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Q8N7H5 (PAF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA polymerase II-associated factor 1 homolog

Short name=hPAF1
Alternative name(s):
Pancreatic differentiation protein 2
Gene names
Name:PAF1
Synonyms:PD2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length531 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-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. Ref.1 Ref.10 Ref.11 Ref.12 Ref.13 Ref.16 Ref.17

Subunit structure

Component of the PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. Interacts with POLR2A, TCEA1, TTC37, KMT2A/MLL1, SUPT5H, RNF20 and RNF40. Interacts with UBE2E1. Interacts with influenza A strain H3N2 NS1 protein; the interaction interferes with host cell gene transcription, specifically with that of antiviral genes. Ref.1 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.17

Subcellular location

Nucleus. Note: Punctuate distribution throughout the nucleus except in nucleoli and the perinuclear chromatin. Ref.1

Sequence similarities

Belongs to the PAF1 family.

Sequence caution

The sequence AAC25503.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAW56880.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAW56881.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Wnt signaling pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseTumor suppressor
   DomainCoiled coil
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to lipopolysaccharide

Inferred from sequence or structural similarity. Source: UniProtKB

endodermal cell fate commitment

Inferred from sequence or structural similarity. Source: UniProtKB

histone H2B ubiquitination

Inferred from direct assay Ref.7. Source: UniProtKB

histone monoubiquitination

Inferred from direct assay Ref.7. Source: UniProtKB

mRNA polyadenylation

Inferred from mutant phenotype Ref.16. Source: UniProtKB

negative regulation of myeloid cell differentiation

Inferred from direct assay Ref.12. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mRNA 3'-end processing

Inferred from mutant phenotype Ref.16. Source: UniProtKB

positive regulation of transcription elongation from RNA polymerase II promoter

Inferred from direct assay Ref.13. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.13. Source: UniProtKB

stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCdc73/Paf1 complex

Inferred from direct assay Ref.7Ref.13. Source: UniProtKB

   Molecular_functionRNA polymerase II core binding

Inferred from direct assay Ref.8. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.8Ref.6Ref.7Ref.10Ref.13Ref.12Ref.17. Source: IntAct

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N7H5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8N7H5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     17-26: Missing.
     190-212: Missing.
     395-508: DEEQEKGSSS...SASPFPSGSE → VMLILRTMPT...QQSTFLVVCL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 531531RNA polymerase II-associated factor 1 homolog
PRO_0000326400

Regions

Coiled coil352 – 40049 Potential
Compositional bias358 – 45295Glu-rich

Natural variations

Alternative sequence17 – 2610Missing in isoform 2.
VSP_032650
Alternative sequence190 – 21223Missing in isoform 2.
VSP_032651
Alternative sequence395 – 508114DEEQE…PSGSE → VMLILRTMPTLMMRTEDRPK VAVTMIQTAAAMGVASGAGA TAAAPVPSPVAASTRPRRMA VKLQLLIPVKLIVTVTESQG IQGWFRHHYCEQQSTFLVVC L in isoform 2.
VSP_032652

Experimental info

Sequence conflict581F → I in BAA92020. Ref.3
Sequence conflict681K → R in BAC05305. Ref.3
Sequence conflict1521E → G in BAA92020. Ref.3
Sequence conflict3781E → G in BAA92020. Ref.3

Secondary structure

............. 531
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 8, 2008. Version 2.
Checksum: 756F800AA64255D6

FASTA53159,976
        10         20         30         40         50         60 
MAPTIQTQAQ REDGHRPNSH RTLPERSGVV CRVKYCNSLP DIPFDPKFIT YPFDQNRFVQ 

        70         80         90        100        110        120 
YKATSLEKQH KHDLLTEPDL GVTIDLINPD TYRIDPNVLL DPADEKLLEE EIQAPTSSKR 

       130        140        150        160        170        180 
SQQHAKVVPW MRKTEYISTE FNRYGISNEK PEVKIGVSVK QQFTEEEIYK DRDSQITAIE 

       190        200        210        220        230        240 
KTFEDAQKSI SQHYSKPRVT PVEVMPVFPD FKMWINPCAQ VIFDSDPAPK DTSGAAALEM 

       250        260        270        280        290        300 
MSQAMIRGMM DEEGNQFVAY FLPVEETLKK RKRDQEEEMD YAPDDVYDYK IAREYNWNVK 

       310        320        330        340        350        360 
NKASKGYEEN YFFIFREGDG VYYNELETRV RLSKRRAKAG VQSGTNALLV VKHRDMNEKE 

       370        380        390        400        410        420 
LEAQEARKAQ LENHEPEEEE EEEMETEEKE AGGSDEEQEK GSSSEKEGSE DEHSGSESER 

       430        440        450        460        470        480 
EEGDRDEASD KSGSGEDESS EDEARAARDK EEIFGSDADS EDDADSDDED RGQAQGGSDN 

       490        500        510        520        530 
DSDSGSNGGG QRSRSHSRSA SPFPSGSEHS AQEDGSEAAA SDSSEADSDS D 

« Hide

Isoform 2 [UniParc].

Checksum: 619FCF62CF34627D
Show »

FASTA48555,039

References

« Hide 'large scale' references
[1]"The human homologue of the RNA polymerase II-associated factor 1 (hPaf1), localized on the 19q13 amplicon, is associated with tumorigenesis."
Moniaux N., Nemos C., Schmied B.M., Chauhan S.C., Deb S., Morikane K., Choudhury A., Vanlith M., Sutherlin M., Sikela J.M., Hollingsworth M.A., Batra S.K.
Oncogene 25:3247-3257(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH POLR2A, FUNCTION.
Tissue: Fetal pancreas.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 1).
Tissue: Muscle and Placenta.
[6]"The human PAF complex coordinates transcription with events downstream of RNA synthesis."
Zhu B., Mandal S.S., Pham A.D., Zheng Y., Erdjument-Bromage H., Batra S.K., Tempst P., Reinberg D.
Genes Dev. 19:1668-1673(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TTC37.
[7]"Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation."
Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P., Reinberg D.
Mol. Cell 20:601-611(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBE2E1.
[8]"The HRPT2 tumor suppressor gene product parafibromin associates with human PAF1 and RNA polymerase II."
Yart A., Gstaiger M., Wirbelauer C., Pecnik M., Anastasiou D., Hess D., Krek W.
Mol. Cell. Biol. 25:5052-5060(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDC73 AND POLR2A.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"RAD6-mediated transcription-coupled H2B ubiquitylation directly stimulates H3K4 methylation in human cells."
Kim J., Guermah M., McGinty R.K., Lee J.S., Tang Z., Milne T.A., Shilatifard A., Muir T.W., Roeder R.G.
Cell 137:459-471(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE PAF1 COMPLEX, INTERACTION WITH RNF20 AND RNF40.
[11]"DSIF, the Paf1 complex, and Tat-SF1 have nonredundant, cooperative roles in RNA polymerase II elongation."
Chen Y., Yamaguchi Y., Tsugeno Y., Yamamoto J., Yamada T., Nakamura M., Hisatake K., Handa H.
Genes Dev. 23:2765-2777(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE PAF1 COMPLEX, FUNCTION OF THE PAF1 COMPLEX, INTERACTION WITH SUPT5H.
[12]"The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis."
Muntean A.G., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly J.A., Basrur V., Elenitoba-Johnson K.S., Hess J.L.
Cancer Cell 17:609-621(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE PAF1 COMPLEX, INTERACTION WITH KMT2A.
[13]"The human PAF1 complex acts in chromatin transcription elongation both independently and cooperatively with SII/TFIIS."
Kim J., Guermah M., Roeder R.G.
Cell 140:491-503(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX, FUNCTION OF THE PAF1 COMPLEX, INTERACTION WITH TCEA1.
[14]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Transcriptional activators enhance polyadenylation of mRNA precursors."
Nagaike T., Logan C., Hotta I., Rozenblatt-Rosen O., Meyerson M., Manley J.L.
Mol. Cell 41:409-418(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, FUNCTION OF THE PAF1 COMPLEX.
[17]"Suppression of the antiviral response by an influenza histone mimic."
Marazzi I., Ho J.S., Kim J., Manicassamy B., Dewell S., Albrecht R.A., Seibert C.W., Schaefer U., Jeffrey K.L., Prinjha R.K., Lee K., Garcia-Sastre A., Roeder R.G., Tarakhovsky A.
Nature 483:428-433(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE PAF1 COMPLEX, INTERACTION WITH INFLUENZA A NS1 PROTEIN.
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ401156 mRNA. Translation: CAC20564.1.
AK001985 mRNA. Translation: BAA92020.1.
AK098423 mRNA. Translation: BAC05305.1.
AC005239 Genomic DNA. Translation: AAC25503.1. Sequence problems.
CH471126 Genomic DNA. Translation: EAW56880.1. Sequence problems.
CH471126 Genomic DNA. Translation: EAW56881.1. Sequence problems.
BC000017 mRNA. Translation: AAH00017.1.
BC013402 mRNA. Translation: AAH13402.1.
CCDSCCDS12533.1. [Q8N7H5-1]
RefSeqNP_001243755.1. NM_001256826.1.
NP_061961.2. NM_019088.3. [Q8N7H5-1]
UniGeneHs.466714.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4M6TX-ray2.50A170-250[»]
ProteinModelPortalQ8N7H5.
SMRQ8N7H5. Positions 170-257.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120081. 36 interactions.
DIPDIP-48673N.
IntActQ8N7H5. 19 interactions.
STRING9606.ENSP00000221265.

Polymorphism databases

DMDM182670295.

Proteomic databases

MaxQBQ8N7H5.
PaxDbQ8N7H5.
PRIDEQ8N7H5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000221265; ENSP00000221265; ENSG00000006712. [Q8N7H5-1]
GeneID54623.
KEGGhsa:54623.
UCSCuc002old.4. human. [Q8N7H5-1]

Organism-specific databases

CTD54623.
GeneCardsGC19M039876.
HGNCHGNC:25459. PAF1.
HPAHPA041875.
MIM610506. gene.
neXtProtNX_Q8N7H5.
PharmGKBPA142671206.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG297168.
HOGENOMHOG000115425.
HOVERGENHBG053131.
InParanoidQ8N7H5.
KOK15174.
OMAYEVLTEH.
PhylomeDBQ8N7H5.
TreeFamTF313642.

Gene expression databases

ArrayExpressQ8N7H5.
BgeeQ8N7H5.
CleanExHS_PAF1.
GenevestigatorQ8N7H5.

Family and domain databases

InterProIPR007133. RNA_pol_II-assoc_Paf1.
[Graphical view]
PANTHERPTHR23188. PTHR23188. 1 hit.
PfamPF03985. Paf1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPAF1. human.
GenomeRNAi54623.
NextBio57158.
PROQ8N7H5.
SOURCESearch...

Entry information

Entry namePAF1_HUMAN
AccessionPrimary (citable) accession number: Q8N7H5
Secondary accession number(s): O75239, Q9H166, Q9NUU9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: April 8, 2008
Last modified: July 9, 2014
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM