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Q9H074

- PAIP1_HUMAN

UniProt

Q9H074 - PAIP1_HUMAN

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
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    2. RNA binding Source: ProtInc
    3. 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

    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

    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

    ArrayExpressiQ9H074.
    BgeeiQ9H074.
    CleanExiHS_PAIP1.
    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. 16 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.
    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

    MSDGFDRAPG AGRGRSRGLG RGGGGPEGGG FPNGAGPAER ARHQPPQPKA    50
    PGFLQPPPLR QPRTTPPPGA QCEVPASPQR PSRPGALPEQ TRPLRAPPSS 100
    QDKIPQQNSE SAMAKPQVVV APVLMSKLSV NAPEFYPSGY SSSYTESYED 150
    GCEDYPTLSE YVQDFLNHLT EQPGSFETEI EQFAETLNGC VTTDDALQEL 200
    VELIYQQATS IPNFSYMGAR LCNYLSHHLT ISPQSGNFRQ LLLQRCRTEY 250
    EVKDQAAKGD EVTRKRFHAF VLFLGELYLN LEIKGTNGQV TRADILQVGL 300
    RELLNALFSN PMDDNLICAV KLLKLTGSVL EDAWKEKGKM DMEEIIQRIE 350
    NVVLDANCSR DVKQMLLKLV ELRSSNWGRV HATSTYREAT PENDPNYFMN 400
    EPTFYTSDGV PFTAADPDYQ EKYQELLERE DFFPDYEENG TDLSGAGDPY 450
    LDDIDDEMDP EIEEAYEKFC LESERKRKQ 479
    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. 16 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.
    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

    ArrayExpressi Q9H074.
    Bgeei Q9H074.
    CleanExi HS_PAIP1.
    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

    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 1, 2014
    This is version 124 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