEA
A386 EEEEEMEAEEKEAGG
S456 DKEEIFGSDADSEDD
S460 IFGSDADSEDDADSD
S466 DSEDDADSDDEDRGQ
S520 HSAQEDGSEAAASDS
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.