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Q7Z5R6

- AB1IP_HUMAN

UniProt

Q7Z5R6 - AB1IP_HUMAN

Protein

Amyloid beta A4 precursor protein-binding family B member 1-interacting protein

Gene

APBB1IP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    Functioni

    Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling. Suppresses insulin-induced promoter activities through AP1 and SRE. Mediates Rap1-induced adhesion.2 Publications

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. platelet activation Source: Reactome
    3. signal transduction Source: InterPro

    Enzyme and pathway databases

    ReactomeiREACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_15523. Integrin alphaIIb beta3 signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
    Alternative name(s):
    APBB1-interacting protein 1
    Proline-rich EVH1 ligand 1
    Short name:
    PREL-1
    Proline-rich protein 73
    Rap1-GTP-interacting adapter molecule
    Short name:
    RIAM
    Retinoic acid-responsive proline-rich protein 1
    Short name:
    RARP-1
    Gene namesi
    Name:APBB1IP
    Synonyms:PREL1, RARP1, RIAM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:17379. APBB1IP.

    Subcellular locationi

    Cell membrane By similarity; Peripheral membrane protein By similarity. Cell projectionlamellipodium By similarity. Cell junctionfocal adhesion By similarity. Cytoplasmcytoskeleton By similarity
    Note: Colocalizes with ENA/VASP proteins at lamellipodia tips and focal adhesions, and F-actin at the leading edge. At the membrane surface, associates, via the PH domain, preferentially with the inositol phosphates, PtdIns5P and PtdIns3P. This binding appears to be necessary for the efficient interaction of the RA domain to Ras-GTPases By similarity.By similarity

    GO - Cellular componenti

    1. cytoskeleton Source: UniProtKB-SubCell
    2. cytosol Source: Reactome
    3. focal adhesion Source: UniProtKB-SubCell
    4. lamellipodium Source: UniProtKB-SubCell
    5. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134933955.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 666666Amyloid beta A4 precursor protein-binding family B member 1-interacting proteinPRO_0000181347Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei55 – 551Phosphoserine1 Publication
    Modified residuei526 – 5261Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ7Z5R6.
    PaxDbiQ7Z5R6.
    PeptideAtlasiQ7Z5R6.
    PRIDEiQ7Z5R6.

    PTM databases

    PhosphoSiteiQ7Z5R6.

    Expressioni

    Tissue specificityi

    Widely expressed with high expression in thymus, spleen, lymph node, bone marrow and peripheral leukocytes.2 Publications

    Inductioni

    By all-trans-retinoic acid (ATRA).

    Gene expression databases

    ArrayExpressiQ7Z5R6.
    BgeeiQ7Z5R6.
    CleanExiHS_APBB1IP.
    GenevestigatoriQ7Z5R6.

    Organism-specific databases

    HPAiHPA017009.

    Interactioni

    Subunit structurei

    Interacts, through the N-terminal Pro-rich region, with the WW domain of APBB1. Interacts with RAP1A, PFN1, TLN1, VASP, VCL and ENAH.2 Publications

    Protein-protein interaction databases

    BioGridi120012. 6 interactions.
    IntActiQ7Z5R6. 5 interactions.
    STRINGi9606.ENSP00000365411.

    Structurei

    Secondary structure

    1
    666
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 2518
    Turni26 – 316

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZDLX-ray2.30B1-31[»]
    ProteinModelPortaliQ7Z5R6.
    SMRiQ7Z5R6. Positions 175-434.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini176 – 26388Ras-associatingPROSITE-ProRule annotationAdd
    BLAST
    Domaini310 – 419110PHPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi129 – 14820Pro-richAdd
    BLAST
    Compositional biasi152 – 1554Poly-Glu
    Compositional biasi503 – 640138Pro-richAdd
    BLAST

    Domaini

    The two Pro-rich regions are required for the suppression of AP1 transcription activity.

    Sequence similaritiesi

    Belongs to the MRL family.Curated
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 Ras-associating domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG279449.
    HOGENOMiHOG000033749.
    HOVERGENiHBG080806.
    InParanoidiQ7Z5R6.
    KOiK17704.
    OMAiQNFYLAN.
    OrthoDBiEOG715Q3B.
    PhylomeDBiQ7Z5R6.
    TreeFamiTF317511.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR000159. Ras-assoc.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF00169. PH. 1 hit.
    PF00788. RA. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    SM00314. RA. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    PS50200. RA. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7Z5R6-1) [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

    MGESSEDIDQ MFSTLLGEMD LLTQSLGVDT LPPPDPNPPR AEFNYSVGFK    50
    DLNESLNALE DQDLDALMAD LVADISEAEQ RTIQAQKESL QNQHHSASLQ 100
    ASIFSGAASL GYGTNVAATG ISQYEDDLPP PPADPVLDLP LPPPPPEPLS 150
    QEEEEAQAKA DKIKLALEKL KEAKVKKLVV KVHMNDNSTK SLMVDERQLA 200
    RDVLDNLFEK THCDCNVDWC LYEIYPELQI ERFFEDHENV VEVLSDWTRD 250
    TENKILFLEK EEKYAVFKNP QNFYLDNRGK KESKETNEKM NAKNKESLLE 300
    ESFCGTSIIV PELEGALYLK EDGKKSWKRR YFLLRASGIY YVPKGKTKTS 350
    RDLACFIQFE NVNIYYGTQH KMKYKAPTDY CFVLKHPQIQ KESQYIKYLC 400
    CDDTRTLNQW VMGIRIAKYG KTLYDNYQRA VAKAGLASRW TNLGTVNAAA 450
    PAQPSTGPKT GTTQPNGQIP QATHSVSAVL QEAQRHAETS KDKKPALGNH 500
    HDPAVPRAPH APKSSLPPPP PVRRSSDTSG SPATPLKAKG TGGGGLPAPP 550
    DDFLPPPPPP PPLDDPELPP PPPDFMEPPP DFVPPPPPSY AGIAGSELPP 600
    PPPPPPAPAP APVPDSARPP PAVAKRPPVP PKRQENPGHP GGAGGGEQDF 650
    MSDLMKALQK KRGNVS 666
    Length:666
    Mass (Da):73,183
    Last modified:October 1, 2003 - v1
    Checksum:i525C906C490D8D97
    GO
    Isoform 2 (identifier: Q7Z5R6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         152-172: EEEEAQAKADKIKLALEKLKE → VSMWDQRWQDHQPLLPITDVP
         173-666: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:172
    Mass (Da):18,686
    Checksum:i21314883C4E8C7B9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti423 – 4231L → F in BAC41256. (PubMed:14530287)Curated
    Sequence conflicti599 – 5991Missing in AAN75525. (PubMed:15469846)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti404 – 4041T → A.
    Corresponds to variant rs34081356 [ dbSNP | Ensembl ].
    VAR_050098
    Natural varianti617 – 6171A → T.
    Corresponds to variant rs7903226 [ dbSNP | Ensembl ].
    VAR_059447

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei152 – 17221EEEEA…EKLKE → VSMWDQRWQDHQPLLPITDV P in isoform 2. 1 PublicationVSP_056542Add
    BLAST
    Alternative sequencei173 – 666494Missing in isoform 2. 1 PublicationVSP_056543Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB085852 mRNA. Translation: BAC41256.1.
    AY152730 mRNA. Translation: AAN75525.1.
    AL160287 Genomic DNA. Translation: CAH70339.1.
    AL355798 Genomic DNA. No translation available.
    CH471072 Genomic DNA. Translation: EAW86097.1.
    BC035636 mRNA. Translation: AAH35636.1.
    BC054516 mRNA. Translation: AAH54516.1.
    CCDSiCCDS31167.1.
    RefSeqiNP_061916.3. NM_019043.3.
    XP_006717514.1. XM_006717451.1.
    UniGeneiHs.310421.

    Genome annotation databases

    EnsembliENST00000356785; ENSP00000349237; ENSG00000077420.
    ENST00000376236; ENSP00000365411; ENSG00000077420.
    GeneIDi54518.
    KEGGihsa:54518.
    UCSCiuc001iss.3. human.

    Polymorphism databases

    DMDMi74750143.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB085852 mRNA. Translation: BAC41256.1 .
    AY152730 mRNA. Translation: AAN75525.1 .
    AL160287 Genomic DNA. Translation: CAH70339.1 .
    AL355798 Genomic DNA. No translation available.
    CH471072 Genomic DNA. Translation: EAW86097.1 .
    BC035636 mRNA. Translation: AAH35636.1 .
    BC054516 mRNA. Translation: AAH54516.1 .
    CCDSi CCDS31167.1.
    RefSeqi NP_061916.3. NM_019043.3.
    XP_006717514.1. XM_006717451.1.
    UniGenei Hs.310421.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ZDL X-ray 2.30 B 1-31 [» ]
    ProteinModelPortali Q7Z5R6.
    SMRi Q7Z5R6. Positions 175-434.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120012. 6 interactions.
    IntActi Q7Z5R6. 5 interactions.
    STRINGi 9606.ENSP00000365411.

    PTM databases

    PhosphoSitei Q7Z5R6.

    Polymorphism databases

    DMDMi 74750143.

    Proteomic databases

    MaxQBi Q7Z5R6.
    PaxDbi Q7Z5R6.
    PeptideAtlasi Q7Z5R6.
    PRIDEi Q7Z5R6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356785 ; ENSP00000349237 ; ENSG00000077420 .
    ENST00000376236 ; ENSP00000365411 ; ENSG00000077420 .
    GeneIDi 54518.
    KEGGi hsa:54518.
    UCSCi uc001iss.3. human.

    Organism-specific databases

    CTDi 54518.
    GeneCardsi GC10P026767.
    H-InvDB HIX0008723.
    HIX0035713.
    HGNCi HGNC:17379. APBB1IP.
    HPAi HPA017009.
    MIMi 609036. gene.
    neXtProti NX_Q7Z5R6.
    PharmGKBi PA134933955.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG279449.
    HOGENOMi HOG000033749.
    HOVERGENi HBG080806.
    InParanoidi Q7Z5R6.
    KOi K17704.
    OMAi QNFYLAN.
    OrthoDBi EOG715Q3B.
    PhylomeDBi Q7Z5R6.
    TreeFami TF317511.

    Enzyme and pathway databases

    Reactomei REACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_15523. Integrin alphaIIb beta3 signaling.

    Miscellaneous databases

    ChiTaRSi APBB1IP. human.
    GeneWikii APBB1IP.
    GenomeRNAii 54518.
    NextBioi 56912.
    PROi Q7Z5R6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7Z5R6.
    Bgeei Q7Z5R6.
    CleanExi HS_APBB1IP.
    Genevestigatori Q7Z5R6.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR000159. Ras-assoc.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF00169. PH. 1 hit.
    PF00788. RA. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    SM00314. RA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    PS50200. RA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The retinoic acid-responsive proline-rich protein is identified in promyeloleukemic HL-60 cells."
      Inagaki T., Suzuki S., Miyamoto T., Takeda T., Yamashita K., Komatsu A., Yamauchi K., Hashizume K.
      J. Biol. Chem. 278:51685-51692(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Thymus.
    2. "RIAM, an Ena/VASP and profilin ligand, interacts with Rap1-GTP and mediates Rap1-induced adhesion."
      Lafuente E.M., van Puijenbroek A.A., Krause M., Carman C.V., Freeman G.J., Berezovskaya A., Constantine E., Springer T.A., Gertler F.B., Boussiotis V.A.
      Dev. Cell 7:585-595(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH RAP1A; PFN1; VASP AND ENAH.
      Tissue: T-cell.
    3. "PREL1 provides a link from Ras signalling to the actin cytoskeleton via Ena/VASP proteins."
      Jenzora A., Behrendt B., Small J.V., Wehland J., Stradal T.E.
      FEBS Lett. 579:455-463(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Cervix carcinoma.
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 1 AND 2).
      Tissue: Blood.
    7. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55 AND SER-526, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover."
      Goult B.T., Zacharchenko T., Bate N., Tsang R., Hey F., Gingras A.R., Elliott P.R., Roberts G.C., Ballestrem C., Critchley D.R., Barsukov I.L.
      J. Biol. Chem. 288:8238-8249(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-31 IN COMPLEX WITH VCL, INTERACTION WITH VCL AND TLN1.

    Entry informationi

    Entry nameiAB1IP_HUMAN
    AccessioniPrimary (citable) accession number: Q7Z5R6
    Secondary accession number(s): Q8IWS8, Q8IYL7, Q8IZZ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 105 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 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3