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Reviewed, UniProtKB/Swiss-Prot Q7Z5R6 (AB1IP_HUMAN)

Last modified November 25, 2008. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
    Rap1-GTP-interacting adapter molecule
      Short name=RIAM
    Proline-rich EVH1 ligand 1
      Short name=PREL-1
    Proline-rich protein 73
    Retinoic acid-responsive proline-rich protein 1
      Short name=RARP-1
Gene names
Name: APBB1IP
Synonyms: PREL1, RARP1, RIAM
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length666 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Subunit structure

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

Subcellular location

Cell membrane; Peripheral membrane proteinBy similarity. Cell projectionlamellipodiumBy similarity. Cell junctionfocal adhesionBy similarity. CytoplasmcytoskeletonBy 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, PtdIns(5)P and PtdIns(3)P. This binding appears to be necessary for the efficient interaction of the RA domain to Ras-GTPases By similarity.

Tissue specificity

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

Induction

Induced by all-trans-retinoic acid.

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 residue5311Phosphoserine By similarity

Experimental info

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

Sequences

Sequence LengthMass (Da)Tools
Q7Z5R6-1 [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: 14530287] [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: 15469846] [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: 15642358] [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: 15164054] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

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

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteQ7Z5R6.

Proteomic databases

PeptideAtlasQ7Z5R6.

Genome annotation databases

EnsemblENSG00000077420. Homo sapiens. [Contig view]
GeneID54518.
KEGGhsa:54518.

Organism-specific databases

H-InvDBHIX0008719.
HIX0035713.
HGNCHGNC:17379. APBB1IP.
MIM609036. gene.
PharmGKBPA134933955.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMQ7Z5R6.
HOVERGENQ7Z5R6.

Gene expression databases

ArrayExpressQ7Z5R6.
CleanExHS_APBB1IP.
GermOnlineENSG00000077420. Homo sapiens.

Family and domain databases

InterProIPR001849. PH.
IPR011993. PH_type.
IPR000159. Ras-assoc.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 1 hit.
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 Resources

LinkHubQ7Z5R6.
NextBio56912.
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: November 25, 2008
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 10

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

MIM cross-references

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

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents