Q13310 (PABP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	644 AA.
Sequence status	Complete.
Protein existence	Evidence 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 mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with NFX1. Ref.9
Subcellular location	Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.10
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 Ref.7
Sequence similarities	Belongs to the polyadenylate-binding protein type-1 family. Contains 1 PABC domain. Contains 4 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	RNA-binding
PTM	Acetylation Methylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	RNA catabolic process Traceable author statement. Source: ProtInc RNA processing Traceable author statement. Source: ProtInc blood coagulation Traceable author statement. Source: ProtInc translation Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from direct assay Ref.1. Source: MGI ribonucleoprotein complex Inferred from direct assay Ref.10. Source: UniProtKB
Molecular function	nucleotide binding Inferred from electronic annotation. Source: InterPro poly(A) RNA binding Inferred from direct assay Ref.1. Source: MGI poly(U) RNA binding Inferred from direct assay Ref.1. Source: MGI protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PHLDA1	Q8WV24	2	EBI-372844,EBI-738731

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 644	644	Polyadenylate-binding protein 4		PRO_0000081703
Regions
	Domain	11 – 89	79	RRM 1
	Domain	99 – 175	77	RRM 2
	Domain	191 – 268	78	RRM 3
	Domain	294 – 370	77	RRM 4
	Domain	551 – 628	78	PABC
	Compositional bias	510 – 516	7	Poly-Ala
Amino acid modifications
	Modified residue	54	1	Phosphotyrosine Ref.8
	Modified residue	96	1	Phosphoserine Ref.11
	Modified residue	104	1	N6-acetyllysine Ref.12
	Modified residue	108	1	N6-acetyllysine Ref.12
	Modified residue	140	1	Phosphotyrosine Ref.8
	Modified residue	361	1	N6,N6-dimethyllysine Ref.6
	Modified residue	518	1	Dimethylated arginine; alternate Ref.6 Ref.7
	Modified residue	518	1	Omega-N-methylated arginine; alternate Ref.6 Ref.7
	Modified residue	531	1	Phosphoserine Ref.11
Natural variations
	Alternative sequence	470 – 497	28	SECPD…SCQSG → NAPASRGLPTTTQRV in isoform 2.		VSP_013335
	Natural variant	382	1	Y → F. Corresponds to variant rs9820 [ dbSNP | Ensembl ].		VAR_054048
Experimental info
	Sequence conflict	114	1	A → V in AAH65540. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: A761488F0B10DF5A	FASTA	644	70,783
	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
	Isoform 2 [UniParc]. Checksum: 1891E205916695F6	FASTA	631	69,579
	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 TLRHLAPTGN APASRGLPTT 490 500 510 520 530 540 TQRVGVPTAV QNLAPRAAVA AAAPRAVAPY KYASSVRSPH PAIQPLQAPQ PAVHVQGQEP 550 560 570 580 590 600 LTASMLAAAP PQEQKQMLGE RLFPLIQTMH SNLAGKITGM LLEIDNSELL HMLESPESLR 610 620 630 SKVDEAVAVL QAHHAKKEAA QKVGAVAAAT S

References

	« Hide 'large scale' referencesShow '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: 8524242] [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: 9030741] [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. , 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: 16710414] [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. , 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC." Ong S.E., Mittler G., Mann M. Nat. Methods 1:119-126(2004) [PubMed: 15782174] [Abstract] Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-518, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-54 AND TYR-140, MASS SPECTROMETRY.
[9]	"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: 17267499] [Abstract] Cited for: INTERACTION WITH NFX1.
[10]	"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: 17289661] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[11]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-531, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-104 AND LYS-108, MASS SPECTROMETRY.
[13]	"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: 21269460] [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: CAI16414.1. AL845289, AL365277 Genomic DNA. Translation: CAI12300.1. CH471059 Genomic DNA. Translation: EAX07264.1. BC065540 mRNA. Translation: AAH65540.1.
IPI	IPI00012726. IPI00555747.
RefSeq	NP_001129126.1. NM_001135654.1. NP_003810.1. NM_003819.3.
UniGene	Hs.169900.
3D structure databases
ProteinModelPortal	Q13310.
SMR	Q13310. Positions 9-376, 510-643.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13310. 10 interactions.
MINT	MINT-1189867.
STRING	Q13310.
PTM databases
PhosphoSite	Q13310.
Polymorphism databases
DMDM	12229875.
Proteomic databases
PRIDE	Q13310.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000372857; ENSP00000361948; ENSG00000090621.
GeneID	8761.
KEGG	hsa:8761.
UCSC	uc001cdn.1. human.
Organism-specific databases
CTD	8761.
GeneCards	GC01M040026.
H-InvDB	HIX0000457.
HGNC	HGNC:8557. PABPC4.
MIM	603407. gene.
neXtProt	NX_Q13310.
PharmGKB	PA32883.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10942.
HOVERGEN	HBG002295.
OrthoDB	EOG4T1HM1.
PhylomeDB	Q13310.
Gene expression databases
ArrayExpress	Q13310.
Bgee	Q13310.
CleanEx	HS_PABPC4.
Genevestigator	Q13310.
GermOnline	ENSG00000090621. Homo sapiens.
Family and domain databases
InterPro	IPR012677. Nucleotide-bd_a/b_plait. IPR006515. PABP_1234. IPR002004. PABP_HYD. IPR000504. RRM_dom. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 4 hits. G3DSA:1.10.1900.10. PABP_HYD. 1 hit.
KO	K13126.
Pfam	PF00658. PABP. 1 hit. PF00076. RRM_1. 4 hits. [Graphical view]
SMART	SM00517. PolyA. 1 hit. SM00360. RRM. 4 hits. [Graphical view]
SUPFAM	SSF63570. PABP_HYD. 1 hit.
TIGRFAMs	TIGR01628. PABP-1234. 1 hit.
PROSITE	PS51309. PABC. 1 hit. PS50102. RRM. 4 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	32864.
SOURCE	Search...

Entry information

Entry name

PABP4_HUMAN

Accession

Primary (citable) accession number: Q13310
Secondary accession number(s): B1ANQ8, Q6P0N3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.