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Protein

Polyadenylate-binding protein-interacting protein 1

Gene

PAIP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. RNA binding Source: ProtInc
  2. translation activator activity Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA stabilization Source: UniProtKB
  3. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  4. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
  5. positive regulation of translation Source: GOC
  6. translational initiation Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Translation regulation

Enzyme and pathway databases

ReactomeiREACT_20514. Deadenylation of mRNA.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PAIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:16945. PAIP1.

Subcellular locationi

  1. Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134941557.

Polymorphism and mutation databases

BioMutaiPAIP1.
DMDMi46397025.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 479479Polyadenylate-binding protein-interacting protein 1PRO_0000058177Add
BLAST

Proteomic databases

MaxQBiQ9H074.
PaxDbiQ9H074.
PRIDEiQ9H074.

PTM databases

PhosphoSiteiQ9H074.

Expressioni

Gene expression databases

BgeeiQ9H074.
CleanExiHS_PAIP1.
ExpressionAtlasiQ9H074. baseline and differential.
GenevestigatoriQ9H074.

Interactioni

Subunit structurei

Interacts with the RRM1-RRM2 and C-terminus regions of PABPC1 in a 1:1 stoichiometry. Interacts with EIF4A.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PABPC1P1194010EBI-81519,EBI-81531

Protein-protein interaction databases

BioGridi115851. 28 interactions.
IntActiQ9H074. 7 interactions.
MINTiMINT-196116.
STRINGi9606.ENSP00000302768.

Structurei

Secondary structure

1
479
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi158 – 17114Combined sources
Helixi173 – 1753Combined sources
Helixi176 – 19015Combined sources
Helixi194 – 20916Combined sources
Helixi215 – 22814Combined sources
Helixi238 – 25013Combined sources
Helixi253 – 2564Combined sources
Helixi261 – 28020Combined sources
Beta strandi288 – 2914Combined sources
Helixi294 – 30916Combined sources
Helixi313 – 33624Combined sources
Helixi341 – 35515Combined sources
Helixi360 – 37213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JH4NMR-B123-144[»]
3NTWX-ray2.60B/D123-144[»]
3RK6X-ray2.00A/B157-373[»]
ProteinModelPortaliQ9H074.
SMRiQ9H074. Positions 157-373.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H074.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini159 – 376218MIF4GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni116 – 14328PABPC1-interacting motif-2 (PAM2)Add
BLAST
Regioni440 – 47940PABPC1-interacting motif-1 (PAM1)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi10 – 3627Gly-richAdd
BLAST
Compositional biasi45 – 9854Pro-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 MIF4G domain.Curated

Phylogenomic databases

eggNOGiNOG253454.
GeneTreeiENSGT00630000089897.
HOGENOMiHOG000285987.
HOVERGENiHBG053492.
InParanoidiQ9H074.
KOiK14322.
OMAiDNIPQQN.
OrthoDBiEOG70CR75.
PhylomeDBiQ9H074.
TreeFamiTF325625.

Family and domain databases

Gene3Di1.25.40.180. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR009818. Ataxin-2_C.
IPR016021. MIF4-like_typ_1/2/3.
IPR003890. MIF4G-like_typ-3.
[Graphical view]
PfamiPF02854. MIF4G. 1 hit.
PF07145. PAM2. 1 hit.
[Graphical view]
SMARTiSM00543. MIF4G. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H074-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MSDGFDRAPG AGRGRSRGLG RGGGGPEGGG FPNGAGPAER ARHQPPQPKA
60 70 80 90 100
PGFLQPPPLR QPRTTPPPGA QCEVPASPQR PSRPGALPEQ TRPLRAPPSS
110 120 130 140 150
QDKIPQQNSE SAMAKPQVVV APVLMSKLSV NAPEFYPSGY SSSYTESYED
160 170 180 190 200
GCEDYPTLSE YVQDFLNHLT EQPGSFETEI EQFAETLNGC VTTDDALQEL
210 220 230 240 250
VELIYQQATS IPNFSYMGAR LCNYLSHHLT ISPQSGNFRQ LLLQRCRTEY
260 270 280 290 300
EVKDQAAKGD EVTRKRFHAF VLFLGELYLN LEIKGTNGQV TRADILQVGL
310 320 330 340 350
RELLNALFSN PMDDNLICAV KLLKLTGSVL EDAWKEKGKM DMEEIIQRIE
360 370 380 390 400
NVVLDANCSR DVKQMLLKLV ELRSSNWGRV HATSTYREAT PENDPNYFMN
410 420 430 440 450
EPTFYTSDGV PFTAADPDYQ EKYQELLERE DFFPDYEENG TDLSGAGDPY
460 470
LDDIDDEMDP EIEEAYEKFC LESERKRKQ
Length:479
Mass (Da):53,525
Last modified:March 1, 2001 - v1
Checksum:iA4820607190A3A43
GO
Isoform 2 (identifier: Q9H074-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     10-88: Missing.

Show »
Length:400
Mass (Da):45,631
Checksum:i9743587A6F54BA25
GO
Isoform 3 (identifier: Q9H074-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-112: Missing.

Note: No experimental confirmation available.

Show »
Length:367
Mass (Da):42,007
Checksum:iF03BA773A062FA9B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti239 – 2391R → C in AAH15937 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 112112Missing in isoform 3. 1 PublicationVSP_047503Add
BLAST
Alternative sequencei10 – 8879Missing in isoform 2. 1 PublicationVSP_010005Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3947.1. [Q9H074-1]
CCDS3948.1. [Q9H074-3]
CCDS47204.1. [Q9H074-2]
RefSeqiNP_006442.2. NM_006451.4. [Q9H074-1]
NP_877590.1. NM_182789.3. [Q9H074-2]
NP_899152.1. NM_183323.2. [Q9H074-3]
XP_005248287.1. XM_005248230.2. [Q9H074-3]
UniGeneiHs.482038.

Genome annotation databases

EnsembliENST00000306846; ENSP00000302768; ENSG00000172239. [Q9H074-1]
ENST00000338972; ENSP00000339622; ENSG00000172239. [Q9H074-3]
ENST00000436644; ENSP00000387729; ENSG00000172239. [Q9H074-2]
GeneIDi10605.
KEGGihsa:10605.
UCSCiuc003joa.3. human. [Q9H074-2]
uc003job.3. human. [Q9H074-1]

Polymorphism and mutation databases

BioMutaiPAIP1.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3947.1. [Q9H074-1]
CCDS3948.1. [Q9H074-3]
CCDS47204.1. [Q9H074-2]
RefSeqiNP_006442.2. NM_006451.4. [Q9H074-1]
NP_877590.1. NM_182789.3. [Q9H074-2]
NP_899152.1. NM_183323.2. [Q9H074-3]
XP_005248287.1. XM_005248230.2. [Q9H074-3]
UniGeneiHs.482038.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JH4NMR-B123-144[»]
3NTWX-ray2.60B/D123-144[»]
3RK6X-ray2.00A/B157-373[»]
ProteinModelPortaliQ9H074.
SMRiQ9H074. Positions 157-373.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115851. 28 interactions.
IntActiQ9H074. 7 interactions.
MINTiMINT-196116.
STRINGi9606.ENSP00000302768.

PTM databases

PhosphoSiteiQ9H074.

Polymorphism and mutation databases

BioMutaiPAIP1.
DMDMi46397025.

Proteomic databases

MaxQBiQ9H074.
PaxDbiQ9H074.
PRIDEiQ9H074.

Protocols and materials databases

DNASUi10605.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306846; ENSP00000302768; ENSG00000172239. [Q9H074-1]
ENST00000338972; ENSP00000339622; ENSG00000172239. [Q9H074-3]
ENST00000436644; ENSP00000387729; ENSG00000172239. [Q9H074-2]
GeneIDi10605.
KEGGihsa:10605.
UCSCiuc003joa.3. human. [Q9H074-2]
uc003job.3. human. [Q9H074-1]

Organism-specific databases

CTDi10605.
GeneCardsiGC05M043526.
HGNCiHGNC:16945. PAIP1.
MIMi605184. gene.
neXtProtiNX_Q9H074.
PharmGKBiPA134941557.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG253454.
GeneTreeiENSGT00630000089897.
HOGENOMiHOG000285987.
HOVERGENiHBG053492.
InParanoidiQ9H074.
KOiK14322.
OMAiDNIPQQN.
OrthoDBiEOG70CR75.
PhylomeDBiQ9H074.
TreeFamiTF325625.

Enzyme and pathway databases

ReactomeiREACT_20514. Deadenylation of mRNA.

Miscellaneous databases

ChiTaRSiPAIP1. human.
EvolutionaryTraceiQ9H074.
GeneWikiiPAIP1.
GenomeRNAii10605.
NextBioi40270.
PROiQ9H074.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H074.
CleanExiHS_PAIP1.
ExpressionAtlasiQ9H074. baseline and differential.
GenevestigatoriQ9H074.

Family and domain databases

Gene3Di1.25.40.180. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR009818. Ataxin-2_C.
IPR016021. MIF4-like_typ_1/2/3.
IPR003890. MIF4G-like_typ-3.
[Graphical view]
PfamiPF02854. MIF4G. 1 hit.
PF07145. PAM2. 1 hit.
[Graphical view]
SMARTiSM00543. MIF4G. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPAIP1_HUMAN
AccessioniPrimary (citable) accession number: Q9H074
Secondary accession number(s): A6NKV8
, O60455, Q96B61, Q9BS63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 1, 2001
Last modified: April 29, 2015
This is version 130 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.