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Q8JZM7

- CDC73_MOUSE

UniProt

Q8JZM7 - CDC73_MOUSE

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Protein

Parafibromin

Gene

Cdc73

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

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. 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. 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 (By similarity).By similarity

GO - Molecular functioni

  1. 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: Ensembl
  5. histone monoubiquitination Source: Ensembl
  6. mRNA polyadenylation Source: UniProtKB
  7. negative regulation of cell proliferation Source: UniProtKB
  8. negative regulation of epithelial cell proliferation Source: Ensembl
  9. negative regulation of fibroblast proliferation Source: Ensembl
  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: Ensembl
  18. stem cell maintenance Source: UniProtKB
  19. transcription, DNA-templated Source: UniProtKB-KW
  20. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Transcription, Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_216539. formation of the beta-catenin:TCF transactivating complex.

Names & Taxonomyi

Protein namesi
Recommended name:
Parafibromin
Alternative name(s):
Cell division cycle protein 73 homolog
Hyperparathyroidism 2 protein homolog
Gene namesi
Name:Cdc73
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:2384876. Cdc73.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. Cdc73/Paf1 complex Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 531530ParafibrominPRO_0000191804Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei212 – 2121PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8JZM7.
PaxDbiQ8JZM7.
PRIDEiQ8JZM7.

PTM databases

PhosphoSiteiQ8JZM7.

Expressioni

Tissue specificityi

Found in the adrenal gland, kidney, heart, ovary and liver.1 Publication

Gene expression databases

BgeeiQ8JZM7.
GenevestigatoriQ8JZM7.

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi229532. 6 interactions.
IntActiQ8JZM7. 7 interactions.
MINTiMINT-4116595.
STRINGi10090.ENSMUSP00000018337.

Structurei

3D structure databases

ProteinModelPortaliQ8JZM7.
SMRiQ8JZM7. Positions 358-523.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni200 – 531332Interaction with POLR2A and PAF1By similarityAdd
BLAST
Regioni200 – 25051Interaction with CTNNB1By similarityAdd
BLAST

Motif

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

Compositional bias

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

Sequence similaritiesi

Belongs to the CDC73 family.Curated

Phylogenomic databases

eggNOGiCOG5157.
GeneTreeiENSGT00390000001114.
HOGENOMiHOG000007819.
HOVERGENiHBG055033.
InParanoidiQ8JZM7.
KOiK15175.
OMAiEYYTLEC.
OrthoDBiEOG7KM5SP.
PhylomeDBiQ8JZM7.
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.

Q8JZM7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MADVLSVLRQ YNIQKKEIVV KGDEVIFGEF SWPKNVKTNY VVWGTGKEGQ
60 70 80 90 100
PREYYTLDSI LFLLNNVHLS HPVYVRRAAT ENIPVVRRPD RKDLLGYLNG
110 120 130 140 150
EASTSASIDR SAPLEIGLQR STQVKRAADE VLAEAKKPRI EDEECVRLDK
160 170 180 190 200
ERLAARLEGH KEGIVQTEQI RSLSEAMSVE KIAAIKAKIM AKKRSTIKTD
210 220 230 240 250
LDDDITALKQ RSFVDAEVDV TRDIVSRERV WRTRTTILQS TGKNFSKNIF
260 270 280 290 300
AILQSVKARE EGRAPEQRPA PNAAPVDPTL RTKQPIPAAY NRYDQERFKG
310 320 330 340 350
KEETEGFKID TMGTYHGMTL KSVTEGASAR KTQTPAAQPV PRPVSQARPP
360 370 380 390 400
PNQKKGSRTP IIIIPAATTS LITMLNAKDL LQDLKFVPSD EKKKQGCQRE
410 420 430 440 450
NETLIQRRKD QMQPGGTAIS VTVPYRVVDQ PLKLMPQDWD RVVAVFVQGP
460 470 480 490 500
AWQFKGWPWL LPDGSPVDIF AKIKAFHLKY DEVRLDPNVQ KWDVTVLELS
510 520 530
YHKRHLDRPV FLRFWETLDR YMVKHKSHLR F
Length:531
Mass (Da):60,577
Last modified:October 1, 2002 - v1
Checksum:i894A7448DBC0E793
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK080861 mRNA. Translation: BAC38048.1.
BC027756 mRNA. Translation: AAH27756.1.
BC031127 mRNA. Translation: AAH31127.1.
CCDSiCCDS15341.1.
RefSeqiNP_666103.1. NM_145991.1.
UniGeneiMm.156727.
Mm.393505.
Mm.398849.

Genome annotation databases

EnsembliENSMUST00000018337; ENSMUSP00000018337; ENSMUSG00000026361.
GeneIDi214498.
KEGGimmu:214498.
UCSCiuc007cwx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK080861 mRNA. Translation: BAC38048.1 .
BC027756 mRNA. Translation: AAH27756.1 .
BC031127 mRNA. Translation: AAH31127.1 .
CCDSi CCDS15341.1.
RefSeqi NP_666103.1. NM_145991.1.
UniGenei Mm.156727.
Mm.393505.
Mm.398849.

3D structure databases

ProteinModelPortali Q8JZM7.
SMRi Q8JZM7. Positions 358-523.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 229532. 6 interactions.
IntActi Q8JZM7. 7 interactions.
MINTi MINT-4116595.
STRINGi 10090.ENSMUSP00000018337.

PTM databases

PhosphoSitei Q8JZM7.

Proteomic databases

MaxQBi Q8JZM7.
PaxDbi Q8JZM7.
PRIDEi Q8JZM7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000018337 ; ENSMUSP00000018337 ; ENSMUSG00000026361 .
GeneIDi 214498.
KEGGi mmu:214498.
UCSCi uc007cwx.1. mouse.

Organism-specific databases

CTDi 79577.
MGIi MGI:2384876. Cdc73.

Phylogenomic databases

eggNOGi COG5157.
GeneTreei ENSGT00390000001114.
HOGENOMi HOG000007819.
HOVERGENi HBG055033.
InParanoidi Q8JZM7.
KOi K15175.
OMAi EYYTLEC.
OrthoDBi EOG7KM5SP.
PhylomeDBi Q8JZM7.
TreeFami TF313016.

Enzyme and pathway databases

Reactomei REACT_216539. formation of the beta-catenin:TCF transactivating complex.

Miscellaneous databases

ChiTaRSi Cdc73. mouse.
NextBioi 374332.
PROi Q8JZM7.
SOURCEi Search...

Gene expression databases

Bgeei Q8JZM7.
Genevestigatori Q8JZM7.

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

« Hide 'large scale' publications
  1. "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.
    , 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.
    Tissue: Adrenal gland.
  2. "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 and FVB/N.
    Tissue: Kidney and Mammary tumor.
  3. "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: TISSUE SPECIFICITY.
  4. Cited for: FUNCTION.

Entry informationi

Entry nameiCDC73_MOUSE
AccessioniPrimary (citable) accession number: Q8JZM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2002
Last modified: November 26, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3