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Q13310 (PABP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polyadenylate-binding protein 4

Short name=PABP-4
Short name=Poly(A)-binding protein 4
Alternative name(s):
Activated-platelet protein 1
Short name=APP-1
Inducible poly(A)-binding protein
Short name=iPABP
Gene names
Name:PABPC4
Synonyms:APP1, PABP4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length644 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds the poly(A) tail of mRNA. May be involved in cytoplasmic regulatory processes of mRNA metabolism. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo By similarity.

Subunit structure

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with NFX1. Ref.8 Ref.9

Subcellular location

Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.9

Tissue specificity

Expressed at low levels in resting normal T cells; following T-cell activation, however, mRNA levels are rapidly up-regulated.

Post-translational modification

Arg-518 is dimethylated, probably to asymmetric dimethylarginine. Ref.6

Sequence similarities

Belongs to the polyadenylate-binding protein type-1 family.

Contains 1 PABC domain.

Contains 4 RRM (RNA recognition motif) domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PHLDA1Q8WV242EBI-372844,EBI-738731

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13310-1)

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: Q13310-2)

The sequence of this isoform differs from the canonical sequence as follows:
     470-497: SECPDRLAMDFGGAGAAQQGLTDSCQSG → NAPASRGLPTTTQRV
Note: No experimental confirmation available.
Isoform 3 (identifier: Q13310-3)

The sequence of this isoform differs from the canonical sequence as follows:
     468-468: T → TGNAPASRGLPTTTQRV
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 644644Polyadenylate-binding protein 4
PRO_0000081703

Regions

Domain11 – 8979RRM 1
Domain99 – 17577RRM 2
Domain191 – 26878RRM 3
Domain294 – 37077RRM 4
Domain551 – 62878PABC
Compositional bias510 – 5167Poly-Ala

Amino acid modifications

Modified residue1401Phosphotyrosine Ref.7
Modified residue3151Phosphoserine Ref.11
Modified residue3611N6,N6-dimethyllysine Ref.6
Modified residue5181Dimethylated arginine; alternate Ref.6
Modified residue5181Omega-N-methylated arginine; alternate Ref.6
Modified residue5311Phosphoserine Ref.10

Natural variations

Alternative sequence4681T → TGNAPASRGLPTTTQRV in isoform 3.
VSP_043357
Alternative sequence470 – 49728SECPD…SCQSG → NAPASRGLPTTTQRV in isoform 2.
VSP_013335
Natural variant3821Y → F.
Corresponds to variant rs9820 [ dbSNP | Ensembl ].
VAR_054048

Experimental info

Sequence conflict1141A → V in AAH65540. Ref.5

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: A761488F0B10DF5A

FASTA64470,783
        10         20         30         40         50         60 
MNAAASSYPM ASLYVGDLHS DVTEAMLYEK FSPAGPVLSI RVCRDMITRR SLGYAYVNFQ 

        70         80         90        100        110        120 
QPADAERALD TMNFDVIKGK PIRIMWSQRD PSLRKSGVGN VFIKNLDKSI DNKALYDTFS 

       130        140        150        160        170        180 
AFGNILSCKV VCDENGSKGY AFVHFETQEA ADKAIEKMNG MLLNDRKVFV GRFKSRKERE 

       190        200        210        220        230        240 
AELGAKAKEF TNVYIKNFGE EVDDESLKEL FSQFGKTLSV KVMRDPNGKS KGFGFVSYEK 

       250        260        270        280        290        300 
HEDANKAVEE MNGKEISGKI IFVGRAQKKV ERQAELKRKF EQLKQERISR YQGVNLYIKN 

       310        320        330        340        350        360 
LDDTIDDEKL RKEFSPFGSI TSAKVMLEDG RSKGFGFVCF SSPEEATKAV TEMNGRIVGS 

       370        380        390        400        410        420 
KPLYVALAQR KEERKAHLTN QYMQRVAGMR ALPANAILNQ FQPAAGGYFV PAVPQAQGRP 

       430        440        450        460        470        480 
PYYTPNQLAQ MRPNPRWQQG GRPQGFQGMP SAIRQSGPRP TLRHLAPTGS ECPDRLAMDF 

       490        500        510        520        530        540 
GGAGAAQQGL TDSCQSGGVP TAVQNLAPRA AVAAAAPRAV APYKYASSVR SPHPAIQPLQ 

       550        560        570        580        590        600 
APQPAVHVQG QEPLTASMLA AAPPQEQKQM LGERLFPLIQ TMHSNLAGKI TGMLLEIDNS 

       610        620        630        640 
ELLHMLESPE SLRSKVDEAV AVLQAHHAKK EAAQKVGAVA AATS 

« Hide

Isoform 2 [UniParc].

Checksum: 1891E205916695F6
Show »

FASTA63169,579
Isoform 3 [UniParc].

Checksum: BC4FB29689689633
Show »

FASTA66072,391

References

« Hide 'large scale' references
[1]"iPABP, an inducible poly(A)-binding protein detected in activated human T cells."
Yang H., Duckett C.S., Lindsten T.
Mol. Cell. Biol. 15:6770-6776(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Identification and structure of activated-platelet protein-1, a protein with RNA-binding domain motifs that is expressed by activated platelets."
Houng A.K., Maggini L., Clement C.Y., Reed G.L.
Eur. J. Biochem. 243:209-218(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORMS 2 AND 3).
Tissue: Placenta and Skin.
[6]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 31-41; 51-78; 84-89; 96-104; 114-129; 139-153; 158-166; 187-216; 232-240; 291-311; 313-324; 334-348; 357-370; 376-385; 510-524 AND 575-629, METHYLATION AT LYS-361 AND ARG-518, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[7]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"NFX1-123 and poly(A) binding proteins synergistically augment activation of telomerase in human papillomavirus type 16 E6-expressing cells."
Katzenellenbogen R.A., Egelkrout E.M., Vliet-Gregg P., Gewin L.C., Gafken P.R., Galloway D.A.
J. Virol. 81:3786-3796(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NFX1.
[9]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-531, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U33818 mRNA. Translation: AAC50350.1.
U75686 mRNA. Translation: AAB97309.1.
AL365277, AL845289 Genomic DNA. Translation: CAI16412.1.
AL365277, AL845289 Genomic DNA. Translation: CAI16414.1.
AL845289, AL365277 Genomic DNA. Translation: CAI12298.1.
AL845289, AL365277 Genomic DNA. Translation: CAI12300.1.
CH471059 Genomic DNA. Translation: EAX07263.1.
CH471059 Genomic DNA. Translation: EAX07264.1.
BC065540 mRNA. Translation: AAH65540.1.
BC094755 mRNA. Translation: AAH94755.1.
RefSeqNP_001129125.1. NM_001135653.1.
NP_001129126.1. NM_001135654.1.
NP_003810.1. NM_003819.3.
UniGeneHs.169900.

3D structure databases

ProteinModelPortalQ13310.
SMRQ13310. Positions 1-376, 510-643.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114296. 55 interactions.
IntActQ13310. 30 interactions.
MINTMINT-1189867.
STRING9606.ENSP00000361949.

Chemistry

ChEMBLCHEMBL5333.

PTM databases

PhosphoSiteQ13310.

Polymorphism databases

DMDM12229875.

Proteomic databases

PaxDbQ13310.
PRIDEQ13310.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372856; ENSP00000361947; ENSG00000090621. [Q13310-2]
ENST00000372857; ENSP00000361948; ENSG00000090621. [Q13310-1]
ENST00000372858; ENSP00000361949; ENSG00000090621. [Q13310-3]
GeneID8761.
KEGGhsa:8761.
UCSCuc001cdl.2. human. [Q13310-3]
uc001cdm.2. human. [Q13310-2]
uc010oiv.1. human. [Q13310-1]

Organism-specific databases

CTD8761.
GeneCardsGC01M040026.
HGNCHGNC:8557. PABPC4.
HPAHPA027301.
HPA056496.
MIM603407. gene.
neXtProtNX_Q13310.
PharmGKBPA32883.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000217922.
HOVERGENHBG002295.
KOK13126.
OMAYANHESA.
PhylomeDBQ13310.
TreeFamTF300458.

Gene expression databases

BgeeQ13310.
CleanExHS_PABPC4.
GenevestigatorQ13310.

Family and domain databases

Gene3D1.10.1900.10. 1 hit.
3.30.70.330. 4 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR006515. PABP_1234.
IPR002004. PABP_HYD.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00658. PABP. 1 hit.
PF00076. RRM_1. 4 hits.
[Graphical view]
SMARTSM00517. PolyA. 1 hit.
SM00360. RRM. 4 hits.
[Graphical view]
SUPFAMSSF63570. SSF63570. 1 hit.
TIGRFAMsTIGR01628. PABP-1234. 1 hit.
PROSITEPS51309. PABC. 1 hit.
PS50102. RRM. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPABPC4. human.
GeneWikiPABPC4.
GenomeRNAi8761.
NextBio32864.
PROQ13310.
SOURCESearch...

Entry information

Entry namePABP4_HUMAN
AccessionPrimary (citable) accession number: Q13310
Secondary accession number(s): B1ANQ8, Q4VC03, Q6P0N3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 144 of the entry and version 1 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM