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Protein

Polyadenylate-binding protein-interacting protein 2

Gene

PAIP2

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

Functioni

Acts as a repressor in the regulation of translation initiation of poly(A)-containing mRNAs. Its inhibitory activity on translation is mediated via its action on PABPC1. Displaces the interaction of PABPC1 with poly(A) RNA and competes with PAIP1 for binding to PABPC1. Its association with PABPC1 results in disruption of the cytoplasmic poly(A) RNP structure organization.1 Publication

GO - Molecular functioni

  • mRNA binding Source: Ensembl
  • translation repressor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Translation regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Polyadenylate-binding protein-interacting protein 2
Short name:
PABP-interacting protein 2
Short name:
PAIP-2
Short name:
Poly(A)-binding protein-interacting protein 2
Gene namesi
Name:PAIP2
Synonyms:PAIP2A
ORF Names:HSPC218
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:17970. PAIP2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134897284.

Polymorphism and mutation databases

DMDMi46397013.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 127127Polyadenylate-binding protein-interacting protein 2PRO_0000058179Add
BLAST

Post-translational modificationi

Ubiquitinated, leading to its degradation by the proteasome.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiQ9BPZ3.
MaxQBiQ9BPZ3.
PaxDbiQ9BPZ3.
PeptideAtlasiQ9BPZ3.
PRIDEiQ9BPZ3.

PTM databases

iPTMnetiQ9BPZ3.
PhosphoSiteiQ9BPZ3.

Expressioni

Tissue specificityi

Expressed at highest level in testis, but also abundant in brain, cervix, lung, ovary, placenta, adipose tissue, thymus and thyroid.1 Publication

Gene expression databases

BgeeiQ9BPZ3.
CleanExiHS_PAIP2.
ExpressionAtlasiQ9BPZ3. baseline and differential.
GenevisibleiQ9BPZ3. HS.

Organism-specific databases

HPAiCAB037212.
HPA035945.
HPA056766.

Interactioni

Subunit structurei

Interacts with the second and third RRM domains and C-terminus regions of PABPC1 in a 2:1 stoichiometry.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PABPC1P119405EBI-2957445,EBI-81531
UBR5O950715EBI-2957445,EBI-358329

Protein-protein interaction databases

BioGridi119404. 12 interactions.
IntActiQ9BPZ3. 6 interactions.
MINTiMINT-1899106.
STRINGi9606.ENSP00000265192.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JGNNMR-B106-127[»]
3KUSX-ray1.40C/D109-123[»]
3KUTX-ray1.50C/D109-125[»]
ProteinModelPortaliQ9BPZ3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BPZ3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 7554PABPC1-interacting motif-1 (PAM1)Add
BLAST
Regioni105 – 12016PABPC1-interacting motif-2 (PAM2)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi33 – 7240Glu-richAdd
BLAST

Domaini

Only the PABPC1-interacting motif-1 (PAM1) interferes with the binding of PABPC1 to poly(A) RNA and translation initiation.

Sequence similaritiesi

Belongs to the PAIP2 family.Curated

Phylogenomic databases

eggNOGiENOG410IW9Y. Eukaryota.
ENOG410Y214. LUCA.
GeneTreeiENSGT00390000017284.
HOGENOMiHOG000008098.
HOVERGENiHBG053493.
InParanoidiQ9BPZ3.
OMAiWTDQIVY.
PhylomeDBiQ9BPZ3.
TreeFamiTF326855.

Family and domain databases

InterProiIPR009818. Ataxin-2_C.
[Graphical view]
PfamiPF07145. PAM2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BPZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKDPSRSSTS PSIINEDVII NGHSHEDDNP FAEYMWMENE EEFNRQIEEE
60 70 80 90 100
LWEEEFIERC FQEMLEEEEE HEWFIPARDL PQTMDQIQDQ FNDLVISDGS
110 120
SLEDLVVKSN LNPNAKEFVP GVKYGNI
Length:127
Mass (Da):14,984
Last modified:June 1, 2001 - v1
Checksum:iCAC27C537E5C6E22
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 981D → E in CAB66575 (PubMed:11230166).Curated
Sequence conflicti116 – 1161K → T in AAF36138 (PubMed:11042152).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF317675 mRNA. Translation: AAK11562.1.
AF151052 mRNA. Translation: AAF36138.1.
AL136640 mRNA. Translation: CAB66575.1.
AK314672 mRNA. Translation: BAG37228.1.
CH471062 Genomic DNA. Translation: EAW62107.1.
CH471062 Genomic DNA. Translation: EAW62108.1.
CH471062 Genomic DNA. Translation: EAW62111.1.
CH471062 Genomic DNA. Translation: EAW62112.1.
BC001716 mRNA. Translation: AAH01716.1.
BC048106 mRNA. Translation: AAH48106.1.
BC062718 mRNA. Translation: AAH62718.1.
CCDSiCCDS4211.1.
RefSeqiNP_001028284.1. NM_001033112.2.
NP_057564.3. NM_016480.4.
XP_011541730.1. XM_011543428.1.
UniGeneiHs.396644.

Genome annotation databases

EnsembliENST00000265192; ENSP00000265192; ENSG00000120727.
ENST00000394795; ENSP00000378275; ENSG00000120727.
ENST00000510080; ENSP00000422508; ENSG00000120727.
GeneIDi51247.
KEGGihsa:51247.
UCSCiuc003led.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF317675 mRNA. Translation: AAK11562.1.
AF151052 mRNA. Translation: AAF36138.1.
AL136640 mRNA. Translation: CAB66575.1.
AK314672 mRNA. Translation: BAG37228.1.
CH471062 Genomic DNA. Translation: EAW62107.1.
CH471062 Genomic DNA. Translation: EAW62108.1.
CH471062 Genomic DNA. Translation: EAW62111.1.
CH471062 Genomic DNA. Translation: EAW62112.1.
BC001716 mRNA. Translation: AAH01716.1.
BC048106 mRNA. Translation: AAH48106.1.
BC062718 mRNA. Translation: AAH62718.1.
CCDSiCCDS4211.1.
RefSeqiNP_001028284.1. NM_001033112.2.
NP_057564.3. NM_016480.4.
XP_011541730.1. XM_011543428.1.
UniGeneiHs.396644.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JGNNMR-B106-127[»]
3KUSX-ray1.40C/D109-123[»]
3KUTX-ray1.50C/D109-125[»]
ProteinModelPortaliQ9BPZ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119404. 12 interactions.
IntActiQ9BPZ3. 6 interactions.
MINTiMINT-1899106.
STRINGi9606.ENSP00000265192.

PTM databases

iPTMnetiQ9BPZ3.
PhosphoSiteiQ9BPZ3.

Polymorphism and mutation databases

DMDMi46397013.

Proteomic databases

EPDiQ9BPZ3.
MaxQBiQ9BPZ3.
PaxDbiQ9BPZ3.
PeptideAtlasiQ9BPZ3.
PRIDEiQ9BPZ3.

Protocols and materials databases

DNASUi51247.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265192; ENSP00000265192; ENSG00000120727.
ENST00000394795; ENSP00000378275; ENSG00000120727.
ENST00000510080; ENSP00000422508; ENSG00000120727.
GeneIDi51247.
KEGGihsa:51247.
UCSCiuc003led.5. human.

Organism-specific databases

CTDi51247.
GeneCardsiPAIP2.
HGNCiHGNC:17970. PAIP2.
HPAiCAB037212.
HPA035945.
HPA056766.
MIMi605604. gene.
neXtProtiNX_Q9BPZ3.
PharmGKBiPA134897284.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IW9Y. Eukaryota.
ENOG410Y214. LUCA.
GeneTreeiENSGT00390000017284.
HOGENOMiHOG000008098.
HOVERGENiHBG053493.
InParanoidiQ9BPZ3.
OMAiWTDQIVY.
PhylomeDBiQ9BPZ3.
TreeFamiTF326855.

Miscellaneous databases

ChiTaRSiPAIP2. human.
EvolutionaryTraceiQ9BPZ3.
GeneWikiiPAIP2.
GenomeRNAii51247.
NextBioi54373.
PROiQ9BPZ3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BPZ3.
CleanExiHS_PAIP2.
ExpressionAtlasiQ9BPZ3. baseline and differential.
GenevisibleiQ9BPZ3. HS.

Family and domain databases

InterProiIPR009818. Ataxin-2_C.
[Graphical view]
PfamiPF07145. PAM2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, FUNCTION IN TRANSLATION INHIBITION, INTERACTION WITH PABPC1.
    Tissue: Placenta.
  2. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Umbilical cord blood.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal brain.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Eye and Testis.
  7. "Dual interactions of the translational repressor Paip2 with poly(A) binding protein."
    Khaleghpour K., Kahvejian A., De Crescenzo G., Roy G., Svitkin Y.V., Imataka H., O'Connor-McCourt M., Sonenberg N.
    Mol. Cell. Biol. 21:5200-5213(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PABPC1.
  8. "Regulation of poly(A) binding protein function in translation: Characterization of the Paip2 homolog, Paip2B."
    Berlanga J.J., Baass A., Sonenberg N.
    RNA 12:1556-1568(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, UBIQUITINATION.
  9. "Structure and function of the C-terminal PABC domain of human poly(A)-binding protein."
    Kozlov G., Trempe J.F., Khaleghpour K., Kahvejian A., Ekiel I., Gehring K.
    Proc. Natl. Acad. Sci. U.S.A. 98:4409-4413(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 106-127.

Entry informationi

Entry nameiPAIP2_HUMAN
AccessioniPrimary (citable) accession number: Q9BPZ3
Secondary accession number(s): B2RBI1
, D3DQC6, Q49A06, Q9H0Y5, Q9P0Q8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 110 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

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 one 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.