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Q58A45

- PAN3_HUMAN

UniProt

Q58A45 - PAN3_HUMAN

Protein

PAB-dependent poly(A)-specific ribonuclease subunit PAN3

Gene

PAN3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA when the poly(A) stretch is bound by poly(A)-binding protein (PABP), which is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with PABP and to miRNA targets via its interaction with GW182 family proteins.2 PublicationsUniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei521 – 5211ATPUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri43 – 7129C3H1-typeUniRule annotationAdd
    BLAST
    Nucleotide bindingi570 – 5756ATPUniRule annotation
    Nucleotide bindingi644 – 6452ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. protein kinase activity Source: InterPro

    GO - Biological processi

    1. deadenylation-dependent decapping of nuclear-transcribed mRNA Source: Ensembl
    2. gene expression Source: Reactome
    3. mRNA metabolic process Source: Reactome
    4. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    5. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
    6. positive regulation of cytoplasmic mRNA processing body assembly Source: Ensembl
    7. protein targeting Source: Ensembl
    8. RNA metabolic process Source: Reactome
    9. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_20514. Deadenylation of mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PAB-dependent poly(A)-specific ribonuclease subunit PAN3UniRule annotation
    Alternative name(s):
    PAB1P-dependent poly(A)-nucleaseUniRule annotation
    PAN deadenylation complex subunit 3UniRule annotation
    Short name:
    hPan3
    Gene namesi
    Name:PAN3UniRule annotation
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:29991. PAN3.

    Subcellular locationi

    CytoplasmP-body 2 PublicationsUniRule annotation

    GO - Cellular componenti

    1. cytoplasmic mRNA processing body Source: UniProtKB-SubCell
    2. cytosol Source: Reactome
    3. PAN complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi203 – 2031Y → A: Reduces interaction with polyadenylate-binding protein. 1 Publication
    Mutagenesisi293 – 2931F → A: Reduces interaction with polyadenylate-binding protein. 2 Publications

    Organism-specific databases

    PharmGKBiPA144596398.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 887887PAB-dependent poly(A)-specific ribonuclease subunit PAN3PRO_0000280525Add
    BLAST

    Proteomic databases

    MaxQBiQ58A45.
    PaxDbiQ58A45.
    PRIDEiQ58A45.

    PTM databases

    PhosphoSiteiQ58A45.

    Expressioni

    Gene expression databases

    ArrayExpressiQ58A45.
    BgeeiQ58A45.
    CleanExiHS_PAN3.
    GenevestigatoriQ58A45.

    Organism-specific databases

    HPAiHPA028817.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with the catalytic subunit PAN2 to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts (via PAM-2 motif) with poly(A)-binding protein PABPC1 (via PABC domain), conferring substrate-specificity of the enzyme complex. Interacts with the GW182 family proteins TNRC6A, TNRC6B and TNRC6C.5 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PABPC1P119404EBI-2513054,EBI-81531
    PAN2Q504Q36EBI-2513054,EBI-1058976
    TNRC6AQ8NDV72EBI-2513054,EBI-2269715
    TNRC6BQ9UPQ94EBI-2513054,EBI-947158
    TNRC6CQ9HCJ04EBI-2513054,EBI-6507625

    Protein-protein interaction databases

    BioGridi129129. 6 interactions.
    IntActiQ58A45. 8 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ58A45.
    SMRiQ58A45. Positions 473-882.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini492 – 754263Protein kinaseUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 491491Interaction with polyadenylate-binding proteinAdd
    BLAST
    Regioni492 – 887396Interaction with PAN2Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili756 – 77722UniRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi284 – 29916PABPC-interacting motif-2 (PAM-2)Add
    BLAST

    Domaini

    The protein kinase domain is predicted to be catalytically inactive. However it still binds ATP and ATP-binding is required for mRNA degradation.UniRule annotation

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. PAN3 family.UniRule annotation
    Contains 1 C3H1-type zinc finger.UniRule annotation
    Contains 1 protein kinase domain.UniRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri43 – 7129C3H1-typeUniRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG260889.
    HOVERGENiHBG058849.
    InParanoidiQ58A45.
    KOiK12572.
    OMAiYYAKDKT.
    OrthoDBiEOG7BS48S.
    PhylomeDBiQ58A45.
    TreeFamiTF105865.

    Family and domain databases

    Gene3Di4.10.1000.10. 1 hit.
    HAMAPiMF_03181. PAN3.
    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR000571. Znf_CCCH.
    [Graphical view]
    SMARTiSM00356. ZnF_C3H1. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS50103. ZF_C3H1. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q58A45-1) [UniParc]FASTAAdd to Basket

    Also known as: Pan3b

    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.

    « Hide

    MNSGGGLPPP SAAASPSSSS LAAAVAVVAP PGVGGVPGGA AVGVKLKYCR    50
    YYAKDKTCFY GEECQFLHED PAAGAAPGLG LHSNSVPLAL AGAPVAGFPP 100
    GAVAGGGAGP PPGPKKPDLG DPGTGAAAGG GGSSGGLDGP RLAIPGMDGG 150
    ALTDTSLTDS YFSTSFIGVN GFGSPVETKY PLMQRMTNSS SSPSLLNDSA 200
    KPYSAHDPLT SPASSLFNDF GALNISQRRK PRKYRLGMLE ERLVPMGSKA 250
    RKAKNPIGCL ADRCKSGVPI NMVWWNRVTE NNLQTPNPTA SEFIPKGGST 300
    SRLSNVSQSN MSAFSQVFSH PSMGSPATAG LAPGMSLSAG SSPLHSPKIT 350
    PHTSPAPRRR SHTPNPASYM VPSSASTSVN NPVSQTPSSG QVIQKETVGG 400
    TTYFYTDTTP APLTGMVFPN YHIYPPTAPH VAYMQPKANA PSFFMADELR 450
    QELINRHLIT MAQIDQADMP AVPTEVDSYH SLFPLEPLPP PNRIQKSSNF 500
    GYITSCYKAV NSKDDLPYCL RRIHGFRLVN TKCMVLVDMW KKIQHSNIVT 550
    LREVFTTKAF AEPSLVFAYD FHAGGETMMS RHFNDPNADA YFTKRKWGQH 600
    EGPLPRQHAG LLPESLIWAY IVQLSSALRT IHTAGLACRV MDPTKILITG 650
    KTRLRVNCVG VFDVLTFDNS QNNNPLALMA QYQQADLISL GKVVLALACN 700
    SLAGIQRENL QKAMELVTIN YSSDLKNLIL YLLTDQNRMR SVNDIMPMIG 750
    ARFYTQLDAA QMRNDVIEED LAKEVQNGRL FRLLAKLGTI NERPEFQKDP 800
    TWSETGDRYL LKLFRDHLFH QVTEAGAPWI DLSHIISCLN KLDAGVPEKI 850
    SLISRDEKSV LVVTYSDLKR CFENTFQELI AAANGQL 887
    Length:887
    Mass (Da):95,613
    Last modified:July 27, 2011 - v3
    Checksum:i4883F859D2A642D2
    GO
    Isoform 2 (identifier: Q58A45-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-332: Missing.
         333-333: P → MKLTDSTKGWIVWAALDSSMR

    Show »
    Length:575
    Mass (Da):64,465
    Checksum:i8FF7B393A072FD8D
    GO
    Isoform 3 (identifier: Q58A45-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         231-284: Missing.

    Show »
    Length:833
    Mass (Da):89,405
    Checksum:i06EAD23E1B205A4F
    GO
    Isoform 4 (identifier: Q58A45-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         684-687: QADL → VSKN
         688-887: Missing.

    Show »
    Length:687
    Mass (Da):72,933
    Checksum:iC3AFEB0807CE9F3B
    GO

    Sequence cautioni

    The sequence AAI28180.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAC03632.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence ABK41888.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI12449.2 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI12450.2 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI14848.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAM20921.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti229 – 2291R → Q in BAD02262. (PubMed:14583602)Curated
    Sequence conflicti569 – 5691Y → H in AAI28181. (PubMed:15489334)Curated
    Sequence conflicti793 – 7931R → G in BAC03632. (PubMed:14702039)Curated
    Sequence conflicti856 – 8561D → G in BAD02262. (PubMed:14583602)Curated
    Sequence conflicti856 – 8561D → G in BAD93184. (PubMed:14583602)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 332332Missing in isoform 2. 1 PublicationVSP_023753Add
    BLAST
    Alternative sequencei231 – 28454Missing in isoform 3. 2 PublicationsVSP_023754Add
    BLAST
    Alternative sequencei333 – 3331P → MKLTDSTKGWIVWAALDSSM R in isoform 2. 1 PublicationVSP_023755
    Alternative sequencei684 – 6874QADL → VSKN in isoform 4. 1 PublicationVSP_041648
    Alternative sequencei688 – 887200Missing in isoform 4. 1 PublicationVSP_041649Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK091307 mRNA. Translation: BAC03632.1. Different initiation.
    AK296435 mRNA. Translation: BAH12353.1.
    EF088216 Genomic DNA. Translation: ABK41888.1. Sequence problems.
    AL356915, AL138712 Genomic DNA. Translation: CAI12449.2. Sequence problems.
    AL356915, AL138712 Genomic DNA. Translation: CAI12450.2. Sequence problems.
    AL138712, AL356915 Genomic DNA. Translation: CAI14848.1. Sequence problems.
    AL138712, AL356915 Genomic DNA. Translation: CAM20921.1. Sequence problems.
    BC024318 mRNA. Translation: AAH24318.1.
    BC128179 mRNA. Translation: AAI28180.1. Different initiation.
    BC128180 mRNA. Translation: AAI28181.1.
    AB107584 mRNA. Translation: BAD02262.1.
    AB109552 mRNA. Translation: BAD93184.1.
    BX647740 mRNA. Translation: CAI45987.2.
    CCDSiCCDS9329.2. [Q58A45-1]
    RefSeqiNP_787050.6. NM_175854.7. [Q58A45-1]
    XP_005266390.1. XM_005266333.1. [Q58A45-3]
    XP_005266391.1. XM_005266334.1. [Q58A45-2]
    XP_006719864.1. XM_006719801.1. [Q58A45-2]
    XP_006719865.1. XM_006719802.1.
    UniGeneiHs.645015.

    Genome annotation databases

    EnsembliENST00000380958; ENSP00000370345; ENSG00000152520. [Q58A45-1]
    ENST00000399613; ENSP00000382522; ENSG00000152520.
    GeneIDi255967.
    KEGGihsa:255967.
    UCSCiuc001urx.3. human. [Q58A45-3]
    uc001ury.3. human. [Q58A45-2]
    uc001urz.3. human. [Q58A45-1]
    uc010tdo.1. human. [Q58A45-4]

    Polymorphism databases

    DMDMi341942213.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK091307 mRNA. Translation: BAC03632.1 . Different initiation.
    AK296435 mRNA. Translation: BAH12353.1 .
    EF088216 Genomic DNA. Translation: ABK41888.1 . Sequence problems.
    AL356915 , AL138712 Genomic DNA. Translation: CAI12449.2 . Sequence problems.
    AL356915 , AL138712 Genomic DNA. Translation: CAI12450.2 . Sequence problems.
    AL138712 , AL356915 Genomic DNA. Translation: CAI14848.1 . Sequence problems.
    AL138712 , AL356915 Genomic DNA. Translation: CAM20921.1 . Sequence problems.
    BC024318 mRNA. Translation: AAH24318.1 .
    BC128179 mRNA. Translation: AAI28180.1 . Different initiation.
    BC128180 mRNA. Translation: AAI28181.1 .
    AB107584 mRNA. Translation: BAD02262.1 .
    AB109552 mRNA. Translation: BAD93184.1 .
    BX647740 mRNA. Translation: CAI45987.2 .
    CCDSi CCDS9329.2. [Q58A45-1 ]
    RefSeqi NP_787050.6. NM_175854.7. [Q58A45-1 ]
    XP_005266390.1. XM_005266333.1. [Q58A45-3 ]
    XP_005266391.1. XM_005266334.1. [Q58A45-2 ]
    XP_006719864.1. XM_006719801.1. [Q58A45-2 ]
    XP_006719865.1. XM_006719802.1.
    UniGenei Hs.645015.

    3D structure databases

    ProteinModelPortali Q58A45.
    SMRi Q58A45. Positions 473-882.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 129129. 6 interactions.
    IntActi Q58A45. 8 interactions.

    PTM databases

    PhosphoSitei Q58A45.

    Polymorphism databases

    DMDMi 341942213.

    Proteomic databases

    MaxQBi Q58A45.
    PaxDbi Q58A45.
    PRIDEi Q58A45.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380958 ; ENSP00000370345 ; ENSG00000152520 . [Q58A45-1 ]
    ENST00000399613 ; ENSP00000382522 ; ENSG00000152520 .
    GeneIDi 255967.
    KEGGi hsa:255967.
    UCSCi uc001urx.3. human. [Q58A45-3 ]
    uc001ury.3. human. [Q58A45-2 ]
    uc001urz.3. human. [Q58A45-1 ]
    uc010tdo.1. human. [Q58A45-4 ]

    Organism-specific databases

    CTDi 255967.
    GeneCardsi GC13P028713.
    H-InvDB HIX0011200.
    HGNCi HGNC:29991. PAN3.
    HPAi HPA028817.
    neXtProti NX_Q58A45.
    PharmGKBi PA144596398.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG260889.
    HOVERGENi HBG058849.
    InParanoidi Q58A45.
    KOi K12572.
    OMAi YYAKDKT.
    OrthoDBi EOG7BS48S.
    PhylomeDBi Q58A45.
    TreeFami TF105865.

    Enzyme and pathway databases

    Reactomei REACT_20514. Deadenylation of mRNA.

    Miscellaneous databases

    ChiTaRSi PAN3. human.
    GenomeRNAii 255967.
    NextBioi 92689.
    PROi Q58A45.

    Gene expression databases

    ArrayExpressi Q58A45.
    Bgeei Q58A45.
    CleanExi HS_PAN3.
    Genevestigatori Q58A45.

    Family and domain databases

    Gene3Di 4.10.1000.10. 1 hit.
    HAMAPi MF_03181. PAN3.
    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR000571. Znf_CCCH.
    [Graphical view ]
    SMARTi SM00356. ZnF_C3H1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS50103. ZF_C3H1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 754-887 (ISOFORMS 1/2/3).
      Tissue: Skin fibroblast.
    2. SeattleSNPs variation discovery resource
      Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 147-887 (ISOFORM 1).
      Tissue: Uterus.
    5. "Identification of a human cytoplasmic poly(A) nuclease complex stimulated by poly(A)-binding protein."
      Uchida N., Hoshino S., Katada T.
      J. Biol. Chem. 279:1383-1391(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 147-887 (ISOFORMS 1 AND 3), FUNCTION, INTERACTION WITH PAN2 AND POLYADENYLATE-BINDING PROTEIN, SUBCELLULAR LOCATION.
      Tissue: Cervix carcinoma.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 654-887 (ISOFORMS 1/2/3).
      Tissue: Adrenal gland.
    7. "Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases."
      Funakoshi Y., Doi Y., Hosoda N., Uchida N., Osawa M., Shimada I., Tsujimoto M., Suzuki T., Katada T., Hoshino S.
      Genes Dev. 21:3135-3148(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PABPC1, MUTAGENESIS OF TYR-203 AND PHE-293.
    8. "Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein."
      Siddiqui N., Mangus D.A., Chang T.C., Palermino J.M., Shyu A.B., Gehring K.
      J. Biol. Chem. 282:25067-25075(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PABPC, MUTAGENESIS OF PHE-293.
    9. "Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells."
      Zheng D., Ezzeddine N., Chen C.Y., Zhu W., He X., Shyu A.B.
      J. Cell Biol. 182:89-101(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets."
      Braun J.E., Huntzinger E., Fauser M., Izaurralde E.
      Mol. Cell 44:120-133(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNRC6A; TNRC6B AND TNRC6C.
    12. "Structure of the PAN3 pseudokinase reveals the basis for interactions with the PAN2 deadenylase and the GW182 proteins."
      Christie M., Boland A., Huntzinger E., Weichenrieder O., Izaurralde E.
      Mol. Cell 51:360-373(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, INTERACTION WITH PAN2, ATP-BINDING.

    Entry informationi

    Entry nameiPAN3_HUMAN
    AccessioniPrimary (citable) accession number: Q58A45
    Secondary accession number(s): A0N0X1
    , A1A4Y8, A1A4Y9, B1ALF1, B7Z3W7, Q0D2P2, Q5HYG6, Q5T515, Q5T516, Q5TBA0, Q76E13, Q8NBA6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 90 of the entry and version 3 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, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3