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Q7Z5R6 (AB1IP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:APBB1IP
Synonyms:PREL1, RARP1, RIAM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length666 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2

Subunit structure

Interacts, through the N-terminal Pro-rich region, with the WW domain of APBB1. Interacts with RAP1A, PFN1, TLN1, VASP, VCL and ENAH. Ref.2 Ref.9

Subcellular location

Cell membrane; 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. Ref.2

Tissue specificity

Widely expressed with high expression in thymus, spleen, lymph node, bone marrow and peripheral leukocytes. Ref.1 Ref.2

Induction

By all-trans-retinoic acid (ATRA).

Domain

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

Sequence similarities

Belongs to the MRL family.

Contains 1 PH domain.

Contains 1 Ras-associating domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 666666Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
PRO_0000181347

Regions

Domain176 – 26388Ras-associating
Domain310 – 419110PH
Compositional bias129 – 14820Pro-rich
Compositional bias152 – 1554Poly-Glu
Compositional bias503 – 640138Pro-rich

Amino acid modifications

Modified residue551Phosphoserine Ref.7
Modified residue5261Phosphoserine Ref.7

Natural variations

Natural variant4041T → A.
Corresponds to variant rs34081356 [ dbSNP | Ensembl ].
VAR_050098
Natural variant6171A → T.
Corresponds to variant rs7903226 [ dbSNP | Ensembl ].
VAR_059447

Experimental info

Sequence conflict4231L → F in BAC41256. Ref.1
Sequence conflict5991Missing in AAN75525. Ref.2

Secondary structure

.... 666
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7Z5R6 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 525C906C490D8D97

FASTA66673,183
        10         20         30         40         50         60 
MGESSEDIDQ MFSTLLGEMD LLTQSLGVDT LPPPDPNPPR AEFNYSVGFK DLNESLNALE 

        70         80         90        100        110        120 
DQDLDALMAD LVADISEAEQ RTIQAQKESL QNQHHSASLQ ASIFSGAASL GYGTNVAATG 

       130        140        150        160        170        180 
ISQYEDDLPP PPADPVLDLP LPPPPPEPLS QEEEEAQAKA DKIKLALEKL KEAKVKKLVV 

       190        200        210        220        230        240 
KVHMNDNSTK SLMVDERQLA RDVLDNLFEK THCDCNVDWC LYEIYPELQI ERFFEDHENV 

       250        260        270        280        290        300 
VEVLSDWTRD TENKILFLEK EEKYAVFKNP QNFYLDNRGK KESKETNEKM NAKNKESLLE 

       310        320        330        340        350        360 
ESFCGTSIIV PELEGALYLK EDGKKSWKRR YFLLRASGIY YVPKGKTKTS RDLACFIQFE 

       370        380        390        400        410        420 
NVNIYYGTQH KMKYKAPTDY CFVLKHPQIQ KESQYIKYLC CDDTRTLNQW VMGIRIAKYG 

       430        440        450        460        470        480 
KTLYDNYQRA VAKAGLASRW TNLGTVNAAA PAQPSTGPKT GTTQPNGQIP QATHSVSAVL 

       490        500        510        520        530        540 
QEAQRHAETS KDKKPALGNH HDPAVPRAPH APKSSLPPPP PVRRSSDTSG SPATPLKAKG 

       550        560        570        580        590        600 
TGGGGLPAPP DDFLPPPPPP PPLDDPELPP PPPDFMEPPP DFVPPPPPSY AGIAGSELPP 

       610        620        630        640        650        660 
PPPPPPAPAP APVPDSARPP PAVAKRPPVP PKRQENPGHP GGAGGGEQDF MSDLMKALQK 


KRGNVS 

« Hide

References

« Hide 'large scale' references
[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], 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], 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].
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. expand/collapse author list , 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]"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].
[6]"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.
[7]"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.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB085852 mRNA. Translation: BAC41256.1.
AY152730 mRNA. Translation: AAN75525.1.
AL160287 Genomic DNA. Translation: CAH70339.1.
BC054516 mRNA. Translation: AAH54516.1.
RefSeqNP_061916.3. NM_019043.3.
UniGeneHs.310421.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZDLX-ray2.30B1-31[»]
ProteinModelPortalQ7Z5R6.
SMRQ7Z5R6. Positions 175-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120012. 6 interactions.
IntActQ7Z5R6. 5 interactions.
STRING9606.ENSP00000365411.

PTM databases

PhosphoSiteQ7Z5R6.

Polymorphism databases

DMDM74750143.

Proteomic databases

PaxDbQ7Z5R6.
PeptideAtlasQ7Z5R6.
PRIDEQ7Z5R6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376236; ENSP00000365411; ENSG00000077420.
GeneID54518.
KEGGhsa:54518.
UCSCuc001iss.3. human.

Organism-specific databases

CTD54518.
GeneCardsGC10P026767.
H-InvDBHIX0008723.
HIX0035713.
HGNCHGNC:17379. APBB1IP.
HPAHPA017009.
MIM609036. gene.
neXtProtNX_Q7Z5R6.
PharmGKBPA134933955.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG279449.
HOGENOMHOG000033749.
HOVERGENHBG080806.
InParanoidQ7Z5R6.
KOK17704.
OMANDDIDQM.
OrthoDBEOG715Q3B.
PhylomeDBQ7Z5R6.
TreeFamTF317511.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ7Z5R6.
BgeeQ7Z5R6.
CleanExHS_APBB1IP.
GenevestigatorQ7Z5R6.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR000159. Ras-assoc.
[Graphical view]
PfamPF00169. PH. 1 hit.
PF00788. RA. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
SM00314. RA. 1 hit.
[Graphical view]
PROSITEPS50003. PH_DOMAIN. 1 hit.
PS50200. RA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAPBB1IP. human.
GeneWikiAPBB1IP.
GenomeRNAi54518.
NextBio56912.
PROQ7Z5R6.
SOURCESearch...

Entry information

Entry nameAB1IP_HUMAN
AccessionPrimary (citable) accession number: Q7Z5R6
Secondary accession number(s): Q8IWS8, Q8IZZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: October 1, 2003
Last modified: April 16, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM