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Q9H074

- PAIP1_HUMAN

UniProt

Q9H074 - PAIP1_HUMAN

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Protein

Polyadenylate-binding protein-interacting protein 1

Gene

PAIP1

Organism
Homo sapiens (Human)
Status
Reviewed - 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 metabolic process Source: Reactome
  3. mRNA stabilization Source: UniProtKB
  4. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  5. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
  6. positive regulation of translation Source: GOC
  7. RNA metabolic process Source: Reactome
  8. 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: Chromosome 5

Organism-specific databases

HGNCiHGNC:16945. PAIP1.

Subcellular locationi

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.

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.

Organism-specific databases

HPAiHPA057695.

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. 31 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 – 17114
Helixi173 – 1753
Helixi176 – 19015
Helixi194 – 20916
Helixi215 – 22814
Helixi238 – 25013
Helixi253 – 2564
Helixi261 – 28020
Beta strandi288 – 2914
Helixi294 – 30916
Helixi313 – 33624
Helixi341 – 35515
Helixi360 – 37213

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiEPTFYTE.
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. Align

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:
EMBL
GenBank
DDBJ
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_005248230.1. [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 databases

DMDMi46397025.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS3947.1. [Q9H074-1 ]
CCDS3948.1. [Q9H074-3 ]
CCDS47204.1. [Q9H074-2 ]
RefSeqi NP_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_005248230.1. [Q9H074-3 ]
UniGenei Hs.482038.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JH4 NMR - B 123-144 [» ]
3NTW X-ray 2.60 B/D 123-144 [» ]
3RK6 X-ray 2.00 A/B 157-373 [» ]
ProteinModelPortali Q9H074.
SMRi Q9H074. Positions 157-373.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115851. 31 interactions.
IntActi Q9H074. 7 interactions.
MINTi MINT-196116.
STRINGi 9606.ENSP00000302768.

PTM databases

PhosphoSitei Q9H074.

Polymorphism databases

DMDMi 46397025.

Proteomic databases

MaxQBi Q9H074.
PaxDbi Q9H074.
PRIDEi Q9H074.

Protocols and materials databases

DNASUi 10605.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000306846 ; ENSP00000302768 ; ENSG00000172239 . [Q9H074-1 ]
ENST00000338972 ; ENSP00000339622 ; ENSG00000172239 . [Q9H074-3 ]
ENST00000436644 ; ENSP00000387729 ; ENSG00000172239 . [Q9H074-2 ]
GeneIDi 10605.
KEGGi hsa:10605.
UCSCi uc003joa.3. human. [Q9H074-2 ]
uc003job.3. human. [Q9H074-1 ]

Organism-specific databases

CTDi 10605.
GeneCardsi GC05M043526.
HGNCi HGNC:16945. PAIP1.
HPAi HPA057695.
MIMi 605184. gene.
neXtProti NX_Q9H074.
PharmGKBi PA134941557.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG253454.
GeneTreei ENSGT00630000089897.
HOGENOMi HOG000285987.
HOVERGENi HBG053492.
InParanoidi Q9H074.
KOi K14322.
OMAi EPTFYTE.
OrthoDBi EOG70CR75.
PhylomeDBi Q9H074.
TreeFami TF325625.

Enzyme and pathway databases

Reactomei REACT_20514. Deadenylation of mRNA.

Miscellaneous databases

ChiTaRSi PAIP1. human.
EvolutionaryTracei Q9H074.
GeneWikii PAIP1.
GenomeRNAii 10605.
NextBioi 40270.
PROi Q9H074.
SOURCEi Search...

Gene expression databases

Bgeei Q9H074.
CleanExi HS_PAIP1.
ExpressionAtlasi Q9H074. baseline and differential.
Genevestigatori Q9H074.

Family and domain databases

Gene3Di 1.25.40.180. 1 hit.
InterProi IPR016024. ARM-type_fold.
IPR009818. Ataxin-2_C.
IPR016021. MIF4-like_typ_1/2/3.
IPR003890. MIF4G-like_typ-3.
[Graphical view ]
Pfami PF02854. MIF4G. 1 hit.
PF07145. PAM2. 1 hit.
[Graphical view ]
SMARTi SM00543. MIF4G. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 125 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