SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q58A45

- PAN3_HUMAN

UniProt

Q58A45 - PAN3_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei521 – 5211ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri43 – 7129C3H1-typeUniRule annotation
Add
BLAST
Nucleotide bindingi570 – 5756ATP By similarity
Nucleotide bindingi644 – 6452ATP By similarity

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

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 PAN3
Alternative name(s):
PAB1P-dependent poly(A)-nuclease
PAN deadenylation complex subunit 3
Short name:
hPan3
Gene namesi
Name:PAN3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:29991. PAN3.

Subcellular locationi

CytoplasmP-body 2 Publications

GO - Cellular componenti

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

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 PAN3UniRule annotation
PRO_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 Publications

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini492 – 754263Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 491491Interaction with polyadenylate-binding proteinUniRule annotation
Add
BLAST
Regioni492 – 887396Interaction with PAN2UniRule annotation
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili756 – 77722 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi284 – 29916PABPC-interacting motif-2 (PAM-2)UniRule annotation
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 By similarity.UniRule annotation

Sequence similaritiesi

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 332332Missing in isoform 2.
VSP_023753Add
BLAST
Alternative sequencei231 – 28454Missing in isoform 3.
VSP_023754Add
BLAST
Alternative sequencei333 – 3331P → MKLTDSTKGWIVWAALDSSM R in isoform 2.
VSP_023755
Alternative sequencei684 – 6874QADL → VSKN in isoform 4.
VSP_041648
Alternative sequencei688 – 887200Missing in isoform 4.
VSP_041649Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti229 – 2291R → Q in BAD02262. 1 Publication
Sequence conflicti569 – 5691Y → H in AAI28181. 1 Publication
Sequence conflicti793 – 7931R → G in BAC03632. 1 Publication
Sequence conflicti856 – 8561D → G in BAD02262. 1 Publication
Sequence conflicti856 – 8561D → G in BAD93184. 1 Publication

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

EnsembliENST00000282391; ENSP00000282391; ENSG00000152520. [Q58A45-2]
ENST00000380958; 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 ENST00000282391 ; ENSP00000282391 ; ENSG00000152520 . [Q58A45-2 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 89 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

Similar proteinsi