Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q58A45 (PAN3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PAN3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length887 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.12

Subunit structure

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. Ref.5 Ref.7 Ref.8 Ref.11 Ref.12

Subcellular location

CytoplasmP-body Ref.5 Ref.9.

Domain

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. HAMAP-Rule MF_03181

Sequence similarities

Belongs to the protein kinase superfamily. PAN3 family.

Contains 1 C3H1-type zinc finger.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAI28180.1 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 BAC03632.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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.

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Zinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

RNA phosphodiester bond hydrolysis, exonucleolytic

Inferred from direct assay Ref.5. Source: GOC

deadenylation-dependent decapping of nuclear-transcribed mRNA

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA poly(A) tail shortening

Traceable author statement. Source: Reactome

positive regulation of cytoplasmic mRNA processing body assembly

Inferred from electronic annotation. Source: Ensembl

protein targeting

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentPAN complex

Inferred from direct assay Ref.5. Source: UniProtKB

cytoplasmic mRNA processing body

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.5Ref.8PubMed 19615732Ref.11PubMed 23340509. Source: IntAct

protein kinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q58A45-1)

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.
Isoform 2 (identifier: Q58A45-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-332: Missing.
     333-333: P → MKLTDSTKGWIVWAALDSSMR
Isoform 3 (identifier: Q58A45-3)

The sequence of this isoform differs from the canonical sequence as follows:
     231-284: Missing.
Isoform 4 (identifier: Q58A45-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 887887PAB-dependent poly(A)-specific ribonuclease subunit PAN3 HAMAP-Rule MF_03181
PRO_0000280525

Regions

Domain492 – 754263Protein kinase
Zinc finger43 – 7129C3H1-type HAMAP-Rule MF_03181
Nucleotide binding570 – 5756ATP By similarity
Nucleotide binding644 – 6452ATP By similarity
Region1 – 491491Interaction with polyadenylate-binding protein HAMAP-Rule MF_03181
Region492 – 887396Interaction with PAN2 HAMAP-Rule MF_03181
Coiled coil756 – 77722 Potential
Motif284 – 29916PABPC-interacting motif-2 (PAM-2) HAMAP-Rule MF_03181

Sites

Binding site5211ATP By similarity

Natural variations

Alternative sequence1 – 332332Missing in isoform 2.
VSP_023753
Alternative sequence231 – 28454Missing in isoform 3.
VSP_023754
Alternative sequence3331P → MKLTDSTKGWIVWAALDSSM R in isoform 2.
VSP_023755
Alternative sequence684 – 6874QADL → VSKN in isoform 4.
VSP_041648
Alternative sequence688 – 887200Missing in isoform 4.
VSP_041649

Experimental info

Mutagenesis2031Y → A: Reduces interaction with polyadenylate-binding protein. Ref.7
Mutagenesis2931F → A: Reduces interaction with polyadenylate-binding protein. Ref.7 Ref.8
Sequence conflict2291R → Q in BAD02262. Ref.5
Sequence conflict5691Y → H in AAI28181. Ref.4
Sequence conflict7931R → G in BAC03632. Ref.1
Sequence conflict8561D → G in BAD02262. Ref.5
Sequence conflict8561D → G in BAD93184. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Pan3b) [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 4883F859D2A642D2

FASTA88795,613
        10         20         30         40         50         60 
MNSGGGLPPP SAAASPSSSS LAAAVAVVAP PGVGGVPGGA AVGVKLKYCR YYAKDKTCFY 

        70         80         90        100        110        120 
GEECQFLHED PAAGAAPGLG LHSNSVPLAL AGAPVAGFPP GAVAGGGAGP PPGPKKPDLG 

       130        140        150        160        170        180 
DPGTGAAAGG GGSSGGLDGP RLAIPGMDGG ALTDTSLTDS YFSTSFIGVN GFGSPVETKY 

       190        200        210        220        230        240 
PLMQRMTNSS SSPSLLNDSA KPYSAHDPLT SPASSLFNDF GALNISQRRK PRKYRLGMLE 

       250        260        270        280        290        300 
ERLVPMGSKA RKAKNPIGCL ADRCKSGVPI NMVWWNRVTE NNLQTPNPTA SEFIPKGGST 

       310        320        330        340        350        360 
SRLSNVSQSN MSAFSQVFSH PSMGSPATAG LAPGMSLSAG SSPLHSPKIT PHTSPAPRRR 

       370        380        390        400        410        420 
SHTPNPASYM VPSSASTSVN NPVSQTPSSG QVIQKETVGG TTYFYTDTTP APLTGMVFPN 

       430        440        450        460        470        480 
YHIYPPTAPH VAYMQPKANA PSFFMADELR QELINRHLIT MAQIDQADMP AVPTEVDSYH 

       490        500        510        520        530        540 
SLFPLEPLPP PNRIQKSSNF GYITSCYKAV NSKDDLPYCL RRIHGFRLVN TKCMVLVDMW 

       550        560        570        580        590        600 
KKIQHSNIVT LREVFTTKAF AEPSLVFAYD FHAGGETMMS RHFNDPNADA YFTKRKWGQH 

       610        620        630        640        650        660 
EGPLPRQHAG LLPESLIWAY IVQLSSALRT IHTAGLACRV MDPTKILITG KTRLRVNCVG 

       670        680        690        700        710        720 
VFDVLTFDNS QNNNPLALMA QYQQADLISL GKVVLALACN SLAGIQRENL QKAMELVTIN 

       730        740        750        760        770        780 
YSSDLKNLIL YLLTDQNRMR SVNDIMPMIG ARFYTQLDAA QMRNDVIEED LAKEVQNGRL 

       790        800        810        820        830        840 
FRLLAKLGTI NERPEFQKDP TWSETGDRYL LKLFRDHLFH QVTEAGAPWI DLSHIISCLN 

       850        860        870        880 
KLDAGVPEKI SLISRDEKSV LVVTYSDLKR CFENTFQELI AAANGQL 

« Hide

Isoform 2 [UniParc].

Checksum: 8FF7B393A072FD8D
Show »

FASTA57564,465
Isoform 3 [UniParc].

Checksum: 06EAD23E1B205A4F
Show »

FASTA83389,405
Isoform 4 [UniParc].

Checksum: C3AFEB0807CE9F3B
Show »

FASTA68772,933

References

« Hide 'large scale' references
[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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: 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.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9329.2. [Q58A45-1]
RefSeqNP_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.
UniGeneHs.645015.

3D structure databases

ProteinModelPortalQ58A45.
SMRQ58A45. Positions 473-882.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid129129. 6 interactions.
IntActQ58A45. 8 interactions.

PTM databases

PhosphoSiteQ58A45.

Polymorphism databases

DMDM341942213.

Proteomic databases

MaxQBQ58A45.
PaxDbQ58A45.
PRIDEQ58A45.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000282391; ENSP00000282391; ENSG00000152520. [Q58A45-2]
ENST00000380958; ENSP00000370345; ENSG00000152520. [Q58A45-1]
ENST00000399613; ENSP00000382522; ENSG00000152520.
GeneID255967.
KEGGhsa:255967.
UCSCuc001urx.3. human. [Q58A45-3]
uc001ury.3. human. [Q58A45-2]
uc001urz.3. human. [Q58A45-1]
uc010tdo.1. human. [Q58A45-4]

Organism-specific databases

CTD255967.
GeneCardsGC13P028713.
H-InvDBHIX0011200.
HGNCHGNC:29991. PAN3.
HPAHPA028817.
neXtProtNX_Q58A45.
PharmGKBPA144596398.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG260889.
HOVERGENHBG058849.
InParanoidQ58A45.
KOK12572.
OMAYYAKDKT.
OrthoDBEOG7BS48S.
PhylomeDBQ58A45.
TreeFamTF105865.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ58A45.
BgeeQ58A45.
CleanExHS_PAN3.
GenevestigatorQ58A45.

Family and domain databases

Gene3D4.10.1000.10. 1 hit.
HAMAPMF_03181. PAN3.
InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR000571. Znf_CCCH.
[Graphical view]
SMARTSM00356. ZnF_C3H1. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPAN3. human.
GenomeRNAi255967.
NextBio92689.
PROQ58A45.

Entry information

Entry namePAN3_HUMAN
AccessionPrimary (citable) accession number: Q58A45
Secondary accession number(s): A0N0X1 expand/collapse secondary AC list , A1A4Y8, A1A4Y9, B1ALF1, B7Z3W7, Q0D2P2, Q5HYG6, Q5T515, Q5T516, Q5TBA0, Q76E13, Q8NBA6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM