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Q6P1J9

- CDC73_HUMAN

UniProt

Q6P1J9 - CDC73_HUMAN

Protein

Parafibromin

Gene

CDC73

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    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.10 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. RNA polymerase II core binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cellular response to lipopolysaccharide Source: UniProtKB
    3. endodermal cell fate commitment Source: UniProtKB
    4. histone H2B ubiquitination Source: UniProtKB
    5. histone monoubiquitination Source: UniProtKB
    6. mRNA polyadenylation Source: UniProtKB
    7. negative regulation of cell proliferation Source: UniProtKB
    8. negative regulation of epithelial cell proliferation Source: UniProtKB
    9. negative regulation of fibroblast proliferation Source: UniProtKB
    10. negative regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
    11. negative regulation of myeloid cell differentiation Source: UniProtKB
    12. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    13. positive regulation of mRNA 3'-end processing Source: UniProtKB
    14. positive regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB
    15. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    16. positive regulation of Wnt signaling pathway Source: UniProtKB
    17. protein destabilization Source: UniProtKB
    18. stem cell maintenance Source: UniProtKB
    19. transcription, DNA-templated Source: UniProtKB-KW
    20. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Transcription, Transcription regulation, Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_200753. formation of the beta-catenin:TCF transactivating complex.
    SignaLinkiQ6P1J9.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Parafibromin
    Alternative name(s):
    Cell division cycle protein 73 homolog
    Hyperparathyroidism 2 protein
    Gene namesi
    Name:CDC73
    Synonyms:C1orf28, HRPT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:16783. CDC73.

    Subcellular locationi

    Nucleus 3 Publications

    GO - Cellular componenti

    1. Cdc73/Paf1 complex Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Familial isolated hyperparathyroidism (FIHP) [MIM:145000]: Autosomal dominant disorder characterized by hypercalcemia, elevated parathyroid hormone (PTH) levels, and uniglandular or multiglandular parathyroid tumors.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti64 – 641L → P in FIHP; does not affect interaction with the Pfa1 complex. 2 Publications
    VAR_024082
    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti379 – 3791D → N in HPT-JT. 1 Publication
    VAR_064936
    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.1 Publication
    Note: The gene represented in this entry is involved in disease pathogenesis.

    Keywords - Diseasei

    Disease mutation, Tumor suppressor

    Organism-specific databases

    MIMi145000. phenotype.
    145001. phenotype.
    608266. phenotype.
    Orphaneti99879. Familial isolated hyperparathyroidism.
    99877. Familial parathyroid adenoma.
    99880. Hyperparathyroidism - jaw tumor syndrome.
    143. Parathyroid carcinoma.
    PharmGKBiPA29464.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 531530ParafibrominPRO_0000191803Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei212 – 2121Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ6P1J9.
    PaxDbiQ6P1J9.
    PRIDEiQ6P1J9.

    PTM databases

    PhosphoSiteiQ6P1J9.

    Expressioni

    Tissue specificityi

    Found in adrenal and parathyroid glands, kidney and heart.1 Publication

    Gene expression databases

    BgeeiQ6P1J9.
    CleanExiHS_CDC73.
    GenevestigatoriQ6P1J9.

    Organism-specific databases

    HPAiCAB016359.

    Interactioni

    Subunit structurei

    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.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCL9O005122EBI-930143,EBI-533127
    CTNNB1P352229EBI-930143,EBI-491549
    CTR9Q6PD6215EBI-930143,EBI-1019583
    KMT2AQ031644EBI-930143,EBI-591370
    LEO1Q8WVC011EBI-930143,EBI-932432
    PAF1Q8N7H525EBI-930143,EBI-2607770
    POLR2AP249285EBI-930143,EBI-295301
    RTF1Q9254112EBI-930143,EBI-1055239

    Protein-protein interaction databases

    BioGridi122724. 57 interactions.
    DIPiDIP-37884N.
    IntActiQ6P1J9. 36 interactions.
    MINTiMINT-2817439.
    STRINGi9606.ENSP00000356405.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6P1J9.
    SMRiQ6P1J9. Positions 358-523.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni200 – 531332Interaction with POLR2A and PAF1Add
    BLAST
    Regioni200 – 25051Interaction with CTNNB1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi125 – 13915Nuclear localization signalAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi361 – 3644Poly-Ile

    Sequence similaritiesi

    Belongs to the CDC73 family.Curated

    Phylogenomic databases

    eggNOGiCOG5157.
    HOVERGENiHBG055033.
    InParanoidiQ6P1J9.
    KOiK15175.
    OMAiEYYTLEC.
    OrthoDBiEOG7KM5SP.
    PhylomeDBiQ6P1J9.
    TreeFamiTF313016.

    Family and domain databases

    InterProiIPR007852. RNA_pol_access_fac_Cdc73.
    [Graphical view]
    PANTHERiPTHR12466. PTHR12466. 1 hit.
    PfamiPF05179. CDC73. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q6P1J9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADVLSVLRQ YNIQKKEIVV KGDEVIFGEF SWPKNVKTNY VVWGTGKEGQ    50
    PREYYTLDSI LFLLNNVHLS HPVYVRRAAT ENIPVVRRPD RKDLLGYLNG 100
    EASTSASIDR SAPLEIGLQR STQVKRAADE VLAEAKKPRI EDEECVRLDK 150
    ERLAARLEGH KEGIVQTEQI RSLSEAMSVE KIAAIKAKIM AKKRSTIKTD 200
    LDDDITALKQ RSFVDAEVDV TRDIVSRERV WRTRTTILQS TGKNFSKNIF 250
    AILQSVKARE EGRAPEQRPA PNAAPVDPTL RTKQPIPAAY NRYDQERFKG 300
    KEETEGFKID TMGTYHGMTL KSVTEGASAR KTQTPAAQPV PRPVSQARPP 350
    PNQKKGSRTP IIIIPAATTS LITMLNAKDL LQDLKFVPSD EKKKQGCQRE 400
    NETLIQRRKD QMQPGGTAIS VTVPYRVVDQ PLKLMPQDWD RVVAVFVQGP 450
    AWQFKGWPWL LPDGSPVDIF AKIKAFHLKY DEVRLDPNVQ KWDVTVLELS 500
    YHKRHLDRPV FLRFWETLDR YMVKHKSHLR F 531
    Length:531
    Mass (Da):60,577
    Last modified:July 5, 2004 - v1
    Checksum:i894A7448DBC0E793
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti123 – 1231Q → G in AAH14351. (PubMed:15489334)Curated
    Sequence conflicti184 – 1874AIKA → CNQT in BAB15608. (PubMed:14702039)Curated
    Sequence conflicti372 – 3721I → K in BAB15608. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21A → 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. 1 Publication
    VAR_064927
    Natural varianti5 – 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. 1 Publication
    VAR_064928
    Natural varianti34 – 341K → 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. 1 Publication
    VAR_064929
    Natural varianti59 – 591S → F Found in a parathyroid carcinoma sample; somatic mutation. 1 Publication
    VAR_064930
    Natural varianti63 – 631L → P Found in a kindred with familial hyperparathyroidism. 1 Publication
    VAR_064931
    Natural varianti64 – 641L → P in FIHP; does not affect interaction with the Pfa1 complex. 2 Publications
    VAR_024082
    Natural varianti91 – 911R → P Found in a patient with isolated hyperparathyroidism and parathyroid adenomas. 1 Publication
    VAR_064932
    Natural varianti95 – 951L → 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. 1 Publication
    VAR_064933
    Natural varianti272 – 2721N → S Found in a parathyroid adenoma sample. 1 Publication
    VAR_064934
    Natural varianti292 – 2921R → K Found in a Wilms tumor sample; somatic mutation. 1 Publication
    VAR_064935
    Natural varianti379 – 3791D → N in HPT-JT. 1 Publication
    VAR_064936
    Natural varianti384 – 3841L → P.
    Corresponds to variant rs35590728 [ dbSNP | Ensembl ].
    VAR_031825

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS1382.1.
    RefSeqiNP_078805.3. NM_024529.4.
    UniGeneiHs.378996.

    Genome annotation databases

    EnsembliENST00000367435; ENSP00000356405; ENSG00000134371.
    GeneIDi79577.
    KEGGihsa:79577.
    UCSCiuc001gtb.3. human.

    Polymorphism databases

    DMDMi74749063.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS1382.1.
    RefSeqi NP_078805.3. NM_024529.4.
    UniGenei Hs.378996.

    3D structure databases

    ProteinModelPortali Q6P1J9.
    SMRi Q6P1J9. Positions 358-523.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122724. 57 interactions.
    DIPi DIP-37884N.
    IntActi Q6P1J9. 36 interactions.
    MINTi MINT-2817439.
    STRINGi 9606.ENSP00000356405.

    PTM databases

    PhosphoSitei Q6P1J9.

    Polymorphism databases

    DMDMi 74749063.

    Proteomic databases

    MaxQBi Q6P1J9.
    PaxDbi Q6P1J9.
    PRIDEi Q6P1J9.

    Protocols and materials databases

    DNASUi 79577.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367435 ; ENSP00000356405 ; ENSG00000134371 .
    GeneIDi 79577.
    KEGGi hsa:79577.
    UCSCi uc001gtb.3. human.

    Organism-specific databases

    CTDi 79577.
    GeneCardsi GC01P193090.
    GeneReviewsi CDC73.
    HGNCi HGNC:16783. CDC73.
    HPAi CAB016359.
    MIMi 145000. phenotype.
    145001. phenotype.
    607393. gene.
    608266. phenotype.
    neXtProti NX_Q6P1J9.
    Orphaneti 99879. Familial isolated hyperparathyroidism.
    99877. Familial parathyroid adenoma.
    99880. Hyperparathyroidism - jaw tumor syndrome.
    143. Parathyroid carcinoma.
    PharmGKBi PA29464.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5157.
    HOVERGENi HBG055033.
    InParanoidi Q6P1J9.
    KOi K15175.
    OMAi EYYTLEC.
    OrthoDBi EOG7KM5SP.
    PhylomeDBi Q6P1J9.
    TreeFami TF313016.

    Enzyme and pathway databases

    Reactomei REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    SignaLinki Q6P1J9.

    Miscellaneous databases

    ChiTaRSi CDC73. human.
    GeneWikii CDC73.
    GenomeRNAii 79577.
    NextBioi 68562.
    PROi Q6P1J9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q6P1J9.
    CleanExi HS_CDC73.
    Genevestigatori Q6P1J9.

    Family and domain databases

    InterProi IPR007852. RNA_pol_access_fac_Cdc73.
    [Graphical view ]
    PANTHERi PTHR12466. PTHR12466. 1 hit.
    Pfami PF05179. CDC73. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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. 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. Cited for: INVOLVEMENT IN HPT-JT, VARIANT FIHP PRO-64.
    12. Cited for: INVOLVEMENT IN PRTC.
    13. 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. 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. Cited for: VARIANT HPT-JT ASN-379, VARIANT PRO-95, ASSOCIATION WITH FIHP.
    29. 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.

    Entry informationi

    Entry nameiCDC73_HUMAN
    AccessioniPrimary (citable) accession number: Q6P1J9
    Secondary accession number(s): A6NLZ8
    , B2RBR2, Q6PK51, Q96A07, Q9H245, Q9H5L7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 117 of the entry and version 1 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3