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Q9H074 (PAIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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-interacting protein 1

Short name=PABP-interacting protein 1
Short name=PAIP-1
Short name=Poly(A)-binding protein-interacting protein 1
Gene names
Name:PAIP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a coactivator in the regulation of translation initiation of poly(A)-containing mRNAs. Its stimulatory activity on translation is mediated via its action on PABPC1. Competes with PAIP2 for binding to PABPC1. Its association with EIF4A and PABPC1 may potentiate contacts between mRNA termini. May also be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Ref.1 Ref.6

Subunit structure

Interacts with the RRM1-RRM2 and C-terminus regions of PABPC1 in a 1:1 stoichiometry. Interacts with EIF4A. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9

Subcellular location

Cytoplasm Probable.

Domain

Only the PABPC1-interacting motif-1 (PAM1) stimulates translation initiation.

Sequence similarities

Contains 1 MIF4G domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PABPC1P1194010EBI-81519,EBI-81531

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H074-1)

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: Q9H074-2)

The sequence of this isoform differs from the canonical sequence as follows:
     10-88: Missing.
Isoform 3 (identifier: Q9H074-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-112: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 479479Polyadenylate-binding protein-interacting protein 1
PRO_0000058177

Regions

Domain159 – 376218MIF4G
Region116 – 14328PABPC1-interacting motif-2 (PAM2)
Region440 – 47940PABPC1-interacting motif-1 (PAM1)
Compositional bias10 – 3627Gly-rich
Compositional bias45 – 9854Pro-rich

Natural variations

Alternative sequence1 – 112112Missing in isoform 3.
VSP_047503
Alternative sequence10 – 8879Missing in isoform 2.
VSP_010005

Experimental info

Sequence conflict2391R → C in AAH15937. Ref.4

Secondary structure

.......................... 479
Helix Strand Turn

Details...

Sequences

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

Last modified March 1, 2001. Version 1.
Checksum: A4820607190A3A43

FASTA47953,525
        10         20         30         40         50         60 
MSDGFDRAPG AGRGRSRGLG RGGGGPEGGG FPNGAGPAER ARHQPPQPKA PGFLQPPPLR 

        70         80         90        100        110        120 
QPRTTPPPGA QCEVPASPQR PSRPGALPEQ TRPLRAPPSS QDKIPQQNSE SAMAKPQVVV 

       130        140        150        160        170        180 
APVLMSKLSV NAPEFYPSGY SSSYTESYED GCEDYPTLSE YVQDFLNHLT EQPGSFETEI 

       190        200        210        220        230        240 
EQFAETLNGC VTTDDALQEL VELIYQQATS IPNFSYMGAR LCNYLSHHLT ISPQSGNFRQ 

       250        260        270        280        290        300 
LLLQRCRTEY EVKDQAAKGD EVTRKRFHAF VLFLGELYLN LEIKGTNGQV TRADILQVGL 

       310        320        330        340        350        360 
RELLNALFSN PMDDNLICAV KLLKLTGSVL EDAWKEKGKM DMEEIIQRIE NVVLDANCSR 

       370        380        390        400        410        420 
DVKQMLLKLV ELRSSNWGRV HATSTYREAT PENDPNYFMN EPTFYTSDGV PFTAADPDYQ 

       430        440        450        460        470 
EKYQELLERE DFFPDYEENG TDLSGAGDPY LDDIDDEMDP EIEEAYEKFC LESERKRKQ 

« Hide

Isoform 2 [UniParc].

Checksum: 9743587A6F54BA25
Show »

FASTA40045,631
Isoform 3 [UniParc].

Checksum: F03BA773A062FA9B
Show »

FASTA36742,007

References

« Hide 'large scale' references
[1]"Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation."
Craig A.W.B., Haghighat A., Yu A.T.K., Sonenberg N.
Nature 392:520-523(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN TRANSLATION INITIATION STIMULATION, INTERACTION WITH PABPC1 AND EIF4A.
Tissue: Placenta.
[2]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Uterus.
[3]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(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 1 AND 2).
Tissue: Kidney and Skin.
[5]"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] OF 1-249 (ISOFORM 3).
[6]"A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex."
Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H., Shyu A.-B.
Cell 103:29-40(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, IDENTIFICATION IN A COMPLEX WITH HNRPD; SYNCRIP; PABPC1 AND UNR.
[7]"Multiple portions of poly(A)-binding protein stimulate translation in vivo."
Gray N.K., Coller J.M., Dickson K.S., Wickens M.
EMBO J. 19:4723-4733(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PABPC1.
[8]"Translational repression by a novel partner of human poly(A) binding protein, Paip2."
Khaleghpour K., Svitkin Y.V., Craig A.W.B., DeMaria C.T., Deo R.C., Burley S.K., Sonenberg N.
Mol. Cell 7:205-216(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PABPC1.
[9]"Paip1 interacts with poly(A) binding protein through two independent binding motifs."
Roy G., De Crescenzo G., Khaleghpour K., Kahvejian A., O'Connor-McCourt M., Sonenberg N.
Mol. Cell. Biol. 22:3769-3782(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PABPC1.
[10]"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
AF013758 mRNA. Translation: AAC39697.2.
AL136920 mRNA. Translation: CAB66854.1.
AC114956 Genomic DNA. No translation available.
BC005295 mRNA. Translation: AAH05295.1.
BC015937 mRNA. Translation: AAH15937.1.
DB089732 mRNA. No translation available.
RefSeqNP_006442.2. NM_006451.4.
NP_877590.1. NM_182789.3.
NP_899152.1. NM_183323.2.
XP_005248287.1. XM_005248230.1.
UniGeneHs.482038.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JH4NMR-B124-144[»]
3NTWX-ray2.60B/D123-144[»]
3RK6X-ray2.00A/B157-373[»]
ProteinModelPortalQ9H074.
SMRQ9H074. Positions 157-373.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115851. 15 interactions.
IntActQ9H074. 6 interactions.
MINTMINT-196116.
STRING9606.ENSP00000302768.

PTM databases

PhosphoSiteQ9H074.

Polymorphism databases

DMDM46397025.

Proteomic databases

PaxDbQ9H074.
PRIDEQ9H074.

Protocols and materials databases

DNASU10605.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306846; ENSP00000302768; ENSG00000172239. [Q9H074-1]
ENST00000338972; ENSP00000339622; ENSG00000172239. [Q9H074-3]
ENST00000436644; ENSP00000387729; ENSG00000172239. [Q9H074-2]
GeneID10605.
KEGGhsa:10605.
UCSCuc003joa.3. human. [Q9H074-2]
uc003job.3. human. [Q9H074-1]

Organism-specific databases

CTD10605.
GeneCardsGC05M043526.
HGNCHGNC:16945. PAIP1.
HPAHPA057695.
MIM605184. gene.
neXtProtNX_Q9H074.
PharmGKBPA134941557.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253454.
HOGENOMHOG000285987.
HOVERGENHBG053492.
InParanoidQ9H074.
KOK14322.
OMAEPTFYTE.
OrthoDBEOG70CR75.
PhylomeDBQ9H074.
TreeFamTF325625.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9H074.
BgeeQ9H074.
CleanExHS_PAIP1.
GenevestigatorQ9H074.

Family and domain databases

Gene3D1.25.40.180. 1 hit.
InterProIPR016024. ARM-type_fold.
IPR009818. Ataxin-2_C.
IPR016021. MIF4-like_typ_1/2/3.
IPR003890. MIF4G-like_typ-3.
[Graphical view]
PfamPF02854. MIF4G. 1 hit.
PF07145. PAM2. 1 hit.
[Graphical view]
SMARTSM00543. MIF4G. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPAIP1. human.
EvolutionaryTraceQ9H074.
GeneWikiPAIP1.
GenomeRNAi10605.
NextBio40270.
PROQ9H074.
SOURCESearch...

Entry information

Entry namePAIP1_HUMAN
AccessionPrimary (citable) accession number: Q9H074
Secondary accession number(s): A6NKV8 expand/collapse secondary AC list , O60455, Q96B61, Q9BS63
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 119 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM