Q7Z5R6 (AB1IP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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
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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	666 AA.
Sequence status	Complete.
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. 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 projection › lamellipodium By similarity. Cell junction › focal adhesion By similarity. Cytoplasm › cytoskeleton 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.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Polymorphism
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	platelet activation Traceable author statement. Source: Reactome signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome focal adhesion Inferred from electronic annotation. Source: UniProtKB-SubCell lamellipodium Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phospholipid binding Inferred from electronic annotation. Source: InterPro
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

55

1

Phosphoserine Ref.7

Modified residue

526

1

Phosphoserine Ref.7

Modified residue

531

1

Phosphoserine By similarity

Natural variations

Natural variant

404

1

T → A.
Corresponds to variant rs34081356 [ dbSNP | Ensembl ].

VAR_050098

Natural variant

617

1

A → T.
Corresponds to variant rs7903226 [ dbSNP | Ensembl ].

VAR_059447

Experimental info

Sequence conflict

423

1

L → F in BAC41256. Ref.1

Sequence conflict

599

1

Missing in AAN75525. Ref.2

Secondary structure

1

.

.

.

.

666

Helix Strand Turn

Details...

Helix

8 – 25

18

Turn

26 – 31

6

Sequences

	Sequence		Length	Mass (Da)
	Q7Z5R6 [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] [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. , 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, MASS SPECTROMETRY. 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. 0:0-0(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.

IPI

IPI00376219.

RefSeq

NP_061916.3. NM_019043.3.

UniGene

Hs.310421.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ZDL	X-ray	2.30	B	1-31	[»]

ProteinModelPortal

Q7Z5R6.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q7Z5R6. 4 interactions.

STRING

9606.ENSP00000365411.

PTM databases

PhosphoSite

Q7Z5R6.

Polymorphism databases

DMDM

74750143.

Proteomic databases

PaxDb

Q7Z5R6.

PeptideAtlas

Q7Z5R6.

PRIDE

Q7Z5R6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000376236; ENSP00000365411; ENSG00000077420.

GeneID

54518.

KEGG

hsa:54518.

UCSC

uc001iss.3. human.

Organism-specific databases

CTD

54518.

GeneCards

GC10P026767.

H-InvDB

HIX0008723.
HIX0035713.

HGNC

HGNC:17379. APBB1IP.

HPA

HPA017009.

MIM

609036. gene.

neXtProt

NX_Q7Z5R6.

PharmGKB

PA134933955.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG279449.

HOGENOM

HOG000033749.

HOVERGEN

HBG080806.

InParanoid

Q7Z5R6.

OMA

RDTENKI.

OrthoDB

EOG49W2FB.

PhylomeDB

Q7Z5R6.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q7Z5R6.

Bgee

Q7Z5R6.

CleanEx

HS_APBB1IP.

Genevestigator

Q7Z5R6.

GermOnline

ENSG00000077420. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR000159. Ras-assoc.
[Graphical view]

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

ChiTaRS

APBB1IP. human.

GenomeRNAi

54518.

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:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.