Reviewed, UniProtKB/Swiss-Prot Q7Z5R6 (AB1IP_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	666 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 projection › lamellipodiumBy similarity. Cell junction › focal adhesionBy similarity. Cytoplasm › cytoskeletonBy 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.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cell projection Inferred from electronic annotation. Source: UniProtKB-KW cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 666	666	Amyloid beta A4 precursor protein-binding family B member 1-interacting protein		PRO_0000181347
Regions
	Domain	176 – 263	88	Ras-associating
	Domain	310 – 419	110	PH
	Compositional bias	129 – 148	20	Pro-rich
	Compositional bias	152 – 155	4	Poly-Glu
	Compositional bias	503 – 640	138	Pro-rich
Amino acid modifications
	Modified residue	531	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	423	1	L → F in BAC41256. Ref.1
	Sequence conflict	599	1	Missing in AAN75525. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q7Z5R6-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 525C906C490D8D97	FASTA	666	73,183
	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

References

	« Hide 'large scale' referencesShow '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. , 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
EMBLGenBankDDBJ	AB085852 mRNA. Translation: BAC41256.1. AY152730 mRNA. Translation: AAN75525.1. AL160287 Genomic DNA. Translation: CAH70339.1. BC054516 mRNA. Translation: AAH54516.1.
RefSeq	NP_061916.3.
UniGene	Hs.310421
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q7Z5R6.
Proteomic databases
PeptideAtlas	Q7Z5R6.
Genome annotation databases
Ensembl	ENSG00000077420. Homo sapiens. [Contig view]
GeneID	54518.
KEGG	hsa:54518.
Organism-specific databases
H-InvDB	HIX0008719. HIX0035713.
HGNC	HGNC:17379. APBB1IP.
MIM	609036. gene.
PharmGKB	PA134933955.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	Q7Z5R6.
HOVERGEN	Q7Z5R6.
Gene expression databases
ArrayExpress	Q7Z5R6.
CleanEx	HS_APBB1IP.
GermOnline	ENSG00000077420. Homo sapiens.
Family and domain databases
InterPro	IPR001849. PH. IPR011993. PH_type. IPR000159. Ras-assoc. [Graphical view]
Gene3D	G3DSA:2.30.29.30. PH_type. 1 hit.
Pfam	PF00169. PH. 1 hit. PF00788. RA. 1 hit. [Graphical view]
SMART	SM00233. PH. 1 hit. SM00314. RA. 1 hit. [Graphical view]
PROSITE	PS50003. PH_DOMAIN. 1 hit. PS50200. RA. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
LinkHub	Q7Z5R6.
NextBio	56912.
SOURCE	Search...

Entry information

Entry name

AB1IP_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)