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Q6P1J9 (CDC73_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Parafibromin
Alternative name(s):
Cell division cycle protein 73 homolog
Hyperparathyroidism 2 protein
Gene names
Name:CDC73
Synonyms:C1orf28, HRPT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length531 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tumor suppressor probably involved in transcriptional and post-transcriptional control pathways. May be involved in cell cycle progression through the regulation of cyclin D1/PRAD1 expression. 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 cleavage and polyadenylation specificity factor (CPSF) complex and the cleavage stimulation factor (CSTF) complex, and with Wnt signaling. Involved in polyadenylation of mRNA precursors. Ref.7 Ref.8 Ref.9 Ref.13 Ref.14 Ref.17 Ref.18 Ref.19 Ref.20 Ref.23

Subunit structure

Component of the PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. Interacts with POLR2A, CPSF1, CPSF4, CSTF2, KMT2A/MLL1 and CTNNB1. Interacts with a Set1-like complex that has histone methyltransferase activity and methylates histone H3. Found in a complex with BCL9L or BCL9, CDC73, CTNNB1 and PYGO1 indicative for the participation in a nuclear Wnt signaling complex. Ref.7 Ref.8 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20

Subcellular location

Nucleus Ref.7 Ref.8 Ref.9.

Tissue specificity

Found in adrenal and parathyroid glands, kidney and heart. Ref.9

Involvement in disease

Familial isolated hyperparathyroidism (FIHP) [MIM:145000]: Autosomal dominant disorder characterized by hypercalcemia, elevated parathyroid hormone (PTH) levels, and uniglandular or multiglandular parathyroid tumors.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.11 Ref.26 Ref.28 Ref.33

Hyperparathyroidism-jaw tumor syndrome (HPT-JT) [MIM:145001]: Autosomal dominant, multiple neoplasia syndrome primarily characterized by hyperparathyroidism due to parathyroid tumors. Thirty percent of individuals with HPT-JT may also develop ossifying fibromas, primarily of the mandible and maxilla, which are distinct from the brown tumors associated with severe hyperparathyroidism. Kidney lesions may also occur in HPT-JT as bilateral cysts, renal hamartomas or Wilms tumors.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.27 Ref.28

Parathyroid carcinoma (PRTC) [MIM:608266]: These cancers characteristically result in more profound clinical manifestations of hyperparathyroidism than do parathyroid adenomas, the most frequent cause of primary hyperparathyroidism. Early en bloc resection of the primary tumor is the only curative treatment.
Note: The gene represented in this entry is involved in disease pathogenesis. Ref.12

Sequence similarities

Belongs to the CDC73 family.

Sequence caution

The sequence AAH07325.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 300.

The sequence BAB15608.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processCell cycle
Transcription
Transcription regulation
Wnt signaling pathway
   Cellular componentNucleus
   DiseaseDisease mutation
Tumor suppressor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle

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 PubMed 16307923. Source: UniProtKB

histone monoubiquitination

Inferred from direct assay PubMed 16307923. Source: UniProtKB

mRNA polyadenylation

Inferred from mutant phenotype Ref.23. Source: UniProtKB

negative regulation of G1/S transition of mitotic cell cycle

Inferred from direct assay Ref.13. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay Ref.13. Source: UniProtKB

negative regulation of epithelial cell proliferation

Inferred from mutant phenotype PubMed 18987311. Source: UniProtKB

negative regulation of fibroblast proliferation

Inferred from mutant phenotype PubMed 18987311. Source: UniProtKB

negative regulation of myeloid cell differentiation

Inferred from direct assay Ref.19. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 18987311. Source: UniProtKB

positive regulation of Wnt signaling pathway

Inferred from direct assay Ref.14. Source: UniProtKB

positive regulation of mRNA 3'-end processing

Inferred from mutant phenotype Ref.18. Source: UniProtKB

positive regulation of transcription elongation from RNA polymerase II promoter

Inferred from direct assay Ref.20. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.20. Source: UniProtKB

protein destabilization

Inferred from mutant phenotype PubMed 18987311. Source: UniProtKB

stem cell maintenance

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCdc73/Paf1 complex

Inferred from direct assay PubMed 16307923PubMed 18987311Ref.20. Source: UniProtKB

nucleus

Inferred from direct assay Ref.8. Source: UniProtKB

   Molecular_functionRNA polymerase II core binding

Inferred from direct assay Ref.8. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8PubMed 16024656Ref.14Ref.15PubMed 19410543Ref.20Ref.19. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 531530Parafibromin
PRO_0000191803

Regions

Region200 – 531332Interaction with POLR2A and PAF1
Region200 – 25051Interaction with CTNNB1
Motif125 – 13915Nuclear localization signal Ref.10
Compositional bias361 – 3644Poly-Ile

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.24 Ref.25
Modified residue2121Phosphoserine Ref.16 Ref.21

Natural variations

Natural variant21A → S Found in parathyroid adenoma samples; somatic mutation; parathyroid adenoma samples are from a patient with isolated hyperparathyroidism who also carries germline mutation P-91. Ref.31
VAR_064927
Natural variant5 – 106Missing Found in a parathyroid carcinoma sample; somatic mutation; parathyroid carcinoma sample is from a patient with hyperparathyroidism-jaw tumor syndrome who also carries a germline mutation causing a splicing defect.
VAR_064928
Natural variant341K → Q Found in a clear cell renal carcinoma sample; somatic mutation; unlike wild-type protein the mutant is defective in suppressing CCND1 expression in vivo. Ref.32
VAR_064929
Natural variant591S → F Found in a parathyroid carcinoma sample; somatic mutation. Ref.30
VAR_064930
Natural variant631L → P Found in a kindred with familial hyperparathyroidism. Ref.33
VAR_064931
Natural variant641L → P in FIHP; does not affect interaction with the Pfa1 complex. Ref.7 Ref.11 Ref.26
VAR_024082
Natural variant911R → P Found in a patient with isolated hyperparathyroidism and parathyroid adenomas. Ref.31
VAR_064932
Natural variant951L → P Found in a parathyroid adenoma sample; somatic mutation; parathyroid adenoma sample is from a patient with familial hyperparathyroidism who also carries a germline frameshift mutation. Ref.28
VAR_064933
Natural variant2721N → S Found in a parathyroid adenoma sample. Ref.29
VAR_064934
Natural variant2921R → K Found in a Wilms tumor sample; somatic mutation. Ref.32
VAR_064935
Natural variant3791D → N in HPT-JT. Ref.28
VAR_064936
Natural variant3841L → P.
Corresponds to variant rs35590728 [ dbSNP | Ensembl ].
VAR_031825

Experimental info

Sequence conflict1231Q → G in AAH14351. Ref.5
Sequence conflict184 – 1874AIKA → CNQT in BAB15608. Ref.2
Sequence conflict3721I → K in BAB15608. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q6P1J9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 894A7448DBC0E793

FASTA53160,577
        10         20         30         40         50         60 
MADVLSVLRQ YNIQKKEIVV KGDEVIFGEF SWPKNVKTNY VVWGTGKEGQ PREYYTLDSI 

        70         80         90        100        110        120 
LFLLNNVHLS HPVYVRRAAT ENIPVVRRPD RKDLLGYLNG EASTSASIDR SAPLEIGLQR 

       130        140        150        160        170        180 
STQVKRAADE VLAEAKKPRI EDEECVRLDK ERLAARLEGH KEGIVQTEQI RSLSEAMSVE 

       190        200        210        220        230        240 
KIAAIKAKIM AKKRSTIKTD LDDDITALKQ RSFVDAEVDV TRDIVSRERV WRTRTTILQS 

       250        260        270        280        290        300 
TGKNFSKNIF AILQSVKARE EGRAPEQRPA PNAAPVDPTL RTKQPIPAAY NRYDQERFKG 

       310        320        330        340        350        360 
KEETEGFKID TMGTYHGMTL KSVTEGASAR KTQTPAAQPV PRPVSQARPP PNQKKGSRTP 

       370        380        390        400        410        420 
IIIIPAATTS LITMLNAKDL LQDLKFVPSD EKKKQGCQRE NETLIQRRKD QMQPGGTAIS 

       430        440        450        460        470        480 
VTVPYRVVDQ PLKLMPQDWD RVVAVFVQGP AWQFKGWPWL LPDGSPVDIF AKIKAFHLKY 

       490        500        510        520        530 
DEVRLDPNVQ KWDVTVLELS YHKRHLDRPV FLRFWETLDR YMVKHKSHLR F 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of 13 novel transcripts and the human RGS8 gene from the 1q25 region encompassing the hereditary prostate cancer (HPC1) locus."
Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M., Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H., Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M., Carpten J.D.
Genomics 73:211-222(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [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].
Tissue: Eye and Urinary bladder.
[6]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W., Ramsay A., Leung H.Y.
Submitted (FEB-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-9; 38-47; 78-87; 111-120; 127-136; 172-181; 212-222; 235-243; 248-257; 332-342; 379-385 AND 400-407, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic kidney and Ovarian carcinoma.
[7]"The parafibromin tumor suppressor protein is part of a human Paf1 complex."
Rozenblatt-Rosen O., Hughes C.M., Nannepaga S.J., Shanmugam K.S., Copeland T.D., Guszczynski T., Resau J.H., Meyerson M.
Mol. Cell. Biol. 25:612-620(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PAF1; LEO1 AND POLR2A, INTERACTION WITH SET1-LIKE COMPLEX, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT FIHP PRO-64.
[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: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PAF1 AND POLR2A.
[9]"Parafibromin, product of the hyperparathyroidism-jaw tumor syndrome gene HRPT2, regulates cyclin D1/PRAD1 expression."
Woodard G.E., Lin L., Zhang J.-H., Agarwal S.K., Marx S.J., Simonds W.F.
Oncogene 24:1272-1276(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[10]"Identification of a functional bipartite nuclear localization signal in the tumor suppressor parafibromin."
Hahn M.A., Marsh D.J.
Oncogene 24:6241-6248(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF NUCLEAR LOCALIZATION SIGNAL.
[11]"HRPT2, encoding parafibromin, is mutated in hyperparathyroidism-jaw tumor syndrome."
Carpten J.D., Robbins C.M., Villablanca A., Forsberg L., Presciuttini S., Bailey-Wilson J., Simonds W.F., Gillanders E.M., Kennedy A.M., Chen J.D., Agarwal S.K., Sood R., Jones M.P., Moses T.Y., Haven C., Petillo D., Leotlela P.D., Harding B. expand/collapse author list , Cameron D., Pannett A.A., Hoeoeg A., Heath H. III, James-Newton L.A., Robinson B., Zarbo R.J., Cavaco B.M., Wassif W., Perrier N.D., Rosen I.B., Kristoffersson U., Turnpenny P.D., Farnebo L.-O., Besser G.M., Jackson C.E., Morreau H., Trent J.M., Thakker R.V., Marx S.J., Teh B.T., Larsson C., Hobbs M.R.
Nat. Genet. 32:676-680(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HPT-JT, VARIANT FIHP PRO-64.
[12]"Somatic and germ-line mutations of the HRPT2 gene in sporadic parathyroid carcinoma."
Shattuck T.M., Vaelimaeki S., Obara T., Gaz R.D., Clark O.H., Shoback D., Wierman M.E., Tojo K., Robbins C.M., Carpten J.D., Farnebo L.-O., Larsson C., Arnold A.
N. Engl. J. Med. 349:1722-1729(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PRTC.
[13]"Parafibromin inhibits cancer cell growth and causes G1 phase arrest."
Zhang C., Kong D., Tan M.H., Pappas D.L. Jr., Wang P.F., Chen J., Farber L., Zhang N., Koo H.M., Weinreich M., Williams B.O., Teh B.T.
Biochem. Biophys. Res. Commun. 350:17-24(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Parafibromin/Hyrax activates Wnt/Wg target gene transcription by direct association with beta-catenin/Armadillo."
Mosimann C., Hausmann G., Basler K.
Cell 125:327-341(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CTNNB1.
[15]"BCL9-2 binds Arm/beta-catenin in a Tyr142-independent manner and requires Pygopus for its function in Wg/Wnt signaling."
Hoffmans R., Basler K.
Mech. Dev. 124:59-67(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH BCL9L; CTNNB1 AND PYGO1.
[16]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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.
[18]"The tumor suppressor Cdc73 functionally associates with CPSF and CstF 3' mRNA processing factors."
Rozenblatt-Rosen O., Nagaike T., Francis J.M., Kaneko S., Glatt K.A., Hughes C.M., LaFramboise T., Manley J.L., Meyerson M.
Proc. Natl. Acad. Sci. U.S.A. 106:755-760(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CPSF1; CPSF4 AND CSTF2.
[19]"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.
[20]"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.
[21]"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-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"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].
[23]"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.
[24]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"HRPT2 mutations are associated with malignancy in sporadic parathyroid tumours."
Howell V.M., Haven C.J., Kahnoski K., Khoo S.K., Petillo D., Chen J., Fleuren G.J., Robinson B.G., Delbridge L.W., Philips J., Nelson A.E., Krause U., Hammje K., Dralle H., Hoang-Vu C., Gimm O., Marsh D.J., Morreau H., Teh B.T.
J. Med. Genet. 40:657-663(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FIHP PRO-64.
[27]"A Novel IVS2-1G>A mutation causes aberrant splicing of the HRPT2 gene in a family with hyperparathyroidism-jaw tumor syndrome."
Moon S.D., Park J.H., Kim E.M., Kim J.H., Han J.H., Yoo S.J., Yoon K.H., Kang M.I., Lee K.W., Son H.Y., Kang S.K., Oh S.J., Kim K.M., Yoon S.J., Park J.G., Kim I.J., Kang H.C., Hong S.W., Kim K.R., Cha B.Y.
J. Clin. Endocrinol. Metab. 90:878-883(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT 5-LEU--GLN-10 DEL, INVOLVEMENT IN HPT-JT.
[28]"Parafibromin mutations in hereditary hyperparathyroidism syndromes and parathyroid tumours."
Bradley K.J., Cavaco B.M., Bowl M.R., Harding B., Cranston T., Fratter C., Besser G.M., Conceicao Pereira M., Davie M.W., Dudley N., Leite V., Sadler G.P., Seller A., Thakker R.V.
Clin. Endocrinol. (Oxf.) 64:299-306(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HPT-JT ASN-379, VARIANT PRO-95, ASSOCIATION WITH FIHP.
[29]"Loss of parafibromin expression in a subset of parathyroid adenomas."
Juhlin C., Larsson C., Yakoleva T., Leibiger I., Leibiger B., Alimov A., Weber G., Hoog A., Villablanca A.
Endocr. Relat. Cancer 13:509-523(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-272, ASSOCIATION WITH PARATHYROID ADENOMA.
[30]"Identification of MEN1 and HRPT2 somatic mutations in paraffin-embedded (sporadic) parathyroid carcinomas."
Haven C.J., van Puijenbroek M., Tan M.H., Teh B.T., Fleuren G.J., van Wezel T., Morreau H.
Clin. Endocrinol. (Oxf.) 67:370-376(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PHE-59, ASSOCIATION WITH PARATHYROID CARCINOMA.
[31]"Different somatic alterations of the HRPT2 gene in a patient with recurrent sporadic primary hyperparathyroidism carrying an HRPT2 germline mutation."
Cetani F., Pardi E., Ambrogini E., Viacava P., Borsari S., Lemmi M., Cianferotti L., Miccoli P., Pinchera A., Arnold A., Marcocci C.
Endocr. Relat. Cancer 14:493-499(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-2 AND PRO-91, ASSOCIATION WITH PARATHYROID ADENOMA.
[32]"Sporadic human renal tumors display frequent allelic imbalances and novel mutations of the HRPT2 gene."
Zhao J., Yart A., Frigerio S., Perren A., Schraml P., Weisstanner C., Stallmach T., Krek W., Moch H.
Oncogene 26:3440-3449(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLN-34 AND LYS-292, CHARACTERIZATION OF VARIANT GLN-34, ASSOCIATION WITH RENAL TUMORS.
[33]"Clinical, genetic, and histopathologic investigation of CDC73-related familial hyperparathyroidism."
Masi G., Barzon L., Iacobone M., Viel G., Porzionato A., Macchi V., De Caro R., Favia G., Palu G.
Endocr. Relat. Cancer 15:1115-1126(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PRO-63, ASSOCIATION WITH FIHP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF312865 mRNA. Translation: AAG45339.1.
AK026969 mRNA. Translation: BAB15608.1. Different initiation.
AK314772 mRNA. Translation: BAG37309.1.
AL139133, AL390863 Genomic DNA. Translation: CAH71049.1.
AL390863, AL139133 Genomic DNA. Translation: CAH71589.1.
CH471067 Genomic DNA. Translation: EAW91250.1.
BC007325 mRNA. Translation: AAH07325.1. Sequence problems.
BC014351 mRNA. Translation: AAH14351.2.
BC065037 mRNA. Translation: AAH65037.1.
CCDSCCDS1382.1.
RefSeqNP_078805.3. NM_024529.4.
UniGeneHs.378996.

3D structure databases

ProteinModelPortalQ6P1J9.
SMRQ6P1J9. Positions 358-523.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122724. 56 interactions.
DIPDIP-37884N.
IntActQ6P1J9. 36 interactions.
MINTMINT-2817439.
STRING9606.ENSP00000356405.

PTM databases

PhosphoSiteQ6P1J9.

Polymorphism databases

DMDM74749063.

Proteomic databases

MaxQBQ6P1J9.
PaxDbQ6P1J9.
PRIDEQ6P1J9.

Protocols and materials databases

DNASU79577.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367435; ENSP00000356405; ENSG00000134371.
GeneID79577.
KEGGhsa:79577.
UCSCuc001gtb.3. human.

Organism-specific databases

CTD79577.
GeneCardsGC01P193090.
GeneReviewsCDC73.
HGNCHGNC:16783. CDC73.
HPACAB016359.
MIM145000. phenotype.
145001. phenotype.
607393. gene.
608266. phenotype.
neXtProtNX_Q6P1J9.
Orphanet99879. Familial isolated hyperparathyroidism.
99877. Familial parathyroid adenoma.
99880. Hyperparathyroidism - jaw tumor syndrome.
143. Parathyroid carcinoma.
PharmGKBPA29464.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5157.
HOVERGENHBG055033.
InParanoidQ6P1J9.
KOK15175.
OMAEYYTLEC.
OrthoDBEOG7KM5SP.
PhylomeDBQ6P1J9.
TreeFamTF313016.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ6P1J9.

Gene expression databases

BgeeQ6P1J9.
CleanExHS_CDC73.
GenevestigatorQ6P1J9.

Family and domain databases

InterProIPR007852. RNA_pol_access_fac_Cdc73.
[Graphical view]
PANTHERPTHR12466. PTHR12466. 1 hit.
PfamPF05179. CDC73. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDC73. human.
GeneWikiCDC73.
GenomeRNAi79577.
NextBio68562.
PROQ6P1J9.
SOURCESearch...

Entry information

Entry nameCDC73_HUMAN
AccessionPrimary (citable) accession number: Q6P1J9
Secondary accession number(s): A6NLZ8 expand/collapse secondary AC list , B2RBR2, Q6PK51, Q96A07, Q9H245, Q9H5L7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 115 of the entry and version 1 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM