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Q7Z5R6

- AB1IP_HUMAN

UniProt

Q7Z5R6 - AB1IP_HUMAN

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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

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
Complete GO annotation...

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. cell junction Source: UniProtKB-KW
  2. cell projection Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB-KW
  4. cytosol Source: Reactome
  5. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

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

BgeeiQ7Z5R6.
CleanExiHS_APBB1IP.
ExpressionAtlasiQ7Z5R6. baseline and differential.
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. 9 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.
GeneTreeiENSGT00550000074537.
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

        10         20         30         40         50
MGESSEDIDQ MFSTLLGEMD LLTQSLGVDT LPPPDPNPPR AEFNYSVGFK
60 70 80 90 100
DLNESLNALE DQDLDALMAD LVADISEAEQ RTIQAQKESL QNQHHSASLQ
110 120 130 140 150
ASIFSGAASL GYGTNVAATG ISQYEDDLPP PPADPVLDLP LPPPPPEPLS
160 170 180 190 200
QEEEEAQAKA DKIKLALEKL KEAKVKKLVV KVHMNDNSTK SLMVDERQLA
210 220 230 240 250
RDVLDNLFEK THCDCNVDWC LYEIYPELQI ERFFEDHENV VEVLSDWTRD
260 270 280 290 300
TENKILFLEK EEKYAVFKNP QNFYLDNRGK KESKETNEKM NAKNKESLLE
310 320 330 340 350
ESFCGTSIIV PELEGALYLK EDGKKSWKRR YFLLRASGIY YVPKGKTKTS
360 370 380 390 400
RDLACFIQFE NVNIYYGTQH KMKYKAPTDY CFVLKHPQIQ KESQYIKYLC
410 420 430 440 450
CDDTRTLNQW VMGIRIAKYG KTLYDNYQRA VAKAGLASRW TNLGTVNAAA
460 470 480 490 500
PAQPSTGPKT GTTQPNGQIP QATHSVSAVL QEAQRHAETS KDKKPALGNH
510 520 530 540 550
HDPAVPRAPH APKSSLPPPP PVRRSSDTSG SPATPLKAKG TGGGGLPAPP
560 570 580 590 600
DDFLPPPPPP PPLDDPELPP PPPDFMEPPP DFVPPPPPSY AGIAGSELPP
610 620 630 640 650
PPPPPPAPAP APVPDSARPP PAVAKRPPVP PKRQENPGHP GGAGGGEQDF
660
MSDLMKALQK KRGNVS
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. [Q7Z5R6-1]
RefSeqiNP_061916.3. NM_019043.3.
XP_006717514.1. XM_006717451.1.
UniGeneiHs.310421.

Genome annotation databases

EnsembliENST00000356785; ENSP00000349237; ENSG00000077420. [Q7Z5R6-2]
ENST00000376236; ENSP00000365411; ENSG00000077420. [Q7Z5R6-1]
GeneIDi54518.
KEGGihsa:54518.
UCSCiuc001iss.3. human. [Q7Z5R6-1]

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. [Q7Z5R6-1 ]
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. 9 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 . [Q7Z5R6-2 ]
ENST00000376236 ; ENSP00000365411 ; ENSG00000077420 . [Q7Z5R6-1 ]
GeneIDi 54518.
KEGGi hsa:54518.
UCSCi uc001iss.3. human. [Q7Z5R6-1 ]

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.
GeneTreei ENSGT00550000074537.
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

Bgeei Q7Z5R6.
CleanExi HS_APBB1IP.
ExpressionAtlasi Q7Z5R6. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 106 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